|
Name |
Accession |
Description |
Interval |
E-value |
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
18-531 |
0e+00 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 788.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 18 SDNVAVIVPETDTQVTYRDLSHMVGHFQTMFTNPNSPlygavfRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYK 97
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIK------KGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 98 EKEFNFYLNDLKSKAICVPKGTtklqSSEILKSASTFGCFIVELAFDATRFRVeydiyspednykRVIYRSLNNAKFVNT 177
Cdd:cd05926 75 KAEFEFYLADLGSKLVLTPKGE----LGPASRAASKLGLAILELALDVGVLIR------------APSAESLSNLLADKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 178 NpVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQG 257
Cdd:cd05926 139 N-AKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPN---PFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAY 334
Cdd:cd05926 218 SVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNpesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 335 AMTEASHQMTSNNLPPGKRKPGTVGQPQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFR 414
Cdd:cd05926 298 GMTEAAHQMTSNPLPPGPRKPGSVGKPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFK-DGWFR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 415 TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELV 494
Cdd:cd05926 377 TGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELR 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 398365585 495 NFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd05926 457 AFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
19-535 |
1.22e-142 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 418.83 E-value: 1.22e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIvpETDTQVTYRDLSHMV----GHFQTMftnpnsplygAVFRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---P 91
Cdd:COG0318 14 DRPALV--FGGRRLTYAELDARArrlaAALRAL----------GVGPGDRVALLLPNSPEFVVAFLAA---LRAGAvvvP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 92 LNPNYKEKEFNFYLNDLKSKAICVpkgttklqsseilksastfgcfivelafdatrfrveydiyspednykrviyrslnn 171
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 172 akfvntnpvkfpgfarssdvALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLS 251
Cdd:COG0318 103 --------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 252 TFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFNAP 329
Cdd:COG0318 163 PLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERFGVR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 VLEAYAMTEASHQMTSNNLPPGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtk 408
Cdd:COG0318 243 IVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLpGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 409 RENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKM 488
Cdd:COG0318 321 RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAEL 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 398365585 489 TYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAK 535
Cdd:COG0318 401 DAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
18-528 |
5.72e-115 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 348.78 E-value: 5.72e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 18 SDNVAVIVPetDTQVTYRDLSHMVGHFQTMFTNPNsplygaVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYK 97
Cdd:cd05936 13 PDKTALIFM--GRKLTYRELDALAEAFAAGLQNLG------VQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 98 EKEFNFYLNDLKSKAICVPKGTTKLqsseilksastfgcfiveLAFDATRFRVEYDiySPEDnykrviyrslnnakfvnt 177
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDL------------------LAAGAPLGERVAL--TPED------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 178 npvkfpgfarssdVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYK--LTPLDRSYVVMPLFHVHGLIGVLLSTFRT 255
Cdd:cd05936 127 -------------VAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALLLPLAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 256 QGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPN--PFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEA 333
Cdd:cd05936 194 GATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKkrDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 334 YAMTEAShQMTSNNLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRENY 412
Cdd:cd05936 274 YGLTETS-PVVAVNPLDGPRKPGSIGIPlPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF--VDGW 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 413 FRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEE 492
Cdd:cd05936 351 LRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEE 430
|
490 500 510
....*....|....*....|....*....|....*.
gi 398365585 493 LVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRV 528
Cdd:cd05936 431 IIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRE 466
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
190-525 |
5.36e-114 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 341.57 E-value: 5.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTqGSVVVPDGFHPKL 269
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAG-GTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 270 FWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNN 347
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGydLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 348 LPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKenFTKRENYFRTGDQGYFDPEGF 426
Cdd:cd04433 160 PDDDARKPGSVGRPvPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA--AVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 427 LVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKI 506
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKV 317
|
330
....*....|....*....
gi 398365585 507 PTKVYFVDKLPKTATGKIQ 525
Cdd:cd04433 318 PRRVVFVDALPRTASGKID 336
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
22-536 |
1.03e-113 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 347.64 E-value: 1.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 22 AVIVPETDTQVTYRDLSHMVGHFQTMFTNpnsplyGAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEF 101
Cdd:PRK05852 34 ALVVTADRIAISYRDLARLVDDLAGQLTR------SGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 102 NFYLNDLKSKAICVPK--------GTTKLQSSEILKSASTFGCF-IVELAFDATrfrveydiyspednykrviyrslnna 172
Cdd:PRK05852 108 RVRSQAAGARVVLIDAdgphdraePTTRWWPLTVNVGGDSGPSGgTLSVHLDAA-------------------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 173 kfVNTNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLST 252
Cdd:PRK05852 162 --TEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 253 FRTQGSVVVP--DGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPH----IRFIRSCSSALAPATFHKLEKEF 326
Cdd:PRK05852 240 LASGGAVLLParGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpaaLRFIRSCSAPLTAETAQALQTEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 327 NAPVLEAYAMTEASHQMTSNNLPPGKR------KPGTVGQPQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPK 400
Cdd:PRK05852 320 AAPVVCAFGMTEATHQVTTTQIEGIGQtenpvvSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 401 ANKENFTkrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAI 480
Cdd:PRK05852 400 ITAANFT--DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVI 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 481 VLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKS 536
Cdd:PRK05852 478 VPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFGHS 533
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
22-535 |
3.90e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 325.22 E-value: 3.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 22 AVIVPETDTQVTYRDL---SHMVGHFqtmftnpnspLYGA-VFRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNP 94
Cdd:PRK06187 22 KEAVYFDGRRTTYAELderVNRLANA----------LRALgVKKGDRVAVFDWNSHEYLEAYFAV---PKIGAvlhPINI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 95 NYKEKEFNFYLNDLKSKAICVpkgttklqSSEILKSAStfgcfIVELAFDATRFRVEYDIYSPEDNYKRVI-YRSLNNAK 173
Cdd:PRK06187 89 RLKPEEIAYILNDAEDRVVLV--------DSEFVPLLA-----AILPQLPTVRTVIVEGDGPAAPLAPEVGeYEELLAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 174 fvNTNPVkFPGFaRSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTF 253
Cdd:PRK06187 156 --SDTFD-FPDI-DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW-GLPYLAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 254 RTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFNAPVL 331
Cdd:PRK06187 231 MAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLREFKEKFGIDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 332 EAYAMTEASHQMTSNNLPPG----KRKPGTVGQP-QGVTVVILDDNDNVLPP--GKVGEVSIRGENVTLGYANNPKANKE 404
Cdd:PRK06187 311 QGYGMTETSPVVSVLPPEDQlpgqWTKRRSAGRPlPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 405 NFTKreNYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKK 484
Cdd:PRK06187 391 TIDG--GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKP 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 398365585 485 GEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAK 535
Cdd:PRK06187 469 GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
27-525 |
1.47e-91 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 288.73 E-value: 1.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 27 ETDTQVTYRDLSHMVGHFqtmftnpnsplyGAVFRQ------DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKE 100
Cdd:cd05911 6 DTGKELTYAQLRTLSRRL------------AAGLRKlglkkgDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 101 FNFYLNDLKSKAICV-PKGTTKLQssEILKSASTFGCFIVelaFDATRFRVEYdiyspednykrvIYRSLNNAKFVNTNP 179
Cdd:cd05911 74 LAHQLKISKPKVIFTdPDGLEKVK--EAAKELGPKDKIIV---LDDKPDGVLS------------IEDLLSPTLGEEDED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 180 VKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLT--PLDRSYVVMPLFHVHGLIGVLLSTFRtQG 257
Cdd:cd05911 137 LPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLFTTLASLLN-GA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEF-NAPVLEAY 334
Cdd:cd05911 216 TVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYdlSSLRVILSGGAPLSKELQELLAKRFpNATIKQGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 335 AMTEASHQMTSNnlPPGKRKPGTVGQP-QGVTVVILDDNDN-VLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENY 412
Cdd:cd05911 296 GMTETGGILTVN--PDGDDKPGSVGRLlPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE-DGW 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 413 FRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEE 492
Cdd:cd05911 373 LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKE 452
|
490 500 510
....*....|....*....|....*....|....
gi 398365585 493 LVNFLKKHLASFKIPTK-VYFVDKLPKTATGKIQ 525
Cdd:cd05911 453 VKDYVAKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
19-526 |
2.02e-91 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 286.81 E-value: 2.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPetDTQVTYRDLSHMVGHFQTMFTNPnsplygAVFRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPN 95
Cdd:cd17631 10 DRTALVFG--GRSLTYAELDERVNRLAHALRAL------GVAKGDRVAVLSKNSPEFLELLFAA---ARLGAvfvPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 96 YKEKEFNFYLNDLKSKAIcvpkgttklqsseilksastfgcfivelaFDatrfrveydiyspednykrviyrslnnakfv 175
Cdd:cd17631 79 LTPPEVAYILADSGAKVL-----------------------------FD------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 176 ntnpvkfpgfarssDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRT 255
Cdd:cd17631 99 --------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 256 QGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEkEFNAPVLEA 333
Cdd:cd17631 165 GGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATtdLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 334 YAMTEAShqMTSNNLPPG--KRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRE 410
Cdd:cd17631 244 YGMTETS--PGVTFLSPEdhRRKLGSAGRPvFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--RD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 411 NYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTY 490
Cdd:cd17631 320 GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDE 399
|
490 500 510
....*....|....*....|....*....|....*.
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:cd17631 400 DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
19-531 |
9.70e-89 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 280.33 E-value: 9.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPETdtQVTYRDLSHMVGHFQTMFTnpnspLYGAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKE 98
Cdd:cd05941 1 DRIAIVDDGD--SITYADLVARAARLANRLL-----ALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 99 KEFNFYLNDLkskaicvpkgttklQSSEILksastfgcfivelafdatrfrveydiyspednykrviyrslnnakfvntn 178
Cdd:cd05941 74 AELEYVITDS--------------EPSLVL-------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 pvkfpgfarssDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGS 258
Cdd:cd05941 90 -----------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGAS 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 259 VVVPDGFHPKLFWDQFVKYNCNWFSCVPTI----------SMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNA 328
Cdd:cd05941 159 VEFLPKFDPKEVAISRLMPSITVFMGVPTIytrllqyyeaHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGH 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 329 PVLEAYAMTEAShqM-TSNNLpPGKRKPGTVGQP-QGVTVVILDDNDN-VLPPGKVGEVSIRGENVTLGYANNPKANKEN 405
Cdd:cd05941 239 TLLERYGMTEIG--MaLSNPL-DGERRPGTVGMPlPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 406 FTKrENYFRTGDQGYFDPEGFLVLTGRIK-ELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKK 484
Cdd:cd05941 316 FTD-DGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 398365585 485 GEK-MTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd05941 395 GAAaLSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
63-528 |
1.23e-88 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 279.18 E-value: 1.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPNYKEKEFNFYLNDLKSKAICVpkgttklqsseilksastfgcfiv 139
Cdd:cd05934 29 DRVALMLDNCPEFLFAWFAL---AKLGAvlvPINTALRGDELAYIIDHSGAQLVVV------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 140 elafdatrfrveydiyspednykrviyrslnnakfvntnpvkfpgfarssDVALILHTSGTTSTPKTVPLLHLNIVRSTL 219
Cdd:cd05934 82 --------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 220 NIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPT-ISMIMLNMPKP 298
Cdd:cd05934 112 YSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAmLSYLLAQPPSP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 299 NPFPHIrfIRSCSSALAPATFHK-LEKEFNAPVLEAYAMTEASHQMTSNnlPPGKRKPGTVGQP-QGVTVVILDDNDNVL 376
Cdd:cd05934 192 DDRAHR--LRAAYGAPNPPELHEeFEERFGVRLLEGYGMTETIVGVIGP--RDEPRRPGSIGRPaPGYEVRIVDDDGQEL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 377 PPGKVGEVSIRGEN---VTLGYANNPKANKENFtkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIM 453
Cdd:cd05934 268 PAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM--RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAI 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 454 LSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRV 528
Cdd:cd05934 346 LRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
19-440 |
7.25e-84 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 266.87 E-value: 7.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPEtDTQVTYRDLSHMVGHFQTMFTNPNsplygaVFRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPN 95
Cdd:pfam00501 10 DKTALEVGE-GRRLTYRELDERANRLAAGLRALG------VGKGDRVAILLPNSPEWVVAFLAC---LKAGAvyvPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 96 YKEKEFNFYLNDLKSKAICVpkgTTKLQSSEILKSASTFGCFIVELAFDATRFRVEYDIYSPEDNYKrviyrslnnakfv 175
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLIT---DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAD------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 176 ntNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTY----KLTPLDRSYVVMPLFHVHGLIGVLLS 251
Cdd:pfam00501 144 --VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 252 TFRTQGSVVVPDGF---HPKLFWDQFVKYNCNWFSCVPTISMIMLNM--PKPNPFPHIRFIRSCSSALAPATFHKLEKEF 326
Cdd:pfam00501 222 PLLAGATVVLPPGFpalDPAALLELIERYKVTVLYGVPTLLNMLLEAgaPKRALLSSLRLVLSGGAPLPPELARRFRELF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 327 NAPVLEAYAMTEASHQMTSNNLPPGK-RKPGTVGQP-QGVTVVILDDND-NVLPPGKVGEVSIRGENVTLGYANNPKANK 403
Cdd:pfam00501 302 GGALVNGYGLTETTGVVTTPLPLDEDlRSLGSVGRPlPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTA 381
|
410 420 430
....*....|....*....|....*....|....*..
gi 398365585 404 ENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRG 440
Cdd:pfam00501 382 EAFDE-DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
19-529 |
8.48e-84 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 270.83 E-value: 8.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVI---VPETDTQVTYRDLSHMVGHFQTMFTNpnsplYGaVFRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---PL 92
Cdd:COG0365 24 DKVALIwegEDGEERTLTYAELRREVNRFANALRA-----LG-VKKGDRVAIYLPNIPEAVIAMLAC---ARIGAvhsPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 93 NPNYKEKEFNFYLNDLKSKA-ICVPKGTTKLQS-------SEILKSAST-FGCFIVElafdatrfRVEYDIYSPED-NYK 162
Cdd:COG0365 95 FPGFGAEALADRIEDAEAKVlITADGGLRGGKVidlkekvDEALEELPSlEHVIVVG--------RTGADVPMEGDlDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 163 RVIYRSLNNAKFVNTNpvkfpgfarSSDVALILHTSGTTSTPKTV------PLLHLnivrsTLNIANTYKLTPLDRSYVV 236
Cdd:COG0365 167 ELLAAASAEFEPEPTD---------ADDPLFILYTSGTTGKPKGVvhthggYLVHA-----ATTAKYVLDLKPGDVFWCT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 237 MPLFHVHGLIGVLLSTFRTQGSVVV----PDGFHPKLFWDQFVKYNCNWFSCVPT-ISMIMLNMPKPNPFPHIRFIRSCS 311
Cdd:COG0365 233 ADIGWATGHSYIVYGPLLNGATVVLyegrPDFPDPGRLWELIEKYGVTVFFTAPTaIRALMKAGDEPLKKYDLSSLRLLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 312 SA---LAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNnLPPGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIR 387
Cdd:COG0365 313 SAgepLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISN-LPGLPVKPGSMGKPVpGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 388 GEN--VTLGYANNPKANKEN-FTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVA 464
Cdd:COG0365 392 GPWpgMFRGYWNDPERYRETyFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 465 FGVPDDMYGQVVQAAIVLKKGEKMTYE---ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
19-532 |
1.68e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 258.30 E-value: 1.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIvpETDTQVTYRDLSHMVGHFQtmftnpnSPLYGAVFRQ-DTVAISMRNGLEFIVAFLGATMdakIGA---PLNP 94
Cdd:PRK07656 20 DKEAYV--FGDQRLTYAELNARVRRAA-------AALAALGIGKgDRVAIWAPNSPHWVIAALGALK---AGAvvvPLNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 95 NYKEKEFNFYLNDLKSKAICVpkgttklqsseilksASTF-GCFIVELAFDATrfrVEYDIYSPEDNYKRVIYRSLNNAK 173
Cdd:PRK07656 88 RYTADEAAYILARGDAKALFV---------------LGLFlGVDYSATTRLPA---LEHVVICETEEDDPHTEKMKTFTD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 174 FV-NTNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLST 252
Cdd:PRK07656 150 FLaAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 253 FRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFNAP- 329
Cdd:PRK07656 230 LMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAedLSSLRLAVTGAASMPVALLERFESELGVDi 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 VLEAYAMTEAShQMTSNNLPPGKRK--PGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF 406
Cdd:PRK07656 310 VLTGYGLSEAS-GVTTFNRLDDDRKtvAGTIGTAiAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 407 tKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGE 486
Cdd:PRK07656 389 -DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGA 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 398365585 487 KMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAET 532
Cdd:PRK07656 468 ELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
31-529 |
3.52e-79 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 255.10 E-value: 3.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 31 QVTYRDLSHMVGHFQTMFTNPnsplygAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKS 110
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNK------GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 111 KAIcvpkgttklqsseilksastfgcfivelafdatrfrveydiyspednykrVIYRSLNnakfvntnpvkfpgfarssD 190
Cdd:cd05935 75 KVA--------------------------------------------------VVGSELD-------------------D 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 191 VALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLF 270
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETA 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 271 WDQFVKYNCNWFSCVPTISMIMLNMP--KPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNnl 348
Cdd:cd05935 166 LELIEKYKVTFWTNIPTMLVDLLATPefKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTN-- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 349 PPGKRKPGTVGQP-QGVTVVILDDNDN-VLPPGKVGEVSIRGENVTLGYANNPKANKENFT--KRENYFRTGDQGYFDPE 424
Cdd:cd05935 244 PPLRPKLQCLGIP*FGVDARVIDIETGrELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIeiKGRRFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 425 GFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKM--TYEELVNFLKKHLA 502
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGkvTEEDIIEWAREQMA 403
|
490 500
....*....|....*....|....*..
gi 398365585 503 SFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:cd05935 404 AYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-526 |
1.91e-74 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 239.87 E-value: 1.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGL-IGVLLSTFRTQGSVVVPDGFHPK 268
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSvLGVLACLTHGATMVFPSPSFDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRfIRSCSSALAP---ATFHKLEKEFNAP-VLEAYAMTEAS--HQ 342
Cdd:cd05917 83 AVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSS-LRTGIMAGAPcppELMKRVIEVMNMKdVTIAYGMTETSpvST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 343 MTSNNLPPGKRKpGTVGQPQGVT-VVILD-DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGY 420
Cdd:cd05917 162 QTRTDDSIEKRV-NTVGRIMPHTeAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDG-DGWLHTGDLAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 421 FDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKH 500
Cdd:cd05917 240 MDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGK 319
|
330 340
....*....|....*....|....*.
gi 398365585 501 LASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:cd05917 320 IAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
59-526 |
1.76e-72 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 237.66 E-value: 1.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 59 VFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICVPkgttklqsseilksastfgcfi 138
Cdd:cd05903 23 VGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP---------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 139 velafdaTRFRveydiyspednykrviyrslnnakfvNTNPVKFPGfarssDVALILHTSGTTSTPKTVPLLHLNIVRST 218
Cdd:cd05903 81 -------ERFR--------------------------QFDPAAMPD-----AVALLLFTSGTTGEPKGVMHSHNTLSASI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 219 LNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPK- 297
Cdd:cd05903 123 RQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEe 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 298 -PNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNLPPGKRKPGTVGQP-QGVTVVILDDNDNV 375
Cdd:cd05903 203 aGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPlPGVEIKVVDDTGAT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 376 LPPGKVGEVSIRGENVTLGYANNPKANKENFTkrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLS 455
Cdd:cd05903 283 LAPGVEGELLSRGPSVFLGYLDRPDLTADAAP--EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLG 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365585 456 HPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKH-LASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:cd05903 361 HPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
18-527 |
2.17e-71 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 236.75 E-value: 2.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 18 SDNVAVIVPETDTQVTYRDLSHMVGHFQtmftnpnSPLYGAVFRQ-DTVAISMRNGLEFIVAFLGATmdaKIGA---PLN 93
Cdd:cd05904 19 PSRPALIDAATGRALTYAELERRVRRLA-------AGLAKRGGRKgDVVLLLSPNSIEFPVAFLAVL---SLGAvvtTAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 94 PNYKEKEFNFYLNDLKSK-AICVPKGTTKLQSSE----ILKSASTFGCFIVELAFDAtrfrveydiysPEDNYKRViyrs 168
Cdd:cd05904 89 PLSTPAEIAKQVKDSGAKlAFTTAELAEKLASLAlpvvLLDSAEFDSLSFSDLLFEA-----------DEAEPPVV---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 169 lnnakfvntnPVKfpgfarSSDVALILHTSGTTSTPKTVPLLHLNIvrstlnIANTYKLTPL--------DRSYVVMPLF 240
Cdd:cd05904 154 ----------VIK------QDDVAALLYSSGTTGRSKGVMLTHRNL------IAMVAQFVAGegsnsdseDVFLCVLPMF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 241 HVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF--PHIRFIRSCSSALAPAT 318
Cdd:cd05904 212 HIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 319 FHKLEKEF-NAPVLEAYAMTEASHQMTSNNLPPGKR-KPGTVGQ--PqGVTVVILDDNDN-VLPPGKVGEVSIRGENVTL 393
Cdd:cd05904 292 IEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRaKYGSVGRlvP-NVEAKIVDPETGeSLPPNQTGELWIRGPSIMK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 394 GYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYG 473
Cdd:cd05904 371 GYLNNPEATAATIDK-EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAG 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 398365585 474 QVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05904 450 EVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRK 503
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
189-527 |
3.05e-71 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 233.78 E-value: 3.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVPDGFHPK 268
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNCNWFSCVPTismiMLN-----MPKPNPfPHIRFIRsCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQM 343
Cdd:cd05912 156 QVLHLINSGKVTIISVVPT----MLQrlleiLGEGYP-NNLRCIL-LGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 344 TSNNLPPGKRKPGTVGQP-QGVTVVILDDNDnvlPPGKVGEVSIRGENVTLGYANNPKANKENFtkRENYFRTGDQGYFD 422
Cdd:cd05912 230 VTLSPEDALNKIGSAGKPlFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESF--ENGWFKTGDIGYLD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 423 PEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKgeKMTYEELVNFLKKHLA 502
Cdd:cd05912 305 EEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLA 382
|
330 340
....*....|....*....|....*
gi 398365585 503 SFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05912 383 KYKVPKKIYFVDELPRTASGKLLRH 407
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
190-526 |
6.52e-70 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 227.54 E-value: 6.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVPDGFHP-- 267
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 268 --KLFWDQFVKYncnWFSCVPTISMIMLNMPKPNPfpHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTs 345
Cdd:cd17637 80 alELIEEEKVTL---MGSFPPILSNLLDAAEKSGV--DLSSLRHVLGLDAPETIQRFEETTGATFWSLYGQTETSGLVT- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 346 nnLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANkeNFTKRENYFRTGDQGYFDPE 424
Cdd:cd17637 154 --LSPYRERPGSAGRPgPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELT--AYTFRNGWHHTGDLGRFDED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 425 GFLVLTGRI--KELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLA 502
Cdd:cd17637 230 GYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIA 309
|
330 340
....*....|....*....|....
gi 398365585 503 SFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:cd17637 310 RYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
19-531 |
4.79e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 227.82 E-value: 4.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPETdtQVTYRDLSHMVGHFQTMFTNPNSplygaVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKE 98
Cdd:PRK06839 17 DRIAIITEEE--EMTYKQLHEYVSKVAAYLIYELN-----VKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 99 KEFNFYLNDLKSKAICVPKgttklqsseilksasTFGCFIVELAFDATRFRVEYdIYSPEDnykrviyrsLNNAKFVNTN 178
Cdd:PRK06839 90 NELIFQLKDSGTTVLFVEK---------------TFQNMALSMQKVSYVQRVIS-ITSLKE---------IEDRKIDNFV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 PvkfPGfarSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGS 258
Cdd:PRK06839 145 E---KN---ESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 259 VVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMP---KPNpFPHIRFIRScSSALAPATFHKLEKEFNAPVLEAYA 335
Cdd:PRK06839 219 IIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSkfeTTN-LQSVRWFYN-GGAPCPEELMREFIDRGFLFGQGFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 336 MTEASHQMTSNNLPPGKRKPGTVGQPQGVT-VVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKEnfTKRENYFR 414
Cdd:PRK06839 297 MTETSPTVFMLSEEDARRKVGSIGKPVLFCdYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--TIQDGWLC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 415 TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELV 494
Cdd:PRK06839 375 TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVI 454
|
490 500 510
....*....|....*....|....*....|....*..
gi 398365585 495 NFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK06839 455 EHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
29-531 |
5.57e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 228.69 E-value: 5.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 29 DTQVTYRDLSH----MVGHFQTMFtnpnsplygAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFY 104
Cdd:PRK08314 33 GRAISYRELLEeaerLAGYLQQEC---------GVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 105 LNDLKSK-AICvpkGTTKLQSSEILKSASTFGCFIVELAFDAtrFRVEYDIYSPEDNYKRVIYRSLNNAKFV------NT 177
Cdd:PRK08314 104 VTDSGARvAIV---GSELAPKVAPAVGNLRLRHVIVAQYSDY--LPAEPEIAVPAWLRAEPPLQALAPGGVVawkealAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 178 NPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQG 257
Cdd:PRK08314 179 GLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVpdgfHPKlfWDQ------FVKYNCNWFSCVPTISMIMLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEFNAP 329
Cdd:PRK08314 259 TVVL----MPR--WDReaaarlIERYRVTHWTNIPTMVVDFLASPGLAERdlSSLRYIGGGGAAMPEAVAERLKELTGLD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 VLEAYAMTEASHQMTSNnlPPGKRKPGTVGQP-QGVTVVILD-DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFT 407
Cdd:PRK08314 333 YVEGYGLTETMAQTHSN--PPDRPKLQCLGIPtFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 408 ----KRenYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLK 483
Cdd:PRK08314 411 eidgKR--FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLR 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 398365585 484 KGE--KMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK08314 489 PEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQE 538
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
33-526 |
5.58e-67 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 223.09 E-value: 5.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 33 TYRDLSHMVGHFQTMFTNPnsplygAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKska 112
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQ------GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 113 icvpkgttklqsseilksastfgcfiVELAFDATRFRVEYdiyspednykrVIYRSLNNAKFVNTNPVKFPGFARSSDVA 192
Cdd:TIGR01923 72 --------------------------VQLLLTDSLLEEKD-----------FQADSLDRIEAAGRYETSLSASFNMDQIA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 193 LILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVPDGFHPklFWD 272
Cdd:TIGR01923 115 TLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFNQ--LLE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 273 QFVKYNCNWFSCVPTismiMLN--MPKPNPFPHIRFIRSCSSALaPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNlPP 350
Cdd:TIGR01923 192 MIANERVTHISLVPT----QLNrlLDEGGHNENLRKILLGGSAI-PAPLIEEAQQYGLPIYLSYGMTETCSQVTTAT-PE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 351 GKRKPGTVGQP-QGVTVVILDDNdnvlpPGKVGEVSIRGENVTLGYANNPKANKenFTKRENYFRTGDQGYFDPEGFLVL 429
Cdd:TIGR01923 266 MLHARPDVGRPlAGREIKIKVDN-----KEGHGEIMVKGANLMKGYLYQGELTP--AFEQQGWFNTGDIGELDGEGFLYV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 430 TGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEkmTYEELVNFLKKHLASFKIPTK 509
Cdd:TIGR01923 339 LGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDI--SQAKLIAYLTEKLAKYKVPIA 416
|
490
....*....|....*..
gi 398365585 510 VYFVDKLPKTATGKIQR 526
Cdd:TIGR01923 417 FEKLDELPYNASGKILR 433
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
6-532 |
3.49e-66 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 224.27 E-value: 3.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 6 TVTASFNDTFS-VSDNVAVIVPETDTQVTYRDLSHMVGHFQtmftnpnSPLYG-AVFRQDTVAISMRNGLEFIVAFLgAT 83
Cdd:PRK12583 19 TIGDAFDATVArFPDREALVVRHQALRYTWRQLADAVDRLA-------RGLLAlGVQPGDRVGIWAPNCAEWLLTQF-AT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 84 mdAKIGAPL---NPNYKEKEFNFYLNDLKSKA-ICVP--KGTTKLQS-SEILKSASTFGCfiVELA---FDATRFRVEYD 153
Cdd:PRK12583 91 --ARIGAILvniNPAYRASELEYALGQSGVRWvICADafKTSDYHAMlQELLPGLAEGQP--GALAcerLPELRGVVSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 154 IYSPED--NYKRVIYRslnnAKFVNTNPVkfpgFARSS-----DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYK 226
Cdd:PRK12583 167 PAPPPGflAWHELQAR----GETVSREAL----AERQAsldrdDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 227 LTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVP-DGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFpHIR 305
Cdd:PRK12583 239 LTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPnEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNF-DLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 306 FIRSCSSALAP---ATFHKLEKEFNAP-VLEAYAMTEAS---HQMTSNNlpPGKRKPGTVG--QPQgVTVVILDDNDNVL 376
Cdd:PRK12583 318 SLRTGIMAGAPcpiEVMRRVMDEMHMAeVQIAYGMTETSpvsLQTTAAD--DLERRVETVGrtQPH-LEVKVVDPDGATV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 377 PPGKVGEVSIRGENVTLGYANNPKANKENFtKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSH 456
Cdd:PRK12583 395 PRGEIGELCTRGYSVMKGYWNNPEATAESI-DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTH 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 457 PKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAET 532
Cdd:PRK12583 474 PAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
19-527 |
4.81e-66 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 222.14 E-value: 4.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIvpETDTQVTYRDLSHMVGHFQTMFTNPNSPlygavfRQDTVAISMRNGLEFIVA-----FLGATMdakigAPLN 93
Cdd:PRK03640 17 DRTAIE--FEEKKVTFMELHEAVVSVAGKLAALGVK------KGDRVALLMKNGMEMILVihalqQLGAVA-----VLLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 94 PNYKEKEFNFYLNDlkSKAICVpkgttklqsseilksastfgcfIVELAFDATRFRVEYDIYSPednykrVIYRSLNNAK 173
Cdd:PRK03640 84 TRLSREELLWQLDD--AEVKCL----------------------ITDDDFEAKLIPGISVKFAE------LMNGPKEEAE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 174 FVNTNPVkfpgfarsSDVALILHTSGTTSTPKTVPLLHLN----IVRSTLNIAntykLTPLDRSYVVMPLFHVHGLiGVL 249
Cdd:PRK03640 134 IQEEFDL--------DEVATIMYTSGTTGKPKGVIQTYGNhwwsAVGSALNLG----LTEDDCWLAAVPIFHISGL-SIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 250 LSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTismiMLN-----MPKPNPFPHIRFIrscssaL---APATFHK 321
Cdd:PRK03640 201 MRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVST----MLQrllerLGEGTYPSSFRCM------LlggGPAPKPL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 322 LE--KEFNAPVLEAYAMTEASHQMTSnnLPP--GKRKPGTVGQPQ-GVTVVILDDNdNVLPPGKVGEVSIRGENVTLGYA 396
Cdd:PRK03640 271 LEqcKEKGIPVYQSYGMTETASQIVT--LSPedALTKLGSAGKPLfPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 397 NNPKANKENFtkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVV 476
Cdd:PRK03640 348 NREDATRETF--QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVP 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 398365585 477 QAAIVlkKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK03640 426 VAFVV--KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
63-527 |
2.14e-65 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 221.09 E-value: 2.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPNYKEKEFNFYLNdlkskaicvpkgttKLQSSEILKSASTFGCFIV 139
Cdd:PRK08008 63 DKVALHLDNCPEFIFCWFGL---AKIGAimvPINARLLREESAWILQ--------------NSQASLLVTSAQFYPMYRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 140 ELAFDATRFR--VEYDIYSPED----NYKRViyRSLNNAKFVNTNPVKfpgfarSSDVALILHTSGTTSTPKTVPLLHLN 213
Cdd:PRK08008 126 IQQEDATPLRhiCLTRVALPADdgvsSFTQL--KAQQPATLCYAPPLS------TDDTAEILFTSGTTSRPKGVVITHYN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 214 IVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVP-TISMIM 292
Cdd:PRK08008 198 LRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPmMIRTLM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 293 LNMPKPNPFPHIrfIRSCSSALAPATFHKL--EKEFNAPVLEAYAMTEASHQMTSNNlPPGKRKPGTVGQPQ-GVTVVIL 369
Cdd:PRK08008 278 VQPPSANDRQHC--LREVMFYLNLSDQEKDafEERFGVRLLTSYGMTETIVGIIGDR-PGDKRRWPSIGRPGfCYEAEIR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 370 DDNDNVLPPGKVGEVSIRGE-NVTL--GYANNPKANKENFTkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISP 446
Cdd:PRK08008 355 DDHNRPLPAGEIGEICIKGVpGKTIfkEYYLDPKATAKVLE-ADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 447 IELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:PRK08008 434 VELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIK 513
|
.
gi 398365585 527 R 527
Cdd:PRK08008 514 K 514
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
58-540 |
7.23e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 221.06 E-value: 7.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 58 AVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAI-CV----PK-----GTTKLQSSeI 127
Cdd:PRK06710 70 GVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlCLdlvfPRvtnvqSATKIEHV-I 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 128 LKSASTFGCFIVELAFDATRFRVEYDIYSPEDNYKRVIYRSLNnaKFVNTNpVKFPgFARSSDVALILHTSGTTSTPKTV 207
Cdd:PRK06710 149 VTRIADFLPFPKNLLYPFVQKKQSNLVVKVSESETIHLWNSVE--KEVNTG-VEVP-CDPENDLALLQYTGGTTGFPKGV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 208 PLLHLNIVRSTL-NIANTYKLTPLDRSYV-VMPLFHVHGLIGVL-LSTFRTQGSVVVPDgFHPKLFWDQFVKYNCNWFSC 284
Cdd:PRK06710 225 MLTHKNLVSNTLmGVQWLYNCKEGEEVVLgVLPFFHVYGMTAVMnLSIMQGYKMVLIPK-FDMKMVFEAIKKHKVTLFPG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 285 VPTISMIMLNMPKPNPFpHIRFIRSCSSALAPATFH---KLEKEFNAPVLEAYAMTEAShQMTSNNLPPGKRKPGTVGQP 361
Cdd:PRK06710 304 APTIYIALLNSPLLKEY-DISSIRACISGSAPLPVEvqeKFETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 362 QGVT--VVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRENYFRTGDQGYFDPEGFLVLTGRIKELINR 439
Cdd:PRK06710 382 WPDTeaMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL--QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 440 GGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKT 519
Cdd:PRK06710 460 SGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKT 539
|
490 500
....*....|....*....|.
gi 398365585 520 ATGKIQRRVIAETFAKSSRNK 540
Cdd:PRK06710 540 TVGKILRRVLIEEEKRKNEDE 560
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
188-529 |
2.13e-64 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 216.05 E-value: 2.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTV------PLLHLNIVRSTLNI-ANTYKLTPLDRSYVVMPLFhvhGLIGVLLStfrtqGSVV 260
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVlhthsyPLGHIPTAAYWLGLrPDDIHWNIADPGWAKGAWS---SFFGPWLL-----GATV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 261 VP---DGFHPKLFWDQFVKYNCNWFSCVPT-ISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAM 336
Cdd:cd05972 152 FVyegPRFDAERILELLERYGVTSFCGPPTaYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 337 TEAShqMTSNNLPPGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTL--GYANNPKANKENFtkRENYF 413
Cdd:cd05972 232 TETG--LTVGNFPDMPVKPGSMGRPTpGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLflGYVGDPEKTEASI--RGDYY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 414 RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMT---Y 490
Cdd:cd05972 308 LTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelA 387
|
330 340 350
....*....|....*....|....*....|....*....
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:cd05972 388 EELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-527 |
2.93e-64 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 216.54 E-value: 2.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVV-PDGFHPK 268
Cdd:cd05922 118 DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLtNDGVLDD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNCNWFSCVPTISMIMLNMP-KPNPFPHIRFIRSCSSALAPATFHKL-EKEFNAPVLEAYAMTEASHQMTSn 346
Cdd:cd05922 197 AFWEDLREHGATGLAGVPSTYAMLTRLGfDPAKLPSLRYLTQAGGRLPQETIARLrELLPGAQVYVMYGQTEATRRMTY- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 347 nLPPG--KRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDP 423
Cdd:cd05922 276 -LPPEriLEKPGSIGLAiPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRG-GGVLHTGDLARRDE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 424 EGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMyGQVVQAAIVLKkgEKMTYEELVNFLKKHLAS 503
Cdd:cd05922 354 DGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAP--DKIDPKDVLRSLAERLPP 430
|
330 340
....*....|....*....|....
gi 398365585 504 FKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05922 431 YKVPATVRVVDELPLTASGKVDYA 454
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
19-525 |
3.52e-64 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 218.91 E-value: 3.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPETDTQVTYRDLSHMVGHFQTMFtnpnspLYGAVFRQDTVAISMRNGLEFiVAFLGATmdAKIGAPL---NPN 95
Cdd:PRK08315 31 DREALVYRDQGLRWTYREFNEEVDALAKGL------LALGIEKGDRVGIWAPNVPEW-VLTQFAT--AKIGAILvtiNPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 96 YKEKEFNFYLNDLKSKAICVPKGttkLQSS---EILKSAstfgcfIVELA------FDATRFrveydiysPEdnYKRVIY 166
Cdd:PRK08315 102 YRLSELEYALNQSGCKALIAADG---FKDSdyvAMLYEL------APELAtcepgqLQSARL--------PE--LRRVIF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 167 rslnnakfvnTNPVKFPGFARSSDVAL------------------------ILHTSGTTSTPKTVPLLHLNIVRSTLNIA 222
Cdd:PRK08315 163 ----------LGDEKHPGMLNFDELLAlgravddaelaarqatldpddpinIQYTSGTTGFPKGATLTHRNILNNGYFIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 223 NTYKLTPLDRSYVVMPLFHVHGLI-GVLLSTfrTQGS-VVVP-DGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNmpkpn 299
Cdd:PRK08315 233 EAMKLTEEDRLCIPVPLYHCFGMVlGNLACV--THGAtMVYPgEGFDPLATLAAVEEERCTALYGVPTMFIAELD----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 300 pfpHIRF-------IRSCSSALAP---ATFHKLEKEFNAP-VLEAYAMTEAS---HQMTSNNlpPGKRKPGTVGQPQ-GV 364
Cdd:PRK08315 306 ---HPDFarfdlssLRTGIMAGSPcpiEVMKRVIDKMHMSeVTIAYGMTETSpvsTQTRTDD--PLEKRVTTVGRALpHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 365 TVVILD-DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEK 443
Cdd:PRK08315 381 EVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDA-DGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGEN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 444 ISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGK 523
Cdd:PRK08315 460 IYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
..
gi 398365585 524 IQ 525
Cdd:PRK08315 540 IQ 541
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
187-538 |
4.51e-63 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 217.52 E-value: 4.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVV--PDG 264
Cdd:PRK07529 211 GPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLatPQG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 F-HPKL---FWDQFVKYNCNWFSCVPTISMIMLNMPKPNP-FPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEA 339
Cdd:PRK07529 291 YrGPGVianFWKIVERYRINFLSGVPTVYAALLQVPVDGHdISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 ShQMTSNNLPPGKRKPGTVGQP---QGVTVVILDDNDNVL---PPGKVGEVSIRGENVTLGYANnPKANKENFTKrENYF 413
Cdd:PRK07529 371 T-CVSSVNPPDGERRIGSVGLRlpyQRVRVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLE-DGWL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 414 RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEEL 493
Cdd:PRK07529 448 NTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAEL 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 398365585 494 VNFLKKHLAS-FKIPTKVYFVDKLPKTATGKI-----QRRVIAETFAKSSR 538
Cdd:PRK07529 528 LAFARDHIAErAAVPKHVRILDALPKTAVGKIfkpalRRDAIRRVLRAALR 578
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-524 |
3.23e-62 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 208.10 E-value: 3.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVV--PDGF 265
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 H-PKL---FWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASh 341
Cdd:cd05944 81 RnPGLfdnFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 342 QMTSNNLPPGKRKPGTVGQP---QGVTVVILDDNDNVL---PPGKVGEVSIRGENVTLGYANNpKANKENFTKrENYFRT 415
Cdd:cd05944 160 CLVAVNPPDGPKRPGSVGLRlpyARVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVA-DGWLNT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 416 GDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVN 495
Cdd:cd05944 238 GDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLA 317
|
330 340 350
....*....|....*....|....*....|
gi 398365585 496 FLKKHLAS-FKIPTKVYFVDKLPKTATGKI 524
Cdd:cd05944 318 WARDHVPErAAVPKHIEVLEELPVTAVGKV 347
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
63-535 |
1.00e-61 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 212.30 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATmdaKIGA---PLNPNYKEKEFNFYLNDLKSKAICVPkgtTKLQSSEILKsastfgcFIV 139
Cdd:PRK06087 75 DRVAFQLPGWCEFTIIYLACL---KVGAvsvPLLPSWREAELVWVLNKCQAKMFFAP---TLFKQTRPVD-------LIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 140 ELAFDATRFR--VEYDIYSPEDN---YKRVIYRSLNNAKFVNTNpvkfpgfarSSDVALILHTSGTTSTPKTVPLLHLNI 214
Cdd:PRK06087 142 PLQNQLPQLQqiVGVDKLAPATSslsLSQIIADYEPLTTAITTH---------GDELAAVLFTSGTEGLPKGVMLTHNNI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 215 VRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLN 294
Cdd:PRK06087 213 LASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 295 MPKPNP--FPHIRFIRsCSSALAPATFHKLEKEFNAPVLEAYAMTEAS-HQMtsnnLPPGK---RKPGTVGQP-QGVTVV 367
Cdd:PRK06087 293 LLEKQPadLSALRFFL-CGGTTIPKKVARECQQRGIKLLSVYGSTESSpHAV----VNLDDplsRFMHTDGYAaAGVEIK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 368 ILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKAnkenfTKR----ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEK 443
Cdd:PRK06087 368 VVDEARKTLPPGCEGEEASRGPNVFMGYLDEPEL-----TARaldeEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGEN 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 444 ISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEK-MTYEELVNFL-KKHLASFKIPTKVYFVDKLPKTAT 521
Cdd:PRK06087 443 ISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHsLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTAS 522
|
490
....*....|....
gi 398365585 522 GKIQRRVIAETFAK 535
Cdd:PRK06087 523 GKIQKFLLRKDIMR 536
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
59-529 |
5.86e-61 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 209.15 E-value: 5.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 59 VFRQDTVAISMRNGLEFIVAFLGATmdaKIGA---PLNPNYKEKEFNFYLNDLKSKAICVpkgttklqSSEILKSastfg 135
Cdd:cd05959 51 VKREERVLLIMLDTVDFPTAFLGAI---RAGIvpvPVNTLLTPDDYAYYLEDSRARVVVV--------SGELAPV----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 136 cfIVELAFDATRFRVEYDIYSPEDNYKRVIYRslnnAKFVNTNPVKF-PGFARSSDVALILHTSGTTSTPKTVPLLHLNI 214
Cdd:cd05959 115 --LAAALTKSEHTLVVLIVSGGAGPEAGALLL----AELVAAEAEQLkPAATHADDPAFWLYSSGSTGRPKGVVHLHADI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 215 VRSTLNIA-NTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGF-HPKLFWDQFVKYNCNWFSCVPTISMIM 292
Cdd:cd05959 189 YWTAELYArNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 293 LNMPKPNPFPHIRfIRSCSSA---LAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNlpPGKRKPGTVGQP-QGVTVVI 368
Cdd:cd05959 269 LAAPNLPSRDLSS-LRLCVSAgeaLPAEVGERWKARFGLDILDGIGSTEMLHIFLSNR--PGRVRYGTTGKPvPGYEVEL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 369 LDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIE 448
Cdd:cd05959 346 RDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF--QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 449 LDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMT---YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQ 525
Cdd:cd05959 424 VESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSealEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQ 503
|
....
gi 398365585 526 RRVI 529
Cdd:cd05959 504 RFKL 507
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
190-531 |
6.00e-61 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 209.41 E-value: 6.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTyKLTPLDRSYVVM---PLFHVHGLiGVLLSTFRTQGSVVVPDGF- 265
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLT-DGLGLSESDVVLpvvPMFHVNAW-GLPYAAAMVGAKLVLPGPYl 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 HPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFnAPVLEAYAMTEASHQM 343
Cdd:cd12119 242 DPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGrdLSSLRRVVIGGSAVPRSLIEAFEERG-VRVIHAWGMTETSPLG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 344 TSNNLPPGKRKPG---------TVGQPQ-GVTVVILDDNDNVLP--PGKVGEVSIRGENVTLGYANNPKANKENFtkREN 411
Cdd:cd12119 321 TVARPPSEHSNLSedeqlalraKQGRPVpGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEALT--EDG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 412 YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYE 491
Cdd:cd12119 399 WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE 478
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 398365585 492 ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
16-531 |
7.39e-60 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 206.99 E-value: 7.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 16 SVSDNVAVIVPETDTQVTYRDLSHMVGHFQTMFTNpnsplYGaVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPN 95
Cdd:cd17642 29 SVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKK-----YG-LKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 96 YKEKEFNFYLNDLKSKAICVPKGTTKlqssEILKSASTFGCFIVELAFDAtrfRVEYDIYSPEDNYKrviyrSLNNAKFV 175
Cdd:cd17642 103 YNERELDHSLNISKPTIVFCSKKGLQ----KVLNVQKKLKIIKTIIILDS---KEDYKGYQCLYTFI-----TQNLPPGF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 176 NTNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIV-RSTLNIANTYKLTPLDRSYV--VMPLFHVHG---LIGVL 249
Cdd:cd17642 171 NEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVaRFSHARDPIFGNQIIPDTAIltVIPFHHGFGmftTLGYL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 250 LSTFRtqgsVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEFN 327
Cdd:cd17642 251 ICGFR----VVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYdlSNLHEIASGGAPLSKEVGEAVAKRFK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 328 AP-VLEAYAMTEAshqmTSNNL--PPGKRKPGTVGQ--PQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKAN 402
Cdd:cd17642 327 LPgIRQGYGLTET----TSAILitPEGDDKPGAVGKvvPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEAT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 403 KENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVL 482
Cdd:cd17642 403 KALIDK-DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 398365585 483 KKGEKMTYEELVNFLKKHLASFK-IPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd17642 482 EAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
190-535 |
3.02e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 203.31 E-value: 3.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRstlNIANTYKLTPL-----DRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDG 264
Cdd:PRK05605 220 DVALILYTSGTTGKPKGAQLTHRNLFA---NAAQGKAWVPGlgdgpERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 FHPKLFWDQFVKYNCNWFSCVPTI-SMIMLNMPKPN-PFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQ 342
Cdd:PRK05605 297 PDIDLILDAMKKHPPTWLPGVPPLyEKIAEAAEERGvDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPI 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 343 MTSNNLPPGkRKPGTVGQP---QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTkrENYFRTGDQG 419
Cdd:PRK05605 377 IVGNPMSDD-RRPGYVGVPfpdTEVRIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL--DGWFRTGDVV 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 420 YFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKK 499
Cdd:PRK05605 454 VMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCRE 533
|
330 340 350
....*....|....*....|....*....|....*.
gi 398365585 500 HLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAK 535
Cdd:PRK05605 534 HLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLE 569
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
197-529 |
6.41e-58 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 200.60 E-value: 6.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 197 TSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVPDGFHPKLFWDQFVK 276
Cdd:cd12118 141 TSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGW-CFPWTVAAVGGTNVCLRKVDAKAIYDLIEK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 277 YNCNWFSCVPTISMIMLNMPKPN--PFPHIRFIRSCSSALAPATFHKLEkEFNAPVLEAYAMTEASHQMT-------SNN 347
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANAPPSDarPLPHRVHVMTAGAPPPAAVLAKME-ELGFDVTHVYGLTETYGPATvcawkpeWDE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 348 LPPGKRKP-------GTVGQpQGVTVVILDDNDNVLPPGK-VGEVSIRGENVTLGYANNPKANKENFtkRENYFRTGDQG 419
Cdd:cd12118 299 LPTEERARlkarqgvRYVGL-EEVDVLDPETMKPVPRDGKtIGEIVFRGNIVMKGYLKNPEATAEAF--RGGWFHSGDLA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 420 YFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKK 499
Cdd:cd12118 376 VIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCRE 455
|
330 340 350
....*....|....*....|....*....|
gi 398365585 500 HLASFKIPTKVYFVDkLPKTATGKIQRRVI 529
Cdd:cd12118 456 HLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
179-534 |
2.84e-56 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 196.64 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 PVKFPGFARS-SDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLI----GVLLStf 253
Cdd:PRK07514 145 PDDFETVPRGaDDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFvatnVALLA-- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 254 rtqGSVVVpdgFHPKLFWDQFVKY--NCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFNAP 329
Cdd:PRK07514 223 ---GASMI---FLPKFDPDAVLALmpRATVMMGVPTFYTRLLQEPRLTReaAAHMRLFISGSAPLLAETHREFQERTGHA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 VLEAYAMTEAShqM-TSNnlpP--GKRKPGTVGQP-QGVTVVILD-DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKE 404
Cdd:PRK07514 297 ILERYGMTETN--MnTSN---PydGERRAGTVGFPlPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 405 NFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKK 484
Cdd:PRK07514 372 EFRA-DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKP 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398365585 485 GEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFA 534
Cdd:PRK07514 451 GAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYA 500
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
197-531 |
2.86e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 194.49 E-value: 2.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 197 TSGTTSTPKTVPLLH--LNIVrstlnIAN-----TYKLTPLDRSYVVMPLFH---VHGLIGVLlstfRTQGSVVVP-DGF 265
Cdd:PRK07470 171 TSGTTGRPKAAVLTHgqMAFV-----ITNhladlMPGTTEQDASLVVAPLSHgagIHQLCQVA----RGAATVLLPsERF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 HPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPH--IRFIrscSSALAPATF----HKLEKEfnAPVL-EAYAMTE 338
Cdd:PRK07470 242 DPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHssLRYV---IYAGAPMYRadqkRALAKL--GKVLvQYFGLGE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 339 ASHQMTSnnLPPGKRKP--------GTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkR 409
Cdd:PRK07470 317 VTGNITV--LPPALHDAedgpdariGTCGFERtGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF--R 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMT 489
Cdd:PRK07470 393 DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD 472
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 398365585 490 YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK07470 473 EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
188-530 |
1.62e-54 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 190.00 E-value: 1.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVPLLHlnivRSTLNIANTY-----KLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVP 262
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFH----RDPLASADRYavnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 263 DGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPkPNPFPHIRFIRSCSSA---LAPATFHKLEKEFNAPVLEAYAMTEA 339
Cdd:cd05958 172 EEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHP-DAAGPDLSSLRKCVSAgeaLPAALHRAWKEATGIPIIDGIGSTEM 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 SHQMTSNNlpPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGenvtlgyannPKANKENFTKRE-NYFR--- 414
Cdd:cd05958 251 FHIFISAR--PGDARPGATGKPvPGYEAKVVDDEGNPVPDGTIGRLAVRG----------PTGCRYLADKRQrTYVQggw 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 415 --TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGE---KMT 489
Cdd:cd05958 319 niTGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVipgPVL 398
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 398365585 490 YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIA 530
Cdd:cd05958 399 ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
19-527 |
2.25e-53 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 187.35 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPetDTQVTYRDL---SHMVGHFqtmftnpnspLYGA-VFRQDTVAISMRNGLEFIVAFLGAtmdakigaplnp 94
Cdd:cd05930 2 DAVAVVDG--DQSLTYAELdarANRLARY----------LRERgVGPGDLVAVLLERSLEMVVAILAV------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 95 nykekefnfylndLKSKAICVPkgttklqsseilksastfgcfiVELAFDATRfrVEYdiyspednykrVIYRSlnNAKF 174
Cdd:cd05930 58 -------------LKAGAAYVP----------------------LDPSYPAER--LAY-----------ILEDS--GAKL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 175 VNTNPvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPL---FHVHGLIGVLLS 251
Cdd:cd05930 88 VLTDP---------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFsfdVSVWEIFGALLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 252 tfrtqGS--VVVPDGFH--PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFN 327
Cdd:cd05930 159 -----GAtlVVLPEEVRkdPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLP 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 328 APVLE-AYAMTEASHQMTSNNLPPGKRKPGTV--GQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANK 403
Cdd:cd05930 234 GARLVnLYGPTEATVDATYYRVPPDDEEDGRVpiGRPiPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 404 ENFT-----KRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQA 478
Cdd:cd05930 314 ERFVpnpfgPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVA 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 398365585 479 AIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05930 394 YVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
29-534 |
5.07e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 188.22 E-value: 5.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 29 DTQVTYRDLSHMVGHFqtmftnpnsplyGAVFRQ------DTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPNYKEK 99
Cdd:PRK08316 34 DRSWTYAELDAAVNRV------------AAALLDlglkkgDRVAALGHNSDAYALLWLAC---ARAGAvhvPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 100 EFNFYLNDLKSKAICVPKGttklqsseilksastfgcfIVELAFDATR-FRVEYDIYSPEDNYKRVIYRSLNNAKFVNTN 178
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPA-------------------LAPTAEAALAlLPVDTLILSLVLGGREAPGGWLDFADWAEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 PVKFPG-FARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQG 257
Cdd:PRK08316 160 SVAEPDvELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFpHIRFIRSC---SSALAPATFHKLEKEF-NAPVLEA 333
Cdd:PRK08316 240 TNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTR-DLSSLRKGyygASIMPVEVLKELRERLpGLRFYNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 334 YAMTEASHQMTSnnLPPG--KRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRE 410
Cdd:PRK08316 319 YGQTEIAPLATV--LGPEehLRRPGSAGRPVlNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF--RG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 411 NYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTY 490
Cdd:PRK08316 395 GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFA 534
Cdd:PRK08316 475 DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYA 518
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
183-534 |
1.20e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 186.55 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 183 PGFARSSD---VALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSV 259
Cdd:PRK09088 126 PADTPSIPperVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 260 VVPDGFHPK--LFWDQFVKYNCNWFSCVPTISMIMLNMP--KPNPFPHIRFIRScSSALAPATFHKLEKEFNAPVLEAYA 335
Cdd:PRK09088 206 LVSNGFEPKrtLGRLGDPALGITHYFCVPQMAQAFRAQPgfDAAALRHLTALFT-GGAPHAAEDILGWLDDGIPMVDGFG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 336 MTEAShqmTSNNLPPG----KRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrE 410
Cdd:PRK09088 285 MSEAG---TVFGMSVDcdviRAKAGAAGIPTpTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTG-D 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 411 NYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTY 490
Cdd:PRK09088 361 GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDL 440
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFA 534
Cdd:PRK09088 441 ERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
190-529 |
1.72e-52 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 184.63 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDG-FHPK 268
Cdd:cd05969 90 DPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGrFDAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNCNWFSCVPT-ISMIM---LNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMT 344
Cdd:cd05969 170 SWYGIIERVKVTVWYTAPTaIRMLMkegDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNnLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGE--NVTLGYANNPKANKENFTkrENYFRTGDQGYF 421
Cdd:cd05969 250 AN-YPCMPIKPGSMGKPlPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFI--DGWYLTGDLAYR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 422 DPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYE---ELVNFLK 498
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVR 406
|
330 340 350
....*....|....*....|....*....|.
gi 398365585 499 KHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:cd05969 407 QKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
192-527 |
2.35e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 185.19 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 192 ALILHTSGTTSTPKTVPLLHLNIvRSTLN-IANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVV-----VPDGF 265
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAI-AADLDaLAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVhtgrpTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 HPKLFWDQFVkyncnWFScVPTI-SMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEAshQMT 344
Cdd:PRK07787 210 AQALSEGGTL-----YFG-VPTVwSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTET--LIT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNNLPPGKRKPGTVGQP-QGVTVVILDDNDNVLP--PGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYF 421
Cdd:PRK07787 282 LSTRADGERRPGWVGLPlAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTA-DGWFRTGDVAVV 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 422 DPEGFLVLTGRIK-ELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVlkKGEKMTYEELVNFLKKH 500
Cdd:PRK07787 361 DPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQ 438
|
330 340
....*....|....*....|....*..
gi 398365585 501 LASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK07787 439 LSVHKRPREVRFVDALPRNAMGKVLKK 465
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
188-529 |
4.99e-52 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 183.40 E-value: 4.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPK------TVPLLHLNIVRSTLNIA----NTYkLTPLDRSYVvmplfhvHGLIGVLLSTFRTQG 257
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKgalhahRVLLGHLPGVQFPFNLFprdgDLY-WTPADWAWI-------GGLLDVLLPSLYFGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVV--PDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRfIRSCSSALAPATFHKL---EKEFNAPVLE 332
Cdd:cd05971 159 PVLAhrMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK-LRAIATGGESLGEELLgwaREQFGVEVNE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 333 AYAMTEAShQMTSNNLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIR--GENVTLGYANNPKANKENFTKr 409
Cdd:cd05971 238 FYGQTECN-LVIGNCSALFPIKPGSMGKPiPGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAG- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 eNYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMT 489
Cdd:cd05971 316 -DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPS 394
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398365585 490 YE---ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:cd05971 395 DAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
19-537 |
8.69e-52 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 185.26 E-value: 8.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPETDT----QVTYRDLSHMVGHFQTMFTNPnsplygAVFRQDTVAISMRNGLEFIVAFLGATmdaKIGA---P 91
Cdd:PRK13295 39 DKTAVTAVRLGTgaprRFTYRELAALVDRVAVGLARL------GVGRGDVVSCQLPNWWEFTVLYLACS---RIGAvlnP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 92 LNPNYKEKEFNFYLNDLKSKAICVPKG---------TTKLQSS-----EIL----KSASTFGCFIVELAFDATRfrveyD 153
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaamARRLRPElpalrHVVvvggDGADSFEALLITPAWEQEP-----D 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 154 IYSPEDNYKrviyrslnnakfvntnpvkfPGfarSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRS 233
Cdd:PRK13295 185 APAILARLR--------------------PG---PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 234 YVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPK--PNPFPHIRFIRSCS 311
Cdd:PRK13295 242 LMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKesGRPVSSLRTFLCAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 312 SALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGEN 390
Cdd:PRK13295 322 APIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPlPGVEVRVVDADGAPLPAGQIGRLQVRGCS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 391 VTLGYANNPKANKenfTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDD 470
Cdd:PRK13295 402 NFGGYLKRPQLNG---TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDE 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 471 MYGQVVQAAIVLKKGEKMTYEELVNFLK-KHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKSS 537
Cdd:PRK13295 479 RLGERACAFVVPRPGQSLDFEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
181-532 |
1.43e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 184.75 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 181 KFPGFARSSdvALILHTSGTTSTPKTVPllhlnivRSTLNIantykLTP----LDR------SYVVM--PLFHVHGLIGV 248
Cdd:PRK07788 201 PLPKPPKPG--GIVILTSGTTGTPKGAP-------RPEPSP-----LAPlaglLSRvpfragETTLLpaPMFHATGWAHL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 249 LLST-FRTQgsVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPkPNPFPH-----IRFIRSCSSALAPATFHKL 322
Cdd:PRK07788 267 TLAMaLGST--VVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLG-PEVLAKydtssLKIIFVSGSALSPELATRA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 323 EKEFNaPVL-EAYAMTEASHQMTSN--NLppgKRKPGTVGQ-PQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANN 398
Cdd:PRK07788 344 LEAFG-PVLyNLYGSTEVAFATIATpeDL---AEAPGTVGRpPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDG 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 399 PKANKENftkreNYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQA 478
Cdd:PRK07788 420 RDKQIID-----GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRA 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 398365585 479 AIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAET 532
Cdd:PRK07788 495 FVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
188-524 |
2.07e-51 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 182.92 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVV-PDGFH 266
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFhPNPLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 267 PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEAShQMTSN 346
Cdd:cd05909 226 YKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECS-PVISV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 347 NLPPGKRKPGTVGQP-QGVTVVILDDNDNV-LPPGKVGEVSIRGENVTLGYANNPKanKENFTKRENYFRTGDQGYFDPE 424
Cdd:cd05909 305 NTPQSPNKEGTVGRPlPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPE--LTSFAFGDGWYDTGDIGKIDGE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 425 GFLVLTGRIKELINRGGEKISPIELDGIMLSHPKID-EAVAFGVPDDMYGQVVqaaIVLKKGEKMTYEELVNFLKKH-LA 502
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKI---VLLTTTTDTDPSSLNDILKNAgIS 459
|
330 340
....*....|....*....|..
gi 398365585 503 SFKIPTKVYFVDKLPKTATGKI 524
Cdd:cd05909 460 NLAKPSYIHQVEEIPLLGTGKP 481
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
19-527 |
3.63e-51 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 182.32 E-value: 3.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPETDTQVTYRDLSHMVGHFQTMFtnpnspLYGAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKE 98
Cdd:cd05923 16 DACAIADPARGLRLTYSELRARIEAVAARL------HARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 99 KEFNFYL--NDLKSKAICVPKGTTKlqsseilKSASTFGCFIVELAFDATRfrvEYDIYSPednykrviyrslnnakfvn 176
Cdd:cd05923 90 AELAELIerGEMTAAVIAVDAQVMD-------AIFQSGVRVLALSDLVGLG---EPESAGP------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 177 tnPVKFPGfARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYV--VMPLFHVHGLIGVLLSTFR 254
Cdd:cd05923 141 --LIEDPP-REPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVlgLMPLYHVIGFFAVLVAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 255 TQGSVVVPDGFHPK--LFWDQFVKYNCNWfsCVPTI--SMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPV 330
Cdd:cd05923 218 LDGTYVVVEEFDPAdaLKLIEQERVTSLF--ATPTHldALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 331 LEAYAMTEAshqMTSNNLPpgKRKPGTVGQP---QGVTVV-ILDDNDNVLPPGKVGE--VSIRGENVTLGYANNPKANKE 404
Cdd:cd05923 296 VNIYGTTEA---MNSLYMR--DARTGTEMRPgffSEVRIVrIGGSPDEALANGEEGEliVAAAADAAFTGYLNQPEATAK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 405 NftKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKK 484
Cdd:cd05923 371 K--LQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 398365585 485 GeKMTYEELVNF-LKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05923 449 G-TLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
188-534 |
6.07e-51 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 182.65 E-value: 6.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVPLLH---LNIVRSTLNIANtykLTPLDRSYVVMPLFH-----VHGLIGVLLstfrTQGSV 259
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPKLIPRTHddyLYSVRASAEICG---LDADTVYLAALPAAHnfplsSPGVLGVLY----AGGTV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 260 VVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMT 337
Cdd:COG1021 256 VLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYdlSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 338 EASHQMTSNNLPPGKRKpGTVGQPQGV--TVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRT 415
Cdd:COG1021 336 EGLVNYTRLDDPEEVIL-TTQGRPISPddEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTP-DGFYRT 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 416 GDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLkKGEKMTYEELVN 495
Cdd:COG1021 414 GDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRR 492
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 398365585 496 FLK-KHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFA 534
Cdd:COG1021 493 FLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
183-532 |
1.35e-50 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 181.88 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 183 PGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGL---IGVLLstfrTQGSV 259
Cdd:PRK06155 174 AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALnafFQALL----AGATY 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 260 VVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPK-PNPFPHirfirSCSSALAPATFHKLEKEFNA----PVLEAY 334
Cdd:PRK06155 250 VLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPArESDRAH-----RVRVALGPGVPAALHAAFRErfgvDLLDGY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 335 AMTEASHQMTsnnLPPGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGEN---VTLGYANNPKANKENFtkRE 410
Cdd:PRK06155 325 GSTETNFVIA---VTHGSQRPGSMGRLApGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW--RN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 411 NYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTY 490
Cdd:PRK06155 400 LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP 479
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAET 532
Cdd:PRK06155 480 VALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
189-538 |
5.21e-50 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 180.56 E-value: 5.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRstlNIANT-YKLTPLDRSYVV----MPLFHVHGLIGVLLSTFRTQGSVVVPD 263
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRNLVA---NLCSSlFSVGPEMIGQVVtlglIPFFHIYGITGICCATLRNKGKVVVMS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 264 GFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFP----HIRFIRSCSSALAPATFHKLEKEF-NAPVLEAYAMTE 338
Cdd:PLN02330 261 RFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDlsklKLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 339 ASHQMTSNNLPP---GKRKPGTVG--QPQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNpKANKENFTKRENYF 413
Cdd:PLN02330 341 HSCITLTHGDPEkghGIAKKNSVGfiLPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNN-KEETDRTIDEDGWL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 414 RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEEL 493
Cdd:PLN02330 420 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDI 499
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398365585 494 VNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKSSR 538
Cdd:PLN02330 500 LNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINK 544
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
190-533 |
1.14e-49 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 174.06 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVPDGFHPKL 269
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 270 fwDQFVKYNCNWFSCVPT-ISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEfNAPVLEAYAMTEASHQMTSnnL 348
Cdd:cd17630 80 --EDLAPPGVTHVSLVPTqLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVAT--K 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 349 PPGKRKPGTVGQP-QGVTVVILDDndnvlppgkvGEVSIRGENVTLGYANNPKankENFTKRENYFRTGDQGYFDPEGFL 427
Cdd:cd17630 155 RPDGFGRGGVGVLlPGRELRIVED----------GEIWVGGASLAMGYLRGQL---VPEFNEDGWFTTKDLGELHADGRL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 428 VLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLkkGEKMTYEELVNFLKKHLASFKIP 507
Cdd:cd17630 222 TVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG--RGPADPAELRAWLKDKLARFKLP 299
|
330 340
....*....|....*....|....*.
gi 398365585 508 TKVYFVDKLPKTATGKIQRRVIAETF 533
Cdd:cd17630 300 KRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
190-526 |
1.15e-48 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 174.19 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHlnivRSTLNIANTY-----KLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDG 264
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAH----RDPLLFADAMarealGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 F-HPKLFWDQFVKYNCNWFSCVPTI--SMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASH 341
Cdd:cd05919 168 WpTAERVLATLARFRPTVLYGVPTFyaNLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGH 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 342 QMTSNNlpPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRENYFRTGDQGY 420
Cdd:cd05919 248 IFLSNR--PGAWRLGSTGRPvPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF--NGGWYRTGDKFC 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 421 FDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKG---EKMTYEELVNFL 497
Cdd:cd05919 324 RDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapQESLARDIHRHL 403
|
330 340
....*....|....*....|....*....
gi 398365585 498 KKHLASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:cd05919 404 LERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
189-529 |
1.22e-48 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 174.71 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDG---- 264
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSaetl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 ------FHPKLF------WDQFvkYNCNWFSCVPTISMIMLnmpKPNPFPHIRFIRSCSSALAPATFHKLEKeFNAPVLE 332
Cdd:cd05907 167 lddlseVRPTVFlavprvWEKV--YAAIKVKAVPGLKRKLF---DLAVGGRLRFAASGGAPLPAELLHFFRA-LGIPVYE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 333 AYAMTEASHQMTSNnlPPGKRKPGTVGQP-QGVTVVILDDndnvlppgkvGEVSIRGENVTLGYANNPKANKENFTKrEN 411
Cdd:cd05907 241 GYGLTETSAVVTLN--PPGDNRIGTVGKPlPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDA-DG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 412 YFRTGDQGYFDPEGFLVLTGRIKELI-NRGGEKISPIELDGIMLSHPKIDEAVAFG----------VPDDmygQVVQAAI 480
Cdd:cd05907 308 WLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDP---EALEAWA 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 481 VLKKGEKMTYEEL-------------VNFLKKHLASFKIPTKVYFVDKLP------KTATGKIQRRVI 529
Cdd:cd05907 385 EEHGIAYTDVAELaanpavraeieaaVEAANARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRPVI 452
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
61-535 |
1.67e-48 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 177.21 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 61 RQDTVAISMRNGLEFIVAFLGATMdakIGA---PLNPNYKEKEFNFYLNDLKSKAICV--PKGTTKLQssEILKSASTFG 135
Cdd:COG1022 64 PGDRVAILSDNRPEWVIADLAILA---AGAvtvPIYPTSSAEEVAYILNDSGAKVLFVedQEQLDKLL--EVRDELPSLR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 136 CFIVelaFDATRFRVEYDIYSPEDNYKRViyRSLNNAKFVNTNPVKfpgfARSSDVALILHTSGTTSTPKTVPLLHLNIV 215
Cdd:COG1022 139 HIVV---LDPRGLRDDPRLLSLDELLALG--REVADPAELEARRAA----VKPDDLATIIYTSGTTGRPKGVMLTHRNLL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 216 RSTLNIANTYKLTPLDRSYVVMPLFHVHG-LIGVLLstFRTQGSVVVPDGfhPKLFWDQFVKYNCNWFSCVPTI-----S 289
Cdd:COG1022 210 SNARALLERLPLGPGDRTLSFLPLAHVFErTVSYYA--LAAGATVAFAES--PDTLAEDLREVKPTFMLAVPRVwekvyA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 290 MIMLNM---------------------------PKPNPFP----------------------HIRFIRSCSSALAPATFH 320
Cdd:COG1022 286 GIQAKAeeagglkrklfrwalavgrryararlaGKSPSLLlrlkhaladklvfsklrealggRLRFAVSGGAALGPELAR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 321 klekEFNA---PVLEAYAMTEASHQMTSNnlPPGKRKPGTVGQP-QGVTVVILDDndnvlppgkvGEVSIRGENVTLGYA 396
Cdd:COG1022 366 ----FFRAlgiPVLEGYGLTETSPVITVN--RPGDNRIGTVGPPlPGVEVKIAED----------GEILVRGPNVMKGYY 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 397 NNPKANKENFTkRENYFRTGDQGYFDPEGFLVLTGRIKELI-NRGGEKISPIELDGIMLSHPKIDEAVAFG--------- 466
Cdd:COG1022 430 KNPEATAEAFD-ADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVGdgrpflaal 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 467 -VPD---------------DMYGQVVQAAIVLKKgekmtYEELVNFLKKHLASFKIPTKVYFvdkLPK---------TAT 521
Cdd:COG1022 509 iVPDfealgewaeenglpyTSYAELAQDPEVRAL-----IQEEVDRANAGLSRAEQIKRFRL---LPKeftiengelTPT 580
|
570
....*....|....
gi 398365585 522 GKIQRRVIAETFAK 535
Cdd:COG1022 581 LKLKRKVILEKYAD 594
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
197-526 |
2.51e-48 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 170.28 E-value: 2.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 197 TSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGvLLSTFRTQGSVVVPDGFHPKLFWDQFVK 276
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYG-AISALYLGGTFIGQRKFNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 277 YNCNWFSCVPTisMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEF-NAPVLEAYAMTEAShqMTSNNLPPGKRKP 355
Cdd:cd17633 87 YNATVIYLVPT--MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELS--FITYNFNQESRPP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 356 GTVGQP-QGVTVVILDDNDnvlppGKVGEVSIRGENVTLGYAnnpkanKENFTKRENYFRTGDQGYFDPEGFLVLTGRIK 434
Cdd:cd17633 163 NSVGRPfPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYV------RGGFSNPDGWMSVGDIGYVDEEGYLYLVGRES 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 435 ELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVvqaAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVD 514
Cdd:cd17633 232 DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEI---AVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVD 308
|
330
....*....|..
gi 398365585 515 KLPKTATGKIQR 526
Cdd:cd17633 309 SLPYTSSGKIAR 320
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
187-529 |
1.46e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 172.76 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFH 266
Cdd:PRK06145 147 APTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 267 PKLFWDQFVKY--NCNWFScvPTISMIMLNMPKPNPF---------------PHIRfIRSCSSALAPATFhklekefnap 329
Cdd:PRK06145 227 PEAVLAAIERHrlTCAWMA--PVMLSRVLTVPDRDRFdldslawcigggektPESR-IRDFTRVFTRARY---------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 vLEAYAMTEASHQMTSNNLPPGKRKPGTVGQPQG-VTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTk 408
Cdd:PRK06145 294 -IDAYGLTETCSGDTLMEAGREIEKIGSTGRALAhVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 409 rENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKM 488
Cdd:PRK06145 372 -GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATL 450
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 398365585 489 TYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:PRK06145 451 TLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
63-537 |
2.28e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 173.04 E-value: 2.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICVPKGTTKLqSSEILKSASTFGCFIVELA 142
Cdd:PRK07786 68 DRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPV-ATAVRDIVPLLSTVVVAGG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 143 fdatrfrveydiySPEDNYkrVIYRSLNNAKFVNTNPVKFPgfarSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIA 222
Cdd:PRK07786 147 -------------SSDDSV--LGYEDLLAEAGPAHAPVDIP----NDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 223 NTYKL-TPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDG-FHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP 300
Cdd:PRK07786 208 RTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGaFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 301 FP-HIRFIrscSSALAPAT---FHKLEKEF-NAPVLEAYAMTEAShQMTSNNLppGK---RKPGTVGQP-QGVTVVILDD 371
Cdd:PRK07786 288 RDlALRVL---SWGAAPASdtlLRQMAATFpEAQILAAFGQTEMS-PVTCMLL--GEdaiRKLGSVGKViPTVAARVVDE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 372 NDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKreNYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDG 451
Cdd:PRK07786 362 NMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG--GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVEN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 452 IMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKG-EKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIA 530
Cdd:PRK07786 440 VLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
....*..
gi 398365585 531 ETFAKSS 537
Cdd:PRK07786 520 ERYGACV 526
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
190-526 |
7.36e-47 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 166.52 E-value: 7.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGL-IGVLLSTFrtQGSVVVPDG-FHP 267
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYkAGIVACLL--TGATVVPVAvFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 268 KLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEFN-APVLEAYAMTEASHQMT 344
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLDHPGRKKFdlSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNNLPPGKRKPGTVGQP-QGVTVVILDDndnvlppgkvGEVSIRGENVTLGYANNPKANKENFTKReNYFRTGDQGYFDP 423
Cdd:cd17638 159 CRPGDDAETVATTCGRAcPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDAD-GWLHTGDVGELDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 424 EGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLAS 503
Cdd:cd17638 228 RGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLAN 307
|
330 340
....*....|....*....|...
gi 398365585 504 FKIPTKVYFVDKLPKTATGKIQR 526
Cdd:cd17638 308 YKVPRFVRFLDELPRNASGKVMK 330
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
190-527 |
4.74e-46 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 168.27 E-value: 4.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLH----LNIVRStlniANTYKLTPLDRSYVVMPLFH-----VHGLIGVLLSTfrtqGSVV 260
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHndyaYNVRAS----AEVCGLDQDTVYLAVLPAAHnfplaCPGVLGTLLAG----GRVV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 261 VPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLN--MPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTE 338
Cdd:cd05920 212 LAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 339 ASHQMTSNNLPPgKRKPGTVGQP--QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTG 416
Cdd:cd05920 292 GLLNYTRLDDPD-EVIIHTQGRPmsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP-DGFYRTG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 417 DQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLkKGEKMTYEELVNF 496
Cdd:cd05920 370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVL-RDPPPSAAQLRRF 448
|
330 340 350
....*....|....*....|....*....|..
gi 398365585 497 LKKH-LASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05920 449 LRERgLAAYKLPDRIEFVDSLPLTAVGKIDKK 480
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
188-530 |
1.54e-45 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 169.42 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVpllhlniVRST--------LNIANTYKLTPLD-------------RSYVVM-PLfhVHGL 245
Cdd:cd05967 229 ATDPLYILYTSGTTGKPKGV-------VRDNgghavalnWSMRNIYGIKPGDvwwaasdvgwvvgHSYIVYgPL--LHGA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 246 IGVLLstfrtQGS-VVVPDgfhPKLFWDQFVKYNCNWFSCVPT-ISMImlnmpKPNPfPHIRFIRSCS-SALA------- 315
Cdd:cd05967 300 TTVLY-----EGKpVGTPD---PGAFWRVIEKYQVNALFTAPTaIRAI-----RKED-PDGKYIKKYDlSSLRtlflage 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 316 ---PATFHKLEKEFNAPVLEAYAMTEASHQMTSN-----NLPPgkrKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSI 386
Cdd:cd05967 366 rldPPTLEWAENTLGVPVIDHWWQTETGWPITANpvglePLPI---KAGSPGKPvPGYQVQVLDEDGEPVGPNELGNIVI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 387 R-----GENVTLgYANNPKANKENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDE 461
Cdd:cd05967 443 KlplppGCLLTL-WKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 462 AVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKH-------LASFKiptKVYFVDKLPKTATGKIQRRVIA 530
Cdd:cd05967 522 CAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALvreqigpVAAFR---LVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
187-527 |
1.67e-45 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 168.01 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDValILHTSGTTSTPKTVPllhlnivRSTLNIANTYKlTPLDR--------SYVVMPLFHVHGLIGVLL-STFRTqg 257
Cdd:PRK13382 196 RKGRV--ILLTSGTTGTPKGAR-------RSGPGGIGTLK-AILDRtpwraeepTVIVAPMFHAWGFSQLVLaASLAC-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPH----IRFIRSCSSALAPATFHKLEKEFNAPVLEA 333
Cdd:PRK13382 264 TIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYsgrsLRFAAASGSRMRPDVVIAFMDQFGDVIYNN 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 334 YAMTEAShqMTSNNLPPGKRK-PGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYAnnPKANKENftkREN 411
Cdd:PRK13382 344 YNATEAG--MIATATPADLRAaPDTAGRPaEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYT--SGSTKDF---HDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 412 YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYE 491
Cdd:PRK13382 417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPE 496
|
330 340 350
....*....|....*....|....*....|....*.
gi 398365585 492 ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRR 532
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
60-540 |
2.35e-45 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 167.71 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 60 FRQ-DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLK-SKAICVPKGTTKLQSSEIlksastfGCF 137
Cdd:PLN02574 89 VRQgDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSvGLAFTSPENVEKLSPLGV-------PVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 138 IVELAFDatrfrveYDIYSPEDNYKRVIYRSlnnakfvNTNPVKFPgFARSSDVALILHTSGTTSTPKTVPLLHLNIVrS 217
Cdd:PLN02574 162 GVPENYD-------FDSKRIEFPKFYELIKE-------DFDFVPKP-VIKQDDVAAIMYSSGTTGASKGVVLTHRNLI-A 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 218 TLNI-----ANTYKLTPLDRSYV-VMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMI 291
Cdd:PLN02574 226 MVELfvrfeASQYEYPGSDNVYLaALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 292 MLNMPKPNPFPHIRFIRSCSSALAPaTFHKLEKEF-----NAPVLEAYAMTEASHQMTSNNLPPGKRKPGTVG--QPQGV 364
Cdd:PLN02574 306 LTKKAKGVCGEVLKSLKQVSCGAAP-LSGKFIQDFvqtlpHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGllAPNMQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 365 TVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKI 444
Cdd:PLN02574 385 AKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK-DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQI 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 445 SPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:PLN02574 464 APADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKI 543
|
490
....*....|....*.
gi 398365585 525 QRRVIAETFAKSSRNK 540
Cdd:PLN02574 544 LRRELKRSLTNSVSSR 559
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
22-531 |
2.91e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 166.62 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 22 AVIVPETDTQVTYRDL----SHMVGHFQTMftnpnsplygAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYK 97
Cdd:PRK08276 2 AVIMAPSGEVVTYGELearsNRLAHGLRAL----------GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 98 EKEFNFYLNDLKSKAICVpkgttklqSSEILKSASTFGCfivELAFDATRFRVEYDIYSPEDNYkrviyrslnnAKFVNT 177
Cdd:PRK08276 72 AAEIAYIVDDSGAKVLIV--------SAALADTAAELAA---ELPAGVPLLLVVAGPVPGFRSY----------EEALAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 178 NPvKFPGfARSSDVALILHTSGTTSTPKTV--PLLHLNI-----VRSTLnIANTYKLTPLDRSYVVMPLFHVhgliGVLL 250
Cdd:PRK08276 131 QP-DTPI-ADETAGADMLYSSGTTGRPKGIkrPLPGLDPdeapgMMLAL-LGFGMYGGPDSVYLSPAPLYHT----APLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 251 ---STFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPkpnpfPHIRF------IRSCSSALAPATFHK 321
Cdd:PRK08276 204 fgmSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKLP-----EEVRArydvssLRVAIHAAAPCPVEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 322 LEK--EFNAPVL-EAYAMTEAsHQMTSNNLPPGKRKPGTVGQPQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANN 398
Cdd:PRK08276 279 KRAmiDWWGPIIhEYYASSEG-GGVTVITSEDWLAHPGSVGKAVLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHND 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 399 PKANKENFTKReNYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQA 478
Cdd:PRK08276 358 PEKTAAARNPH-GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 479 AIVLKKGEKMT---YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK08276 437 VVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
32-527 |
8.75e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 166.48 E-value: 8.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 32 VTYRDLSHMVGHFQTMFTNPNSPLYGavfrqDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSK 111
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHTDLKPG-----DRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 112 AICVPKGTTKLqSSEILKSASTFGCFIVELAfdatrfrveyDIYSPednykrvIYRSLNNA--KFVNT--------NPVK 181
Cdd:PRK05677 125 ALVCLANMAHL-AEKVLPKTGVKHVIVTEVA----------DMLPP-------LKRLLINAvvKHVKKmvpayhlpQAVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 182 F-------------PGFARSSDVALILHTSGTTSTPKTVPLLHLNIVR----------STLNIANTYKLTPLdrsyvvmP 238
Cdd:PRK05677 187 FndalakgagqpvtEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcralmgSNLNEGCEILIAPL-------P 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 239 LFHVHGLIGVLLSTFRTQG-SVVVPDgfhPKLFwDQFVKYNCNW-FSCVPTISMIMLNMPKPNPFPHIRFIR-----SCS 311
Cdd:PRK05677 260 LYHIYAFTFHCMAMMLIGNhNILISN---PRDL-PAMVKELGKWkFSGFVGLNTLFVALCNNEAFRKLDFSAlkltlSGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 312 SALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNnlPPGKRKPGTVGQPQGVTVV-ILDDNDNVLPPGKVGEVSIRGEN 390
Cdd:PRK05677 336 MALQLATAERWKEVTGCAICEGYGMTETSPVVSVN--PSQAIQVGTIGIPVPSTLCkVIDDDGNELPLGEVGELCVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 391 VTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDD 470
Cdd:PRK05677 414 VMKGYWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDE 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365585 471 MYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK05677 493 KSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRR 549
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
187-529 |
1.54e-44 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 164.95 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNI-VRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFrTQGSVV----V 261
Cdd:cd05928 172 GSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPW-IQGACVfvhhL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 262 PDgFHPKLFWDQFVKYNCNWFSCVPTI-SMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEAS 340
Cdd:cd05928 251 PR-FDPLVILKTLSSYPITTFCGAPTVyRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 341 hqMTSNNLPPGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVT-----LGYANNPKANKENFtkRENYFR 414
Cdd:cd05928 330 --LICANFKGMKIKPGSMGKASpPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRpfglfSGYVDNPEKTAATI--RGDFYL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 415 TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKG------EKM 488
Cdd:cd05928 406 TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQflshdpEQL 485
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 398365585 489 TyEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:cd05928 486 T-KELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
17-534 |
2.77e-44 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 164.38 E-value: 2.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 17 VSDNVAVIVPETDTQVTYRD---LSHMVGhfqtmftnpnSPLYGAVFRQ-DTVAISMRNGLEFIVAFLGATMDAKIGAPL 92
Cdd:PLN02246 36 FSDRPCLIDGATGRVYTYADvelLSRRVA----------AGLHKLGIRQgDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 93 NPnykekefnFYlndlkskaicvpkgttklQSSEILKSAS--------TFGCFIVELA-FDATRFRVEYDIYSPEDNYkr 163
Cdd:PLN02246 106 NP--------FY------------------TPAEIAKQAKasgakliiTQSCYVDKLKgLAEDDGVTVVTIDDPPEGC-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 164 VIYRSLNNAKFVNTNPVKFpgfaRSSDVALILHTSGTTSTPKTVPLLHLNIVRStlnIA--------NTYkLTPLDRSYV 235
Cdd:PLN02246 158 LHFSELTQADENELPEVEI----SPDDVVALPYSSGTTGLPKGVMLTHKGLVTS---VAqqvdgenpNLY-FHSDDVILC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 236 VMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNcnwFSCVPTISMIMLNMPKpNPFPH------IRFIRS 309
Cdd:PLN02246 230 VLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHK---VTIAPFVPPIVLAIAK-SPVVEkydlssIRMVLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 310 CSSALApatfHKLEKEFNAPVLEA-----YAMTEAShQMTSNNLP----PGKRKPGTVGqpqgvTVV------ILD-DND 373
Cdd:PLN02246 306 GAAPLG----KELEDAFRAKLPNAvlgqgYGMTEAG-PVLAMCLAfakePFPVKSGSCG-----TVVrnaelkIVDpETG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 374 NVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIM 453
Cdd:PLN02246 376 ASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDK-DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 454 LSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETF 533
Cdd:PLN02246 455 ISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKL 534
|
.
gi 398365585 534 A 534
Cdd:PLN02246 535 A 535
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
183-531 |
3.68e-44 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 164.21 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 183 PGFARSSDVALILHTSGTTSTPKTV------PLLHLNIVRSTLNiantykLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQ 256
Cdd:cd05970 179 NSYPCGEDILLVYFSSGTTGMPKMVehdftyPLGHIVTAKYWQN------VREGGLHLTVADTGWGKAVWGKIYGQWIAG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 257 GSVVVPD--GFHPKLFWDQFVKYNCNWFSCVPTIS--MIMLNMPKPNpFPHIRFIRSCSSALAPATFHKLEKEFNAPVLE 332
Cdd:cd05970 253 AAVFVYDydKFDPKALLEKLSKYGVTTFCAPPTIYrfLIREDLSRYD-LSSLRYCTTAGEALNPEVFNTFKEKTGIKLME 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 333 AYAMTEAShqMTSNNLPPGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIR---GENVTL--GYANNPKANKENF 406
Cdd:cd05970 332 GFGQTETT--LTIATFPWMEPKPGSMGKPApGYEIDLIDREGRSCEAGEEGEIVIRtskGKPVGLfgGYYKDAEKTAEVW 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 407 tkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGE 486
Cdd:cd05970 410 --HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGY 487
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 398365585 487 KMTYE---ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd05970 488 EPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
185-533 |
4.77e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 163.62 E-value: 4.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 185 FARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIgvLLSTFRTQGSVVVPDG 264
Cdd:PRK06188 164 AALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF--FLPTLLRGGTVIVLAK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 FHPKLFWDQFVKYNCNWFSCVPTisMIMLNMPKPNP----FPHIRFIRSCSSALAPATFHKLEKEFnAPVL-EAYAMTEA 339
Cdd:PRK06188 242 FDPAEVLRAIEEQRITATFLVPT--MIYALLDHPDLrtrdLSSLETVYYGASPMSPVRLAEAIERF-GPIFaQYYGQTEA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 ShqMTSNNLPPGKRKP------GTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRENY 412
Cdd:PRK06188 319 P--MVITYLRKRDHDPddpkrlTSCGRPTpGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--RDGW 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 413 FRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEE 492
Cdd:PRK06188 395 LHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAE 474
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 398365585 493 LVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETF 533
Cdd:PRK06188 475 LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARY 515
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
18-536 |
1.13e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 159.47 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 18 SDNVAVIVPETDTQVTYRDL---SHMVGHFqtmftnpnsplygavFRQ------DTVAISMRNGLEFIVAFLGATMDAKI 88
Cdd:PRK13391 11 PDKPAVIMASTGEVVTYRELderSNRLAHL---------------FRSlglkrgDHVAIFMENNLRYLEVCWAAERSGLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 89 GAPLNPNYKEKEFNFYLNDLKSKAICVPKGTTKLQSSEILKSASTFGCFIVELAFDATRFrveydiyspeDNYKRVIyrs 168
Cdd:PRK13391 76 YTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLDGDGELEGF----------VGYAEAV--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 169 lnnaKFVNTNPVkfpgfARSSDVALILHTSGTTSTPKTV--PLLHLNIVrSTLNI----ANTYKLTPLDRSYVVMPLFHV 242
Cdd:PRK13391 143 ----AGLPATPI-----ADESLGTDMLYSSGTTGRPKGIkrPLPEQPPD-TPLPLtaflQRLWGFRSDMVYLSPAPLYHS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 243 HGLIGVLLsTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKpnpfpHIRFIRSCSS------ALAP 316
Cdd:PRK13391 213 APQRAVML-VIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPE-----EVRDKYDLSSlevaihAAAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 317 ATFHKLEK--EFNAPVL-EAYAMTEAShQMTSNNLPPGKRKPGTVGQPQGVTVVILDDNDNVLPPGKVGEVSIRGENvTL 393
Cdd:PRK13391 287 CPPQVKEQmiDWWGPIIhEYYAATEGL-GFTACDSEEWLAHPGTVGRAMFGDLHILDDDGAELPPGEPGTIWFEGGR-PF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 394 GYANNPKANKENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYG 473
Cdd:PRK13391 365 EYLNDPAKTAEARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLG 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 474 QVVQAAIVLKKGEKMT---YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKS 536
Cdd:PRK13391 445 EEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
189-527 |
1.70e-42 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 159.80 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRSTL------NIANTYKLTPLDRSYVV-MPLFHVHGLIGVLLSTFRTQG-SVV 260
Cdd:PRK07059 204 DDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeawlQPAFEKKPRPDQLNFVCaLPLYHIFALTVCGLLGMRTGGrNIL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 261 VPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMP--KPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTE 338
Cdd:PRK07059 284 IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPdfDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 339 ASHQMTSNNLPPGKRKpGTVGQPQGVT-VVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGD 417
Cdd:PRK07059 364 TSPVATCNPVDATEFS-GTIGLPLPSTeVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTA-DGFFRTGD 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 418 QGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVlKKGEKMTYEELVNFL 497
Cdd:PRK07059 442 VGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEEDVKAFC 520
|
330 340 350
....*....|....*....|....*....|
gi 398365585 498 KKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK07059 521 KERLTNYKRPKFVEFRTELPKTNVGKILRR 550
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
59-526 |
1.96e-42 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 158.85 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 59 VFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICVpkgttklqSSEILKsastfgcFI 138
Cdd:TIGR02262 52 VKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFV--------SGALLP-------VI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 139 VELAFDATRFR---VEYDIYSPEDNYkrviyrslnnAKFVNTNPVKF-PGFARSSDVALILHTSGTTSTPKTVPLLHLN- 213
Cdd:TIGR02262 117 KAALGKSPHLEhrvVVGRPEAGEVQL----------AELLATESEQFkPAATQADDPAFWLYSSGSTGMPKGVVHTHSNp 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 214 IVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVV--PDGFHPKLFWDQFVKYNCNWFSCVPTISMI 291
Cdd:TIGR02262 187 YWTAELYARNTLGIREDDVCFSAAKLFFAYGL-GNALTFPMSVGATTVlmGERPTPDAVFDRLRRHQPTIFYGVPTLYAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 292 MLNMPKPNPFPHIRfIRSCSSA---LAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNlpPGKRKPGTVGQP-QGVTVV 367
Cdd:TIGR02262 266 MLADPNLPSEDQVR-LRLCTSAgeaLPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNL--PGDVRYGTSGKPvPGYRLR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 368 ILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKreNYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPI 447
Cdd:TIGR02262 343 LVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQG--EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPF 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365585 448 ELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:TIGR02262 421 EIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
61-540 |
2.37e-42 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 159.45 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 61 RQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICVpkgttklqsseilksASTFGCFIVE 140
Cdd:PRK08974 73 KGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVI---------------VSNFAHTLEK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 141 LAFDA-------TR--------------FRVEYdIYSPEDNYK---RVIYRS-LNNAKFVNTnpVKfPgFARSSDVALIL 195
Cdd:PRK08974 138 VVFKTpvkhvilTRmgdqlstakgtlvnFVVKY-IKRLVPKYHlpdAISFRSaLHKGRRMQY--VK-P-ELVPEDLAFLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 196 HTSGTTSTPKTVPLLHLNIVRSTLNIANTYklTPLDRS---YVV--MPLFHVHGL-IGVLLstFRTQGSVVV----P--- 262
Cdd:PRK08974 213 YTGGTTGVAKGAMLTHRNMLANLEQAKAAY--GPLLHPgkeLVVtaLPLYHIFALtVNCLL--FIELGGQNLlitnPrdi 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 263 DGFHPKLfwdqfVKYNCNWFSCVPTISMIMLNMP--KPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEAS 340
Cdd:PRK08974 289 PGFVKEL-----KKYPFTAITGVNTLFNALLNNEefQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECS 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 341 HQMTSN--NLppgKRKPGTVGQPQGVTVV-ILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKEnfTKRENYFRTGD 417
Cdd:PRK08974 364 PLVSVNpyDL---DYYSGSIGLPVPSTEIkLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE--VIKDGWLATGD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 418 QGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVlKKGEKMTYEELVNFL 497
Cdd:PRK08974 439 IAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV-KKDPSLTEEELITHC 517
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 398365585 498 KKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKSSRNK 540
Cdd:PRK08974 518 RRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 560
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
63-533 |
2.49e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 158.32 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICvpkGTTKLQSSeiLKSASTFGCFIVELA 142
Cdd:PRK12406 37 DCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI---AHADLLHG--LASALPAGVTVLSVP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 143 FD---ATRFRVEYDIYSPEDNYkrVIYRSLNNAKFVNTNPvkfPGFARSSdvalILHTSGTTSTPKTV------PLLHLN 213
Cdd:PRK12406 112 TPpeiAAAYRISPALLTPPAGA--IDWEGWLAQQEPYDGP---PVPQPQS----MIYTSGTTGHPKGVrraaptPEQAAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 214 IVRstlNIANTYKLTPLDRSYVVMPLFH----VHGLigvllSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTIS 289
Cdd:PRK12406 183 AEQ---MRALIYGLKPGIRALLTGPLYHsapnAYGL-----RAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 290 MIMLNMPkpnpfPHIRFIRSCSS--------ALAPATFHKLEKEFNAPVL-EAYAMTEAShQMTSNNLPPGKRKPGTVGQ 360
Cdd:PRK12406 255 IRLLKLP-----EEVRAKYDVSSlrhvihaaAPCPADVKRAMIEWWGPVIyEYYGSTESG-AVTFATSEDALSHPGTVGK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 361 -PQGVTVVILDDNDNVLPPGKVGEVSIRGENVTL-GYANNPKANKEnfTKRENYFRTGDQGYFDPEGFLVLTGRIKELIN 438
Cdd:PRK12406 329 aAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE--IDRGGFITSGDVGYLDADGYLFLCDRKRDMVI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 439 RGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPK 518
Cdd:PRK12406 407 SGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPR 486
|
490
....*....|....*
gi 398365585 519 TATGKIQRRVIAETF 533
Cdd:PRK12406 487 EDSGKIFKRRLRDPY 501
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
17-523 |
4.56e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 158.12 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 17 VSDNVAVIVpeTDTQVTYRDL---SHMVGHFqtmftnpnspLYGAVFR-QDTVAISMRNGLEFIVAFLGATmdaKIGA-P 91
Cdd:PRK07798 16 VPDRVALVC--GDRRLTYAELeerANRLAHY----------LIAQGLGpGDHVGIYARNRIEYVEAMLGAF---KARAvP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 92 LNPN--YKEKEFNFYLNDLKSKAicvpkgttklqsseiLKSASTFGCFIVELAFDATRFRVEYDIYSPEDNYKRVIYRSL 169
Cdd:PRK07798 81 VNVNyrYVEDELRYLLDDSDAVA---------------LVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 170 NNAkfVNTNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLD---------------RSY 234
Cdd:PRK07798 146 EDA--LAAGSPERDFGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEdeeelakraaagpgmRRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 235 VVMPLFHVHGLIGVLLSTFrTQGSVVVPDG--FHPKLFWDQFVKYNCNWFSCV------PTISMimLNMPKPNPFPHIRF 306
Cdd:PRK07798 224 PAPPLMHGAGQWAAFAALF-SGQTVVLLPDvrFDADEVWRTIEREKVNVITIVgdamarPLLDA--LEARGPYDLSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 307 IRSCSSALAPATFHKLEKEF-NAPVLEAYAMTEASHQMTSNNLPPGKRKPGTVGQPQGVTVViLDDNDNVLPPG--KVGE 383
Cdd:PRK07798 301 IASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVV-LDEDGNPVEPGsgEIGW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 384 VSIRGeNVTLGYANNPKANKENFTKREN--YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDE 461
Cdd:PRK07798 380 IARRG-HIPLGYYKDPEKTAETFPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365585 462 AVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGK 523
Cdd:PRK07798 459 ALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
193-528 |
2.24e-41 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 156.98 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 193 LILH-TSGTTSTPKTV------PLLHLNIVRSTLNiantykLTPLDR-------------SY-VVMPLFHvhgliGVLls 251
Cdd:PRK04319 208 AILHyTSGSTGKPKGVlhvhnaMLQHYQTGKYVLD------LHEDDVywctadpgwvtgtSYgIFAPWLN-----GAT-- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 252 tfrtqgSVVVPDGFHPKLFWDQFVKYNCN-WFScVPT-ISMIM---LNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEF 326
Cdd:PRK04319 275 ------NVIDGGRFSPERWYRILEDYKVTvWYT-APTaIRMLMgagDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVF 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 327 NAPVLEAYAMTEASHQMTSNnLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGE--NVTLGYANNPKank 403
Cdd:PRK04319 348 GLPIHDNWWMTETGGIMIAN-YPAMDIKPGSMGKPlPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNPE--- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 404 enftKRENYFR-----TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQA 478
Cdd:PRK04319 424 ----KYESYFAgdwyvSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKA 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 398365585 479 AIVLKKGEKMTYE---ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRV 528
Cdd:PRK04319 500 FVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRV 552
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
189-529 |
4.77e-41 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 153.44 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPK--TVPLLHLNIVRSTLNIAntYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRT-QGSVVVPDGF 265
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKgvPVPLRALAAFGAYLRDA--VDLRPEDSFWNAADPGWAYGLYYAITGPLALgHPTILLEGGF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 HPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF-PHIRfIRSCSSA---LAPATFHKLEKEFNAPVLEAYAMTEasH 341
Cdd:cd05973 166 SVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPArPKGR-LRRVSSAgepLTPEVIRWFDAALGVPIHDHYGQTE--L 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 342 QMTSNN--LPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTL----GYANNPKANKENftkreNYFR 414
Cdd:cd05973 243 GMVLANhhALEHPVHAGSAGRAmPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPAIDG-----GYYL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 415 TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYE--- 491
Cdd:cd05973 318 TGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAlad 397
|
330 340 350
....*....|....*....|....*....|....*...
gi 398365585 492 ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:cd05973 398 ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
63-527 |
4.86e-41 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 155.75 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAicvpkgttklqsseiLKSASTFGCFIVELA 142
Cdd:PRK12492 76 DRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARA---------------LVYLNMFGKLVQEVL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 143 FDAtrfRVEY-------DIYSPE---------DNYKRVI-----------YRSLNNAKFVNTNPVKfpgfARSSDVALIL 195
Cdd:PRK12492 141 PDT---GIEYlieakmgDLLPAAkgwlvntvvDKVKKMVpayhlpqavpfKQALRQGRGLSLKPVP----VGLDDIAVLQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 196 HTSGTTSTPKTVPLLHLNIVRSTLNI-ANTYKLTP-----LDRSYVVM----PLFHVHGligvllstFRTQGSVVVPDGF 265
Cdd:PRK12492 214 YTGGTTGLAKGAMLTHGNLVANMLQVrACLSQLGPdgqplMKEGQEVMiaplPLYHIYA--------FTANCMCMMVSGN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 HPKLFWDQ-----FVKYNCNW-FSC---VPTISMIMLNMP--KPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAY 334
Cdd:PRK12492 286 HNVLITNPrdipgFIKELGKWrFSAllgLNTLFVALMDHPgfKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 335 AMTEASHQMTSNnlPPGKR-KPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENY 412
Cdd:PRK12492 366 GLTETSPVASTN--PYGELaRLGTVGIPvPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA-EGW 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 413 FRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGeKMTYEE 492
Cdd:PRK12492 443 FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEE 521
|
490 500 510
....*....|....*....|....*....|....*
gi 398365585 493 LVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK12492 522 LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRR 556
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
193-522 |
1.57e-40 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 149.37 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 193 LILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVhGLIGVLLSTFRTQGSVVVPDGFHPKLFWD 272
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 273 QFVKYNCNW-FSCVPTISMIM-------LNMPKPNPFPHIRFIRSCSSALAPATFHKLEkefnapvleAYAMTEASHQMT 344
Cdd:cd17636 83 LIEAERCTHaFLLPPTIDQIVelnadglYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG---------GYGQTEVMGLAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNNLppGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFtkRENYFRTGDQGYFDP 423
Cdd:cd17636 154 FAAL--GGGAIGGAGRPSpLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT--RGGWHHTNDLGRREP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 424 EGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLAS 503
Cdd:cd17636 230 DGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIAS 309
|
330
....*....|....*....
gi 398365585 504 FKIPTKVYFVDKLPKTATG 522
Cdd:cd17636 310 YKKPKSVEFADALPRTAGG 328
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
193-531 |
1.59e-40 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 152.92 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 193 LILHTSGTTSTPKTV--PLLHLNIVRSTLNIANTYKLTPLDRSYV-VMPLFHVHGLIgVLLSTFRTQGSVVVPDGFHPKL 269
Cdd:cd05929 129 KMLYSGGTTGRPKGIkrGLPGGPPDNDTLMAAALGFGPGADSVYLsPAPLYHAAPFR-WSMTALFMGGTLVLMEKFDPEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 270 FWDQFVKYNCNWFSCVPTISMIMLNMPK--PNPFpHIRFIRSCSSALAPATFHKLEK--EFNAPVL-EAYAMTEAShQMT 344
Cdd:cd05929 208 FLRLIERYRVTFAQFVPTMFVRLLKLPEavRNAY-DLSSLKRVIHAAAPCPPWVKEQwiDWGGPIIwEYYGGTEGQ-GLT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNNLPPGKRKPGTVGQPQGVTVVILDDNDNVLPPGKVGEVSIRGeNVTLGYANNPkaNKENFTKRENYFRT-GDQGYFDP 423
Cdd:cd05929 286 IINGEEWLTHPGSVGRAVLGKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDP--EKTAAARNEGGWSTlGDVGYLDE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 424 EGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGE---KMTYEELVNFLKKH 500
Cdd:cd05929 363 DGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFLRDR 442
|
330 340 350
....*....|....*....|....*....|.
gi 398365585 501 LASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd05929 443 LSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
6-526 |
2.02e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 152.63 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 6 TVTASFNDTFSVSDNVAVIVpETDTQVTYRDLSHMVGHFQTMFTNPNSplygavfRQDTVAISMRNGLEFIVAFLGATMD 85
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIK-ENDRVLTYKDWFESVCKVANWLNEKES-------KNKTIAILLENRIEFLQLFAGAAMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 86 AKIGAPLNPNYKEKEFNFYLndLKSKA---ICVPKGTTKLQSSEilksastfgCFIVELafdatrfrveydiyspeDNYK 162
Cdd:PRK07638 74 GWTCVPLDIKWKQDELKERL--AISNAdmiVTERYKLNDLPDEE---------GRVIEI-----------------DEWK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 163 RVIYRSLNNAKFVNtNPVKFP---GFarssdvalilhTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPL 239
Cdd:PRK07638 126 RMIEKYLPTYAPIE-NVQNAPfymGF-----------TSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 240 FHVHGLIGVLlSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTismiMLNMP-KPNPFPH--IRFIRSCSSALAP 316
Cdd:PRK07638 194 VHSLFLYGAI-STLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPT----MLESLyKENRVIEnkMKIISSGAKWEAE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 317 ATfHKLEKEF-NAPVLEAYAMTEASHqMTSNNLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLG 394
Cdd:PRK07638 269 AK-EKIKNIFpYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPfHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 395 YANNPKANKEnfTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQ 474
Cdd:PRK07638 347 YIIGGVLARE--LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 398365585 475 VVQAAIvlkKGEKmTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:PRK07638 425 KPVAII---KGSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
189-526 |
2.71e-40 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 148.95 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYK-LTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHP 267
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLnWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 268 KLFWDQFVKYNCNWFSCVPTISMIMLNMPKP--NPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEAShqmTS 345
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSanATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETG---TA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 346 NNLPPGK--RKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTkrENYFRTGDQGYFD 422
Cdd:cd17635 158 LCLPTDDdsIEINAVGRPyPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI--DGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 423 PEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVlKKGE--KMTYEELVNFLKKH 500
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV-ASAEldENAIRALKHTIRRE 314
|
330 340
....*....|....*....|....*.
gi 398365585 501 LASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:cd17635 315 LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
29-526 |
3.28e-40 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 151.83 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 29 DTQVTYRDLSHMVGHFQtMFTNPNSplygaVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDL 108
Cdd:cd05914 5 GEPLTYKDLADNIAKFA-LLLKING-----VGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 109 KSKAIcvpkgttklqsseilksastfgcfivelafdatrfrveydiyspednykrviyrslnnakFVNTNpvkfpgfars 188
Cdd:cd05914 79 EAKAI------------------------------------------------------------FVSDE---------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGF-HP 267
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpSA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 268 KLFWDQFVKYNCNWFSCVPTISM---IMLNMPKPN-----------PFP-----------------HIRFIRSCSSALAP 316
Cdd:cd05914 169 KIIALAFAQVTPTLGVPVPLVIEkifKMDIIPKLTlkkfkfklakkINNrkirklafkkvheafggNIKEFVIGGAKINP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 317 ATFHKLeKEFNAPVLEAYAMTEASHQMTSNnlPPGKRKPGTVGQP-QGVTVVILDDNdnvlPPGKVGEVSIRGENVTLGY 395
Cdd:cd05914 249 DVEEFL-RTIGFPYTIGYGMTETAPIISYS--PPNRIRLGSAGKViDGVEVRIDSPD----PATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 396 ANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRG-GEKISPIELDGIMLSHPKI---------DEAVAF 465
Cdd:cd05914 322 YKNPEATAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVleslvvvqeKKLVAL 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365585 466 GVPDDMYGQVVQAAIVLKKGEKMtyEELVNFLKKHLASFKIPTKVYFV-DKLPKTATGKIQR 526
Cdd:cd05914 401 AYIDPDFLDVKALKQRNIIDAIK--WEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-523 |
4.78e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 146.37 E-value: 4.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLD--------------RSYVVMPLFHVHGLIGVLLST 252
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaagtVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 253 FrTQGSVVVPD-GFHPKLFWDQFVKYNCNWFSCV------PTISMimLNMPKPNPFPHIRFIRSCSSALAPAtfHK---L 322
Cdd:cd05924 81 L-GGQTVVLPDdRFDPEEVWRTIEKHKVTSMTIVgdamarPLIDA--LRDAGPYDLSSLFAISSGGALLSPE--VKqglL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 323 EKEFNAPVLEAYAMTEASHQMTSNNLPPGKrKPGTVGQPQGVTVViLDDNDNVLPPGK--VGEVSIRGeNVTLGYANNPK 400
Cdd:cd05924 156 ELVPNITLVDAFGSSETGFTGSGHSAGSGP-ETGPFTRANPDTVV-LDDDGRVVPPGSggVGWIARRG-HIPLGYYGDEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 401 ANKENFTKREN--YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQA 478
Cdd:cd05924 233 KTAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398365585 479 AIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGK 523
Cdd:cd05924 313 VVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
193-530 |
2.94e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 147.07 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 193 LILHTSGTTSTPKTVPllHLNIVRSTLNIANTY----KLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVPDGFHPK 268
Cdd:PRK13383 178 IVLLTSGTTGKPKGVP--RAPQLRSAVGVWVTIldrtRLRTGSRISVAMPMFHGLGL-GMLMLTIALGGTVLTHRHFDAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNCNWFSCVPTISMIMLNMPKP----NPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEAShqMT 344
Cdd:PRK13383 255 AALAQASLHRADAFTAVPVVLARILELPPRvrarNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVG--IG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNNLPPGKRK-PGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNP-KANKENFTKrenyfrTGDQGYF 421
Cdd:PRK13383 333 ALATPADLRDaPETVGKPvAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGgKAVVDGMTS------TGDMGYL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 422 DPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHL 501
Cdd:PRK13383 407 DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRV 486
|
330 340
....*....|....*....|....*....
gi 398365585 502 ASFKIPTKVYFVDKLPKTATGKIQRRVIA 530
Cdd:PRK13383 487 SRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
189-531 |
8.48e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 146.33 E-value: 8.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPK 268
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSAS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNCNWFSCV-PTISMIMLNMPKP----NPFphirfIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQM 343
Cdd:PRK13388 230 GFLDDVRRYGATYFNYVgKPLAYILATPERPddadNPL-----RVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 344 TsnnLPPGKrKPGTVGQP-QGVTVV-----------ILDDNDNVLPPGK-VGE-VSIRGENVTLGYANNPKANKENFtkR 409
Cdd:PRK13388 305 V---REPGT-PPGSIGRGaPGVAIYnpetltecavaRFDAHGALLNADEaIGElVNTAGAGFFEGYYNNPEATAERM--R 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKIS--PIELdgIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEK 487
Cdd:PRK13388 379 HGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSaaPIER--ILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGAT 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398365585 488 MTYEELVNFL--KKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK13388 457 FDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
153-531 |
1.48e-37 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 143.60 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 153 DIYSPEDNyKRVIYRSLNNAKFVNTNpvkfpgfaRSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDR 232
Cdd:cd17653 78 DAKLPSAR-IQAILRTSGATLLLTTD--------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 233 SYVVM-PLFHVhgLIGVLLSTFRTQGSVVVPDgfHPKLFWDqfVKYNCNWFSCVPTIsmimLNMPKPNPFPHIRFI---- 307
Cdd:cd17653 149 VAQVLsIAFDA--CIGEIFSTLCNGGTLVLAD--PSDPFAH--VARTVDALMSTPSI----LSTLSPQDFPNLKTIflgg 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 308 RSCSSALAPATFHklekefNAPVLEAYAMTEASHQMTSNNLPPGKrkPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSI 386
Cdd:cd17653 219 EAVPPSLLDRWSP------GRRLYNAYGPTECTISSTMTELLPGQ--PVTIGKPiPNSTCYILDADLQPVPEGVVGEICI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 387 RGENVTLGYANNPKANKENFT-----KRENYFRTGDQGYFDPEGFLVLTGRIKELI-NRGGEkispIELDGI----MLSH 456
Cdd:cd17653 291 SGVQVARGYLGNPALTASKFVpdpfwPGSRMYRTGDYGRWTEDGGLEFLGREDNQVkVRGFR----INLEEIeevvLQSQ 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 457 PKIDEAVAFGVPDDMYGQVVQAAIVLkkgekmtyEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd17653 367 PEVTQAAAIVVNGRLVAFVTPETVDV--------DGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
190-527 |
1.90e-37 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 143.54 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPL---FHVHGLIGVLLSTfrtqGSVVVPDG-- 264
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFsfdLSVMDLYPALASG----ATLVPVPRda 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 -FHPKLFWDQFVKYNCN-WFScVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEF-NAPVLEAYAMTEA 339
Cdd:cd05945 174 tADPKQLFRFLAEHGITvWVS-TPSFAAMCLLSPTFTPesLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 -----SHQMTsnNLPPGKRKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKRENY- 412
Cdd:cd05945 253 tvavtYIEVT--PEVLDGYDRLPIGYAKpGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQr 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 413 -FRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGE--KMT 489
Cdd:cd05945 331 aYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAeaGLT 410
|
330 340 350
....*....|....*....|....*....|....*...
gi 398365585 490 yEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05945 411 -KAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
196-534 |
6.18e-37 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 143.74 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 196 HTSGTTSTPKTVPLLHLNIVRSTL--NIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVP----DGFHP-K 268
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSNVLHALmaNNGDALGTSAADTMLPVVPLFHANSW-GIAFSAPSMGTKLVMPgaklDGASVyE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNcnwfSCVPTISMIMLN-MPKPN-PFPHIRFIrSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSN 346
Cdd:PRK06018 263 LLDTEKVTFT----AGVPTVWLMLLQyMEKEGlKLPHLKMV-VCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 347 NLPPGKRK-PG----TVGQPQG-----VTVVILDDNDNVLP-PGKV-GEVSIRGENVTLGYAnnpKANKENFTKrENYFR 414
Cdd:PRK06018 338 ALKPPFSKlPGdarlDVLQKQGyppfgVEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYY---RVDGEILDD-DGFFD 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 415 TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELV 494
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEIL 493
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 398365585 495 NFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFA 534
Cdd:PRK06018 494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFK 533
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
196-524 |
1.22e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 143.62 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 196 HTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFwDQFV 275
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIY-KNIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 276 KYNCNWFSCVPTISMIMLN------MPKPNPfphIRFIRSCSSAlaPATFHKLEKEFNAPVLEAYAMTEASH-------Q 342
Cdd:PLN03102 272 MHNVTHMCCVPTVFNILLKgnsldlSPRSGP---VHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGpvlfcewQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 343 MTSNNLPPGKRKpgTVGQPQGVTVVILDDND--------NVLPPGK-VGEVSIRGENVTLGYANNPKANKENFtkRENYF 413
Cdd:PLN03102 347 DEWNRLPENQQM--ELKARQGVSILGLADVDvknketqeSVPRDGKtMGEIVIKGSSIMKGYLKNPKATSEAF--KHGWL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 414 RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYE-- 491
Cdd:PLN03102 423 NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDrv 502
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 398365585 492 --------ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:PLN03102 503 dklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKI 543
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
196-533 |
5.75e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 141.00 E-value: 5.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 196 HTSGTTSTPKTVPLLHlnivRSTL------NIANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVP----DGf 265
Cdd:PRK07008 183 YTSGTTGNPKGALYSH----RSTVlhaygaALPDAMGLSARDAVLPVVPMFHVNAW-GLPYSAPLTGAKLVLPgpdlDG- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 hpKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSC--SSALAPATFHKLEKEFNAPVLEAYAMTEASHQM 343
Cdd:PRK07008 257 --KSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVigGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 344 TS-------NNLPPGKR-----KPGTVgqPQGVTVVILDDNDNVLP-PGKV-GEVSIRGENVTLGYANNpkankENFTKR 409
Cdd:PRK07008 335 TLcklkwkhSQLPLDEQrklleKQGRV--IYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG-----DASPLV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMT 489
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 398365585 490 YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETF 533
Cdd:PRK07008 488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
186-526 |
7.72e-36 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 140.50 E-value: 7.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 186 ARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLI-----GVLL--STFRTQGS 258
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVelhlrAVYLgcQQVHVPTE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 259 VVVPDgfhPKLFWDQFVKYNCNwFSCVPTISMIMLN--MPKPNPFP----HIRFIRSCSSALAPAT---FHKLEKEFNAP 329
Cdd:cd05906 244 EILAD---PLRWLDLIDRYRVT-ITWAPNFAFALLNdlLEEIEDGTwdlsSLRYLVNAGEAVVAKTirrLLRLLEPYGLP 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 ---VLEAYAMTEASHQMTSNNLPPGKRKPGT-----VGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPK 400
Cdd:cd05906 320 pdaIRPAFGMTETCSGVIYSRSFPTYDHSQAlefvsLGRPiPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 401 ANKENFTKrENYFRTGDQGYFDpEGFLVLTGRIKELINRGGEKISPIELDGImlshpkIDEA--------VAFGVPDDmy 472
Cdd:cd05906 400 ANAEAFTE-DGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAA------VEEVpgvepsftAAFAVRDP-- 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365585 473 GQVV-QAAIVL--KKGEKMTYEELVNFLKKHLA-SFKIPTKvYFV----DKLPKTATGKIQR 526
Cdd:cd05906 470 GAETeELAIFFvpEYDLQDALSETLRAIRSVVSrEVGVSPA-YLIplpkEEIPKTSLGKIQR 530
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
19-524 |
8.25e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 140.14 E-value: 8.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPETDTQVTYRDLSHMVGHFQTMftnpnspLYGAVFRQ-DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYK 97
Cdd:PRK13390 12 DRPAVIVAETGEQVSYRQLDDDSAALARV-------LYDAGLRTgDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 98 EKEFNFYLNDLKSKAICVPKGTTKLqsseilkSASTFGCFIVELAFDAtrfrvEYDIYspednykrviyrslnnAKFVNT 177
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAALDGL-------AAKVGADLPLRLSFGG-----EIDGF----------------GSFEAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 178 NPVKFPGFARSSDVALILHTSGTTSTPKTV-PLLHLNIVRS----TLNIANT-YKLTPLDRSYVVMPLFH---------V 242
Cdd:PRK13390 137 LAGAGPRLTEQPCGAVMLYSSGTTGFPKGIqPDLPGRDVDApgdpIVAIARAfYDISESDIYYSSAPIYHaaplrwcsmV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 243 HGLigvllstfrtQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLnmpKPNPFPHIRF----IRSCSSALAPAT 318
Cdd:PRK13390 217 HAL----------GGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL---KLDADVRTRYdvssLRAVIHAAAPCP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 319 F---HKLEKEFNAPVLEAYAMTEAsHQMTSNNLPPGKRKPGTVGQPQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGY 395
Cdd:PRK13390 284 VdvkHAMIDWLGPIVYEYYSSTEA-HGMTFIDSPDWLAHPGSVGRSVLGDLHICDDDGNELPAGRIGTVYFERDRLPFRY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 396 ANNPKANKENFTKRENYFRT-GDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQ 474
Cdd:PRK13390 363 LNDPEKTAAAQHPAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGE 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 398365585 475 VVQAAIVLKKGEKMTYE---ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:PRK13390 443 QVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
57-464 |
1.16e-35 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 137.78 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 57 GAVFRQDTVAISMRNGLEFIVAFLGATmdaKIGA---PLNPNYKEKEFNFYLNDLKSKAIcvpkgttkLQSSEILKSAST 133
Cdd:TIGR01733 20 GGVGPGDRVAVLLERSAELVVAILAVL---KAGAayvPLDPAYPAERLAFILEDAGARLL--------LTDSALASRLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 134 FGCFIVELAFDATrfrveydiyspednykrviyrslnnaKFVNTNPVKFPGFARSS--DVALILHTSGTTSTPKTVPLLH 211
Cdd:TIGR01733 89 LVLPVILLDPLEL--------------------------AALDDAPAPPPPDAPSGpdDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 212 LNIVRSTLNIANTYKLTPLDRSYVVMPL---FHVHGLIGVLLSTFRTqgSVVVPDGFHPKL-FWDQFV-KYNCNWFSCVP 286
Cdd:TIGR01733 143 RSLVNLLAWLARRYGLDPDDRVLQFASLsfdASVEEIFGALLAGATL--VVPPEDEERDDAaLLAALIaEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 287 TIsMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEF-NAPVLEAYAMTEASHQMTSNNLPPGK---RKPGTVGQP- 361
Cdd:TIGR01733 221 SL-LALLAAALPPALASLRLVILGGEALTPALVDRWRARGpGARLINLYGPTETTVWSTATLVDPDDaprESPVPIGRPl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 362 QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF-------TKRENYFRTGDQGYFDPEGFLVLTGRIK 434
Cdd:TIGR01733 300 ANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfagGDGARLYRTGDLVRYLPDGNLEFLGRID 379
|
410 420 430
....*....|....*....|....*....|
gi 398365585 435 ELINRGGEKISPIELDGIMLSHPKIDEAVA 464
Cdd:TIGR01733 380 DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
18-531 |
1.22e-35 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 139.39 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 18 SDNVAVIVpeTDTQVTYRDLshmvghfqtmftNPNSPLYGAVFRQ-----DT-VAISMRNGLEFIVAFLGATmdaKIGA- 90
Cdd:cd17655 11 PDHTAVVF--EDQTLTYREL------------NERANQLARTLREkgvgpDTiVGIMAERSLEMIVGILGIL---KAGGa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 91 --PLNPNYKEKEFNFYLNDlkskaicvpKGTTKLQSSEILKSASTFGCFIVELAFDatrfrveyDIYS-PEDNYKRVIyr 167
Cdd:cd17655 74 ylPIDPDYPEERIQYILED---------SGADILLTQSHLQPPIAFIGLIDLLDED--------TIYHeESENLEPVS-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 168 slnnakfvntnpvkfpgfaRSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRsyvvMPLF------- 240
Cdd:cd17655 135 -------------------KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLR----VALFasisfda 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 241 HVHGLIGVLLSTFRTqgsVVVPD----GFHPklFWDQFVKYNCNWFSCVPTIsMIMLNMPKPNPFPHIRFIRSCSSALAP 316
Cdd:cd17655 192 SVTEIFASLLSGNTL---YIVRKetvlDGQA--LTQYIRQNRITIIDLTPAH-LKLLDAADDSEGLSLKHLIVGGEALST 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 317 ATFHKLEKEF--NAPVLEAYAMTEASHQMTSNNLPPGKRKPGTV--GQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENV 391
Cdd:cd17655 266 ELAKKIIELFgtNPTITNAYGPTETTVDASIYQYEPETDQQVSVpiGKPlGNTRIYILDQYGRPQPVGVAGELYIGGEGV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 392 TLGYANNPKANKENFTKR-----ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFG 466
Cdd:cd17655 346 ARGYLNRPELTAEKFVDDpfvpgERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIA 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365585 467 VPDDMYGQVVQAAIVLKKgeKMTYEELVNFLKKHLASFKIPTkvYFV--DKLPKTATGKIQRRVIAE 531
Cdd:cd17655 426 RKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPS--YFIklDEIPLTPNGKVDRKALPE 488
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
188-524 |
1.92e-35 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 140.02 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVplLHLN---IVRSTLNIANTYKLTP-------LDRSYVVMPLFHVHGLIGVLLSTFRTQG 257
Cdd:cd17634 231 AEDPLFILYTSGTTGKPKGV--LHTTggyLVYAATTMKYVFDYGPgdiywctADVGWVTGHSYLLYGPLACGATTLLYEG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 svvVPDGFHPKLFWDQFVKYNCNWFSCVPT-ISMIMLNMPKP---NPFPHIRFIRSCSSALAPATF----HKLEKEfNAP 329
Cdd:cd17634 309 ---VPNWPTPARMWQVVDKHGVNILYTAPTaIRALMAAGDDAiegTDRSSLRILGSVGEPINPEAYewywKKIGKE-KCP 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 VLEAYAMTEASHQMTSN--NLPPGKRKPGTVGQPqGVTVVILDDNDNVLPPGKVGEVSIRGE--NVTLGYANNPKANKEN 405
Cdd:cd17634 385 VVDTWWQTETGGFMITPlpGAIELKAGSATRPVF-GVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQT 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 406 FTKR-ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKK 484
Cdd:cd17634 464 YFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNH 543
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398365585 485 GEKMT---YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:cd17634 544 GVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
63-526 |
2.20e-35 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 139.55 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSkAICVPKGT-----TKLQSSEI--LKsastfg 135
Cdd:PLN02860 58 DVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRP-VMLVTDETcsswyEELQNDRLpsLM------ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 136 cFIVELAFDATRFRVEydiyspednykrviyrsLNNakFVNTNPVKFPGFARSS--------DVALILHTSGTTSTPKTV 207
Cdd:PLN02860 131 -WQVFLESPSSSVFIF-----------------LNS--FLTTEMLKQRALGTTEldyawapdDAVLICFTSGTTGRPKGV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 208 PLLHLN-IVRSTLNIA-------NTYKLTPldrsyvvmPLFHVHGLIGVLLSTFRTQGSVVVPDgFHPKLFWDQFVKYNC 279
Cdd:PLN02860 191 TISHSAlIVQSLAKIAivgygedDVYLHTA--------PLCHIGGLSSALAMLMVGACHVLLPK-FDAKAALQAIKQHNV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 280 NWFSCVPTI--SMIMLNMPKPN--PFPHIRFI----RSCSSALAPATfhklEKEF-NAPVLEAYAMTEASHQMT------ 344
Cdd:PLN02860 262 TSMITVPAMmaDLISLTRKSMTwkVFPSVRKIlnggGSLSSRLLPDA----KKLFpNAKLFSAYGMTEACSSLTfmtlhd 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 -------SNNLPPGKRKPGTVGQPQGVTV----------VILDDNDnvlppgKVGEVSIRGENVTLGYANNPKANKENFT 407
Cdd:PLN02860 338 ptlespkQTLQTVNQTKSSSVHQPQGVCVgkpaphvelkIGLDESS------RVGRILTRGPHVMLGYWGQNSETASVLS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 408 kRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEK 487
Cdd:PLN02860 412 -NDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWI 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 488 MTYEELVNF----------LKKH-----LASFKIPtKVYFV--DKLPKTATGKIQR 526
Cdd:PLN02860 491 WSDNEKENAkknltlssetLRHHcreknLSRFKIP-KLFVQwrKPFPLTTTGKIRR 545
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
29-531 |
1.08e-34 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 135.94 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 29 DTQVTYRDLSHMVGHfqtmftnpnsplYGAVFRQ------DTVAISMRNGLEFIVAFLGAtmdAKIGAP---LNPNYKEK 99
Cdd:cd05940 1 DEALTYAELDAMANR------------YARWLKSlglkpgDVVALFMENRPEYVLLWLGL---VKIGAVaalINYNLRGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 100 EFNFYLNDLKSKAICVpkgttklqsseilksastfgcfivelafdatrfrveydiyspednykrviyrslnnakfvntnp 179
Cdd:cd05940 66 SLAHCLNVSSAKHLVV---------------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 180 vkfpgfarssDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSV 259
Cdd:cd05940 82 ----------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 260 VVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMP-KPNPFPH-IRFIrsCSSALAPATFHKLEKEFNAP-VLEAYAM 336
Cdd:cd05940 152 VIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPpKPTERKHkVRMI--FGNGLRPDIWEEFKERFGVPrIAEFYAA 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 337 TEASHQMTsnNLPpgkRKPGTVG-------QPQGVTVVILD-DNDNVL----------PPGKVGE-VS--IRGENVTlGY 395
Cdd:cd05940 230 TEGNSGFI--NFF---GKPGAIGrnpsllrKVAPLALVKYDlESGEPIrdaegrcikvPRGEPGLlISriNPLEPFD-GY 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 396 ANNPKANK----ENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVP-DD 470
Cdd:cd05940 304 TDPAATEKkilrDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPG 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365585 471 MYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd05940 384 TDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
30-527 |
1.79e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 136.93 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 30 TQVTYRDLSHMVGHFQTMFTNPNSPLYGavfrqDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLK 109
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLGELQLKKG-----DRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 110 SKAICVPK--GTTKLQ--SSEILKSASTFGCFIVeLAFDA---TRFRVEY-DIYSPEDNYKRVI-YRSLNNAKFVNTNPv 180
Cdd:PRK08751 124 ASVLVVIDnfGTTVQQviADTPVKQVITTGLGDM-LGFPKaalVNFVVKYvKKLVPEYRINGAIrFREALALGRKHSMP- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 181 kfPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLN----IANTYKLTPLDRSYVV-MPLFHVHGLIGVLLSTFRT 255
Cdd:PRK08751 202 --TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQahqwLAGTGKLEEGCEVVITaLPLYHIFALTANGLVFMKI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 256 QG-SVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFNAPVLE 332
Cdd:PRK08751 280 GGcNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQidFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 333 AYAMTEASHQMTSNNLPPgKRKPGTVGQPQGVT-VVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrEN 411
Cdd:PRK08751 360 AYGLTETSPAACINPLTL-KEYNGSIGLPIPSTdACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDA-DG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 412 YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVlKKGEKMTYE 491
Cdd:PRK08751 438 WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV-KKDPALTAE 516
|
490 500 510
....*....|....*....|....*....|....*.
gi 398365585 492 ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK08751 517 DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRR 552
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
196-536 |
3.04e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 136.23 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 196 HTSGTTSTPKTVPLLH----LNIVRSTLnianTYKLTPLDRSYVVMPLFHVHGL-----------IGVLLSTFRtqgsvv 260
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHrgayLNALSNIL----AWGMPKHPVYLWTLPMFHCNGWcfpwtvaaragTNVCLRKVD------ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 261 vpdgfhPKLFWDQFVKYNCNWFSCVPTISMIMLNMP---KPNPFPHIRFIrSCSSALAPATFHKLEKE-FNapVLEAYAM 336
Cdd:PRK08162 259 ------PKLIFDLIREHGVTHYCGAPIVLSALINAPaewRAGIDHPVHAM-VAGAAPPAAVIAKMEEIgFD--LTHVYGL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 337 TE--------ASHQmTSNNLPPGKRkpGTVGQPQGVTVVILDDNdNVLPP---------GK-VGEVSIRGENVTLGYANN 398
Cdd:PRK08162 330 TEtygpatvcAWQP-EWDALPLDER--AQLKARQGVRYPLQEGV-TVLDPdtmqpvpadGEtIGEIMFRGNIVMKGYLKN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 399 PKANKENFtkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQA 478
Cdd:PRK08162 406 PKATEEAF--AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCA 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 479 AIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFvDKLPKTATGKIQRRVIAETfAKS 536
Cdd:PRK08162 484 FVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ-AKS 539
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
183-531 |
6.19e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 135.19 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 183 PGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVP 262
Cdd:PRK07867 146 FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 263 DGFHPKLFWDQFVKYNCNWFSCV--PtISMIMLNMPKP----NPFpHIRFirscSSALAPATFHKLEKEFNAPVLEAYAM 336
Cdd:PRK07867 226 RKFSASGFLPDVRRYGATYANYVgkP-LSYVLATPERPddadNPL-RIVY----GNEGAPGDIARFARRFGCVVVDGFGS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 337 TEASHQMTSNNLPPgkrkPGTVGQ-PQGVTVV-----------ILDDNDNVLPPGKVGE-VSIRGENVTLGYANNPKANK 403
Cdd:PRK07867 300 TEGGVAITRTPDTP----PGALGPlPPGVAIVdpdtgtecppaEDADGRLLNADEAIGElVNTAGPGGFEGYYNDPEADA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 404 ENFtkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKI--SPIEldGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIV 481
Cdd:PRK07867 376 ERM--RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLgtAPIE--RILLRYPDATEVAVYAVPDPVVGDQVMAALV 451
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 398365585 482 LKKGEKMTYEELVNFL--KKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK07867 452 LAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
196-529 |
7.68e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 135.36 E-value: 7.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 196 HTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLtPLDRSYV-VMPLFHVHGL-----IGVLLSTFRTQGSVVVpdgfhpKL 269
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGM-NEGAVYLwTLPMFHCNGWcftwtLAALCGTNICLRQVTA------KA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 270 FWDQFVKYNCNWFSCVPTISMIMLNMPKPN---PFPHIRFIRSCSSALAPATFHKL-EKEFNapVLEAYAMTEASHQMTS 345
Cdd:PLN02479 275 IYSAIANYGVTHFCAAPVVLNTIVNAPKSEtilPLPRVVHVMTAGAAPPPSVLFAMsEKGFR--VTHTYGLSETYGPSTV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 346 -------NNLPPGKRkpGTVGQPQGVTVVILDDNDNVLPP--------GK-VGEVSIRGENVTLGYANNPKANKENFTKr 409
Cdd:PLN02479 353 cawkpewDSLPPEEQ--ARLNARQGVRYIGLEGLDVVDTKtmkpvpadGKtMGEIVMRGNMVMKGYLKNPKANEEAFAN- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 eNYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKG---- 485
Cdd:PLN02479 430 -GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGvdks 508
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398365585 486 -EKMTYEELVNFLKKHLASFKIPTKVYFvDKLPKTATGKIQRRVI 529
Cdd:PLN02479 509 dEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVL 552
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
188-531 |
6.06e-33 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 133.07 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKtvpllhlNIVRST----LNIANTYKLT----PLDR-------------SYVVM-PLfhVHGL 245
Cdd:cd05966 230 SEDPLFILYTSGSTGKPK-------GVVHTTggylLYAATTFKYVfdyhPDDIywctadigwitghSYIVYgPL--ANGA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 246 IGVLLstfrtQGsvvVPDGFHPKLFWDQFVKYNCNWFSCVPT-ISMIM---LNMPKPNPFPHIRFIRSCSSALAPAT--- 318
Cdd:cd05966 301 TTVMF-----EG---TPTYPDPGRYWDIVEKHKVTIFYTAPTaIRALMkfgDEWVKKHDLSSLRVLGSVGEPINPEAwmw 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 319 FHKLEKEFNAPVLEAYAMTEASHQMTSNnLPPGKR-KPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIR----GENVT 392
Cdd:cd05966 373 YYEVIGKERCPIVDTWWQTETGGIMITP-LPGATPlKPGSATRPfFGIEPAILDEEGNEVEGEVEGYLVIKrpwpGMART 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 393 LgYANNPKANKENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMY 472
Cdd:cd05966 452 I-YGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 473 GQVVQAAIVLKKGEKMT---YEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRV---IAE 531
Cdd:cd05966 531 GEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIlrkIAA 595
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
190-527 |
1.38e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 129.89 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGS-VVVPDG--FH 266
Cdd:cd17650 94 DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTlVICPDEvkLD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 267 PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEFNAP--VLEAYAMTEAS-- 340
Cdd:cd17650 174 PAALYDLILKSRITLMESTPALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQDFKTLAARFGQGmrIINSYGVTEATid 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 341 ---HQMTSNNLPPGKRKPgtVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR-----EN 411
Cdd:cd17650 254 styYEEGRDPLGDSANVP--IGRPlPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENpfapgER 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 412 YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAfGVPDDMYGQVVQAAIVLKKgEKMTYE 491
Cdd:cd17650 332 MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV-AVREDKGGEARLCAYVVAA-ATLNTA 409
|
330 340 350
....*....|....*....|....*....|....*.
gi 398365585 492 ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
187-529 |
2.78e-32 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 130.03 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIA-NTYK-LTPLDR--SYvvMPLFHVHGLIGVLL------------ 250
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGdRVPElLGPDDRylAY--LPLAHIFELAAENVclyrggtigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 251 -------STFRTQGSVVVpdgFHPKLF------WDQFVKYNCNWFSCVPTIS-----------MIMLNMPKPNPF----- 301
Cdd:cd17639 164 prtltdkSKRGCKGDLTE---FKPTLMvgvpaiWDTIRKGVLAKLNPMGGLKrtlfwtayqskLKALKEGPGTPLldelv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 302 ---------PHIRFIRSCSSALAPATfHKLEKEFNAPVLEAYAMTEASHQMTSNNlpPGKRKPGTVGQPQG-VTVVILD- 370
Cdd:cd17639 241 fkkvraalgGRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETCAGGTVQD--PGDLETGRVGPPLPcCEIKLVDw 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 371 -----DNDNvlPPGKvGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELI-NRGGEKI 444
Cdd:cd17639 318 eeggySTDK--PPPR-GEILIRGPNVFKGYYKNPEKTKEAFDG-DGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYI 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 445 SPIELDGIMLSHPKIDEAVAFGVPDDMYgqVVqaAIVL------------KKGEKMTYEELVN---FLKK---------- 499
Cdd:cd17639 394 ALEKLESIYRSNPLVNNICVYADPDKSY--PV--AIVVpnekhltklaekHGVINSEWEELCEdkkLQKAvlkslaetar 469
|
410 420 430
....*....|....*....|....*....|....*...
gi 398365585 500 --HLASFKIPTKVYFVDKL--PK----TATGKIQRRVI 529
Cdd:cd17639 470 aaGLEKFEIPQGVVLLDEEwtPEnglvTAAQKLKRKEI 507
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
165-533 |
4.62e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 129.15 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 165 IYRSLNNAKFVNTNPVkfpgFARSSD-VALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVH 243
Cdd:cd05908 85 VWNTLKNPYLITEEEV----LCELADeLAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 244 GLIGVLLS-TFRTQGSVVVPDGF---HPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP-----FPHIRFIRSCSSAL 314
Cdd:cd05908 161 GLIAFHLApLIAGMNQYLMPTRLfirRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKandwdLSSIRMILNGAEPI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 315 APATFHKLEKEFNA------PVLEAYAMTEASHQMTSNNL-----PP---------GKRKPGT------------VGQPQ 362
Cdd:cd05908 241 DYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLPKAqspfkTItlgrrhvthGEPEPEVdkkdsecltfveVGKPI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 363 GVTVV-ILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGyFDPEGFLVLTGRIKELINRGG 441
Cdd:cd05908 321 DETDIrICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTD-DGWLKTGDLG-FIRNGRLVITGREKDIIFVNG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 442 EKISP-------IELDGIMLShpkidEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFK---IpTKVY 511
Cdd:cd05908 399 QNVYPhdieriaEELEGVELG-----RVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGgwqI-NEVL 472
|
410 420
....*....|....*....|..
gi 398365585 512 FVDKLPKTATGKIQRRVIAETF 533
Cdd:cd05908 473 PIRRIPKTTSGKVKRYELAQRY 494
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
190-524 |
4.88e-32 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 131.58 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIG----VLLSTFrtqGSVVVPDGF 265
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVtlwlPLLEGI---KVVYHPDPT 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 HPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNP--FPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEAShQM 343
Cdd:PRK08633 860 DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPlmFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETS-PV 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 344 TSNNLPPGKR---------KPGTVGQP-QGVTVVILD-DNDNVLPPGKVGEVSIRGENVTLGYANNP----KANKENFTK 408
Cdd:PRK08633 939 ASVNLPDVLAadfkrqtgsKEGSVGMPlPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPektaEVIKDIDGI 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 409 RenYFRTGDQGYFDPEGFLVLTGRIKELINRGGEkispieldgiMLSHPKIDEA------------VAFGVPDDMYGQVV 476
Cdd:PRK08633 1019 G--WYVTGDKGHLDEDGFLTITDRYSRFAKIGGE----------MVPLGAVEEElakalggeevvfAVTAVPDEKKGEKL 1086
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 398365585 477 qaaIVLKKGEKMTYEELVNFLKK-HLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:PRK08633 1087 ---VVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-526 |
6.52e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 129.39 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATmdaKIGA---PLNPNYKEKEFNFYLNDLKSKAICV-----P-----KGTTKLQS----- 124
Cdd:PRK06178 84 DRVAVFLPNCPQFHIVFFGIL---KLGAvhvPVSPLFREHELSYELNDAGAEVLLAldqlaPvveqvRAETSLRHvivts 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 125 -SEILKSASTFgcfIVELAFDATRFRVEYDIyspednykrviyrSLNNAKFVNTNPVKFPGFARSsDVALILHTSGTTST 203
Cdd:PRK06178 161 lADVLPAEPTL---PLPDSLRAPRLAAAGAI-------------DLLPALRACTAPVPLPPPALD-ALAALNYTGGTTGM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 204 PKTVPLLHLNIVRSTlniANTYKLT-PLDRSYVV---MPLFHVHGL-IGVLLSTFrtQGSVVV------PDGFhpklfwd 272
Cdd:PRK06178 224 PKGCEHTQRDMVYTA---AAAYAVAvVGGEDSVFlsfLPEFWIAGEnFGLLFPLF--SGATLVllarwdAVAF------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 273 qfvkyncnwFSCVPTISMIMLNMPKPN-------PFPHIRFIRSCSSALAPATFHKLE-------KEFNAPVLE--AYAM 336
Cdd:PRK06178 292 ---------MAAVERYRVTRTVMLVDNavelmdhPRFAEYDLSSLRQVRVVSFVKKLNpdyrqrwRALTGSVLAeaAWGM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 337 TEaSHqmTSNNLPPG--------KRKPGTVGQP-QGVTVVILD-DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF 406
Cdd:PRK06178 363 TE-TH--TCDTFTAGfqdddfdlLSQPVFVGLPvPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 407 tkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGE 486
Cdd:PRK06178 440 --RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA 517
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 398365585 487 KMTYEELVNFLKKHLASFKIPTkVYFVDKLPKTATGKIQR 526
Cdd:PRK06178 518 DLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRK 556
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-531 |
1.82e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 127.94 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 1 MTSAATVTASFNDTFSVSDNVAVIVPETDTQVTYRDLSHMVghfqtmftNPNSPLYGA--VFRQDTVAISMRNGLEFIVA 78
Cdd:PRK06164 5 AAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALV--------DRLAAWLAAqgVRRGDRVAVWLPNCIEWVVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 79 FLGAtmdAKIGAPL---NPNYKEKEFNFYLNDLKSKAICVPKGTTKLQSSEILKSA------STFGCFIVELAFDAT--- 146
Cdd:PRK06164 77 FLAC---ARLGATViavNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVppdalpPLRAIAVVDDAADATpap 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 147 ---RFRVEYDIYSPEdnykrviyrslnnakfvnTNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIAN 223
Cdd:PRK06164 154 apgARVQLFALPDPA------------------PPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIAR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 224 TYKLTPLDRSYVVMPLFHVHGLIGvLLSTFRTQGSVVVPDGFHP----KLFWDQFVKYNcnwFSCVPTISMIMLNMPKPN 299
Cdd:PRK06164 216 AYGYDPGAVLLAALPFCGVFGFST-LLGALAGGAPLVCEPVFDAartaRALRRHRVTHT---FGNDEMLRRILDTAGERA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 300 PFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTE-----ASHQMTsnnLPPGKRKP--GTVGQPQGvTVVILD-D 371
Cdd:PRK06164 292 DFPSARLFGFASFAPALGELAALARARGVPLTGLYGSSEvqalvALQPAT---DPVSVRIEggGRPASPEA-RVRARDpQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 372 NDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDG 451
Cdd:PRK06164 368 DGALLPDGESGEIEIRAPSLMRGYLDNPDATARALT-DDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 452 IMLSHPKIDEAVAFGVPDDMYGQVVqAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATG---KIQRRV 528
Cdd:PRK06164 447 ALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHR 525
|
...
gi 398365585 529 IAE 531
Cdd:PRK06164 526 LRE 528
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
186-527 |
7.82e-31 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 126.20 E-value: 7.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 186 ARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRsyVV--MPLFHVHGLIGVLLSTFRTQGSVVV-- 261
Cdd:cd05931 146 PDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDV--VVswLPLYHDMGLIGGLLTPLYSGGPSVLms 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 262 PDGF--HPkLFWDQFV-KYNcnwfscvPTISmimlnmPKPN-PFPH-IRFIR----------SCSSALA------PATFH 320
Cdd:cd05931 224 PAAFlrRP-LRWLRLIsRYR-------ATIS------AAPNfAYDLcVRRVRdedlegldlsSWRVALNgaepvrPATLR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 321 KLEKEFnAP-------VLEAYAMTEAS-------------------HQMTSNNLPPGKRKPGTV-----GQPQ-GVTVVI 368
Cdd:cd05931 290 RFAEAF-APfgfrpeaFRPSYGLAEATlfvsggppgtgpvvlrvdrDALAGRAVAVAADDPAARelvscGRPLpDQEVRI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 369 LDDNDN-VLPPGKVGEVSIRGENVTLGYANNPKANKENFTKREN-----YFRTGDQGYFDpEGFLVLTGRIKELINRGGE 442
Cdd:cd05931 369 VDPETGrELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAtdeggWLRTGDLGFLH-DGELYITGRLKDLIIVRGR 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 443 KISP--IELDgIMLSHPKIDE--AVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLAS-FKI-PTKVYFV--D 514
Cdd:cd05931 448 NHYPqdIEAT-AEEAHPALRPgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAReHGVaPADVVLVrpG 526
|
410
....*....|...
gi 398365585 515 KLPKTATGKIQRR 527
Cdd:cd05931 527 SIPRTSSGKIQRR 539
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
19-527 |
1.78e-30 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 124.12 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIvpETDTQVTYRDL---SHMVGHFQTMFtnpnsplygAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPN 95
Cdd:cd17656 3 DAVAVV--FENQKLTYRELnerSNQLARFLREK---------GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 96 YKEKEFNFYLNDlkskaicvpKGTTKLQSSEILKSAstfgcfiveLAFDATRFRVEYDIYSPEDNykrviyrslNNAKFV 175
Cdd:cd17656 72 YPEERRIYIMLD---------SGVRVVLTQRHLKSK---------LSFNKSTILLEDPSISQEDT---------SNIDYI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 176 NTNpvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRStlnIANTYKLTPLDRSYVVM----PLFHV--HGLIGVL 249
Cdd:cd17656 125 NNS----------DDLLYIIYTSGTTGKPKGVQLEHKNMVNL---LHFEREKTNINFSDKVLqfatCSFDVcyQEIFSTL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 250 LSTfrtqGSV-VVPDGFH---PKLFwdQFVKYNCNWFSCVPT--ISMIMLNMPKPNPFP----HIrfIRSCSSALAPATF 319
Cdd:cd17656 192 LSG----GTLyIIREETKrdvEQLF--DLVKRHNIEVVFLPVafLKFIFSEREFINRFPtcvkHI--ITAGEQLVITNEF 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 320 HKLEKEFNAPVLEAYAMTEAsHQMTSNNLPPGKRKP--GTVGQPQGVT-VVILDDNDNVLPPGKVGEVSIRGENVTLGYA 396
Cdd:cd17656 264 KEMLHEHNVHLHNHYGPSET-HVVTTYTINPEAEIPelPPIGKPISNTwIYILDQEQQLQPQGIVGELYISGASVARGYL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 397 NNPKANKENFTKR-----ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDM 471
Cdd:cd17656 343 NRQELTAEKFFPDpfdpnERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDK 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 472 YGQVVQAAIVLKkgEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17656 423 GEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
61-529 |
4.31e-30 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 124.52 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 61 RQDTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPNYKEKEFNFYLNDLKSKAICVPKGTTK----LQSSEILKSAST 133
Cdd:cd05968 115 KGDRVGIYLPMIPEIVPAFLAV---ARIGGivvPIFSGFGKEAAATRLQDAEAKALITADGFTRrgreVNLKEEADKACA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 134 fGCFIVE---------LAFDATRFRveyDIYSPEdnykrviyrslnnakFVNTnpvKFPGFAR--SSDVALILHTSGTTS 202
Cdd:cd05968 192 -QCPTVEkvvvvrhlgNDFTPAKGR---DLSYDE---------------EKET---AGDGAERteSEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 203 TPKTVPLLHLNI-VRSTLNIANTYKLTPLDRSYVVMPLFHVHG---LIGVLLstfrTQGSVVVPDGF--HPKL--FWDQF 274
Cdd:cd05968 250 KPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGpwlIFGGLI----LGATMVLYDGApdHPKAdrLWRMV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 275 VKYNCNWFSCVPTisMIMLNMPKPNPFPH------IRFIRSCSSALAPAT----FHKLEKEfNAPVLEAYAMTEASHQMT 344
Cdd:cd05968 326 EDHEITHLGLSPT--LIRALKPRGDAPVNahdlssLRVLGSTGEPWNPEPwnwlFETVGKG-RNPIINYSGGTEISGGIL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNNLPPGKRKPGTVGQPQGVTVVILDDNDNVLPPgKVGEVSIRGE--NVTLGYANNPKANKENFTKR-ENYFRTGDQGYF 421
Cdd:cd05968 403 GNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPwpGMTRGFWRDEDRYLETYWSRfDNVWVHGDFAYY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 422 DPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMT---YEELVNFLK 498
Cdd:cd05968 482 DEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVA 561
|
490 500 510
....*....|....*....|....*....|.
gi 398365585 499 KHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:cd05968 562 DELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
19-527 |
1.93e-29 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 121.30 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPETdtQVTYRDLSHM---VGHFqtmftnpnspLYG-AVFRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---P 91
Cdd:cd17651 10 DAPALVAEGR--RLTYAELDRRanrLAHR----------LRArGVGPGDLVALCARRSAELVVALLAI---LKAGAayvP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 92 LNPNYKEKEFNFYLNDlkSKAICVpkgttklqsseilksastfgcfiveLAFDATRFRVEYDIYSPEDNYKRVIYRSLNN 171
Cdd:cd17651 75 LDPAYPAERLAFMLAD--AGPVLV-------------------------LTHPALAGELAVELVAVTLLDQPGAAAGADA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 172 AKFVNTNPvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPL---FHVHGLigv 248
Cdd:cd17651 128 EPDPALDA---------DDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLgfdVSVQEI--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 249 lLSTFRTQGSVVVPD---GFHPKLFWDQFVKYNcnwfscvptISMIMLnmpkPNPF---------PHIRF---IRSCSSA 313
Cdd:cd17651 196 -FSTLCAGATLVLPPeevRTDPPALAAWLDEQR---------ISRVFL----PTVAlralaehgrPLGVRlaaLRYLLTG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 314 LAPATFHKLEKEFNA--P---VLEAYAMTEAsHQMTSNNL---PPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEV 384
Cdd:cd17651 262 GEQLVLTEDLREFCAglPglrLHNHYGPTET-HVVTALSLpgdPAAWPAPPPIGRPiDNTRVYVLDAALRPVPPGVPGEL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 385 SIRGENVTLGYANNPKANKENF-----TKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKI 459
Cdd:cd17651 341 YIGGAGLARGYLNRPELTAERFvpdpfVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 460 DEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17651 421 REAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
187-466 |
8.26e-29 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 119.39 E-value: 8.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLigvLLSTFR-TQGSVVVPDGf 265
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYER---SAEYFIfACGCSQAYTS- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 hPKLFWDQFVKYNCNWFSCVPTI-----SMIMLNMPKPNPFPH-----------IRFIRSCSSALAPatfhKLEKEFNA- 328
Cdd:cd17640 162 -IRTLKDDLKRVKPHYIVSVPRLweslySGIQKQVSKSSPIKQflflfflsggiFKFGISGGGALPP----HVDTFFEAi 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 329 --PVLEAYAMTEASHQMTSNNLPPGKRkpGTVGQP-QGVTVVILD-DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKE 404
Cdd:cd17640 237 giEVLNGYGLTETSPVVSARRLKCNVR--GSVGRPlPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365585 405 NFTKrENYFRTGDQGYFDPEGFLVLTGRIKELIN-RGGEKISPIELDGIMLSHPKIDEAVAFG 466
Cdd:cd17640 315 VLDS-DGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
187-526 |
8.61e-29 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 118.82 E-value: 8.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVplLHLNIVRSTLNIANTY--KLTPLDRSY-VVMPLFHVHGLiGVLLSTFRTQGSVVVPD 263
Cdd:cd05974 83 HADDPMLLYFTSGTTSKPKLV--EHTHRSYPVGHLSTMYwiGLKPGDVHWnISSPGWAKHAW-SCFFAPWNAGATVFLFN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 264 --GFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASH 341
Cdd:cd05974 160 yaRFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 342 QMtsNNLPPGKRKPGTVGQP-QGVTVVILDDNDNvlpPGKVGEVSI-----RGENVTLGYANNPKANKEnfTKRENYFRT 415
Cdd:cd05974 240 LV--GNSPGQPVKAGSMGRPlPGYRVALLDPDGA---PATEGEVALdlgdtRPVGLMKGYAGDPDKTAH--AMRGGYYRT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 416 GDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYE---E 492
Cdd:cd05974 313 GDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalE 392
|
330 340 350
....*....|....*....|....*....|....
gi 398365585 493 LVNFLKKHLASFKIPTKVYFVDkLPKTATGKIQR 526
Cdd:cd05974 393 IFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRR 425
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
187-527 |
1.95e-28 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 117.79 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDrsyvVMPLFH-------VHGLIGVLLSTFRTqgsV 259
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD----VWTLFHsyafdfsVWEIWGALLHGGRL---V 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 260 VVPDGFH--PKLFWDQFVKYNCNWFSCVPTI---SMIMLNMPKPNPfPHIRFIRSCSSALAPATFHKLEKEFNAP---VL 331
Cdd:cd17643 164 VVPYEVArsPEDFARLLRDEGVTVLNQTPSAfyqLVEAADRDGRDP-LALRYVIFGGEALEAAMLRPWAGRFGLDrpqLV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 332 EAYAMTEAS-----HQMTSNNLPPGKRKPgtVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKEN 405
Cdd:cd17643 243 NMYGITETTvhvtfRPLDAADLPAAAASP--IGRPlPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAER 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 406 F--------TKRenYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQ 477
Cdd:cd17643 321 FvanpfggpGSR--MYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLV 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398365585 478 AAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17643 399 AYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
169-531 |
2.16e-28 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 117.92 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 169 LNNAKFVntnpvkfpgFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGV 248
Cdd:cd05937 76 LSGSRFV---------IVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 249 LLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPK-PNPFPHiRFIRSCSSALAPATFHKLEKEFN 327
Cdd:cd05937 147 ACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPsPYDRDH-KVRVAWGNGLRPDIWERFRERFN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 328 APVL-EAYAMTEASHQMTSNNLPP---GK-RKPGTVGQ---PQGVTVVILDDNDN------------VLPPGKVGE--VS 385
Cdd:cd05937 226 VPEIgEFYAATEGVFALTNHNVGDfgaGAiGHHGLIRRwkfENQVVLVKMDPETDdpirdpktgfcvRAPVGEPGEmlGR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 386 IRGENVTL--GYANNPKANKEN-----FTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPK 458
Cdd:cd05937 306 VPFKNREAfqGYLHNEDATESKlvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPD 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 459 IDEAVAFGVPDDMY-GQVVQAAIVLKKGEK----MTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:cd05937 386 IAEANVYGVKVPGHdGRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
61-529 |
2.18e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 118.69 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 61 RQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICVpkgttklqSSEILKSASTFGCFIVE 140
Cdd:cd05915 48 VGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF--------DPNLLPLVEAIRGELKT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 141 LAFDATRfRVEYDIYspEDnykrviYRSLNNAKFVNTNPVKfpgfarSSDVALILHTSGTTSTPKTVPLLHLN--IVRST 218
Cdd:cd05915 120 VQHFVVM-DEKAPEG--YL------AYEEALGEEADPVRVP------ERAACGMAYTTGTTGLPKGVVYSHRAlvLHSLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 219 LNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKP 298
Cdd:cd05915 185 ASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLES 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 299 --NPFPHIRFIRSCSSAlAPATFHKLEKEFNAPVLEAYAMTEASHQMTS-------NNLPPG-----KRKPGTVGQPQGV 364
Cdd:cd05915 265 tgHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETSPVVVQnfvkshlESLSEEekltlKAKTGLPIPLVRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 365 TVviLDDNDNVLP-PGK-VGEVSIRGENVTLGYANNPKANkENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGE 442
Cdd:cd05915 344 RV--ADEEGRPVPkDGKaLGEVQLKGPWITGGYYGNEEAT-RSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 443 KISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTyEELVNFLKKHLASFK-IPTKVYFVDKLPKTAT 521
Cdd:cd05915 421 WISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTP-EELNEHLLKAGFAKWqLPDAYVFAEEIPRTSA 499
|
....*...
gi 398365585 522 GKIQRRVI 529
Cdd:cd05915 500 GKFLKRAL 507
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
183-536 |
1.01e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 114.37 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 183 PGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTlnIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVV-- 260
Cdd:PRK07824 29 VGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASA--DATHDRLGGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVEld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 261 VPDGFHPKLFWD--QFVKYNCNWFSCVPTISMIMLNMPKPnpfphIRFIRSCSSAL-----APATFHKLEKEFNAPVLEA 333
Cdd:PRK07824 107 VSAGFDPTALPRavAELGGGRRYTSLVPMQLAKALDDPAA-----TAALAELDAVLvgggpAPAPVLDAAAAAGINVVRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 334 YAMTEASHqmtsnnlppgkrkpGTV--GQP-QGVTVVILDdndnvlppgkvGEVSIRGENVTLGYANNPKankENFTKRE 410
Cdd:PRK07824 182 YGMSETSG--------------GCVydGVPlDGVRVRVED-----------GRIALGGPTLAKGYRNPVD---PDPFAEP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 411 NYFRTGDQGYFDpEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTY 490
Cdd:PRK07824 234 GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKS 536
Cdd:PRK07824 313 EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
233-533 |
2.47e-27 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 114.71 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 233 SYVVMPLFHVHGLIGVLLStFRTQGSVVVPDgFHpKLFWDQFVKYNC-NWF-SCVPTISMIMLNmpkpnpfPHIRFIRSC 310
Cdd:PRK07445 163 SFCVLPLYHVSGLMQFMRS-FLTGGKLVILP-YK-RLKSGQELPPNPsDFFlSLVPTQLQRLLQ-------LRPQWLAQF 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 311 SSAL---APATFHKLEK--EFNAPVLEAYAMTEASHQMTSnnLPP-----GKRkpgTVGQP-QGVTVVIlddndnvlPPG 379
Cdd:PRK07445 233 RTILlggAPAWPSLLEQarQLQLRLAPTYGMTETASQIAT--LKPddflaGNN---SSGQVlPHAQITI--------PAN 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 380 KVGEVSIRGENVTLGYANNPKANKEnftkrenYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKI 459
Cdd:PRK07445 300 QTGNITIQAQSLALGYYPQILDSQG-------IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLV 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365585 460 DEAVAFGVPDDMYGQVVQAAIVLKKGEkMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQR---RVIAETF 533
Cdd:PRK07445 373 QDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRqqlQQIAVQR 448
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
187-527 |
3.01e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 114.34 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHlnivRSTLNIANTYKLTpldrsyvvmplFHVHGLIGVL--------LSTFR---- 254
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEH----RNAAAFLQWAAAA-----------FSAEELAGVLastsicfdLSVFElfgp 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 255 --TQGSVVVPDGF-----HPKLfwDQFVKYNCnwfscVPTISMIMLNMpkpNPFP-HIRFIRSCSSALAPATFHKLEKEF 326
Cdd:cd12115 168 laTGGKVVLADNVlalpdLPAA--AEVTLINT-----VPSAAAELLRH---DALPaSVRVVNLAGEPLPRDLVQRLYARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 327 NAP-VLEAYAMTEASHQMTSNNLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKE 404
Cdd:cd12115 238 QVErVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPlANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 405 NFtkRENYF-------RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQ 477
Cdd:cd12115 318 RF--LPDPFgpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLV 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398365585 478 AAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd12115 396 AYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRS 445
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
192-527 |
4.02e-27 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 114.00 E-value: 4.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 192 ALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPlFHVHGLIGVLLSTFRTQGSVVVPDG---FHPK 268
Cdd:cd17649 97 AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPDelwASAD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 269 LFWDQFVKYNCNWFSCVPT-ISMIMLNM--PKPNPFPHIRFIRSCSSALapaTFHKLEKEFNAPV--LEAYAMTEASHQM 343
Cdd:cd17649 176 ELAEMVRELGVTVLDLPPAyLQQLAEEAdrTGDGRPPSLRLYIFGGEAL---SPELLRRWLKAPVrlFNAYGPTEATVTP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 344 TSNNLPPGKRKPGT---VGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR------ENYF 413
Cdd:cd17649 253 LVWKCEAGAARAGAsmpIGRPlGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgapgSRLY 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 414 RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVqAAIVLKKGekMTYEEL 493
Cdd:cd17649 333 RTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAA--AAQPEL 409
|
330 340 350
....*....|....*....|....*....|....*...
gi 398365585 494 VNFLKKHLA----SFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17649 410 RAQLRTALRaslpDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
19-527 |
4.08e-27 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 114.68 E-value: 4.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIvpETDTQVTYRDLSHMVGHFQTMFTNpnsplYGaVFRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPN 95
Cdd:cd17646 13 DAPAVV--DEGRTLTYRELDERANRLAHLLRA-----RG-VGPEDRVAVLLPRSADLVVALLAV---LKAGAaylPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 96 YKEKEFNFYLNDlkSKAICVpkgttklqsseiLKSASTFGCFIVELAfDATRFRVEYDIYSPEDnykrviyrslnnakfv 175
Cdd:cd17646 82 YPADRLAYMLAD--AGPAVV------------LTTADLAARLPAGGD-VALLGDEALAAPPATP---------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 176 ntnpvkfPG-FARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPL-FHVHglIGVLLSTF 253
Cdd:cd17646 131 -------PLvPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLsFDVS--VWELFWPL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 254 RTQGSVVV--PDGfH------PKLFWDQFVkyNCNWFscVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKE 325
Cdd:cd17646 202 VAGARLVVarPGG-HrdpaylAALIREHGV--TTCHF--VPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLAL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 326 FNAPVLEAYAMTEASHQMTSNNLPPGKRKPGT-VGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANK 403
Cdd:cd17646 277 PGAELHNLYGPTEAAIDVTHWPVRGPAETPSVpIGRPvPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 404 ENFTKR-----ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQA 478
Cdd:cd17646 357 ERFVPDpfgpgSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVG 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 398365585 479 AIVLKKGEK-MTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17646 437 YVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
19-527 |
4.22e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 114.29 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIvpETDTQVTYRDLSHMVGHfqtmftnpnspLYGA-----VFRQDTVAISMRNGLEFIVAFLGAtmdakigapln 93
Cdd:cd12114 2 DATAVI--CGDGTLTYGELAERARR-----------VAGAlkaagVRPGDLVAVTLPKGPEQVVAVLGI----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 94 pnykekefnfylndLKSKAICVPKGTT--KLQSSEILKSASTfGCFIVELAFDATRFRVEydiyspednykRVIYRSLNN 171
Cdd:cd12114 58 --------------LAAGAAYVPVDIDqpAARREAILADAGA-RLVLTDGPDAQLDVAVF-----------DVLILDLDA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 172 AKFVNTNPvkfPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFH---VHGLIGV 248
Cdd:cd12114 112 LAAPAPPP---PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIFGA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 249 LlstfRTQGSVVVPDGFHPK--LFWDQFV-KYNCNWFSCVPTISMIMLNMPKPNPfphirfIRSCSSALA---------- 315
Cdd:cd12114 189 L----SAGATLVLPDEARRRdpAHWAELIeRHGVTLWNSVPALLEMLLDVLEAAQ------ALLPSLRLVllsgdwipld 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 316 -PATFHKLekefnAPVLEAYAM---TEAShqMTSNNLPPGKRKPGTVGQPQGV-----TVVILDDNDNVLPPGKVGEVSI 386
Cdd:cd12114 259 lPARLRAL-----APDARLISLggaTEAS--IWSIYHPIDEVPPDWRSIPYGRplanqRYRVLDPRGRDCPDWVPGELWI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 387 RGENVTLGYANNPKANKENF---TKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAV 463
Cdd:cd12114 332 GGRGVALGYLGDPELTAARFvthPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAV 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 464 AFGVPDDmYGQVVQAAIVLK-KGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd12114 412 VVVLGDP-GGKRLAAFVVPDnDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
19-528 |
8.55e-27 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 114.59 E-value: 8.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIvpETDTQVTYRDLSHMVghfqtmftnpNSplYGAVFRQ------DTVAISMRNGLEFIVAFLGAtmdAKIG--- 89
Cdd:PRK08279 52 DRPALL--FEDQSISYAELNARA----------NR--YAHWAAArgvgkgDVVALLMENRPEYLAAWLGL---AKLGavv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 90 APLNPNYKEKEFNFYLNDLKSKAICVpkgttklqSSEILKSastfgcfIVELAFDATRFRVEYdIYSPEDNYKRVIYRSL 169
Cdd:PRK08279 115 ALLNTQQRGAVLAHSLNLVDAKHLIV--------GEELVEA-------FEEARADLARPPRLW-VAGGDTLDDPEGYEDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 170 NNA--KFVNTNPVkfpgfARSS----DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVH 243
Cdd:PRK08279 179 AAAaaGAPTTNPA-----SRSGvtakDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 244 GLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMP-KPNPFPH-IRFIrsCSSALAPATFHK 321
Cdd:PRK08279 254 GGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPpKPTDRDHrLRLM--IGNGLRPDIWDE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 322 LEKEFNAP-VLEAYAMTEASHQM--------TSNNLPPGKRKPGTV-------GQPqgvtvvILDDNDNVLP--PGKVGE 383
Cdd:PRK08279 332 FQQRFGIPrILEFYAASEGNVGFinvfnfdgTVGRVPLWLAHPYAIvkydvdtGEP------VRDADGRCIKvkPGEVGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 384 ----VSIRG--EnvtlGYaNNPKANKEN-----FTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGI 452
Cdd:PRK08279 406 ligrITDRGpfD----GY-TDPEASEKKilrdvFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENA 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365585 453 MLSHPKIDEAVAFGVP-DDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKiQRRV 528
Cdd:PRK08279 481 LSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFK-YRKV 556
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
186-527 |
3.23e-26 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 111.34 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 186 ARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPlDRSYVVMPL------FHVHGLIGVLLSTfrtQGSV 259
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRD-NGDEAVLFFsnyvfdFFVEQMTLALLNG---QKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 260 VVPDG--FHPKLFWDQFVKYNCNWFSCVPT-ISMIMLNMpkpnpFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAM 336
Cdd:cd17648 167 VPPDEmrFDPDRFYAYINREKVTYLSGTPSvLQQYDLAR-----LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 337 TEASHQMTSNNLPPGKRKPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF------TKR 409
Cdd:cd17648 242 TETTVTNHKRFFPGDQRFDKSLGRPvRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqTEQ 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 E-------NYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEA--VAFGVPDDMYGqVVQAAI 480
Cdd:cd17648 322 ErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECavVAKEDASQAQS-RIQKYL 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398365585 481 V---LKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17648 401 VgyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVR 450
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
63-533 |
6.53e-26 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 111.02 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICVpkgtTKLQSSEILKSASTFGCFIVELA 142
Cdd:cd05932 32 SKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV----GKLDDWKAMAPGVPEGLISISLP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 143 -FDATRFRVEYDiyspednykrviyRSLNNAKFVNTNPVKFPgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNI 221
Cdd:cd05932 108 pPSAANCQYQWD-------------DLIAQHPPLEERPTRFP-----EQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 222 ANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVP---DGF-------HPKLF------WdqfVKYNCNWFSCV 285
Cdd:cd05932 170 IEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAeslDTFvedvqraRPTLFfsvprlW---TKFQQGVQDKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 286 PTISM-IMLNMPKPNP-----------FPHIRFIRSCSSALAPATFHKLEKeFNAPVLEAYAMTEASHQMTSNNlpPGKR 353
Cdd:cd05932 247 PQQKLnLLLKIPVVNSlvkrkvlkglgLDQCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNY--PGRD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 354 KPGTVGQP-QGVTVVILDDndnvlppgkvGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGR 432
Cdd:cd05932 324 KIGTVGNAgPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTA-DGFLRTGDKGELDADGNLTITGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 433 IKELINRG-GEKISPIELDGIMLSHPKIDEAVAFG--VPDDMyGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFK---- 505
Cdd:cd05932 393 VKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGsgLPAPL-ALVVLSEEARLRADAFARAELEASLRAHLARVNstld 471
|
490 500 510
....*....|....*....|....*....|....*..
gi 398365585 506 ---------IPTKVYFVDKLPKTATGKIQRRVIAETF 533
Cdd:cd05932 472 sheqlagivVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
366-527 |
9.01e-26 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 110.85 E-value: 9.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 366 VVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKIS 445
Cdd:PRK10946 365 VWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 446 PIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTyeELVNFLKKH-LASFKIPTKVYFVDKLPKTATGKI 524
Cdd:PRK10946 444 AEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAV--QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKV 521
|
...
gi 398365585 525 QRR 527
Cdd:PRK10946 522 DKK 524
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
19-527 |
1.41e-25 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 111.87 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 19 DNVAVIVPetDTQVTYRDLSHMV----GHFQTMftnpnsplyGAVfRQDTVAISMRNGLEFIVAFLGAtmdAKIGA---P 91
Cdd:COG1020 491 DAVAVVFG--DQSLTYAELNARAnrlaHHLRAL---------GVG-PGDLVGVCLERSLEMVVALLAV---LKAGAayvP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 92 LNPNYKEKEFNFYLNDlkSKAICVpkgttkLQSSEILKSASTFGCFIVELafDATRFRVEydiysPEdnykrviyrslnn 171
Cdd:COG1020 556 LDPAYPAERLAYMLED--AGARLV------LTQSALAARLPELGVPVLAL--DALALAAE-----PA------------- 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 172 akfvnTNPvkfPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPL---FHVHGLIGV 248
Cdd:COG1020 608 -----TNP---PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLsfdASVWEIFGA 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 249 LLStfrtqGS--VVVPDGFH--PKLFWDQFVKYNCNWFSCVPTismiMLNM---PKPNPFPHIRFIRSCSSALAPATFHK 321
Cdd:COG1020 680 LLS-----GAtlVLAPPEARrdPAALAELLARHRVTVLNLTPS----LLRAlldAAPEALPSLRLVLVGGEALPPELVRR 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 322 LEKEF-NAPVLEAYAMTEAS-----HQMTSNNLPPGkrkPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLG 394
Cdd:COG1020 751 WRARLpGARLVNLYGPTETTvdstyYEVTPPDADGG---SVPIGRPiANTRVYVLDAHLQPVPVGVPGELYIGGAGLARG 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 395 YANNPKANKENFtkRENYF--------RTGDQGYFDPEGFLVLTGRIKELInrggeKIS--PIELDGI---MLSHPKIDE 461
Cdd:COG1020 828 YLNRPELTAERF--VADPFgfpgarlyRTGDLARWLPDGNLEFLGRADDQV-----KIRgfRIELGEIeaaLLQHPGVRE 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 462 AVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:COG1020 901 AVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
65-527 |
1.89e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.59 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 65 VAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDlkskaicvpKGTTKLQSSEILKSASTFGCFIVELAFD 144
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLED---------SGAQLLLSQSHLRLPLAQGVQVLDLDRG 3180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 145 AtrfrveyDIYSPEDNYKRVIYRSLnnakfvntnpvkfpgfarssdvALILHTSGTTSTPKTVPLLHLNIVRSTLNIANT 224
Cdd:PRK12316 3181 D-------ENYAEANPAIRTMPENL----------------------AYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA 3231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 225 YKLTPLDRSYVVMPlFHVHGLIGVLLSTFRTQGSVVVPD---GFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPF 301
Cdd:PRK12316 3232 YGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLAGpedWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRC 3310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 302 PHIRFIRSCSSALAPATFHKLEKEfnAPVLEAYAMTEASHQMTSNNLPPGKRKPGTVGQPQGVTVV-ILDDNDNVLPPGK 380
Cdd:PRK12316 3311 TSLKRIVCGGEALPADLQQQVFAG--LPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACyILDGSLEPVPVGA 3388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 381 VGEVSIRGENVTLGYANNPKANKENFTKR-----ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLS 455
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDpfvpgERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLE 3468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365585 456 HPKIDEAVAFGVPddmyGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK12316 3469 HPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRK 3536
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
190-531 |
3.19e-25 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 108.83 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKL---------TPL--DRSyvVMPLFHVHGLIGVLlstfrtqgs 258
Cdd:PRK04813 144 DNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALpegpqflnqAPYsfDLS--VMDLYPTLASGGTL--------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 259 VVVPDGF--HPKLFWDQFVKYNCN-WFSCVPTISMIMLNmpkPNpF-----PHIRFIRSCSSALAPATFHKLEKEF-NAP 329
Cdd:PRK04813 213 VALPKDMtaNFKQLFETLPQLPINvWVSTPSFADMCLLD---PS-FneehlPNLTHFLFCGEELPHKTAKKLLERFpSAT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 VLEAYAMTEASHQMTS-----------NNLPPGKRKPGTvgqpqgvTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANN 398
Cdd:PRK04813 289 IYNTYGPTEATVAVTSieitdemldqyKRLPIGYAKPDS-------PLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNN 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 399 PKANKENFTKRENY--FRTGDQGYFDpEGFLVLTGRIKELINRGGEKispIELDGImlSH-----PKIDEAVAfgVPDDM 471
Cdd:PRK04813 362 PEKTAEAFFTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYR---IELEEI--EQnlrqsSYVESAVV--VPYNK 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365585 472 YGQVVQ--AAIVLKKGE-----KMTyEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK04813 434 DHKVQYliAYVVPKEEDferefELT-KAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
65-531 |
3.95e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.82 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 65 VAISMRNGLEFIVAFLgATMDAKiGA--PLNPNYKEKEFNFYLNDlkSKAICVpkgTTKLQSSEILKSASTFGCfiveLA 142
Cdd:PRK12316 4604 VGIAMERSAEMMVGLL-AVLKAG-GAyvPLDPEYPRERLAYMMED--SGAALL---LTQSHLLQRLPIPDGLAS----LA 4672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 143 FDATRfrvEYDIYSPEDnykrviyrslnnaKFVNTNPvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIA 222
Cdd:PRK12316 4673 LDRDE---DWEGFPAHD-------------PAVRLHP---------DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATG 4727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 223 NTYKLTPLDRSYVVMPL---FHVHGLIGVLLstfrTQGSVVV-PDGFH-PKLFWDQFVKYNCNWFSCVP-TISMIMLNMP 296
Cdd:PRK12316 4728 ERYELTPDDRVLQFMSFsfdGSHEGLYHPLI----NGASVVIrDDSLWdPERLYAEIHEHRVTVLVFPPvYLQQLAEHAE 4803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 297 KPNPFPHIRFIRSCSSALAPATFHKLEKEF-NAPVLEAYAMTEA----SHQMTSNNLPPGkRKPGTVGQPQG-VTVVILD 370
Cdd:PRK12316 4804 RDGEPPSLRVYCFGGEAVAQASYDLAWRALkPVYLFNGYGPTETtvtvLLWKARDGDACG-AAYMPIGTPLGnRSGYVLD 4882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 371 DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFT------KRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKI 444
Cdd:PRK12316 4883 GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgaPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRI 4962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 445 SPIELDGIMLSHPKIDEAVAFGVPDDMYGQVV-----QAAIVLKKGEKMT--YEELVNFLKKHLASFKIPTKVYFVDKLP 517
Cdd:PRK12316 4963 ELGEIEARLREHPAVREAVVIAQEGAVGKQLVgyvvpQDPALADADEAQAelRDELKAALRERLPEYMVPAHLVFLARMP 5042
|
490
....*....|....
gi 398365585 518 KTATGKIQRRVIAE 531
Cdd:PRK12316 5043 LTPNGKLDRKALPQ 5056
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
178-535 |
5.16e-25 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 108.84 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 178 NPVKFPGfARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNI----ANTYKLTPLDRSYVVMPLFHV----------- 242
Cdd:cd05927 104 NKVPPPP-PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNKINPTDVYISYLPLAHIfervvealfly 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 243 --------HGLIGVL---LSTFRTQGSVVVP---DGFHPKLFWDQFVKyncnwfscvPTISMIMLNM------------- 295
Cdd:cd05927 183 hgakigfySGDIRLLlddIKALKPTVFPGVPrvlNRIYDKIFNKVQAK---------GPLKRKLFNFalnyklaelrsgv 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 296 PKPNPF--------------PHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNlpPGKRKPGTVGQP 361
Cdd:cd05927 254 VRASPFwdklvfnkikqalgGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTL--PGDTSVGHVGGP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 362 QGVTVVILDD----NDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELI 437
Cdd:cd05927 332 LPCAEVKLVDvpemNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDE-DGWLHTGDIGEWLPNGTLKIIDRKKNIF 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 438 NRG-GEKISPIELDGIMLSHPKIDEAVAFG-----------VPDDmygQVVQAAIVLKKGEKMTYEELVNF--LKKH--- 500
Cdd:cd05927 411 KLSqGEYVAPEKIENIYARSPFVAQIFVYGdslksflvaivVPDP---DVLKEWAASKGGGTGSFEELCKNpeVKKAile 487
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 398365585 501 ----------LASFKIPTKVYFVDKLPK------TATGKIQRRVIAETFAK 535
Cdd:cd05927 488 dlvrlgkengLKGFEQVKAIHLEPEPFSvengllTPTFKLKRPQLKKYYKK 538
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
63-527 |
6.85e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 107.67 E-value: 6.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGAtmdAKIGA---PLNPNYKEKEFNFYLNDLKSKAIcvpkgttkLQSSEILKSASTFGCFIV 139
Cdd:cd12117 48 DVVGVLAERSPELVVALLAV---LKAGAayvPLDPELPAERLAFMLADAGAKVL--------LTDRSLAGRAGGLEVAVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 140 ELAFDATRfrveydiysPEDNYKRVIyrslnnakfvntnpvkfpgfaRSSDVALILHTSGTTSTPKTVPLLHLNIVRSTL 219
Cdd:cd12117 117 IDEALDAG---------PAGNPAVPV---------------------SPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 220 NiANTYKLTPLDRSYVVMPL-FHVhgligvllSTFRTQGS-------VVVPDGF--HPKLFwDQFVKYNcnwfscvpTIS 289
Cdd:cd12117 167 N-TNYVTLGPDDRVLQTSPLaFDA--------STFEIWGAllngarlVLAPKGTllDPDAL-GALIAEE--------GVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 290 MIMLNMP--------KPNPFPHIRFIRSCSSALAPATFHKLeKEFNAP--VLEAYAMTEASHQMTSNNLPPGKRKPGTV- 358
Cdd:cd12117 229 VLWLTAAlfnqladeDPECFAGLRELLTGGEVVSPPHVRRV-LAACPGlrLVNGYGPTENTTFTTSHVVTELDEVAGSIp 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 359 -GQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF-----TKRENYFRTGDQGYFDPEGFLVLTG 431
Cdd:cd12117 308 iGRPiANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFvadpfGPGERLYRTGDLARWLPDGRLEFLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 432 RIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVlkKGEKMTYEELVNFLKKHLASFKIPTKVY 511
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAAELRAFLRERLPAYMVPAAFV 465
|
490
....*....|....*.
gi 398365585 512 FVDKLPKTATGKIQRR 527
Cdd:cd12117 466 VLDELPLTANGKVDRR 481
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
187-537 |
7.99e-25 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 107.63 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDR-----SYVvmplFHVHglIGVLLSTFRTQGSVVV 261
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRvlqfaSYT----FDVS--ILEIFTTLAAGGCLCI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 262 P--DGFHPKLFwDQFVKYNCNWFSCVPTIsMIMLNmpkPNPFPHIRFIRSCSSALAPATFHKLEKefNAPVLEAYAMTEA 339
Cdd:cd05918 178 PseEDRLNDLA-GFINRLRVTWAFLTPSV-ARLLD---PEDVPSLRTLVLGGEALTQSDVDTWAD--RVRLINAYGPAEC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 ShQMTSNNLPPGKRKPGTVGQPQGVT--VVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF------TKREN 411
Cdd:cd05918 251 T-IAATVSPVVPSTDPRNIGRPLGATcwVVDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpawLKQEG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 412 Y------FRTGDQGYFDPEGFLVLTGRIKELIN-RG-----GEkispIElDGIMLSHPKIDEAVAFGV-PDDMYGQVVQA 478
Cdd:cd05918 330 SgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKiRGqrvelGE----IE-HHLRQSLPGAKEVVVEVVkPKDGSSSPQLV 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365585 479 AIVLKKGEKMTY------------------EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKSS 537
Cdd:cd05918 405 AFVVLDGSSSGSgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
22-527 |
4.45e-24 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 105.21 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 22 AVIVPETDTQVTYRDLSH---MVGHF-QTMFTNPNSplygavfrqdTVAISMRNGLEFIVAFLGATmdaKIGA---PLNP 94
Cdd:cd17644 16 AVAVVFEDQQLTYEELNTkanQLAHYlQSLGVKSES----------LVGICVERSLEMIIGLLAIL---KAGGayvPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 95 NYKEKEFNFYLNDLkskaicvpkgttklQSSEILksastfgcfivelafdatrfrveydiyspednykrviyrslnnakf 174
Cdd:cd17644 83 NYPQERLTYILEDA--------------QISVLL---------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 175 vnTNPvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPL-FHVHglIGVLLSTF 253
Cdd:cd17644 103 --TQP---------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIaFDVA--AEEIYVTL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 254 RTQGSVV-VPDGFHPKLfwDQFVKYNCNW----FSCVPTISMIMLNMPKPNPFP---HIRFIRSCSSALAPATFHKLEKE 325
Cdd:cd17644 170 LSGATLVlRPEEMRSSL--EDFVQYIQQWqltvLSLPPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 326 F--NAPVLEAYAMTEASHQMTSNNL---PPGKRKPGTVGQPQG-VTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNP 399
Cdd:cd17644 248 VgnFIQLINVYGPTEATIAATVCRLtqlTERNITSVPIGRPIAnTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 400 KANKENF-------TKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMY 472
Cdd:cd17644 328 ELTAEKFishpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPG 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 473 GQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17644 408 NKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
182-524 |
1.08e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 105.82 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 182 FPGFARSS----DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIG----VLLSTF 253
Cdd:PRK06814 782 FPLVYFCNrdpdDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGglvlPLLSGV 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 254 RTqgsVVVPDGFH----PKLFWDqfvkyncnwfscvpTISMIML----------NMPKPNPFPHIRFIRSCSSALAPATF 319
Cdd:PRK06814 862 KV---FLYPSPLHyriiPELIYD--------------TNATILFgtdtflngyaRYAHPYDFRSLRYVFAGAEKVKEETR 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 320 HKLEKEFNAPVLEAYAMTEASHQMTSNNlpPGKRKPGTVGQpqgvtvvilddndnvLPPG------KV------GEVSIR 387
Cdd:PRK06814 925 QTWMEKFGIRILEGYGVTETAPVIALNT--PMHNKAGTVGR---------------LLPGieyrlePVpgidegGRLFVR 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 388 GENVTLGY--ANNPKANKEnftKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEkispieldgiMLSHPKIDEAVAF 465
Cdd:PRK06814 988 GPNVMLGYlrAENPGVLEP---PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGE----------MISLAAVEELAAE 1054
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365585 466 GVPDdmYGQVVQAAIVLKKGEKM---------TYEELVNFLKKHLAS-FKIPTKVYFVDKLPKTATGKI 524
Cdd:PRK06814 1055 LWPD--ALHAAVSIPDARKGERIillttasdaTRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
186-527 |
1.98e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 103.14 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 186 ARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDR-SYVVMPLFHVHGLigVLLSTFRTQGSVVVPDG 264
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRlLAVTTYAFDISLL--ELLLPLLAGARVVIAPR 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 FH---PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPfPHIRFIrsC-SSALAPAtfhkLEKEFNAPVLEAYAM---T 337
Cdd:cd12116 201 ETqrdPEALARLIEAHSITVMQATPATWRMLLDAGWQGR-AGLTAL--CgGEALPPD----LAARLLSRVGSLWNLygpT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 338 EASHQMTSNNLPPGKRKPgTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF------TKRE 410
Cdd:cd12116 274 ETTIWSTAARVTAAAGPI-PIGRPlANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfaGPGS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 411 NYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVqAAIVLKKGEKMTY 490
Cdd:cd12116 353 RLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAGAAPDA 431
|
330 340 350
....*....|....*....|....*....|....*..
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd12116 432 AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
193-527 |
2.41e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 102.42 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 193 LILHTSGTTSTPKTvpllhlnIVRSTLNI-----ANTYKLT-PLDRSYVVM-PLFHVHGLI-GVLLSTFRTQGSVVVPDG 264
Cdd:PRK08308 105 LLQYSSGTTGEPKL-------IRRSWTEIdreieAYNEALNcEQDETPIVAcPVTHSYGLIcGVLAALTRGSKPVIITNK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 fHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPkPNPFphiRFIRSCSS-ALAPAT-FHKLeKEFNAPVLEAYAMTEA--- 339
Cdd:PRK08308 178 -NPKFALNILRNTPQHILYAVPLMLHILGRLL-PGTF---QFHAVMTSgTPLPEAwFYKL-RERTTYMMQQYGCSEAgcv 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 --SHQMTSnnlppgkrkPGTVGQPqgvtvvilddndnvLPpgkvgEVSirgenVTLGYA-NNPKANKENFTKREnyFRTG 416
Cdd:PRK08308 252 siCPDMKS---------HLDLGNP--------------LP-----HVS-----VSAGSDeNAPEEIVVKMGDKE--IFTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 417 DQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKkgEKMTYEELVNF 496
Cdd:PRK08308 297 DLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPVQLREW 374
|
330 340 350
....*....|....*....|....*....|.
gi 398365585 497 LKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK08308 375 CIQHLAPYQVPHEIESVTEIPKNANGKVSRK 405
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
354-531 |
2.75e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 103.68 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 354 KPGTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIR----GENVTLgYaNNPkankENFtkRENYFRTGDQGYF------- 421
Cdd:PRK00174 422 KPGSATRPlPGIQPAVVDEEGNPLEGGEGGNLVIKdpwpGMMRTI-Y-GDH----ERF--VKTYFSTFKGMYFtgdgarr 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 422 DPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMT---YEELVNFLK 498
Cdd:PRK00174 494 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWVR 573
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365585 499 KHLASFKIPTKVYFVDKLPKTATGKIQRRV---IAE 531
Cdd:PRK00174 574 KEIGPIAKPDVIQFAPGLPKTRSGKIMRRIlrkIAE 609
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
189-527 |
4.67e-23 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 101.95 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRsyvVM----PLFHvhGLIGVLLSTFRTQGSVVVPDG 264
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSR---VLqfasPSFD--ASVWELLMALLAGATLVLAPA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 fHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPAtfhkLEKEFnAP---VLEAYAMTEASH 341
Cdd:cd17652 168 -EELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDLRTLVVAGEACPAE----LVDRW-APgrrMINAYGPTETTV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 342 QMTSNNLPPGKRKPgTVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF------TKRENYFR 414
Cdd:cd17652 242 CATMAGPLPGGGVP-PIGRPvPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFvadpfgAPGSRMYR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 415 TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELV 494
Cdd:cd17652 321 TGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELR 400
|
330 340 350
....*....|....*....|....*....|...
gi 398365585 495 NFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd17652 401 AHLAERLPGYMVPAAFVVLDALPLTPNGKLDRR 433
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
65-527 |
4.90e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 104.09 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 65 VAISMRNGLEFIVAFLgATMDAKiGA--PLNPNYKEKEFNFYLND------LKSKAICvpkgtTKLQSSEILKSastfgc 136
Cdd:PRK12467 1627 VGIAVERSLEMVVGLL-AILKAG-GAyvPLDPEYPRERLAYMIEDsgiellLTQSHLQ-----ARLPLPDGLRS------ 1693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 137 fiveLAFDATRFRVE-YDIYSPEdnykrviyrslnnakfVNTNPvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIV 215
Cdd:PRK12467 1694 ----LVLDQEDDWLEgYSDSNPA----------------VNLAP---------QNLAYVIYTSGSTGRPKGAGNRHGALV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 216 RSTLNIANTYKLTPLDRSYVVMPL---FHVHGLIGVLLSTFRTqgsVVVPDGFH--PKLFWDQFVKYNCNWFSCVPTISM 290
Cdd:PRK12467 1745 NRLCATQEAYQLSAADVVLQFTSFafdVSVWELFWPLINGARL---VIAPPGAHrdPEQLIQLIERQQVTTLHFVPSMLQ 1821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 291 IMLNMPK--PNPfPHIRFIRSCSSALAPATFHK-LEKEFNAPVLEAYAMTEA----SHQMTSNNLPPGkRKPGTVGQPQG 363
Cdd:PRK12467 1822 QLLQMDEqvEHP-LSLRRVVCGGEALEVEALRPwLERLPDTGLFNLYGPTETavdvTHWTCRRKDLEG-RDSVPIGQPIA 1899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 364 -VTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF------TKRENYFRTGDQGYFDPEGFLVLTGRIKEL 436
Cdd:PRK12467 1900 nLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQ 1979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 437 INRGGEKISPIELDGIMLSHPKIDEA-------------VAFGVPDDmygqvvqAAIVLKKGEKMTY-EELVNFLKKHLA 502
Cdd:PRK12467 1980 VKIRGFRIELGEIEARLREQGGVREAvviaqdgangkqlVAYVVPTD-------PGLVDDDEAQVALrAILKNHLKASLP 2052
|
490 500
....*....|....*....|....*
gi 398365585 503 SFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK12467 2053 EYMVPAHLVFLARMPLTPNGKLDRK 2077
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
65-538 |
5.08e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 104.09 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 65 VAISMRNGLEFIVAFLgATMdaKIGA---PLNPNYKEKEFNFYLNDLKSKAIcvpkgttkLQSSEILKsastfgcfivEL 141
Cdd:PRK12467 3148 VGVAVERSVEMIVALL-AVL--KAGGayvPLDPEYPRERLAYMIEDSGVKLL--------LTQAHLLE----------QL 3206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 142 AFDATRFRVEYDIYSPEdnykrviyrslnnaKFVNTNPVKFpgfARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNI 221
Cdd:PRK12467 3207 PAPAGDTALTLDRLDLN--------------GYSENNPSTR---VMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWI 3269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 222 ANTYKLTPLDRSYVVMPlFHVHGLIGVLLSTFRTQGSVVVPDGFH--PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPN 299
Cdd:PRK12467 3270 AEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRDNDLwdPEELWQAIHAHRISIACFPPAYLQQFAEDAGGA 3348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 300 PFPHIRFIRSCSSALAPATFHKLEKEF-NAPVLEAYAMTEASHQMT-----SNNLPPGKRKPgtVGQP-QGVTVVILDDN 372
Cdd:PRK12467 3349 DCASLDIYVFGGEAVPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTlwkcgGDAVCEAPYAP--IGRPvAGRSIYVLDGQ 3426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 373 DNVLPPGKVGEVSIRGENVTLGYANNPKANKENF------TKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISP 446
Cdd:PRK12467 3427 LNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFvadpfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 3506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 447 IELDGIMLSHPKIDEAVAFGVpDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:PRK12467 3507 GEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
|
490
....*....|..
gi 398365585 527 RVIAETFAKSSR 538
Cdd:PRK12467 3586 KALPDPDAKGSR 3597
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
448-523 |
7.14e-23 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 92.22 E-value: 7.14e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 448 ELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGK 523
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
179-539 |
7.97e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 103.70 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 PVKFPGFARSSD-VALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPlFHVHGLIGVLLSTFRTQG 257
Cdd:PRK12467 645 SGHNPEVALDPDnLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVST-FAFDLGVTELFGALASGA 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVPD---GFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKL-EKEFNAPVLEA 333
Cdd:PRK12467 724 TLHLLPpdcARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVrALGPGARLINH 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 334 YAMTEASHQMTSNNLPPGKRKPGTV--GQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENF---- 406
Cdd:PRK12467 804 YGPTETTVGVSTYELSDEERDFGNVpiGQPlANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpdp 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 407 --TKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQ---AAIV 481
Cdd:PRK12467 884 fgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAylvPAAV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365585 482 LKKGEK-MTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKSSRN 539
Cdd:PRK12467 964 ADGAEHqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQA 1022
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
190-504 |
6.72e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 99.20 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGL-IGVllstfrtqgSVVVP--DGFH 266
Cdd:PRK09274 175 DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPaLGM---------TSVIPdmDPTR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 267 P------KLFwDQFVKYNCNWFSCVPTI------SMIMLNMPKPNpfphirfIRSCSSALAPATFHKLEKeF------NA 328
Cdd:PRK09274 246 PatvdpaKLF-AAIERYGVTNLFGSPALlerlgrYGEANGIKLPS-------LRRVISAGAPVPIAVIER-FramlppDA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 329 PVLEAYAMTEA--------------SHQMTSNNlppgkrkPGT-VGQP-QGVTVVILDDNDN---------VLPPGKVGE 383
Cdd:PRK09274 317 EILTPYGATEAlpissiesreilfaTRAATDNG-------AGIcVGRPvDGVEVRIIAISDApipewddalRLATGEIGE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 384 VSIRGENVTLGYANNPKANKENFTKREN---YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKID 460
Cdd:PRK09274 390 IVVAGPMVTRSYYNRPEATRLAKIPDGQgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVK 469
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398365585 461 EAVAFGVPDDmyGQVVQAAIV-LKKGEKMTYEELVNFLKKHLASF 504
Cdd:PRK09274 470 RSALVGVGVP--GAQRPVLCVeLEPGVACSKSALYQELRALAAAH 512
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
188-529 |
2.41e-21 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 96.85 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSyVVMPLFHVHGLIGVLLSTFRTQGSV-VVPDgfH 266
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKS-LVYASFSFDASAWEIFPHLTAGAALhVVPS--E 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 267 PKLFWDQFVKYnCNwfscVPTISMIMLNMPKPNPFPHIRFiRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSN 346
Cdd:cd17645 180 RRLDLDALNDY-FN----QEGITISFLPTGAAEQFMQLDN-QSLRVLLTGGDKLKKIERKGYKLVNNYGPTENTVVATSF 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 347 NL-PPGKRKPgtVGQP-QGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR-----ENYFRTGDQG 419
Cdd:cd17645 254 EIdKPYANIP--IGKPiDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHpfvpgERMYRTGDLA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 420 YFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKkgEKMTYEELVNFLKK 499
Cdd:cd17645 332 KFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP--EEIPHEELREWLKN 409
|
330 340 350
....*....|....*....|....*....|..
gi 398365585 500 HLASFKIPTkvYFV--DKLPKTATGKIQRRVI 529
Cdd:cd17645 410 DLPDYMIPT--YFVhlKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
64-527 |
5.70e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 64 TVAISMRNGLEFIVAFLgATMDAKiGA--PLNPNYKEKEFNFYLNDlkSKAicvpkgttklqssEILKSASTFGCFiveL 141
Cdd:PRK12316 563 LVGVAMERSIEMVVALL-AILKAG-GAyvPLDPEYPAERLAYMLED--SGV-------------QLLLSQSHLGRK---L 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 142 AFDATRFRVEYDIYSPE-DNYKrviyrslNNAKFVNTNPvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLN 220
Cdd:PRK12316 623 PLAAGVQVLDLDRPAAWlEGYS-------EENPGTELNP---------ENLAYVIYTSGSTGKPKGAGNRHRALSNRLCW 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 221 IANTYKLTPLDRSYVVMPL---FHVHGLIGVLLSTFRTqgsVVVPDGFH--PKLFWDQFVKYNCNWFSCVPTISMIMLNM 295
Cdd:PRK12316 687 MQQAYGLGVGDTVLQKTPFsfdVSVWEFFWPLMSGARL---VVAAPGDHrdPAKLVELINREGVDTLHFVPSMLQAFLQD 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 296 PKPNPFPHIRFI----RSCSSALAPATFHKLEkefNAPVLEAYAMTEASHQMT-SNNLPPGKRKPgTVGQP-QGVTVVIL 369
Cdd:PRK12316 764 EDVASCTSLRRIvcsgEALPADAQEQVFAKLP---QAGLYNLYGPTEAAIDVThWTCVEEGGDSV-PIGRPiANLACYIL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 370 DDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR-----ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKI 444
Cdd:PRK12316 840 DANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSpfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 445 SPIELDGIMLSHPKIDEAVAFGVPddmyGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:PRK12316 920 ELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
...
gi 398365585 525 QRR 527
Cdd:PRK12316 996 DRK 998
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
188-535 |
6.83e-21 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 96.51 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVplLHLN---IVRSTLNIANTYKLTPLD-------------RSYVVM-PLfhvhgLIGVLL 250
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGV--LHTTggyMVYTATTFKYAFDYKPTDvywctadcgwitgHSYVTYgPM-----LNGATV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 251 STFrtQGSVVVPDgfhPKLFWDQFVKYNCNWFSCVPT-ISMIMLNMPKP---NPFPHIRFIRSCSSALAPAT---FHKLE 323
Cdd:PLN02654 347 LVF--EGAPNYPD---SGRCWDIVDKYKVTIFYTAPTlVRSLMRDGDEYvtrHSRKSLRVLGSVGEPINPSAwrwFFNVV 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 324 KEFNAPVLEAYAMTEASHQMTSnnlP-PGK--RKPGTVGQPQ-GVTVVILDDNDNVLPPGKVGEVSIR----GENVTLgY 395
Cdd:PLN02654 422 GDSRCPISDTWWQTETGGFMIT---PlPGAwpQKPGSATFPFfGVQPVIVDEKGKEIEGECSGYLCVKkswpGAFRTL-Y 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 396 ANNPKANKENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQV 475
Cdd:PLN02654 498 GDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQG 577
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365585 476 VQAAIVLKKGEKMTYE---ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAK 535
Cdd:PLN02654 578 IYAFVTLVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASR 640
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
192-535 |
9.62e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 96.25 E-value: 9.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 192 ALILHTSGTTSTPKTVPLLHLNIVRSTLNIA-NTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVV---PDG--- 264
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVInsaPVTpea 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 -------FHPKLFWDqfvkyncnwfscVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNA-PVLEAYAM 336
Cdd:PRK06060 228 aailsarFGPSVLYG------------VPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGiPILDGIGS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 337 TEASHQMTSNNLppGKRKPGTVGQ---PQGVTVVILDDNdnVLPPGKVGEVSIRGENVTLGYANNPKANKENftkrENYF 413
Cdd:PRK06060 296 TEVGQTFVSNRV--DEWRLGTLGRvlpPYEIRVVAPDGT--TAGPGVEGDLWVRGPAIAKGYWNRPDSPVAN----EGWL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 414 RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKM---TY 490
Cdd:PRK06060 368 DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIdgsVM 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398365585 491 EELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI-AETFAK 535
Cdd:PRK06060 448 RDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrKQSPTK 493
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
189-534 |
1.29e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.06 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 189 SDVALILHTSGTTSTPKTVPLLHLNIVRstlNIANTYKLTPLDRSYVVM----PLFHVHGLIGVLLSTFRTQGSVVV--P 262
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYA---NAEAMFVAAEFDVETDVMvswlPLFHDMGMVGFLTVPMYFGAELVKvtP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 263 DGF-HPKLFWDQFV-KYNCNwFSCVPT-----ISMIMLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEfNAP---- 329
Cdd:PRK07768 229 MDFlRDPLLWAELIsKYRGT-MTAAPNfayalLARRLRRQAKPGAFdlSSLRFALNGAEPIDPADVEDLLDA-GARfglr 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 ---VLEAYAMTEAS-------------------------HQMTSNNLPPGKRKPgTVGQP-QGVTVVILDDNDNVLPPGK 380
Cdd:PRK07768 307 peaILPAYGMAEATlavsfspcgaglvvdevdadllaalRRAVPATKGNTRRLA-TLGPPlPGLEVRVVDEDGQVLPPRG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 381 VGEVSIRGENVTLGY--ANNPKANKEnftkRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISP--IE-----LDG 451
Cdd:PRK07768 386 VGVIELRGESVTPGYltMDGFIPAQD----ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPtdIEraaarVEG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 452 ImlshpKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKmtyEELVNFLKKHLASFKI------PTKVYFVDK--LPKTATGK 523
Cdd:PRK07768 462 V-----RPGNAVAVRLDAGHSREGFAVAVESNAFED---PAEVRRIRHQVAHEVVaevgvrPRNVVVLGPgsIPKTPSGK 533
|
410
....*....|.
gi 398365585 524 IQRRVIAETFA 534
Cdd:PRK07768 534 LRRANAAELVT 544
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
178-500 |
1.32e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 94.45 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 178 NPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFhvhGLIGVLLSTfrtqg 257
Cdd:cd05910 74 EPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF---ALFGPALGL----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVPDGFH-------PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPN--PFPHIRFIRSCSSALAPATFHKLEKEFN- 327
Cdd:cd05910 146 TSVIPDMDPtrparadPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHgiTLPSLRRVLSAGAPVPIALAARLRKMLSd 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 328 -APVLEAYAMTEA-------SHQMTSNNLPPGKRKPGT-VGQP-QGVTVVILD---------DNDNVLPPGKVGEVSIRG 388
Cdd:cd05910 226 eAEILTPYGATEAlpvssigSRELLATTTAATSGGAGTcVGRPiPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 389 ENVTLGYANNPKANKenFTK-REN----YFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEA- 462
Cdd:cd05910 306 PTVTPTYVNRPVATA--LAKiDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSa 383
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 398365585 463 -VAFGVPDDMYG-QVVQAAIVLKKGEKMTYEELVNFLKKH 500
Cdd:cd05910 384 lVGVGKPGCQLPvLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
29-527 |
1.61e-20 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 94.41 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 29 DTQVTYRDL---SHMVGHFqtmftnpnspLYGAVFRQ-DTVAISMRNGLEFIVAFLGAtmdAKIG---APLNPNYKEKEF 101
Cdd:cd05939 1 DRHWTFRELneySNKVANF----------FQAQGYRSgDVVALFMENRLEFVALWLGL---AKIGvetALINSNLRLESL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 102 NFYLNDLKSKAIcvpkgttklqsseilksastfgcfivelafdatrfrveydIYSPEDNYKRVIYRSLNNAKFVNtnpvk 181
Cdd:cd05939 68 LHCITVSKAKAL----------------------------------------IFNLLDPLLTQSSTEPPSQDDVN----- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 182 fpgfarSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVV 261
Cdd:cd05939 103 ------FRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 262 PDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPkPNPFPHIRFIR-SCSSALAPATFHKLEKEFNAP-VLEAYAMTEA 339
Cdd:cd05939 177 RKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQP-PSEEEQKHNVRlAVGNGLRPQIWEQFVRRFGIPqIGEFYGATEG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 SHQMTS----------NNLPPGKRKPGTVGQPQGVTVVILDDNDNV-LP--PGKVGEV--SIRGENVTL---GYAN---- 397
Cdd:cd05939 256 NSSLVNidnhvgacgfNSRILPSVYPIRLIKVDEDTGELIRDSDGLcIPcqPGEPGLLvgKIIQNDPLRrfdGYVNegat 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 398 NPKANKENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVP-DDMYGQVV 476
Cdd:cd05939 336 NKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvPGVEGRAG 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 398365585 477 QAAIVLKKgEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:cd05939 416 MAAIVDPE-RKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKT 465
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
190-523 |
2.55e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.38 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNI--ANTYKLTPLDRSYVVMPLFHVHGLiGVLLSTFRTQGSVVVPDG--- 264
Cdd:PRK05620 182 TAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHVLSW-GVPLAAFMSGTPLVFPGPdls 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 265 ----------FHPKlfwdqfVKYNcnwfscVPT--ISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLE 332
Cdd:PRK05620 261 aptlakiiatAMPR------VAHG------VPTlwIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVH 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 333 AYAMTEASHQMTSNNLPPG----KRKPGTVGQ---PQGVTVVILDDnDNVLPPG--KVGEVSIRGENVTLGYANNPKAN- 402
Cdd:PRK05620 329 VWGMTETSPVGTVARPPSGvsgeARWAYRVSQgrfPASLEYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPTEEg 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 403 ---------------KENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGV 467
Cdd:PRK05620 408 ggaastfrgedvedaNDRFTA-DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365585 468 PDDMYGQVVQAAIVLKKG---EKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGK 523
Cdd:PRK05620 487 PDDKWGERPLAVTVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGK 545
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
63-533 |
6.05e-19 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 90.04 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGAtmdAKIGAP---LNPNYKEKEFNFYLNDLKSKAICVpkgTTKLQSS--EILKSASTFG-- 135
Cdd:cd05938 32 DTVALLLGNEPAFLWIWLGL---AKLGCPvafLNTNIRSKSLLHCFRCCGAKVLVV---APELQEAveEVLPALRADGvs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 136 CFIVelafdatrfrveydiySPEDNYKRVIyRSLNNAKFVNTNPVkfPGFARS----SDVALILHTSGTTSTPKTVPLLH 211
Cdd:cd05938 106 VWYL----------------SHTSNTEGVI-SLLDKVDAASDEPV--PASLRAhvtiKSPALYIYTSGTTGLPKAARISH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 212 LNIVRSTlNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMI 291
Cdd:cd05938 167 LRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 292 MLNMPK-PNPFPH-IRFirSCSSALAPATFHKLEKEF-NAPVLEAYAMTEAShqMTSNNLPpgkRKPGTVGQ-------- 360
Cdd:cd05938 246 LCNQPQsPNDRDHkVRL--AIGNGLRADVWREFLRRFgPIRIREFYGSTEGN--IGFFNYT---GKIGAVGRvsylykll 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 361 ------------------PQGVTVVIlddndnvlPPGKVGEV--SIRGENVTLGYANNPKANKEN-----FTKRENYFRT 415
Cdd:cd05938 319 fpfelikfdvekeepvrdAQGFCIPV--------AKGEPGLLvaKITQQSPFLGYAGDKEQTEKKllrdvFKKGDVYFNT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 416 GDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMY-GQVVQAAIVLKKGEKMTYEELV 494
Cdd:cd05938 391 GDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRIGMAAVKLKPGHEFDGKKLY 470
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 398365585 495 NFLKKHLASFKIPTKVYFVDKLPKTATGKIQR-RVIAETF 533
Cdd:cd05938 471 QHVREYLPAYARPRFLRIQDSLEITGTFKQQKvRLVEEGF 510
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
192-447 |
1.05e-18 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 89.34 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 192 ALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDR------SYvvMPLFHV------------HG--------- 244
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvSY--LPLSHIaaqildiwlpikVGgqvyfaqpd 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 245 -LIGVLLSTFRTqgsvVVPDGFH--PKLfWDQFVKYNCNWFSCVPTISMIML----------NMPKPN-PFPHIRFIR-- 308
Cdd:cd05933 231 aLKGTLVKTLRE----VRPTAFMgvPRV-WEKIQEKMKAVGAKSGTLKRKIAswakgvgletNLKLMGgESPSPLFYRla 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 309 ------------------SCSSALAPATfhKLEKEF----NAPVLEAYAMTEASHQMTSNNlpPGKRKPGTVGQP-QGVT 365
Cdd:cd05933 306 kklvfkkvrkalgldrcqKFFTGAAPIS--RETLEFflslNIPIMELYGMSETSGPHTISN--PQAYRLLSCGKAlPGCK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 366 VVILDDNDNvlppgKVGEVSIRGENVTLGYANNPKANKENFtKRENYFRTGDQGYFDPEGFLVLTGRIKELI-NRGGEKI 444
Cdd:cd05933 382 TKIHNPDAD-----GIGEICFWGRHVFMGYLNMEDKTEEAI-DEDGWLHSGDLGKLDEDGFLYITGRIKELIiTAGGENV 455
|
...
gi 398365585 445 SPI 447
Cdd:cd05933 456 PPV 458
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
188-470 |
1.89e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 88.33 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 188 SSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVP-DGFH 266
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAyNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 267 PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKP--NPFPHIRFIRSCSSALAPATFHKLEKEFNAPVL-EAYAMTEASHQM 343
Cdd:PRK06334 262 PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKqeSCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLrQGYGTTECSPVI 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 344 TSNNLPPGKrKPGTVGQP-QGVTVVILDDNDNV-LPPGKVGEVSIRGENVTLGYANNPKANKENFTKRENYFRTGDQGYF 421
Cdd:PRK06334 342 TINTVNSPK-HESCVGMPiRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGETWYVTGDLGYV 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 398365585 422 DPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHpkideavaFGVPDD 470
Cdd:PRK06334 421 DRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAA 461
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
65-527 |
8.09e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.71 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 65 VAISMRNGLEFIVAFLGATmdaKIGA---PLNPNYKEKEFNFYLNDlkskaicvpKGTTKLQSSEILKSASTFGCFIVEL 141
Cdd:PRK12316 2056 VAIAAERSFELVVALLAVL---KAGGayvPLDPNYPAERLAYMLED---------SGAALLLTQRHLLERLPLPAGVARL 2123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 142 AFDATRFRVEYDIYSPEdnykrviyrslnnakfVNTNPvkfpgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNI 221
Cdd:PRK12316 2124 PLDRDAEWADYPDTAPA----------------VQLAG---------ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAA 2178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 222 ANTYKLTPLDRSYVVMPlFHVHGLIGVLLSTFRTQGSVVVPDGFH--PKLFWDQFVKYNCNWFSCVPTISMIMLNMPK-- 297
Cdd:PRK12316 2179 GERYELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIRDDELwdPEQLYDEMERHGVTILDFPPVYLQQLAEHAErd 2257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 298 PNPfPHIRfIRSCSSALAPATFHKLEKEFNAPV--LEAYAMTEA----SHQMTSNNLPPGKRKPgTVGQPQG-VTVVILD 370
Cdd:PRK12316 2258 GRP-PAVR-VYCFGGEAVPAASLRLAWEALRPVylFNGYGPTEAvvtpLLWKCRPQDPCGAAYV-PIGRALGnRRAYILD 2334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 371 DNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR------ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKI 444
Cdd:PRK12316 2335 ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDpfsasgERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRI 2414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 445 SPIELDGIMLSHPKIDEAVAFGVpDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:PRK12316 2415 ELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
...
gi 398365585 525 QRR 527
Cdd:PRK12316 2494 DRK 2496
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
63-531 |
8.32e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 86.53 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATMDAKIGAPLN-PNY--KEKEFNFYLNDLKSKAICvpkgTTKLQSSEILKsastfgcFIV 139
Cdd:PRK05850 60 DRAVILAPQGLEYIVAFLGALQAGLIAVPLSvPQGgaHDERVSAVLRDTSPSVVL----TTSAVVDDVTE-------YVA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 140 ELAFDATRFRVEYDiyspednykrviyrSLNnakfVNTNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTL 219
Cdd:PRK05850 129 PQPGQSAPPVIEVD--------------LLD----LDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 220 NIANTY-----KLTPLDRSYVV-MPLFHVHGLI-GVLLSTFRTQGSVVV-PDGFHPK-LFWDQFVKYNCNWFSCVPTIS- 289
Cdd:PRK05850 191 QLMSDYfgdtgGVPPPDTTVVSwLPFYHDMGLVlGVCAPILGGCPAVLTsPVAFLQRpARWMQLLASNPHAFSAAPNFAf 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 290 -----------MIMLNMPkpnpfpHIRFIRSCSSALAPATFHKLEKEFnAP-------VLEAYAMTEA------------ 339
Cdd:PRK05850 271 elavrktsdddMAGLDLG------GVLGIISGSERVHPATLKRFADRF-APfnlretaIRPSYGLAEAtvyvatrepgqp 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 340 --SHQMTSNNLPPGKRKP-----GT----VGQPQGVTVVILDDNDNV-LPPGKVGEVSIRGENVTLGYANNPKANKENF- 406
Cdd:PRK05850 344 peSVRFDYEKLSAGHAKRcetggGTplvsYGSPRSPTVRIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFg 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 407 ---------TKRENYFRTGDQGYFDpEGFLVLTGRIKELINRGGEKISP--IEldgimlshPKIDE-----AVAFGVPDD 470
Cdd:PRK05850 424 atlvdpspgTPEGPWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPddIE--------ATIQEitggrVAAISVPDD 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 471 MYGQVVqAAIVLKK-----GEKMtyeELVNFLKKHLASfKI-------PTKVYFV--DKLPKTATGKIQRRVIAE 531
Cdd:PRK05850 495 GTEKLV-AIIELKKrgdsdEEAM---DRLRTVKREVTS-AIskshglsVADLVLVapGSIPITTSGKIRRAACVE 564
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
187-523 |
1.04e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 86.69 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVV-PDGF 265
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLyPSPL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 H----PKLFWDQfvkyNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASh 341
Cdd:PRK08043 443 HyrivPELVYDR----NCTVLFGTSTFLGNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECA- 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 342 QMTSNNLPPGKrKPGTVGQpqgvtvvILDDND-NVLP-PG--KVGEVSIRGENVTLGY--------ANNPKANKENFTKR 409
Cdd:PRK08043 518 PVVSINVPMAA-KPGTVGR-------ILPGMDaRLLSvPGieQGGRLQLKGPNIMNGYlrvekpgvLEVPTAENARGEME 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISpieLDGImlshpkidEAVAFGV-PDDMYGQVVQA------AIVL 482
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS---LEMV--------EQLALGVsPDKQHATAIKSdaskgeALVL 658
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398365585 483 -KKGEKMTYEELVNFLKKH-LASFKIPTKVYFVDKLPKTATGK 523
Cdd:PRK08043 659 fTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
313-533 |
2.84e-17 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 84.78 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 313 ALAPATFhkleKEFNA---PVLEAYAMTEASHQMTSNnlPPGKRKPGTVGQPQGVTVVILDDndnvlppgkVGEVSIRGE 389
Cdd:cd17641 335 ALGPDTF----RFFHAigvPLKQLYGQTELAGAYTVH--RDGDVDPDTVGVPFPGTEVRIDE---------VGEILVRSP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 390 NVTLGYANNPKANKENFTkRENYFRTGDQGYFDPEGFLVLTGRIKELINRG-GEKISPIELDGIMLSHPKIDEAVAFGVP 468
Cdd:cd17641 400 GVFVGYYKNPEATAEDFD-EDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 469 DDMYGQVV--QAAIVLKKGEK-----MTYEELVN------FLKKHL----ASFKIPTKVYFVDKLPK---------TATG 522
Cdd:cd17641 479 RPYLTAFIciDYAIVGKWAEQrgiafTTYTDLASrpevyeLIRKEVekvnASLPEAQRIRRFLLLYKeldaddgelTRTR 558
|
250
....*....|.
gi 398365585 523 KIQRRVIAETF 533
Cdd:cd17641 559 KVRRGVIAEKY 569
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
179-530 |
1.13e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 83.13 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 PVKFPGFARSSDVALILhTSGTTSTPKTVPLLHlnivRSTLNIANTYKLTPL--------DRSYVVMPLFHVHGLIGVLL 250
Cdd:PRK05857 160 LAGNADQGSEDPLAMIF-TSGTTGEPKAVLLAN----RTFFAVPDILQKEGLnwvtwvvgETTYSPLPATHIGGLWWILT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 251 STFRtqGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPK--PNPFPHIRFIRSCSSALAPATFHKLEKEfNA 328
Cdd:PRK05857 235 CLMH--GGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKsaNATVPSLRLVGYGGSRAIAADVRFIEAT-GV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 329 PVLEAYAMTEAShqMTSNNLPP-----GKRKPGTVGQP-QGVTVVILDDN------DNVLPPGKVGEVSIRGENVTLGYA 396
Cdd:PRK05857 312 RTAQVYGLSETG--CTALCLPTddgsiVKIEAGAVGRPyPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYW 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 397 NNPKANKENFTkrENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVV 476
Cdd:PRK05857 390 NNPERTAEVLI--DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALV 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365585 477 QAAIVL-----KKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIA 530
Cdd:PRK05857 468 GLAVVAsaeldESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
179-531 |
8.53e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 81.37 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 PVKFPGFARSSD-VALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLtplDRSYVVM---PL-FHVhgliGV----- 248
Cdd:PRK05691 1262 PSQAPGLHLHGDnLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYAL---DDSDVLMqkaPIsFDV----SVwecfw 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 249 -LLSTFRTqgsVVVPDGFH--PKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKE 325
Cdd:PRK05691 1335 pLITGCRL---VLAGPGEHrdPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQR 1411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 326 FNAPVLE-AYAMTEASHQMT--SNNLPPGKRKPgtVGQPQGVTVV-ILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKA 401
Cdd:PRK05691 1412 LPQVQLHnRYGPTETAINVThwQCQAEDGERSP--IGRPLGNVLCrVLDAELNLLPPGVAGELCIGGAGLARGYLGRPAL 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 402 NKENF------TKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFgVPDDMYGQV 475
Cdd:PRK05691 1490 TAERFvpdplgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQ 1568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365585 476 VQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAE 531
Cdd:PRK05691 1569 LVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
327-529 |
1.49e-14 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 76.53 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 327 NAPVLEAYAMTEASHQMTSnnLPPG----KRKPGTVGQPQ-GVTVVILDDND-NVLPPGKVGEVSIRGEnVTLGYANNPK 400
Cdd:PRK10524 380 GVPVIDNYWQTETGWPILA--IARGvedrPTRLGSPGVPMyGYNVKLLNEVTgEPCGPNEKGVLVIEGP-LPPGCMQTVW 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 401 ANKENFTKreNYFR--------TGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMY 472
Cdd:PRK10524 457 GDDDRFVK--TYWSlfgrqvysTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALK 534
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 473 GQVVQAAIVLKKGEKMTYE--------ELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVI 529
Cdd:PRK10524 535 GQVAVAFVVPKDSDSLADRearlalekEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
63-494 |
1.54e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 76.31 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 63 DTVAISMRNGLEFIVAFLGATMDAKIGAPL----NPNYKEKeFNFYLNDLKSKAIcvpkgttkLQSSEILKSASTFgcfi 138
Cdd:PRK07769 80 DRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGR-LHAVLDDCTPSAI--------LTTTDSAEGVRKF---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 139 velafdatrFRVEydiysPEDNYKRVI-YRSLNNAkfVNTNPVKFPgfARSSDVALILHTSGTTSTPKTVPLLHLNIVRS 217
Cdd:PRK07769 147 ---------FRAR-----PAKERPRVIaVDAVPDE--VGATWVPPE--ANEDTIAYLQYTSGSTRIPAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 218 TLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLS-------TFRTQGSvvvpdgfhpklfwdqFVKYNCNW--------- 281
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPallghyiTFMSPAA---------------FVRRPGRWirelarkpg 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 282 -----FSCVPTISM---IMLNMPKPNPFP----HIRFIRSCSSALAPATFHKLEKEFnAP-------VLEAYAMTEASHQ 342
Cdd:PRK07769 274 gtggtFSAAPNFAFehaAARGLPKDGEPPldlsNVKGLLNGSEPVSPASMRKFNEAF-APyglpptaIKPSYGMAEATLF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 343 MTS--------------NNLPPGK------RKPGTVGQPQGVTV------VILD-DNDNVLPPGKVGEVSIRGENVTLGY 395
Cdd:PRK07769 353 VSTtpmdeeptviyvdrDELNAGRfvevpaDAPNAVAQVSAGKVgvsewaVIVDpETASELPDGQIGEIWLHGNNIGTGY 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 396 ANNPKANKENF----TKR------------ENYFRTGDQG-YFDpeGFLVLTGRIKELINRGGEKISPIELDgimLSHPK 458
Cdd:PRK07769 433 WGKPEETAATFqnilKSRlseshaegapddALWVRTGDYGvYFD--GELYITGRVKDLVIIDGRNHYPQDLE---YTAQE 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 398365585 459 IDEAV------AFGVPDDMYGQVV--QAAIVLKKGEKMTYEELV 494
Cdd:PRK07769 508 ATKALrtgyvaAFSVPANQLPQVVfdDSHAGLKFDPEDTSEQLV 551
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
190-526 |
2.88e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 75.43 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIA-NTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSV-VVPDG-F- 265
Cdd:PRK09192 177 DIAYLQYSSGSTRFPRGVIITHRALMANLRAIShDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVdYLPTRdFa 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 266 -HPkLFWDQFVKYNCNWFSCVPT------------------------ISMIMLNMPKPNPfphirfIRSCSSALAPATFH 320
Cdd:PRK09192 257 rRP-LQWLDLISRNRGTISYSPPfgyelcarrvnskdlaeldlscwrVAGIGADMIRPDV------LHQFAEAFAPAGFD 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 321 klEKEFnapvLEAYAMTEA-----------------------SHQMTSNNLPPGKRKPGTV---GQP-QGVTVVILDDND 373
Cdd:PRK09192 330 --DKAF----MPSYGLAEAtlavsfsplgsgivveevdrdrlEYQGKAVAPGAETRRVRTFvncGKAlPGHEIEIRNEAG 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 374 NVLPPGKVGEVSIRGENVTLGYANNPKANKEnfTKRENYFRTGDQGYFDpEGFLVLTGRIKELINRGGEKISPIELDGIM 453
Cdd:PRK09192 404 MPLPERVVGHICVRGPSLMSGYFRDEESQDV--LAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIEWIA 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 454 LSHPKID--EAVAFGVPDDMYGQVVqAAIVLKKGEKMTYEELVNFLKKHL-ASFKIPTKVYFV--DKLPKTATGKIQR 526
Cdd:PRK09192 481 EQEPELRsgDAAAFSIAQENGEKIV-LLVQCRISDEERRGQLIHALAALVrSEFGVEAAVELVppHSLPRTSSGKLSR 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
190-526 |
6.42e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVV--MPLFHVHGLIGVLLSTFRTQGSVVVpdgFHP 267
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVswLPLYHDMGLIGGLLQPIFSGVPCVL---MSP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 268 KLFWDQFVKyncnWFSCVP----TISmimlnmPKPNpFPHirfiRSCSSALAPATFHKLE-------------------- 323
Cdd:PRK05691 244 AYFLERPLR----WLEAISeyggTIS------GGPD-FAY----RLCSERVSESALERLDlsrwrvaysgsepirqdsle 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 324 ---KEFNA------PVLEAYAMTEAS-------------------HQMTSNNLPPGKRKP-GTVGQPQ-GVTVVILDDND 373
Cdd:PRK05691 309 rfaEKFAAcgfdpdSFFASYGLAEATlfvsggrrgqgipaleldaEALARNRAEPGTGSVlMSCGRSQpGHAVLIVDPQS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 374 -NVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR--ENYFRTGDQGyFDPEGFLVLTGRIKELINRGGEKISPIELD 450
Cdd:PRK05691 389 lEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHdgRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 451 GIMLSHPKI---DEAVAFGVPDD-MYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASF--KIPTKVYFVD--KLPKTATG 522
Cdd:PRK05691 468 KTVEREVEVvrkGRVAAFAVNHQgEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEAcqEAPSVVLLLNpgALPKTSSG 547
|
....
gi 398365585 523 KIQR 526
Cdd:PRK05691 548 KLQR 551
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
367-530 |
9.55e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 74.01 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 367 VILDDNDNVLPPGKVGEVSIR----GENVTLGYANNPKAnKENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGE 442
Cdd:PTZ00237 445 SILSEDGKELNVNEIGEVAFKlpmpPSFATTFYKNDEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGN 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 443 KISPIELDGIMLSHPKIDEAVAFGVPD-DMYGQVVqAAIVLKKGEKMTY-------EELVNFLKKHLASFKIPTKVYFVD 514
Cdd:PTZ00237 524 KVQLNTIETSILKHPLVLECCSIGIYDpDCYNVPI-GLLVLKQDQSNQSidlnklkNEINNIITQDIESLAVLRKIIIVN 602
|
170
....*....|....*.
gi 398365585 515 KLPKTATGKIQRRVIA 530
Cdd:PTZ00237 603 QLPKTKTGKIPRQIIS 618
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
187-448 |
2.06e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 72.82 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRT------QGSVV 260
Cdd:PLN02736 219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGvavgfyQGDNL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 261 ----------------VP-------DGFH----------PKLFwdqFVKYNC------NWFSCVPTISMIMLNMPKPNPF 301
Cdd:PLN02736 299 klmddlaalrptifcsVPrlynriyDGITnavkesgglkERLF---NAAYNAkkqaleNGKNPSPMWDRLVFNKIKAKLG 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 302 PHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNlpPGKRKPGTVGQPQGVTVVILDD--------ND 373
Cdd:PLN02736 376 GRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMD--EGDNLSGHVGSPNPACEVKLVDvpemnytsED 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365585 374 NVLPPgkvGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELINRG-GEKISP--IE 448
Cdd:PLN02736 454 QPYPR---GEICVRGPIIFKGYYKDEVQTREVIDE-DGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPekIE 527
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
303-527 |
3.63e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.89 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 303 HIRFIRScssALAPATFhklekeFNApvleaYAMTEAShQMTSNNLPPGKRKPGTVGQPQGVTV-----VILDDNDNVLP 377
Cdd:PRK05691 2464 HLQRIRQ---AFAPQLF------FNA-----YGPTETV-VMPLACLAPEQLEEGAASVPIGRVVgarvaYILDADLALVP 2528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 378 PGKVGEVSIRGENVTLGYANNPKANKENF------TKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDG 451
Cdd:PRK05691 2529 QGATGELYVGGAGLAQGYHDRPGLTAERFvadpfaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIES 2608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 452 IMLSHPKIDEAV--AFGVPD--DMYGQVVQAAIVLKKGEKMTYEELVN-FLKKHLASFKIPTKVYFVDKLPKTATGKIQR 526
Cdd:PRK05691 2609 RLLEHPAVREAVvlALDTPSgkQLAGYLVSAVAGQDDEAQAALREALKaHLKQQLPDYMVPAHLILLDSLPLTANGKLDR 2688
|
.
gi 398365585 527 R 527
Cdd:PRK05691 2689 R 2689
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
183-543 |
4.72e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 71.39 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 183 PGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIgVLLSTFRTQGSVVVP 262
Cdd:PLN03051 113 PVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPW-LLYSAFLNGATLALY 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 263 DGFHPKLFWDQFVK-YNCNWFSCVPTI-----SMIMLNMPKPNpFPHIRFIRSCSSALAPATFHKL--EKEFNAPVLEAY 334
Cdd:PLN03051 192 GGAPLGRGFGKFVQdAGVTVLGLVPSIvkawrHTGAFAMEGLD-WSKLRVFASTGEASAVDDVLWLssVRGYYKPVIEYC 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 335 AMTE-ASHQMTSNNLPPgkRKPGTVGQPQ-GVTVVILDDNDNVLPPGK--VGEVSIRgeNVTLGyANNPKANKENftkRE 410
Cdd:PLN03051 271 GGTElASGYISSTLLQP--QAPGAFSTASlGTRFVLLNDNGVPYPDDQpcVGEVALA--PPMLG-ASDRLLNADH---DK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 411 NYF--------------RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELD-GIMLSHPKIDEAVAFGV------PD 469
Cdd:PLN03051 343 VYYkgmpmygskgmplrRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIErACDRAVAGIAETAAVGVappdggPE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 470 DMYgqVVQAAIVLKKG-EKMTYEELVNFLKKHLAS-----FKIpTKVYFVDKLPKTATGKIQRRVIAETFAKSSRNKSKL 543
Cdd:PLN03051 423 LLV--IFLVLGEEKKGfDQARPEALQKKFQEAIQTnlnplFKV-SRVKIVPELPRNASNKLLRRVLRDQLKKELSGRSKL 499
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
184-527 |
4.80e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 72.00 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 184 GFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDR-------SYVV------MPLfhvhgLIGVLL 250
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVvlqktpcSFDVsvweffWPF-----IAGAKL 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 251 stfrtqgsVVVPDGFH--PKLFWDQFVKYNCNWFSCVPtiSMIMLNMPKPNPFPHIRFIRS-----CSSALAPAT----F 319
Cdd:PRK10252 668 --------VMAEPEAHrdPLAMQQFFAEYGVTTTHFVP--SMLAAFVASLTPEGARQSCASlrqvfCSGEALPADlcreW 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 320 HKLekeFNAPVLEAYAMTEAS-------------HQMTSNNLPpgkrkpgtVGQPQGVT-VVILDDNDNVLPPGKVGEVS 385
Cdd:PRK10252 738 QQL---TGAPLHNLYGPTEAAvdvswypafgeelAAVRGSSVP--------IGYPVWNTgLRILDARMRPVPPGVAGDLY 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 386 IRGENVTLGYANNPKANKENFTKR-----ENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKID 460
Cdd:PRK10252 807 LTGIQLAQGYLGRPDLTASRFIADpfapgERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVE 886
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365585 461 EAVA----FGVPDDMYGQVVQ--AAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRR 527
Cdd:PRK10252 887 QAVThacvINQAAATGGDARQlvGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRK 959
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
173-534 |
1.50e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 70.15 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 173 KFVNTNPVKfPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTY-KLTPLDRSYVVMPLFHVHGL------ 245
Cdd:PLN02387 235 KLGKENPVD-PDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELaaesvm 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 246 ------IG-----VLLST-----FRTQGSV---------VVP-----------------DGFHPKLF----WDQFVKYNC 279
Cdd:PLN02387 314 aavgaaIGygsplTLTDTsnkikKGTKGDAsalkptlmtAVPaildrvrdgvrkkvdakGGLAKKLFdiayKRRLAAIEG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 280 NWFSCVPTISMI--MLNMPKPNPF--PHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNlpPGKRKP 355
Cdd:PLN02387 394 SWFGAWGLEKLLwdALVFKKIRAVlgGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSE--WDDTSV 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 356 GTVGQPQGVTVVILDD--------NDNVLPPGkvgEVSIRGENVTLGYANNPKANKENFTKREN---YFRTGDQGYFDPE 424
Cdd:PLN02387 472 GRVGPPLPCCYVKLVSweeggyliSDKPMPRG---EIVIGGPSVTLGYFKNQEKTDEVYKVDERgmrWFYTGDIGQFHPD 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 425 GFLVLTGRIKELIN-RGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMY--GQVVQAAIVLKKGEK---MTYEELVNFLK 498
Cdd:PLN02387 549 GCLEIIDRKKDIVKlQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYcvALVVPSQQALEKWAKkagIDYSNFAELCE 628
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 499 K------------------HLASFKIPTKVYFVDKL--PK----TATGKIQRRVIAETFA 534
Cdd:PLN02387 629 KeeavkevqqslskaakaaRLEKFEIPAKIKLLPEPwtPEsglvTAALKLKREQIRKKFK 688
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
191-435 |
1.38e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 66.99 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 191 VALILHTSGTTSTPKTVPLLHlnivRS-TLNIANTYKLTPLDRSYVV------MPLFHV----HGLIGVLLS--TFRTQG 257
Cdd:PRK12582 222 VAKYLFTSGSTGMPKAVINTQ----RMmCANIAMQEQLRPREPDPPPpvsldwMPWNHTmggnANFNGLLWGggTLYIDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 258 SVVVPDGFHPKLfwdqfvkynCNWFSCVPTI--------SMIMLNMPK-----PNPFPHIRFIRSCSSALAPATFHKLEK 324
Cdd:PRK12582 298 GKPLPGMFEETI---------RNLREISPTVygnvpagyAMLAEAMEKddalrRSFFKNLRLMAYGGATLSDDLYERMQA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 325 EFNA------PVLEAYAMTEASHQMTSNNLPPgkRKPGTVGQP-QGVTVvilddndNVLPPGKVGEVSIRGENVTLGYAN 397
Cdd:PRK12582 369 LAVRttghriPFYTGYGATETAPTTTGTHWDT--ERVGLIGLPlPGVEL-------KLAPVGDKYEVRVKGPNVTPGYHK 439
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 398365585 398 NPKANKENFTKrENYFRTGDQGYF----DPEGFLVLTGRIKE 435
Cdd:PRK12582 440 DPELTAAAFDE-EGFYRLGDAARFvdpdDPEKGLIFDGRVAE 480
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
190-535 |
2.89e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 66.15 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANtyKLTPL------DRSYVV-MPLFHVHGLIgvLLSTFRTQGSVVvp 262
Cdd:PTZ00216 265 DLALIMYTSGTTGDPKGVMHTHGSLTAGILALED--RLNDLigppeeDETYCSyLPLAHIMEFG--VTNIFLARGALI-- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 263 dGF-HPKLFWDQFVK-------YNCNWFSCVPTI-SMIMLNM----PKPNP-----FPH--------------------- 303
Cdd:PTZ00216 339 -GFgSPRTLTDTFARphgdlteFRPVFLIGVPRIfDTIKKAVeaklPPVGSlkrrvFDHayqsrlralkegkdtpywnek 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 304 ------------IRFIRSCSSALAPATfhkleKEF-N---APVLEAYAMTE----ASHQMTsnnlppGKRKPGTVGQP-Q 362
Cdd:PTZ00216 418 vfsapravlggrVRAMLSGGGPLSAAT-----QEFvNvvfGMVIQGWGLTEtvccGGIQRT------GDLEPNAVGQLlK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 363 GVTVVILDDND--NVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKrENYFRTGDQGYFDPEGFLVLTGRIKELI-NR 439
Cdd:PTZ00216 487 GVEMKLLDTEEykHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDE-DGWFHTGDVGSIAANGTLRIIGRVKALAkNC 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 440 GGEKISPIELDGIMLSHPKIdeaVAFGV-----PDDMYgqvvQAAIVL-----------KKGEKMTYEELVN---FLKKH 500
Cdd:PTZ00216 566 LGEYIALEALEALYGQNELV---VPNGVcvlvhPARSY----ICALVLtdeakamafakEHGIEGEYPAILKdpeFQKKA 638
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 398365585 501 LAS------------FKIPTKVYFVDK--LPK----TATGKIQRRVIAETFAK 535
Cdd:PTZ00216 639 TESlqetaraagrksFEIVRHVRVLSDewTPEngvlTAAMKLKRRVIDERYAD 691
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
197-526 |
5.99e-10 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 61.76 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 197 TSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFrTQGSVVVP---DGFHPKLFWDQ 273
Cdd:cd17647 117 TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLF-LGAQLLVPtqdDIGTPGRLAEW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 274 FVKYNCNWFSCVPTISMImLNMPKPNPFP---HIRFI------RSCSS--ALAPatfhklekefNAPVLEAYAMTEASHQ 342
Cdd:cd17647 196 MAKYGATVTHLTPAMGQL-LTAQATTPFPklhHAFFVgdiltkRDCLRlqTLAE----------NVRIVNMYGTTETQRA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 343 MTSNNLPPGKRKPGTVGQ-----PQG-----VTVVILDDND--NVLPPGKVGEVSIRGENVTLGYANNPKANKENFTK-- 408
Cdd:cd17647 265 VSYFEVPSRSSDPTFLKNlkdvmPAGrgmlnVQLLVVNRNDrtQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNnw 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 409 -------------------------RENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDE-- 461
Cdd:cd17647 345 fvepdhwnyldkdnnepwrqfwlgpRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREni 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 462 ------------AVAFGVPDDMYGQVVQAAIVLKKGEKMT---------YEELVN----FLKKHLASFKIPTKVYFVDKL 516
Cdd:cd17647 425 tlvrrdkdeeptLVSYIVPRFDKPDDESFAQEDVPKEVSTdpivkgligYRKLIKdireFLKKRLASYAIPSLIVVLDKL 504
|
410
....*....|
gi 398365585 517 PKTATGKIQR 526
Cdd:cd17647 505 PLNPNGKVDK 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
368-527 |
8.33e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.11 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 368 ILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR------ENYFRTGDQGYFDPEGFLVLTGRIKELINRGG 441
Cdd:PRK05691 4053 LLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHpfgapgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRG 4132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 442 EKISPIELDGIMLSHPKIDEAvAFGVPDDMYGQV-----VQAAIVLKKGEKMtyEELVNFLKKHLASFKIPTKVYFVDKL 516
Cdd:PRK05691 4133 YRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHlvgylVPHQTVLAQGALL--ERIKQRLRAELPDYMVPLHWLWLDRL 4209
|
170
....*....|.
gi 398365585 517 PKTATGKIQRR 527
Cdd:PRK05691 4210 PLNANGKLDRK 4220
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
381-526 |
2.21e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.78 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 381 VGEVSIRGENVTLGYANNPKankenfTKRENYFRTGDQGYFDPEGfLVLTGRIKELINRGGEKISPIELDGIMLSHPKID 460
Cdd:PRK05851 372 IGEIEIRGASMMSGYLGQAP------IDPDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVR 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365585 461 EA--VAFGVPDDMYGQ-VVQAAIVLKKGEKMTYEELVnflkKHLASF--KIPTKVYFVD--KLPKTATGKIQR 526
Cdd:PRK05851 445 EGavVAVGTGEGSARPgLVIAAEFRGPDEAGARSEVV----QRVASEcgVVPSDVVFVApgSLPRTSSGKLRR 513
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
356-543 |
2.24e-09 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 60.09 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 356 GTVGQPQ----------GVTVVILDDNDNVLP---PGkVGEV----SIRGENVTLGYANNPKAnkenftkrenYF----- 413
Cdd:PLN03052 516 GSLLQPQafaafstpamGCKLFILDDSGNPYPddaPC-TGELalfpLMFGASSTLLNADHYKV----------YFkgmpv 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 414 -------RTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIM-LSHPKIDEAVAFGVPDDMYG--QVVQAAiVLK 483
Cdd:PLN03052 585 fngkilrRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpeQLVIAA-VLK 663
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365585 484 KGEKMTY--EELVNFLKKHLAS-----FKIpTKVYFVDKLPKTATGKIQRRVIAETFAKSSrNKSKL 543
Cdd:PLN03052 664 DPPGSNPdlNELKKIFNSAIQKklnplFKV-SAVVIVPSFPRTASNKVMRRVLRQQLAQEL-SRSKL 728
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
190-435 |
3.18e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 59.37 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVV--MPLFHVHG---LIGVLL---STFRTQGSVVV 261
Cdd:cd05921 166 TVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVdwLPWNHTFGgnhNFNLVLyngGTLYIDDGKPM 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 262 PDGFHPKLfwDQFVKYNCNWFSCVPT-ISMIMLNMPKPNP-----FPHIRFIRSCSSALAPATFHKL------EKEFNAP 329
Cdd:cd05921 246 PGGFEETL--RNLREISPTVYFNVPAgWEMLVAALEKDEAlrrrfFKRLKLMFYAGAGLSQDVWDRLqalavaTVGERIP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 330 VLEAYAMTEASHQMTSNNLPpgKRKPGTVGQP-QGVTVvilddndNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTK 408
Cdd:cd05921 324 MMAGLGATETAPTATFTHWP--TERSGLIGLPaPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDE 394
|
250 260 270
....*....|....*....|....*....|.
gi 398365585 409 rENYFRTGDQGYF----DPEGFLVLTGRIKE 435
Cdd:cd05921 395 -EGFYCLGDAAKLadpdDPAKGLVFDGRVAE 424
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
334-540 |
9.49e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 57.57 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 334 YAMTEASHQMTSnnlppgKR---KPGtVGQP-QGVTVVILDDndnvlppgkvgEVSIRGENVTLGYANNPKANKenFTKR 409
Cdd:PRK09029 271 YGLTEMASTVCA------KRadgLAG-VGSPlPGREVKLVDG-----------EIWLRGASLALGYWRQGQLVP--LVND 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 410 ENYFRTGDQGYFDpEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQ----VVQAAivlkkg 485
Cdd:PRK09029 331 EGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQrpvaVVESD------ 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 486 EKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKSSRNK 540
Cdd:PRK09029 404 SEAAVVNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALKEWVAQQLGNN 458
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
379-524 |
3.09e-08 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 56.61 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 379 GKVGEVSIRGENVTLGYANNPKANKENFTK--------------------RENYF-------RTGDQGYFDPEGFLVLTG 431
Cdd:TIGR03443 619 GEVGEIYVRAGGLAEGYLGLPELNAEKFVNnwfvdpshwidldkennkpeREFWLgprdrlyRTGDLGRYLPDGNVECCG 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 432 RIKELINRGGEKISPIELDGIMLSHPKIDEAV--------------AFGVP----------------DDMYGQVVQAaiv 481
Cdd:TIGR03443 699 RADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlvrrdkdeeptlvSYIVPqdksdeleefksevddEESSDPVVKG--- 775
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365585 482 LKKGEKMTyEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:TIGR03443 776 LIKYRKLI-KDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
367-479 |
1.65e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 53.98 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 367 VILDDN-DNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKR-----------------ENYFRTGDQG-YFDPEgfL 427
Cdd:PRK12476 414 VIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKlqsrlaegshadgaaddGTWLRTGDLGvYLDGE--L 491
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 398365585 428 VLTGRIKELINRGGEKISPIELDG-IMLSHPKIDE--AVAFGVPDDMYGQVVQAA 479
Cdd:PRK12476 492 YITGRIADLIVIDGRNHYPQDIEAtVAEASPMVRRgyVTAFTVPAEDNERLVIVA 546
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
187-503 |
1.77e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 54.05 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 187 RSSDVALILHTSGTTSTPKTVPLLHLN---IVRSTLNIANTY--KLTPLDRSYVVMPLFHV------------------- 242
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFedKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyy 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 243 HGLIGVL---LSTFRTQGSVVVPDGFHP----------------KLFWDQFVKYNCNWFS-------CVPTISMIMLNMP 296
Cdd:PLN02430 298 HGDLNALrddLMELKPTLLAGVPRVFERihegiqkalqelnprrRLIFNALYKYKLAWMNrgyshkkASPMADFLAFRKV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 297 KPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEaSHQMTSNNLPPGKRKPGTVGQPQGVTVVILDD----N 372
Cdd:PLN02430 378 KAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTE-TLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEvpemG 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 373 DNVLPPGKVGEVSIRGENVTLGYANNPKANKEnfTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRG-GEKISPIELDG 451
Cdd:PLN02430 457 YDPLGEPPRGEICVRGKCLFSGYYKNPELTEE--VMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLEN 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365585 452 IMLSHPKIDEAVAFGvpdDMYGQVVQAAIVLKK----------GEKMTYEELVNF--LKKHLAS 503
Cdd:PLN02430 535 VYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEentnkwakdnGFTGSFEELCSLpeLKEHILS 595
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
190-435 |
3.18e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 52.96 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 190 DVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYklTPLDRSYVVM----PLFHVHG---LIGVLLstfRTQGSVVVP 262
Cdd:PRK08180 210 TIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF--PFLAEEPPVLvdwlPWNHTFGgnhNLGIVL---YNGGTLYID 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 263 DGF-HPKLFwDQFVKyncNWFSCVPTISmimLNMPK----------------PNPFPHIRFIRSCSSALAPATFHKLEKE 325
Cdd:PRK08180 285 DGKpTPGGF-DETLR---NLREISPTVY---FNVPKgwemlvpalerdaalrRRFFSRLKLLFYAGAALSQDVWDRLDRV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 326 FNA------PVLEAYAMTEASHQMTSNNLPPGKrkPGTVGQP-QGVTVVILDDNDNVlppgkvgEVSIRGENVTLGYANN 398
Cdd:PRK08180 358 AEAtcgeriRMMTGLGMTETAPSATFTTGPLSR--AGNIGLPaPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRA 428
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 398365585 399 PKANKENFtKRENYFRTGDQGYF----DPEGFLVLTGRIKE 435
Cdd:PRK08180 429 PELTAEAF-DEEGYYRSGDAVRFvdpaDPERGLMFDGRIAE 468
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
363-530 |
8.63e-07 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 51.89 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 363 GVTVVILDDNDNVLPpGKVGE-VSIRGE-NVTLGYANNPKANKEN---FTKRENYFRTGDQGYFDPEGFLVLTGRIKELI 437
Cdd:cd05943 432 GMAVEAFDEEGKPVW-GEKGElVCTKPFpSMPVGFWNDPDGSRYRaayFAKYPGVWAHGDWIEITPRGGVVILGRSDGTL 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 438 NRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTyEELVNFLKKHLAS----FKIPTKVYFV 513
Cdd:cd05943 511 NPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELD-DELRKRIRSTIRSalspRHVPAKIIAV 589
|
170 180
....*....|....*....|.
gi 398365585 514 DKLPKTATGKIQ----RRVIA 530
Cdd:cd05943 590 PDIPRTLSGKKVevavKKIIA 610
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
179-466 |
1.15e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 51.56 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 179 PVKFPgfarsSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYK-----LTPLDRSYVVMPLFHVHGLI------- 246
Cdd:PLN02614 218 PIKKK-----SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIFDRVieecfiq 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 247 -GVLLSTFRTQGSVVVPD------------------------------GFHPKLFWDQFVKYNCNWF-------SCVPTI 288
Cdd:PLN02614 293 hGAAIGFWRGDVKLLIEDlgelkptifcavprvldrvysglqkklsdgGFLKKFVFDSAFSYKFGNMkkgqshvEASPLC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 289 SMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEaSHQMTSNNLPPGKRKPGTVGQPQGVTVVI 368
Cdd:PLN02614 373 DKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTE-SCAGTFVSLPDELDMLGTVGPPVPNVDIR 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 369 LDD----NDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTkrENYFRTGDQGYFDPEGFLVLTGRIKELINRG-GEK 443
Cdd:PLN02614 452 LESvpemEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLI--DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSqGEY 529
|
330 340
....*....|....*....|...
gi 398365585 444 ISPIELDGIMLSHPKIDEAVAFG 466
Cdd:PLN02614 530 VAVENIENIYGEVQAVDSVWVYG 552
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
135-524 |
6.19e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 48.62 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 135 GCFIVELAFdatrfrVEYDIYSPEDNYKRVI-----YRSLNNaKFVNTNPVKFPGFARSSDV------ALILHTSGTTST 203
Cdd:cd17654 60 AILFLGAAY------APIDPASPEQRSLTVMkkchvSYLLQN-KELDNAPLSFTPEHRHFNIrtdeclAYVIHTSGTTGT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 204 PKTVPLLHLNIVRSTLNIANTYKLTPlDRSYVVMPLFHVHGLIGVLLSTFRTQGS-VVVPDGFH--PKLFWDQ-FVKYNC 279
Cdd:cd17654 133 PKIVAVPHKCILPNIQHFRSLFNITS-EDILFLTSPLTFDPSVVEIFLSLSSGATlLIVPTSVKvlPSKLADIlFKRHRI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 280 NWFSCVPTISmimlnmpkpNPFP---HIRFIRSCSSALAPATF-----------HKLEKEFN-APVLEAYAMTEASHQMT 344
Cdd:cd17654 212 TVLQATPTLF---------RRFGsqsIKSTVLSATSSLRVLALggepfpslvilSSWRGKGNrTRIFNIYGITEVSCWAL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 345 SNNLPPGKrKPGTVGQPQGVTVVILDDNDNvlpPGKVGEVSIRGEN---VTLGYANNPKANkenftkrenYFRTGD---- 417
Cdd:cd17654 283 AYKVPEED-SPVQLGSPLLGTVIEVRDQNG---SEGTGQVFLGGLNrvcILDDEVTVPKGT---------MRATGDfvtv 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365585 418 QgyfdpEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIdEAVAFGVPDDmygQVVQAAIVLKKGEKMTYEELVNFL 497
Cdd:cd17654 350 K-----DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESSSSRIHKELQLTL 420
|
410 420
....*....|....*....|....*..
gi 398365585 498 kkhLASFKIPTKVYFVDKLPKTATGKI 524
Cdd:cd17654 421 ---LSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| |
