|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
45-513 |
0e+00 |
|
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: 891.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 45 VPEEFNFASYVLDYWAQKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEW 124
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 125 WLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKLLVSDHSREGWLDFRSLVK 204
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 205 SASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWT 284
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 285 AGCTVFIHHLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLY 364
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 365 ENYGQSETG-------------------------------------------------------------DPEKTAKVEC 383
Cdd:cd05928 321 EGYGQTETGlicanfkgmkikpgsmgkasppydvqiiddngnvlppgtegdigirvkpirpfglfsgyvdNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSH 463
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 578828477 464 DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKET 513
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
39-515 |
1.53e-154 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 452.26 E-value: 1.53e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 39 RWNdyeVPEEFNFASYVLDYWAQKekegkRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALML 118
Cdd:COG0365 1 RWF---VGGRLNIAYNCLDRHAEG-----RGDKVALIWEGEDGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 119 PRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDA---------LASEVDSIASQCPSLKTKLLV- 188
Cdd:COG0365 72 PNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 189 ---SDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH-GLALQPSFPGSRKLRsLKTSDVSW 264
Cdd:COG0365 152 rtgADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHgGYLVHAATTAKYVLD-LKPGDVFW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 265 CLSDSGWIVATIWTLVEPWTAGCTVFIHH-LPQF-DTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIR---FPALEH 339
Cdd:COG0365 231 CTADIGWATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkydLSSLRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 340 CYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG---------------------------------------------- 373
Cdd:COG0365 311 LGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGgifisnlpglpvkpgsmgkpvpgydvavvdedgnpvppgeegelvi 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -------------DPEKTAKV---ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESA 437
Cdd:COG0365 391 kgpwpgmfrgywnDPERYRETyfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828477 438 VVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 515
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGV--EPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
86-510 |
8.19e-152 |
|
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: 440.62 E-value: 8.19e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 86 WSFREMGDLTRRVANVFTQtCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTI 165
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 166 DAlasevdsiasqcpslktkllvsdhsregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHSHGLALQ 245
Cdd:cd05972 80 AE---------------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 246 pSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVIIQTLLKYPINHFWGVSSIYRMIL 325
Cdd:cd05972 109 -HIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 326 QQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG-------------------------------- 373
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGltvgnfpdmpvkpgsmgrptpgydvaiidddg 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 --------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESAL 427
Cdd:cd05972 268 relppgeegdiaiklpppglflgyvgDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 428 VEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKE 507
Cdd:cd05972 348 LEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVE 425
|
...
gi 578828477 508 LRK 510
Cdd:cd05972 426 LRD 428
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
45-512 |
3.79e-140 |
|
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: 414.59 E-value: 3.79e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 45 VPEEFNFASYVLDYWAQKEKEgkrgpNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEW 124
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEYPD-----KLALVWCDDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 125 WLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTI--DALASEVDSIASQCPSLKTKLLVSDHSREGWLDFRSL 202
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 203 VKSASPE----HTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRkLRSLKTSDVSWCLSDSGWIVATIWT 278
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKY-WQNVREGGLHLTVADTGWGKAVWGK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 279 LVEPWTAGCTVFIHHLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRR 358
Cdd:cd05970 245 IYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 359 TGLLLYENYGQSET-------------------------------------------------------------GDPEK 377
Cdd:cd05970 325 TGIKLMEGFGQTETtltiatfpwmepkpgsmgkpapgyeidlidregrsceageegeivirtskgkpvglfggyyKDAEK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 378 TAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLT 457
Cdd:cd05970 405 TAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLA 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 578828477 458 PQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 512
Cdd:cd05970 485 KGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-510 |
1.80e-94 |
|
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: 294.41 E-value: 1.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKG 161
Cdd:COG0318 21 GGRRLTYAELDARARRLAAAL-RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 IVTIdalasevdsiasqcpslktkllvsdhsregwldfrslvksaspehtcvksktldpmVIFFTSGTTGFPKMAKHSHG 241
Cdd:COG0318 100 LVTA--------------------------------------------------------LILYTSGTTGRPKGVMLTHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 ------LALQPSFPGSRKLRSLktsdvsWCLS---DSGWIVATIWtlvePWTAGCTVFIhhLPQFDTKVIIQTLLKYPIN 312
Cdd:COG0318 124 nllanaAAIAAALGLTPGDVVL------VALPlfhVFGLTVGLLA----PLLAGATLVL--LPRFDPERVLELIERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 313 HFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG------------------ 373
Cdd:COG0318 192 VLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSpvvtvnpedpgerrpgsv 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ----------------------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINA 413
Cdd:COG0318 272 grplpgvevrivdedgrelppgevgeivvrgpnvmkgywnDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 414 SGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVS 493
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRP-----GAELDAEELRAFLRERLARYKVPRRVEFVD 426
|
490
....*....|....*..
gi 578828477 494 ELPKTITGKIERKELRK 510
Cdd:COG0318 427 ELPRTASGKIDRRALRE 443
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
36-514 |
1.75e-93 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 295.65 E-value: 1.75e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 36 GAPRWNDYE----------VPEEF--------NFASYVLDYWAqkekEGKRGPNPAFWWVNGQGDEvKWSFREMGDLTRR 97
Cdd:PRK04319 11 GEPNLKDYEetyatfsweeVEKEFswletgkvNIAYEAIDRHA----DGGRKDKVALRYLDASRKE-KYTYKELKELSNK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 98 VANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPatiLLKA---KDILYRLQLSKAKGIVTIDALASEVds 174
Cdd:PRK04319 86 FANVL-KELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGP---LFEAfmeEAVRDRLEDSEAKVLITTPALLERK-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 175 IASQCPSLKTKLLVSDHSR--EGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSR 252
Cdd:PRK04319 160 PADDLPSLKHVLLVGEDVEegPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 253 KLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHlPQFDTKVIIQTLLKYPINHFWGVSSIYRMIL------- 325
Cdd:PRK04319 240 VL-DLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDG-GRFSPERWYRILEDYKVTVWYTAPTAIRMLMgagddlv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 326 -QQDFTSIRFPAlehcyTGGEvvlPKDQE--EWKRRT-GLLLYENYGQSETG---------------------------- 373
Cdd:PRK04319 318 kKYDLSSLRHIL-----SVGE---PLNPEvvRWGMKVfGLPIHDNWWMTETGgimianypamdikpgsmgkplpgieaai 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -------------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAE 422
Cdd:PRK04319 390 vddqgnelppnrmgnlaikkgwpsmmrgiwnNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 423 VESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 502
Cdd:PRK04319 470 VESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY--EPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGK 547
|
570
....*....|..
gi 578828477 503 IERKELRKKETG 514
Cdd:PRK04319 548 IMRRVLKAWELG 559
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
67-509 |
4.47e-86 |
|
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: 273.28 E-value: 4.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 67 KRGPNPAFWWvngqgDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLK 146
Cdd:cd05936 11 RFPDKTALIF-----MGRKLTYRELDALAEAFAAGL-QNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 147 AKDILYRLQLSKAKGIVTIdalasevdsiasqcpslktkllvsdhsregwLDFRSLVKSASPEHTCVKSKTLDPMVIFFT 226
Cdd:cd05936 85 PRELEHILNDSGAKALIVA-------------------------------VSFTDLLAAGAPLGERVALTPEDVAVLQYT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 227 SGTTGFPKMAKHSHG------LALQPSFPGSRKLRslktsDVSWC---LSDS-GWIVAtiwtLVEPWTAGCTVFIhhLPQ 296
Cdd:cd05936 134 SGTTGVPKGAMLTHRnlvanaLQIKAWLEDLLEGD-----DVVLAalpLFHVfGLTVA----LLLPLALGATIVL--IPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 297 FDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSET--- 372
Cdd:cd05936 203 FRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspv 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ------------------------------------------------------GDPEKTAKVECGDFYNTGDRGKMDEE 398
Cdd:cd05936 283 vavnpldgprkpgsigiplpgtevkivdddgeelppgevgelwvrgpqvmkgywNRPEETAEAFVDGWLRTGDIGYMDED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 399 GYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflsHDKDQLTK-ELQQHVK 477
Cdd:cd05936 363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL------KEGASLTEeEIIAFCR 436
|
490 500 510
....*....|....*....|....*....|..
gi 578828477 478 SVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:cd05936 437 EQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-512 |
1.27e-84 |
|
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: 268.28 E-value: 1.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANvFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAkgivtid 166
Cdd:cd05974 2 SFAEMSARSSRVAN-FLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQcpslktkllvsdhsregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHSHGlalqp 246
Cdd:cd05974 74 VYAAVDENTHAD----------------------------------------DPMLLYFTSGTTSKPKLVEHTHR----- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 247 SFP----GSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVIIQTLLKYPINHFWGVSSIYR 322
Cdd:cd05974 109 SYPvghlSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 323 MILQQDFTSIRFPALEHCyTGGEVVLPKDQEEWKRRTGLLLYENYGQSET------------------------------ 372
Cdd:cd05974 189 MLIQQDLASFDVKLREVV-GAGEPLNPEVIEQVRRAWGLTIRDGYGQTETtalvgnspgqpvkagsmgrplpgyrvalld 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ----------------------------GDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVE 424
Cdd:cd05974 268 pdgapategevaldlgdtrpvglmkgyaGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 425 SALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVsELPKTITGKIE 504
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIR 424
|
....*...
gi 578828477 505 RKELRKKE 512
Cdd:cd05974 425 RVELRRRE 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
86-512 |
1.09e-82 |
|
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: 263.59 E-value: 1.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 86 WSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTI 165
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 166 dalasevdsiasqcPSLKTKLlvsdhsregwldfrslvksaSPEhtcvksktlDPMVIFFTSGTTGFPKMAKHSHGLALQ 245
Cdd:cd05969 80 --------------EELYERT--------------------DPE---------DPTLLHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 246 PSFPGSRKLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHlPQFDTKVIIQTLLKYPINHFWGVSSIYRMIL 325
Cdd:cd05969 117 YYFTGKYVL-DLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 326 --------QQDFTSIRFPAlehcyTGGEVVLPkDQEEWKRRT-GLLLYENYGQSETG----------------------- 373
Cdd:cd05969 195 kegdelarKYDLSSLRFIH-----SVGEPLNP-EAIRWGMEVfGVPIHDTWWQTETGsimianypcmpikpgsmgkplpg 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ------------------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYR 417
Cdd:cd05969 269 vkaavvdengnelppgtkgilalkpgwpsmfrgiwnDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 418 IGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKdqLTKELQQHVKSVTAPYKYPRKVEFVSELPK 497
Cdd:cd05969 349 VGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE--LKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|....*
gi 578828477 498 TITGKIERKELRKKE 512
Cdd:cd05969 427 TRSGKIMRRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-509 |
1.04e-81 |
|
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: 260.83 E-value: 1.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 80 QGDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKA 159
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTiDAlasevdsiasqcpslktkllvSDhsregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHS 239
Cdd:cd05971 80 SALVT-DG---------------------SD----------------------------DPALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 240 HGLAL---------QPSFPgsrklrslKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVIIQTLLKYP 310
Cdd:cd05971 110 HRVLLghlpgvqfpFNLFP--------RDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 311 INHFWGVSSIYRMILQQDFTSIRFP-ALEHCYTGGEvvlPKDQEE--WKRRT-GLLLYENYGQSETG------------- 373
Cdd:cd05971 182 VTTAFLPPTALKMMRQQGEQLKHAQvKLRAIATGGE---SLGEELlgWAREQfGVEVNEFYGQTECNlvigncsalfpik 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ----------------------------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRS 407
Cdd:cd05971 259 pgsmgkpipghrvaivddngtplppgevgeiavelpdpvaflgywnNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 408 DDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLshDKDQLTKELQQHVKSVTAPYKYPR 487
Cdd:cd05971 339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPR 416
|
490 500
....*....|....*....|..
gi 578828477 488 KVEFVSELPKTITGKIERKELR 509
Cdd:cd05971 417 EIEFVNELPRTATGKIRRRELR 438
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
219-503 |
3.83e-78 |
|
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: 248.35 E-value: 3.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 219 DPMVIFFTSGTTGFPKMAKHSHGLALQpSFPGSRKLRSLKTSDVSWCLSDSGWIvATIWTLVEPWTAGCTVFIHhlPQFD 298
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 299 TKVIIQTLLKYPINHFWGVSSIYRMILQQD-FTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG---- 373
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtva 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ------------------------------------------------------DPEKTAKVECGDFYNTGDRGKMDEEG 399
Cdd:cd04433 157 tgppdddarkpgsvgrpvpgvevrivdpdggelppgeigelvvrgpsvmkgywnNPEATAAVDEDGWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 400 YICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQQHVKSV 479
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRAHVRER 311
|
330 340
....*....|....*....|....
gi 578828477 480 TAPYKYPRKVEFVSELPKTITGKI 503
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKI 335
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-510 |
1.22e-72 |
|
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: 237.42 E-value: 1.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANvFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:cd05973 2 TFGELRALSARFAN-ALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSiasqcpslktkllvsdhsregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHShgLALQP 246
Cdd:cd05973 81 ANRHKLDS--------------------------------------------DPFVMMFTSGTTGLPKGVPVP--LRALA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 247 SFPG-SRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPqFDTKVIIQTLLKYPINHFWGVSSIYRMIL 325
Cdd:cd05973 115 AFGAyLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 326 QQDFTSIRFPA--LEHCYTGGEVVLPkDQEEWKR-RTGLLLYENYGQSETG----------DPEKT-------------- 378
Cdd:cd05973 194 AAGAEVPARPKgrLRRVSSAGEPLTP-EVIRWFDaALGVPIHDHYGQTELGmvlanhhaleHPVHAgsagrampgwrvav 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 379 ---AKVEC--------------------------------GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEV 423
Cdd:cd05973 273 lddDGDELgpgepgrlaidiansplmwfrgyqlpdtpaidGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 424 ESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKI 503
Cdd:cd05973 353 ESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGH--EGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
....*..
gi 578828477 504 ERKELRK 510
Cdd:cd05973 431 QRFLLRR 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
82-511 |
2.33e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 236.24 E-value: 2.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQtCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKG 161
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 IVTIDALASEVDSIASQCPSLKTKLLVSDHSREG----WLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAK 237
Cdd:PRK06187 107 VLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 238 HSH-GLALQPsfPGSRKLRSLKTSDVSwclsdsgwIVAT------IWTL-VEPWTAGCTVFIHHlpQFDTKVIIQTLLKY 309
Cdd:PRK06187 187 LSHrNLFLHS--LAVCAWLKLSRDDVY--------LVIVpmfhvhAWGLpYLALMAGAKQVIPR--RFDPENLLDLIETE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 310 PINHFWGVSSIYRMILQ------QDFTSIRfpalEHCYtGGEVVLPKDQEEWKRRTGLLLYENYGQSETG---------- 373
Cdd:PRK06187 255 RVTFFFAVPTIWQMLLKaprayfVDFSSLR----LVIY-GGAALPPALLREFKEKFGIDLVQGYGMTETSpvvsvlpped 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ------------------------------------------------------DPEKTAKVECGDFYNTGDRGKMDEEG 399
Cdd:PRK06187 330 qlpgqwtkrrsagrplpgvearivdddgdelppdggevgeiivrgpwlmqgywnRPEATAETIDGGWLHTGDVGYIDEDG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 400 YICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflsHDKDQLT-KELQQHVKS 478
Cdd:PRK06187 410 YLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL------KPGATLDaKELRAFLRG 483
|
490 500 510
....*....|....*....|....*....|...
gi 578828477 479 VTAPYKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK06187 484 RLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
47-509 |
7.96e-67 |
|
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: 224.17 E-value: 7.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 47 EEFNFASYVLDywaqkEKEGKRGPNPAFWwvngqGDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWL 126
Cdd:cd05959 1 EKYNAATLVDL-----NLNEGRGDKTAFI-----DDAGSLTYAELEAEARRVAGAL-RALGVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 127 VAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKLLVSDHSRE--GWLDFRSLVK 204
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 205 SASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVswCLSdsgwiVATIW------- 277
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDV--CFS-----AAKLFfayglgn 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 278 TLVEPWTAGCTVFIhhLPQFDT-KVIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRFpalehCYTGGEVvLPK 350
Cdd:cd05959 223 SLTFPLSVGATTVL--MPERPTpAAVFKRIRRYRPTVFFGVPTLYAAMLaapnlpSRDLSSLRL-----CVSAGEA-LPA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 351 D-QEEWKRRTGLLLYENYGQSE-----------------TGDP------------------------------------- 375
Cdd:cd05959 295 EvGERWKARFGLDILDGIGSTEmlhiflsnrpgrvrygtTGKPvpgyevelrdedggdvadgepgelyvrgpssatmywn 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 376 --EKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 453
Cdd:cd05959 375 nrDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAF 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 578828477 454 IVLTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:cd05959 455 VVLRPGY--EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-503 |
1.09e-62 |
|
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: 210.93 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKg 161
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAK- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 iVTIDalasevdsiasqcpslktkllvsdhsregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHSHG 241
Cdd:cd17631 95 -VLFD----------------------------------------------------DLALLMYTSGTTGRPKGAMLTHR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 ------LALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWtlvepwtAGCTVFIhhLPQFDTKVIIQTLLKYPINHFW 315
Cdd:cd17631 122 nllwnaVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLL-------RGGTVVI--LRKFDPETVLDLIERHRVTSFF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 316 GVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSETG--------------------- 373
Cdd:cd17631 193 LVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpgvtflspedhrrklgsagrp 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -------------------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGY 416
Cdd:cd17631 272 vffvevrivdpdgrevppgevgeivvrgphvmagywnRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 417 RIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshdKDQLT-KELQQHVKSVTAPYKYPRKVEFVSEL 495
Cdd:cd17631 352 NVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP------GAELDeDELIAHCRERLARYKIPKSVEFVDAL 425
|
....*...
gi 578828477 496 PKTITGKI 503
Cdd:cd17631 426 PRNATGKI 433
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
52-515 |
4.31e-62 |
|
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: 213.96 E-value: 4.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 52 ASY-VLDYWAQKekegkRGPNPAFWWvngQGDEV----KWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWL 126
Cdd:cd05966 54 ISYnCLDRHLKE-----RGDKVAIIW---EGDEPdqsrTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 127 VAVGCMRTGIIFipaTILL---KAKDILYRLQLSKAKGIVTIDA---------LASEVDSIASQCPSLKTKLLVSDHSRE 194
Cdd:cd05966 125 AMLACARIGAVH---SVVFagfSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 195 GW------LDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHG-------LALQPSFpgsrklrSLKTSD 261
Cdd:cd05966 202 VPmtegrdLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGgyllyaaTTFKYVF-------DYHPDD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 262 VSWCLSDSGWIVATIWTLVEPWTAGCTVFIHH----LPQFDTKV-IIQtllKYPINHFWGVSSIYRMILQQ--------D 328
Cdd:cd05966 275 IYWCTADIGWITGHSYIVYGPLANGATTVMFEgtptYPDPGRYWdIVE---KHKVTIFYTAPTAIRALMKFgdewvkkhD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 329 FTSIRfpaleHCYTGGEvvlPKDQEEWKrrtglLLYENYG-----------QSETG------------------------ 373
Cdd:cd05966 352 LSSLR-----VLGSVGE---PINPEAWM-----WYYEVIGkercpivdtwwQTETGgimitplpgatplkpgsatrpffg 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -DP----EKTAKVE-------C-------------GD--------------FYNTGDRGKMDEEGYICFLGRSDDIINAS 414
Cdd:cd05966 419 iEPaildEEGNEVEgevegylVikrpwpgmartiyGDheryedtyfskfpgYYFTGDGARRDEDGYYWITGRVDDVINVS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 415 GYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSE 494
Cdd:cd05966 499 GHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGE--EPSDELRKELRKHVRKEIGPIATPDKIQFVPG 576
|
570 580
....*....|....*....|.
gi 578828477 495 LPKTITGKIERKELRKKETGQ 515
Cdd:cd05966 577 LPKTRSGKIMRRILRKIAAGE 597
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-511 |
2.76e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 209.38 E-value: 2.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKG 161
Cdd:PRK07656 27 GDQRLTYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 IVTIDALASEVDSIASQCPSLKTKLLV----SDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAK 237
Cdd:PRK07656 106 LFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 238 HSHG------------LALQPsfpGSRKLRSLKTSDVsWCLSdSGWIVATIwtlvepwtAGCTVFIHhlPQFDTKVIIQT 305
Cdd:PRK07656 186 LTHRqllsnaadwaeyLGLTE---GDRYLAANPFFHV-FGYK-AGVNAPLM--------RGATILPL--PVFDPDEVFRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 306 LLKYPINHFWGVSSIYRMILQQ------DFTSIRFpalehCYTGGEVV----LPKDQEEWKRRTGLllyENYGQSETG-- 373
Cdd:PRK07656 251 IETERITVLPGPPTMYNSLLQHpdrsaeDLSSLRL-----AVTGAASMpvalLERFESELGVDIVL---TGYGLSEASgv 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ---------------------------------------------------------DPEKTAKVECGD-FYNTGDRGKM 395
Cdd:PRK07656 323 ttfnrldddrktvagtigtaiagvenkivnelgeevpvgevgellvrgpnvmkgyydDPEATAAAIDADgWLHTGDLGRL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 396 DEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshdKDQLTKE-LQQ 474
Cdd:PRK07656 403 DEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKP------GAELTEEeLIA 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 578828477 475 HVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK07656 477 YCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
24-503 |
1.39e-60 |
|
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: 209.36 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 24 PSQLRCRSLSEFGAPRWNDYEvPEEFNFASYVLDYWAQKekegkRGPNPAFWWVNGQGDEVK-WSFREMGDLTRRVANVF 102
Cdd:cd17634 28 PYQKVKNTSFAPGAPSIKWFE-DATLNLAANALDRHLRE-----NGDRTAIIYEGDDTSQSRtISYRELHREVCRFAGTL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 103 tQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVT----------IDALASEV 172
Cdd:cd17634 102 -LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrsVPLKKNVD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 173 DSIASQCPSLKTKLLVSdhsREG---------WLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHG-- 241
Cdd:cd17634 181 DALNPNVTSVEHVIVLK---RTGsdidwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGgy 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 -LALQPSFpgsRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHH-LPQF-DTKVIIQTLLKYPINHFWGVS 318
Cdd:cd17634 258 lVYAATTM---KYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 319 SIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLL------LYENYGQSETG------------------- 373
Cdd:cd17634 335 TAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIgkekcpVVDTWWQTETGgfmitplpgaielkagsat 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -----------------------------------------DPEK---TAKVECGDFYNTGDRGKMDEEGYICFLGRSDD 409
Cdd:cd17634 415 rpvfgvqpavvdneghpqpggtegnlvitdpwpgqtrtlfgDHERfeqTYFSTFKGMYFSGDGARRDEDGYYWITGRSDD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 410 IINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLshDKDQLTKELQQHVKSVTAPYKYPRKV 489
Cdd:cd17634 495 VINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVV 572
|
570
....*....|....
gi 578828477 490 EFVSELPKTITGKI 503
Cdd:cd17634 573 HWVDSLPKTRSGKI 586
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
83-509 |
2.04e-58 |
|
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: 200.01 E-value: 2.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 83 EVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGI 162
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIDALaSEVDSIASqcpslktkllvsdhsregwldfrslvksaspehtcvksktldpmvIFFTSGTTGFPKMAKHSHGL 242
Cdd:cd05958 88 LCAHAL-TASDDICI---------------------------------------------LAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 243 ALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTKVIIQTLLKYPINHFWGVSSIYR 322
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 323 MIL------QQDFTSIRFpalehCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSE-----------------TGDP---- 375
Cdd:cd05958 200 AMLahpdaaGPDLSSLRK-----CVSAGEALPAALHRAWKEATGIPIIDGIGSTEmfhifisarpgdarpgaTGKPvpgy 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 376 --------------------------------EKTAKVECGDFYN-TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAE 422
Cdd:cd05958 275 eakvvddegnpvpdgtigrlavrgptgcrylaDKRQRTYVQGGWNiTGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 423 VESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLShdKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 502
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGK 432
|
....*..
gi 578828477 503 IERKELR 509
Cdd:cd05958 433 LQRFALR 439
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
47-510 |
2.53e-57 |
|
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: 198.52 E-value: 2.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 47 EEFNFASYVLDywaqKEKEGKRGPNPAFwwVNGQGdevKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWL 126
Cdd:TIGR02262 1 EKYNAAEDLLD----RNVVEGRGGKTAF--IDDIS---SLSYGELEAQVRRLAAAL-RRLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 127 VAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKLLVSDhSREGWLDFRSLVKSA 206
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 207 SPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVswCLSDSGWIVATIW--TLVEPWT 284
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDV--CFSAAKLFFAYGLgnALTFPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 285 AGCT-VFIHHLPQFDTkvIIQTLLKYPINHFWGVSSIYR-MILQQDFTSIRFPALEHCYTGGEVvLPKD-QEEWKRRTGL 361
Cdd:TIGR02262 228 VGATtVLMGERPTPDA--VFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEA-LPAEvGQRWQARFGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 362 -------------LLYEN------YGQS----------------------ETGD---------------PEKTAKVECGD 385
Cdd:TIGR02262 305 divdgigstemlhIFLSNlpgdvrYGTSgkpvpgyrlrlvgdggqdvadgEPGEllisgpssatmywnnRAKSRDTFQGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlshdk 465
Cdd:TIGR02262 385 WTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ----- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 578828477 466 DQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:TIGR02262 460 TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
81-412 |
5.22e-57 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 195.61 E-value: 5.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFTQtCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTIDAL-ASEVDSIASQCPSLKTKLLVS--DHSREGWLDFRSLVKSASPEHTCVKSKTlDPMVIFFTSGTTGFPKMAK 237
Cdd:pfam00501 96 VLITDDALkLEELLEALGKLEVVKLVLVLDrdPVLKEEPLPEEAKPADVPPPPPPPPDPD-DLAYIIYTSGTTGKPKGVM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 238 HSHG----LALQpSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCT-VFIHHLPQFDTKVIIQTLLKYPIN 312
Cdd:pfam00501 175 LTHRnlvaNVLS-IKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATvVLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 313 HFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSET------------------- 372
Cdd:pfam00501 254 VLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvvttplpldedlrslgs 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -----------------------------------------GDPEKTAKV-ECGDFYNTGDRGKMDEEGYICFLGRSDDI 410
Cdd:pfam00501 334 vgrplpgtevkivddetgepvppgepgelcvrgpgvmkgylNDPELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGRKKDQ 413
|
..
gi 578828477 411 IN 412
Cdd:pfam00501 414 IK 415
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-516 |
1.06e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 192.48 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK08314 37 SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEV------------------DSIASQCP-----SLKTKLLVSDHSREGWLDFRSLVKS--ASPEHTcVKSKTLdpM 221
Cdd:PRK08314 117 ELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPGGVVAWKEALAAglAPPPHT-AGPDDL--A 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 222 VIFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTKV 301
Cdd:PRK08314 194 VLPYTSGTTGVPKGCMHTHR-TVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL--MPRWDREA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 302 IIQTLLKYPINHfWGvsSIYRMIL---------QQDFTSIRfpalehCYTGGEVVLPKD-QEEWKRRTGLLLYENYGQSE 371
Cdd:PRK08314 271 AARLIERYRVTH-WT--NIPTMVVdflaspglaERDLSSLR------YIGGGGAAMPEAvAERLKELTGLDYVEGYGLTE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 372 TG----------------------------DPEKTAKVECGD---------------------------------FYNTG 390
Cdd:PRK08314 342 TMaqthsnppdrpklqclgiptfgvdarviDPETLEELPPGEvgeivvhgpqvfkgywnrpeataeafieidgkrFFRTG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 391 DRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflsHDKDQLTK 470
Cdd:PRK08314 422 DLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRP----EARGKTTE 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 578828477 471 E-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PRK08314 498 EeIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARA 544
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
33-510 |
3.18e-54 |
|
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: 192.53 E-value: 3.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 33 SEFGAPRWNdyeVPEEFNFASYVLDYWAqkekEGKRGPNPAFWWVNG-QGDEVKWSFREMGDLTRRVANVFtQTCGLQQG 111
Cdd:cd05967 36 SNPPFTRWF---VGGRLNTCYNALDRHV----EAGRGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVL-RKLGVVKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 112 DHLALMLPRVPEWWLVAVGCMRTGII-------FipatillKAKDILYRLQLSKAKGIVTIDA------------LASEV 172
Cdd:cd05967 108 DRVIIYMPMIPEAAIAMLACARIGAIhsvvfggF-------AAKELASRIDDAKPKLIVTASCgiepgkvvpykpLLDKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 173 DSIAS---------QCPSLKTKLLVSDhsreGWLDFRSLVKSASPeHTCVKSKTLDPMVIFFTSGTTGFPKMAKHS---H 240
Cdd:cd05967 181 LELSGhkphhvlvlNRPQVPADLTKPG----RDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPKGVVRDnggH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 GLALQPSFpgsRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCT-VFIHHLPQF--DTKVIIQTLLKYPINHFWGV 317
Cdd:cd05967 256 AVALNWSM---RNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATtVLYEGKPVGtpDPGAFWRVIEKYQVNALFTA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 318 SSIYRMILQQD--FTSIR---FPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG------------------- 373
Cdd:cd05967 333 PTAIRAIRKEDpdGKYIKkydLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGwpitanpvgleplpikags 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 --------------------------------------------DPEKTAKVECGDF---YNTGDRGKMDEEGYICFLGR 406
Cdd:cd05967 413 pgkpvpgyqvqvldedgepvgpnelgniviklplppgclltlwkNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGR 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 407 SDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSHDKDQLTKELQQHVKSVTAPYKYP 486
Cdd:cd05967 493 TDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAF 571
|
570 580
....*....|....*....|....
gi 578828477 487 RKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05967 572 RLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
87-508 |
9.36e-53 |
|
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: 184.60 E-value: 9.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANvFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTid 166
Cdd:cd05935 3 TYLELLEVVKKLAS-FLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 alASEVDsiasqcpslktkllvsdhsregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHSHGlALQP 246
Cdd:cd05935 80 --GSELD---------------------------------------------DLALIPYTSGTTGLPKGCMHTHF-SAAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 247 SFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTKVIIQTLLKYPINHFWGVSSIYRMIL- 325
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 326 -----QQDFTSIRFPAlehcyTGGEVVLPKDQEEWKRRTGLLLYENYGQSET-----GDPEKTAKVEC------------ 383
Cdd:cd05935 190 tpefkTRDLSSLKVLT-----GGGAPMPPAVAEKLLKLTGLRFVEGYGLTETmsqthTNPPLRPKLQClgip*fgvdarv 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 --------------GD------------------------------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG 419
Cdd:cd05935 265 idietgrelppnevGEivvrgpqifkgywnrpeeteesfieikgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 420 PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQltkELQQHVKSVTAPYKYPRKVEFVSELPKTI 499
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 578828477 500 TGKIERKEL 508
Cdd:cd05935 422 SGKILWRLL 430
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
84-503 |
2.76e-51 |
|
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: 182.03 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 84 VKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIV 163
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGL-RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 164 TiDALASEVDSIASQCPSLKTKLLVSDHSREGWLDFRSLVKSASPEH-----TCVKSKTLDPMVIFFTSGTTGFPKMAKH 238
Cdd:cd05911 88 T-DPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEdedlpPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 239 SH-GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWtAGCTVFIHhlPQFDTKVIIQTLLKYPINHFWGV 317
Cdd:cd05911 167 SHrNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM--PKFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 318 SSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLL-LYENYGQSETG---------------------- 373
Cdd:cd05911 244 PPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGgiltvnpdgddkpgsvgrllpn 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -----------------------------------DPEKTAkvECGD---FYNTGDRGKMDEEGYICFLGRSDDIINASG 415
Cdd:cd05911 324 veakivdddgkdslgpnepgeicvrgpqvmkgyynNPEATK--ETFDedgWLHTGDIGYFDEDGYLYIVDRKKELIKYKG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 416 YRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflshdkDQLT-KELQQHVKSVTAPYKYPRK-VEFVS 493
Cdd:cd05911 402 FQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG------EKLTeKEVKDYVAKKVASYKQLRGgVVFVD 475
|
490
....*....|
gi 578828477 494 ELPKTITGKI 503
Cdd:cd05911 476 EIPKSASGKI 485
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
87-509 |
1.39e-49 |
|
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: 176.11 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTid 166
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 alasEVDSIASqcpslktkllvsdhsregWLdfrslvksaspehtcvksktldpmvifFTSGTTGFPKMAKHSHGLALQP 246
Cdd:cd05919 89 ----SADDIAY------------------LL---------------------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 247 SFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQfDTKVIIQTLLKYPINHFWGVSSIY-RMIL 325
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 326 QQDFTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRTGLLLYENYGQSETG------------------------------- 373
Cdd:cd05919 199 SCAGSPDALRSLRLCVSAGEA-LPRGLgERWMEHFGGPILDGIGATEVGhiflsnrpgawrlgstgrpvpgyeirlvdee 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALV 428
Cdd:cd05919 278 ghtippgeegdllvrgpsaavgywnNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLII 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 429 EHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKdqLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd05919 358 QHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQES--LARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
.
gi 578828477 509 R 509
Cdd:cd05919 436 R 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
85-509 |
6.14e-49 |
|
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: 174.02 E-value: 6.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 85 KWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVT 164
Cdd:cd05934 3 RWTYAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 165 idalasevdsiasqcpslktkllvsdhsregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHSHglal 244
Cdd:cd05934 82 ------------------------------------------------------DPASILYTSGTTGPPKGVVITH---- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 245 qpsfpgsRKLRSLKTSDVSWCLSDSG----------WIVATIWTLVEPWTAGCTVFIhhLPQFDTKVIIQTLLKYPINHF 314
Cdd:cd05934 104 -------ANLTFAGYYSARRFGLGEDdvyltvlplfHINAQAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 315 WGVSSIYRMILQQdftsirfPALE----HCY--TGGEVVLPKDQEEWKRRTGLLLYENYGQSET---------------- 372
Cdd:cd05934 175 NYLGAMLSYLLAQ-------PPSPddraHRLraAYGAPNPPELHEEFEERFGVRLLEGYGMTETivgvigprdeprrpgs 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -------------------------------------------GDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDD 409
Cdd:cd05934 248 igrpapgyevrivdddgqelpagepgelvirglrgwgffkgyyNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 410 IINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLSHDkdqltkELQQHVKSVTAPYKYPRK 488
Cdd:cd05934 328 MIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgETLDPE------ELFAFCEGQLAYFKVPRY 401
|
490 500
....*....|....*....|.
gi 578828477 489 VEFVSELPKTITGKIERKELR 509
Cdd:cd05934 402 IRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
81-515 |
1.12e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 177.64 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEwwlvAV----GCMRTGII-------FIPATIllkaKD 149
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPE----AAvamlACARIGAVhsvvfggFSAEAL----AD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 150 ilyRLQLSKAKGIVTID---------ALASEVDSIASQCPSLKTKLLVSdhsREG----WLDFR-----SLVKSASPEHT 211
Cdd:PRK00174 165 ---RIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVR---RTGgdvdWVEGRdlwwhELVAGASDECE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 212 CVKSKTLDPMVIFFTSGTTGFPKMAKHSHG-------LALQPSFpgsrklrSLKTSDVSWCLSDSGWIVATIWTLVEPWT 284
Cdd:PRK00174 239 PEPMDAEDPLFILYTSGSTGKPKGVLHTTGgylvyaaMTMKYVF-------DYKDGDVYWCTADVGWVTGHSYIVYGPLA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 285 AGCTVfihhlpqfdtkVIIQTLLKYPINH-FW------GVSSIY------RMILQQ--------DFTSIRfpaLEHcyTG 343
Cdd:PRK00174 312 NGATT-----------LMFEGVPNYPDPGrFWevidkhKVTIFYtaptaiRALMKEgdehpkkyDLSSLR---LLG--SV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 344 GEvvlPKDQEEWKrrtglLLYENYG-----------QSETG--------------------------------------- 373
Cdd:PRK00174 376 GE---PINPEAWE-----WYYKVVGgercpivdtwwQTETGgimitplpgatplkpgsatrplpgiqpavvdeegnpleg 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ---------------------DPEKTAKV---ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVE 429
Cdd:PRK00174 448 geggnlvikdpwpgmmrtiygDHERFVKTyfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 430 HPAVAESAVVGSPDPIRGEVVKAFIVL----TPQflshdkDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIER 505
Cdd:PRK00174 528 HPKVAEAAVVGRPDDIKGQGIYAFVTLkggeEPS------DELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
|
570
....*....|
gi 578828477 506 KELRKKETGQ 515
Cdd:PRK00174 602 RILRKIAEGE 611
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
83-510 |
1.92e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 175.12 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 83 EVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGI 162
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIDALASEVDSIASQCPSLKTKLLVS---DHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHS 239
Cdd:PRK08316 113 LVDPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 240 HglalqpsfpgsrklRSLKTSDVSwCLSDSGWIVATIWTLVEPW--TAGCTVFIhhLPQF------------DTKVIIQT 305
Cdd:PRK08316 193 H--------------RALIAEYVS-CIVAGDMSADDIPLHALPLyhCAQLDVFL--GPYLyvgatnvildapDPELILRT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 306 LLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEV----VLpkdqEEWKRR-TGLLLYENYGQSETG------ 373
Cdd:PRK08316 256 IEAERITSFFAPPTVWISLLRHpDFDTRDLSSLRKGYYGASImpveVL----KELRERlPGLRFYNCYGQTEIAplatvl 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ----------------------------------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYI 401
Cdd:PRK08316 332 gpeehlrrpgsagrpvlnvetrvvdddgndvapgevgeivhrspqlmlgywdDPEKTAEAFRGGWFHSGDLGVMDEEGYI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 402 CFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQQHVKSVTA 481
Cdd:PRK08316 412 TVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA-----GATVTEDELIAHCRARLA 486
|
490 500
....*....|....*....|....*....
gi 578828477 482 PYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
218-510 |
9.17e-48 |
|
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: 171.32 E-value: 9.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 218 LDPMVIFFTSGTTGFPKMAKHSHG-LALQpsfpgsrkLRSLkTSDVSWCLSDS-----------GWIVAtiwtLVEPWTA 285
Cdd:cd05941 89 LDPALILYTSGTTGRPKGVVLTHAnLAAN--------VRAL-VDAWRWTEDDVllhvlplhhvhGLVNA----LLCPLFA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 286 GCTVfiHHLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ---QDFTSIRFPALEHC-----YTGGEVVLPKD-QEEWK 356
Cdd:cd05941 156 GASV--EFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeAHFTDPQFARAAAAerlrlMVSGSAALPVPtLEEWE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 357 RRTGLLLYENYGQSETG---------------------------------------------------------DPEKTA 379
Cdd:cd05941 234 AITGHTLLERYGMTEIGmalsnpldgerrpgtvgmplpgvqarivdeetgeplprgevgeiqvrgpsvfkeywnKPEATK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 380 KVECGD-FYNTGDRGKMDEEGYICFLGR-SDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLT 457
Cdd:cd05941 314 EEFTDDgWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLR 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578828477 458 PQFLSHDKDqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05941 394 AGAAALSLE----ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
36-515 |
5.87e-47 |
|
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: 172.67 E-value: 5.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 36 GAPrWNDYEVPEEFNFASYVLDYWaqkekEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLA 115
Cdd:cd05968 48 GKP-WAAWFVGGRMNIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 116 LMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDA---------LASEVDSIASQCPSLKtKL 186
Cdd:cd05968 121 IYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVE-KV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 187 LVSDHSREGWL----DFRS--LVKSASPEHTcVKSKTLDPMVIFFTSGTTGFPKMAKHSH-GLALQPSFPGSRKLrSLKT 259
Cdd:cd05968 200 VVVRHLGNDFTpakgRDLSydEEKETAGDGA-ERTESEDPLMIIYTSGTTGKPKGTVHVHaGFPLKAAQDMYFQF-DLKP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 260 SDVSWCLSDSGWIVATiWTLVEPWTAGCTVFIHH-LPQFDTKV-IIQTLLKYPINHFwGVS-SIYRMIL--------QQD 328
Cdd:cd05968 278 GDLLTWFTDLGWMMGP-WLIFGGLILGATMVLYDgAPDHPKADrLWRMVEDHEITHL-GLSpTLIRALKprgdapvnAHD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 329 FTSIRFPA-------------------LEHC----YTGGE-----------------------------VVLPKDQEEWK 356
Cdd:cd05968 356 LSSLRVLGstgepwnpepwnwlfetvgKGRNpiinYSGGTeisggilgnvlikpikpssfngpvpgmkaDVLDESGKPAR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 357 RRTGLLLYENYGQSET----GDPEKT-----AKVEcgDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESAL 427
Cdd:cd05968 436 PEVGELVLLAPWPGMTrgfwRDEDRYletywSRFD--NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVL 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 428 VEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKE 507
Cdd:cd05968 514 NAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV--TPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRV 591
|
....*...
gi 578828477 508 LRKKETGQ 515
Cdd:cd05968 592 IRAAYLGK 599
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
67-509 |
9.64e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 167.86 E-value: 9.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 67 KRGPN-PAFWWvngqgDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILL 145
Cdd:PRK06188 23 KRYPDrPALVL-----GDTRLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 146 KAKDILYRLQLSKAKGIVtID--ALASEVDSIASQCPSLKTKLLVSDhsREGWLDFRSLVKSASPEHTCVKSKTLDPMVI 223
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLI-VDpaPFVERALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALPPDIAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 224 FFTSGTTGFPKMAKHSHglalqpsfpgsrklRSLKTSDVsWCLSDSGWIVATIWTLVEPWT--AGCTV--------FIHH 293
Cdd:PRK06188 174 AYTGGTTGKPKGVMGTH--------------RSIATMAQ-IQLAEWEWPADPRFLMCTPLShaGGAFFlptllrggTVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 294 LPQFDTKVIIQTLLKYPINHFWGVSS-IYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSE- 371
Cdd:PRK06188 239 LAKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 372 -------------------------------------------TGD------------------PEKTAKVECGDFYNTG 390
Cdd:PRK06188 319 pmvitylrkrdhdpddpkrltscgrptpglrvalldedgrevaQGEvgeicvrgplvmdgywnrPEETAEAFRDGWLHTG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 391 DRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTK 470
Cdd:PRK06188 399 DVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP-----GAAVDAA 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 578828477 471 ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK06188 474 ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
87-509 |
2.25e-45 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 167.12 E-value: 2.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVAnVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK07059 50 TYGELDELSRALA-AWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQCP-------SL----------------KTKLLVSDHSREGWLDFRSLVKSASpehtcvkSKTLDPM-- 221
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvaSMgdllgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEGA-------RQTFKPVkl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 222 ----VIF--FTSGTTGFPKMAK--HSHGLA--------LQPSFPGSRKLRSLKTsdvswclsdsgwIVA---------TI 276
Cdd:PRK07059 202 gpddVAFlqYTGGTTGVSKGATllHRNIVAnvlqmeawLQPAFEKKPRPDQLNF------------VCAlplyhifalTV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 277 WTLVEPWTAGCTVFIHHlPQfDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEW 355
Cdd:PRK07059 270 CGLLGMRTGGRNILIPN-PR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 356 KRRTGLLLYENYGQSET---------------------------------------GD------------------PEKT 378
Cdd:PRK07059 348 LEMTGCPITEGYGLSETspvatcnpvdatefsgtiglplpstevsirdddgndlplGEpgeicirgpqvmagywnrPDET 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 379 AKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVlt 457
Cdd:PRK07059 428 AKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-- 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 578828477 458 pqflshDKDQ-LT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK07059 506 ------KKDPaLTeEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-511 |
2.27e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 160.84 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 80 QGDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKA 159
Cdd:PRK08276 6 APSGEVVTYGELEARSNRLAHGL-RALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTIDALASEVDSIASQCPSLKTKLLVSDHSREGWLDFRSLVKSASPehTCVKSKTL-DPMVifFTSGTTGFPKMAKH 238
Cdd:PRK08276 85 KVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPD--TPIADETAgADML--YSSGTTGRPKGIKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 239 --SHGLALQPSFPGSRKL-RSLKTSDVSWCLSDS--------GWIVATIwtlvepwTAGCTVFIhhLPQFDTKVIIQTLL 307
Cdd:PRK08276 161 plPGLDPDEAPGMMLALLgFGMYGGPDSVYLSPAplyhtaplRFGMSAL-------ALGGTVVV--MEKFDAEEALALIE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 308 KYPINHFWGVSSIY-RMI-LQQ------DFTSIRF---------------------PALEHCY----TGGEVVLpkDQEE 354
Cdd:PRK08276 232 RYRVTHSQLVPTMFvRMLkLPEevraryDVSSLRVaihaaapcpvevkramidwwgPIIHEYYasseGGGVTVI--TSED 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 355 WKRR--------------------------TGLLLYENYGQSET--GDPEKTAKVECG-DFYNTGDRGKMDEEGYICFLG 405
Cdd:PRK08276 310 WLAHpgsvgkavlgevrildedgnelppgeIGTVYFEMDGYPFEyhNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 406 RSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAfiVLTPQFLSHDKDQLTKELQQHVKSVTAPYKY 485
Cdd:PRK08276 390 RKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADGADAGDALAAELIAWLRGRLAHYKC 467
|
490 500
....*....|....*....|....*.
gi 578828477 486 PRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK08276 468 PRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
87-508 |
2.50e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 161.75 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK06178 60 TYAELDELSDRFAALLRQR-GVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQC-----------------PSLKTKLLVSDHSR--EGWLDFRSLVkSASPEHTCVKSKTLD-PMVIFFT 226
Cdd:PRK06178 139 QLAPVVEQVRAETslrhvivtsladvlpaePTLPLPDSLRAPRLaaAGAIDLLPAL-RACTAPVPLPPPALDaLAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 227 SGTTGFPKMAKHSHG--LALQPSFPGSRKLRSlkTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTKVIIQ 304
Cdd:PRK06178 218 GGTTGMPKGCEHTQRdmVYTAAAAYAVAVVGG--EDSVFLSFLPEFWIAGENFGLLFPLFSGATLVL--LARWDAVAFMA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 305 TLLKYPINHFWGVSSIYRMIL------QQDFTSIRFPaleHCYTGGEVVLPKDQEEWKRRTGLLLYE-NYGQSET----- 372
Cdd:PRK06178 294 AVERYRVTRTVMLVDNAVELMdhprfaEYDLSSLRQV---RVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTEThtcdt 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -----------------------------------------------------------GDPEKTAKVECGDFYNTGDRG 393
Cdd:PRK06178 371 ftagfqdddfdllsqpvfvglpvpgtefkicdfetgellplgaegeivvrtpsllkgywNKPEATAEALRDGWLHTGDIG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 394 KMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQ 473
Cdd:PRK06178 451 KIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP-----GADLTAAALQ 525
|
490 500 510
....*....|....*....|....*....|....*
gi 578828477 474 QHVKSVTAPYKYPrKVEFVSELPKTITGKIERKEL 508
Cdd:PRK06178 526 AWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
87-515 |
4.50e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 160.97 E-value: 4.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANvFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK06710 51 TFSVFHDKVKRFAN-YLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQC----------------------PSLKTK---LLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPM 221
Cdd:PRK06710 130 LVFPRVTNVQSATkiehvivtriadflpfpknllyPFVQKKqsnLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 222 VIFFTSGTTGFPKMAKHSHglalqpsfpgsRKLRSLKTSDVSW---CLSDSGWIVATI-WTLVEPWTAGCTVFIHH---- 293
Cdd:PRK06710 210 LLQYTGGTTGFPKGVMLTH-----------KNLVSNTLMGVQWlynCKEGEEVVLGVLpFFHVYGMTAVMNLSIMQgykm 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 294 --LPQFDTKVIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRfpaleHCYTGGEVVLPKDQEEWKRRTGLLLYE 365
Cdd:PRK06710 279 vlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLnspllkEYDISSIR-----ACISGSAPLPVEVQEKFETVTGGKLVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 366 NYGQSE----------------------------------TGD------------------------PEKTAKVECGDFY 387
Cdd:PRK06710 354 GYGLTEsspvthsnflwekrvpgsigvpwpdteamimsleTGEalppgeigeivvkgpqimkgywnkPEETAAVLQDGWL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 388 NTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqfLSHDKDQ 467
Cdd:PRK06710 434 HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV-----LKEGTEC 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 578828477 468 LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERK-----ELRKKETGQ 515
Cdd:PRK06710 509 SEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRvlieeEKRKNEDEQ 561
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
82-508 |
3.80e-42 |
|
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: 156.15 E-value: 3.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWwLVAV-GCMRTGIIFIPatillkakdilyrlqlskak 160
Cdd:cd05930 9 GDQSLTYAELDARANRLARYL-RERGVGPGDLVAVLLERSLEM-VVAIlAVLKAGAAYVP-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 givtID-ALASE-VDSIASQCpslKTKLLVSDHSregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPK--MA 236
Cdd:cd05930 67 ----LDpSYPAErLAYILEDS---GAKLVLTDPD--------------------------DLAYVIYTSGSTGKPKgvMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 237 KHsHGLA-----LQPSFPGSRKLRSLKTSDVSWclsdsgwiVATIWTLVEPWTAGCTVfiHHLPQ---FDTKVIIQTLLK 308
Cdd:cd05930 114 EH-RGLVnlllwMQEAYPLTPGDRVLQFTSFSF--------DVSVWEIFGALLAGATL--VVLPEevrKDPEALADLLAE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 309 YPINHFWGVSSIYRMILQQDFTSiRFPALEHCYTGGEVVLPKDQEEWKRR-TGLLLYENYGQSET--------------- 372
Cdd:cd05930 183 EGITVLHLTPSLLRLLLQELELA-ALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtvdatyyrvppddee 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ---------------------------------------------GDPEKTAKVECGD-------FYNTGDRGKMDEEGY 400
Cdd:cd05930 262 dgrvpigrpipntrvyvldenlrpvppgvpgelyiggaglargylNRPELTAERFVPNpfgpgerMYRTGDLVRWLPDGN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 401 ICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqfLSHDKDQLTKELQQHVKSVT 480
Cdd:cd05930 342 LEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV-----PDEGGELDEEELRAHLAERL 416
|
490 500
....*....|....*....|....*...
gi 578828477 481 APYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd05930 417 PDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
81-511 |
8.70e-42 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 156.19 E-value: 8.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFTQtCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:PRK07514 24 PDGLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTIDALASEVDSIASQCPSlkTKLLVSDHSREGWLDFRSlvKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH 240
Cdd:PRK07514 103 LVVCDPANFAWLSKIAAAAGA--PHVETLDADGTGSLLEAA--AAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 G------LALQPSF---PGSRKLRSLKTSDVSwclsdsGWIVATIWTLVepwtAGCTVFIhhLPQFDTKVIIQTLLKYPI 311
Cdd:PRK07514 179 GnllsnaLTLVDYWrftPDDVLIHALPIFHTH------GLFVATNVALL----AGASMIF--LPKFDPDAVLALMPRATV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 312 nhFWGVSSIYRMILQQdftsirfPAL--EHC------YTGGEVVLPKDQEEWKRRTGLLLYENYGQSET---------GD 374
Cdd:PRK07514 247 --MMGVPTFYTRLLQE-------PRLtrEAAahmrlfISGSAPLLAETHREFQERTGHAILERYGMTETnmntsnpydGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 375 ------------------------------------------------PEKTAKVECGD-FYNTGDRGKMDEEGYICFLG 405
Cdd:PRK07514 318 rragtvgfplpgvslrvtdpetgaelppgeigmievkgpnvfkgywrmPEKTAEEFRADgFFITGDLGKIDERGYVHIVG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 406 RSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlSHDKDQLTKELQQHVksvtAPYKY 485
Cdd:PRK07514 398 RGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA-ALDEAAILAALKGRL----ARFKQ 472
|
490 500
....*....|....*....|....*.
gi 578828477 486 PRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK07514 473 PKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
87-509 |
2.38e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 156.19 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQCPSLKT------------------------KLLVSDHSREGWLDFRSLVKSASpEHTcVKSKTLDPMV 222
Cdd:PRK08751 132 NFGTTVQQVIADTPVKQVittglgdmlgfpkaalvnfvvkyvKKLVPEYRINGAIRFREALALGR-KHS-MPTLQIEPDD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IFF---TSGTTGFPKMAKHSHglalqpsfpgsRKLRSLKTSDVSWcLSDSGWIVA---TIWTLVEPW-----TAGCTVFI 291
Cdd:PRK08751 210 IAFlqyTGGTTGVAKGAMLTH-----------RNLVANMQQAHQW-LAGTGKLEEgceVVITALPLYhifalTANGLVFM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 292 -----HHL---PQfDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLL 362
Cdd:PRK08751 278 kiggcNHLisnPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 363 LYENYGQSETG---------------------------------------------------------DPEKTAKVECGD 385
Cdd:PRK08751 357 LVEAYGLTETSpaacinpltlkeyngsiglpipstdacikddagtvlaigeigelcikgpqvmkgywkRPEETAKVMDAD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 -FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHD 464
Cdd:PRK08751 437 gWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAE 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 578828477 465 kdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK08751 517 ------DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
86-510 |
3.41e-41 |
|
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: 154.39 E-value: 3.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 86 WSFREMGDLTRRVANVFTqTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTI 165
Cdd:cd05926 15 LTYADLAELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 166 DALASEVDSIASQCPSLKTKLLVSDHSREGWLDFRSLVkSASPEHTCVKSKTL----DPMVIFFTSGTTGFPKMAKHSHG 241
Cdd:cd05926 94 KGELGPASRAASKLGLAILELALDVGVLIRAPSAESLS-NLLADKKNAKSEGVplpdDLALILHTSGTTGRPKGVPLTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 -LAlqpsfpgsrklRSLKTSDVSWCLSDS-------------GWIVATIWTLVepwTAGCTVFIhhlPQFDTKVIIQTLL 307
Cdd:cd05926 173 nLA-----------ASATNITNTYKLTPDdrtlvvmplfhvhGLVASLLSTLA---AGGSVVLP---PRFSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 308 KYPINHFWGVSSIYRMILQ--QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSET------------- 372
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAahqmtsnplppgp 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 --------------------------------------------GDPEKTAKV-ECGDFYNTGDRGKMDEEGYICFLGRS 407
Cdd:cd05926 316 rkpgsvgkpvgvevrildedgeilppgvvgeiclrgpnvtrgylNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 408 DDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlSHDKDQLTKELQQHVksvtAPYKYPR 487
Cdd:cd05926 396 KELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-SVTEEELRAFCRKHL----AAFKVPK 470
|
490 500
....*....|....*....|...
gi 578828477 488 KVEFVSELPKTITGKIERKELRK 510
Cdd:cd05926 471 KVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
84-513 |
1.58e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 154.73 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 84 VKWSFREM-GDLTRrVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFiPATILLKAKDILYRLQLSKAKGI 162
Cdd:PRK07529 57 ETWTYAELlADVTR-TANLLHSL-GVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIDA-----LASEVDSIASQCPSLKTKLLV-----------------SDHSREGWLDFRSLVKSAS-PEHTCVKSKTLD 219
Cdd:PRK07529 134 VTLGPfpgtdIWQKVAEVLAALPELRTVVEVdlarylpgpkrlavpliRRKAHARILDFDAELARQPgDRLFSGRPIGPD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 220 PMVIFF-TSGTTGFPKMAKHSHGlalqpsfpgsrklrslktSDVSwclsdSGWIVATIWTLVEpwtaGCTVFiHHLPQFD 298
Cdd:PRK07529 214 DVAAYFhTGGTTGMPKLAQHTHG------------------NEVA-----NAWLGALLLGLGP----GDTVF-CGLPLFH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 299 TKVIIQTLL-------------------------------KYPINHFWGVSSIYRMILQQ-----DFTSIRFPAlehcyt 342
Cdd:PRK07529 266 VNALLVTGLaplargahvvlatpqgyrgpgvianfwkiveRYRINFLSGVPTVYAALLQVpvdghDISSLRYAL------ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 343 GGEVVLPKD-QEEWKRRTGLLLYENYGQSET-------------------------------GDPEKTAKVEC------- 383
Cdd:PRK07529 340 CGAAPLPVEvFRRFEAATGVRIVEGYGLTEAtcvssvnppdgerrigsvglrlpyqrvrvviLDDAGRYLRDCavdevgv 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 ------------------------GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVV 439
Cdd:PRK07529 420 lciagpnvfsgyleaahnkglwleDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAV 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828477 440 GSPDPIRGEVVKAFIVLTPQfLSHDKDQLTKELQQHVKSVTApykYPRKVEFVSELPKTITGKIERKELRKKET 513
Cdd:PRK07529 500 GRPDAHAGELPVAYVQLKPG-ASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDAI 569
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
83-510 |
3.25e-40 |
|
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: 151.68 E-value: 3.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 83 EVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKgi 162
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAK-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 vtidalasevdsiasqcpslktkLLVSDHSregwLDFRSLVKSASPEHTCVKSKT-LDPMVIFFTSGTTGFPKMAKHSHG 241
Cdd:cd12118 104 -----------------------VLFVDRE----FEYEDLLAEGDPDFEWIPPADeWDPIALNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 LALqpsfpgsrkLRSLKTSdVSWCLSDSG---WIV----ATIWTLvePWT----AGCTVFihhLPQFDTKVIIQTLLKYP 310
Cdd:cd12118 157 GAY---------LNALANI-LEWEMKQHPvylWTLpmfhCNGWCF--PWTvaavGGTNVC---LRKVDAKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 311 INHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGG----EVVLPKDQE-------------------------EW----- 355
Cdd:cd12118 222 VTHFCGAPTVLNMLANaPPSDARPLPHRVHVMTAGapppAAVLAKMEElgfdvthvygltetygpatvcawkpEWdelpt 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 356 ------KRRTGL----LLYENYGQSETG--------------------------DPEKTAKVECGDFYNTGDRGKMDEEG 399
Cdd:cd12118 302 eerarlKARQGVryvgLEEVDVLDPETMkpvprdgktigeivfrgnivmkgylkNPEATAEAFRGGWFHSGDLAVIHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 400 YICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflsHDKDQLT-KELQQHVKS 478
Cdd:cd12118 382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL------KEGAKVTeEEIIAFCRE 455
|
490 500 510
....*....|....*....|....*....|..
gi 578828477 479 VTAPYKYPRKVEFvSELPKTITGKIERKELRK 510
Cdd:cd12118 456 HLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
67-509 |
1.63e-37 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 145.86 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 67 KRGPNPAFWWVNGQGDEVK-WSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGII-------F 138
Cdd:PRK10524 65 KRPEQLALIAVSTETDEERtYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 139 ipATILLKAkdilyRLQLSKAKGIVTIDA------------LASEVDSIASQCPSlktKLLVSDHS------REG----W 196
Cdd:PRK10524 144 --ASHSLAA-----RIDDAKPVLIVSADAgsrggkvvpykpLLDEAIALAQHKPR---HVLLVDRGlapmarVAGrdvdY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 197 LDFRSLVKSASPEHTCVKSKtlDPMVIFFTSGTTGFPKMAKHS---HGLALQPS----FPGsrklrslKTSDVSWCLSDS 269
Cdd:PRK10524 214 ATLRAQHLGARVPVEWLESN--EPSYILYTSGTTGKPKGVQRDtggYAVALATSmdtiFGG-------KAGETFFCASDI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 270 GWIVATIWTLVEPWTAGC-TVFIHHLP-QFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIR---FPALEHCYTGG 344
Cdd:PRK10524 285 GWVVGHSYIVYAPLLAGMaTIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRkhdLSSLRALFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 345 EvvlPKDQE--EWKRRT-GLLLYENYGQSETGDP-------------------------------EKTAKvECGD----- 385
Cdd:PRK10524 365 E---PLDEPtaSWISEAlGVPVIDNYWQTETGWPilaiargvedrptrlgspgvpmygynvkllnEVTGE-PCGPnekgv 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 ---------------------F------------YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPA 432
Cdd:PRK10524 441 lviegplppgcmqtvwgdddrFvktywslfgrqvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPA 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 433 VAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQ---LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK10524 521 VAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
83-509 |
2.70e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 144.53 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 83 EVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGI 162
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIDALASE-----VDSIA-----SQC--------PSLKTKLLVSDHSREGWLDFRSLVKSA---SPEHTCVKSKTL--- 218
Cdd:PRK12583 122 ICADAFKTSdyhamLQELLpglaeGQPgalacerlPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQASLdrd 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 219 DPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRsLKTSD-----------------VSWCLSDSGWIV-------- 273
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG-LTEHDrlcvpvplyhcfgmvlaNLGCMTVGACLVypneafdp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 274 -ATIWTLVEPWTAGC----TVFIHHL--PQFDT----------------------KVI-----IQTLLKY------PINH 313
Cdd:PRK12583 281 lATLQAVEEERCTALygvpTMFIAELdhPQRGNfdlsslrtgimagapcpievmrRVMdemhmAEVQIAYgmtetsPVSL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 314 FWGVSSIyrmiLQQDFTSI--RFPALEH--CYTGGEVVLPKDQEEWKRRtGLLLYENYgqseTGDPEKTAKVECGD-FYN 388
Cdd:PRK12583 361 QTTAADD----LERRVETVgrTQPHLEVkvVDPDGATVPRGEIGELCTR-GYSVMKGY----WNNPEATAESIDEDgWMH 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 389 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLSHDkdq 467
Cdd:PRK12583 432 TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPgHAASEE--- 508
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 578828477 468 ltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK12583 509 ---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
87-516 |
3.44e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 144.52 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASE--------------VDSIASQCPSLK----------TKLLVSDHSREGWLDFRS-LVKSASPEHTCVKSKTLDPM 221
Cdd:PRK05677 131 NMAHLaekvlpktgvkhviVTEVADMLPPLKrllinavvkhVKKMVPAYHLPQAVKFNDaLAKGAGQPVTEANPQADDVA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 222 VIFFTSGTTGFPK--MAKHSHGLA--LQpsfpgsrkLRSLKTSDvswcLSDSGWIVATIWTL--VEPWTAGCTVFI---- 291
Cdd:PRK05677 211 VLQYTGGTTGVAKgaMLTHRNLVAnmLQ--------CRALMGSN----LNEGCEILIAPLPLyhIYAFTFHCMAMMlign 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 292 HHL----PQfDTKVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYEN 366
Cdd:PRK05677 279 HNIlisnPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 367 YGQSET-----------------------------GD---------------------------PEKTAKVECGD-FYNT 389
Cdd:PRK05677 358 YGMTETspvvsvnpsqaiqvgtigipvpstlckviDDdgnelplgevgelcvkgpqvmkgywqrPEATDEILDSDgWLKT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 390 GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshdKDQLT 469
Cdd:PRK05677 438 GDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKP------GETLT 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 578828477 470 KE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PRK05677 512 KEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKA 559
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
87-512 |
5.79e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 143.66 E-value: 5.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQCP-----------SLKT-------------KLLVSDHSREGWLDFRSlVKSASPEHTCVKSKTLDPMV 222
Cdd:PRK08974 130 NFAHTLEKVVFKTPvkhviltrmgdQLSTakgtlvnfvvkyiKRLVPKYHLPDAISFRS-ALHKGRRMQYVKPELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IF--FTSGTTGFPKMAKHSHG--LA--LQPSFPGSRKLRSLKTsdvswclsdsgwIVATIWTL--VEPWTAGCTVFIH-- 292
Cdd:PRK08974 209 AFlqYTGGTTGVAKGAMLTHRnmLAnlEQAKAAYGPLLHPGKE------------LVVTALPLyhIFALTVNCLLFIElg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 293 ----------HLPQFdtkviIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGL 361
Cdd:PRK08974 277 gqnllitnprDIPGF-----VKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 362 LLYENYG------------------------------------------QSETGD---------------PEKTAKVECG 384
Cdd:PRK08974 352 YLLEGYGltecsplvsvnpydldyysgsiglpvpsteiklvdddgnevpPGEPGElwvkgpqvmlgywqrPEATDEVIKD 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 385 DFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqflshD 464
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV--------K 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 578828477 465 KDQ-LTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 512
Cdd:PRK08974 504 KDPsLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-508 |
7.56e-37 |
|
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: 142.37 E-value: 7.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTqTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:cd05904 34 TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVdsiasqcPSLKTKLLVSDHSREGWLDFRSLVKSASPEHTC-VKSKTLDPMVIFFTSGTTGFPKMAKHSHG---- 241
Cdd:cd05904 113 ELAEKL-------ASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPvVVIKQDDVAALLYSSGTTGRSKGVMLTHRnlia 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 -LALQPSFPGSRKLRSlktsDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTKVIIQTLLKYPINHFWGV--- 317
Cdd:cd05904 186 mVAQFVAGEGSNSDSE----DVFLCVLPMFHIYGLSSFALGLLRLGATVVV--MPRFDLEELLAAIERYKVTHLPVVppi 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 318 ---------------SSIyRMI----------LQQDFTSiRFPALE--HCY-----TGGEVVLPKDQEEWKRR--TGLLL 363
Cdd:cd05904 260 vlalvkspivdkydlSSL-RQImsgaaplgkeLIEAFRA-KFPNVDlgQGYgmtesTGVVAMCFAPEKDRAKYgsVGRLV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 364 --YE------NYGQS----ETG---------------DPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASG 415
Cdd:cd05904 338 pnVEakivdpETGESlppnQTGelwirgpsimkgylnNPEATAATIDKEgWLHTGDLCYIDEDGYLFIVDRLKELIKYKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 416 YRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQ-FLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSE 494
Cdd:cd05904 418 FQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGsSLTED------EIMDFVAKQVAPYKKVRKVAFVDA 491
|
490
....*....|....
gi 578828477 495 LPKTITGKIERKEL 508
Cdd:cd05904 492 IPKSPSGKILRKEL 505
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-509 |
1.63e-36 |
|
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: 140.65 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 107 GLQQGDHLALMLPRVPEW-WL---VAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKgIVTIDA-LASEVDSIASQCPS 181
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELsfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGR-IVLADAgAADRLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 182 LKTKLLVsdhsrEGWLDFRSLVKSASPEHTcvksktlDPMVIFFTSGTTGFPKMAKHSH-----GLALQPSFPGSRKL-R 255
Cdd:cd05922 93 PGTVLDA-----DGIRAARASAPAHEVSHE-------DLALLLYTSGSTGSPKLVRLSHqnllaNARSIAEYLGITADdR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 256 SLKTSDVSWCLsdsGWIVATIWTLVepwtaGCTVFIHHLPQFDTKVIiQTLLKYPINHFWGVSSIYRMILQQDFTSIRFP 335
Cdd:cd05922 161 ALTVLPLSYDY---GLSVLNTHLLR-----GATLVLTNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 336 ------------------ALEHCYTGGEVVLPKDQEEWKRR--------------------------------------- 358
Cdd:cd05922 232 slryltqaggrlpqetiaRLRELLPGAQVYVMYGQTEATRRmtylpperilekpgsiglaipggefeildddgtptppge 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 359 ------TGLLLYENYGQSETGDPEKTAKvecGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPA 432
Cdd:cd05922 312 pgeivhRGPNVMKGYWNDPPYRRKEGRG---GGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 433 VAESAVVGSPDPIrGEVVKAFIVLTPQFLSHDkdqltkeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:cd05922 389 IIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
55-510 |
2.34e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 141.81 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 55 VLDYWAQKekeGKRGPNPAFWwVNGQGdeVKWSFREMGDLTRRVANVFTQtCGLQQGDHLALMLPRVPEWWLVAVGCMRT 134
Cdd:PRK06087 25 LADYWQQT---ARAMPDKIAV-VDNHG--ASYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 135 GIIFIPATILLKAKDILYRLQLSKAKGIVTIDALAS-----EVDSIASQCPSLKTKLLVSDHSRE-GWLDFRSLVKSASP 208
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQtrpvdLILPLQNQLPQLQQIVGVDKLAPAtSSLSLSQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 209 EHTCVKSKTLDPMVIFFTSGTTGFPK--MAKHSHGLALQPSFPGSRKLRSLktsDVSWCLSDSGWIVATIWTLVEPWTAG 286
Cdd:PRK06087 178 LTTAITTHGDELAAVLFTSGTEGLPKgvMLTHNNILASERAYCARLNLTWQ---DVFMMPAPLGHATGFLHGVTAPFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 287 CTVFIhhLPQFDTKVIIQTLLKYPINHFWGVSS-IYRMI--LQQ---DFTSIRFpalehcYTGGEVVLPKDQEEWKRRTG 360
Cdd:PRK06087 255 ARSVL--LDIFTPDACLALLEQQRCTCMLGATPfIYDLLnlLEKqpaDLSALRF------FLCGGTTIPKKVARECQQRG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 361 LLLYENYGQSET----------------------------------------------------------GDPEKTAKV- 381
Cdd:PRK06087 327 IKLLSVYGSTESsphavvnlddplsrfmhtdgyaaagveikvvdearktlppgcegeeasrgpnvfmgylDEPELTARAl 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 382 -ECGDFYnTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQF 460
Cdd:PRK06087 407 dEEGWYY-SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPH 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 578828477 461 LSHDKDQLTKEL-QQHVksvtAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK06087 486 HSLTLEEVVAFFsRKRV----AKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
66-511 |
4.06e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 140.95 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 66 GKRGPN-PAFWWvngqGDEVkWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATIL 144
Cdd:PRK07470 17 ARRFPDrIALVW----GDRS-WTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 145 LKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKllVSDHSREGWLDFRSLVKS---ASPEHTCVKSKtlDPM 221
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHV--VAIGGARAGLDYEALVARhlgARVANAAVDHD--DPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 222 VIFFTSGTTGFPKMAKHSHG-LA------LQPSFPGSRKL-RSLKTSDVSwclsdSGwivATIWTLVEPWTAGCTVFihh 293
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGqMAfvitnhLADLMPGTTEQdASLVVAPLS-----HG---AGIHQLCQVARGAATVL--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 294 LP--QFDTKVIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRF---------------------PALEHCYTGG 344
Cdd:PRK07470 236 LPseRFDPAEVWALVERHRVTNLFTVPTILKMLVehpavdRYDHSSLRYviyagapmyradqkralaklgKVLVQYFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 345 EV-----VLP------KDQEEWK------RRTGLLLY------ENYGQSETGD---------------PEKTAKVECGDF 386
Cdd:PRK07470 316 EVtgnitVLPpalhdaEDGPDARigtcgfERTGMEVQiqddegRELPPGETGEicvigpavfagyynnPEANAKAFRDGW 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTpqflshDKD 466
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR------DGA 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 578828477 467 QLTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK07470 470 PVDEaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-510 |
5.55e-36 |
|
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: 140.46 E-value: 5.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 78 NGQGDEVKWSFREMGDLTRRVANVFTQTcGLQQGD-----------HLALMLprvpewwlvAVGCMrtGIIFIPATILLK 146
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDrvatlawnthrHLELYY---------AVPGM--GAVLHTINPRLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 147 AKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKLLVSDHSR------EGWLDFRSLVKSASPEHTCVKSKTLDP 220
Cdd:cd12119 86 PEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 221 MVIFFTSGTTGFPKMAKHSH--------GLALQPSFPgsrklrsLKTSDV-----------SWCLSDSGWIVATiwTLVE 281
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHrslvlhamAALLTDGLG-------LSESDVvlpvvpmfhvnAWGLPYAAAMVGA--KLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 282 PwtaGctvfihhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtG 360
Cdd:cd12119 237 P---G--------PYLDPASLAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-G 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 361 LLLYENYGQSET-------------------------------------------------------------------- 372
Cdd:cd12119 305 VRVIHAWGMTETsplgtvarppsehsnlsedeqlalrakqgrpvpgvelrivdddgrelpwdgkavgelqvrgpwvtksy 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -GDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVK 451
Cdd:cd12119 385 yKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 578828477 452 AFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd12119 465 AVVVLKE-----GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
87-509 |
6.43e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 139.76 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK13390 26 SYRQLDDDSAALARVL-YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQCPslktkLLVSDHSR-EGWLDFRSLVKSASP---EHTCvksktldPMVIFFTSGTTGFPKmakhshgl 242
Cdd:PRK13390 105 ALDGLAAKVGADLP-----LRLSFGGEiDGFGSFEAALAGAGPrltEQPC-------GAVMLYSSGTTGFPK-------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 243 ALQPSFPG-------------SRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHhlpQFDTKVIIQTLLKY 309
Cdd:PRK13390 165 GIQPDLPGrdvdapgdpivaiARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAK---RFDAQATLGHVERY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 310 PINHFWGVSSIYRMILQ--------QDFTSIRfpALEHCYTGGEVVLPKDQEEWkrrTGLLLYENYGQSET--------- 372
Cdd:PRK13390 242 RITVTQMVPTMFVRLLKldadvrtrYDVSSLR--AVIHAAAPCPVDVKHAMIDW---LGPIVYEYYSSTEAhgmtfidsp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -----------------------------------------------GDPEKTAKVE--CGDFYNT-GDRGKMDEEGYIC 402
Cdd:PRK13390 317 dwlahpgsvgrsvlgdlhicdddgnelpagrigtvyferdrlpfrylNDPEKTAAAQhpAHPFWTTvGDLGSVDEDGYLY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 403 FLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVTAP 482
Cdd:PRK13390 397 LADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI--RGSDELARELIDYTRSRIAH 474
|
490 500
....*....|....*....|....*..
gi 578828477 483 YKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK13390 475 YKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
69-510 |
1.33e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 139.75 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 69 GPNPAFWWVNGQGdevkwSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAK 148
Cdd:PRK05605 46 GDRPALDFFGATT-----TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 149 DILYRLQLSKAKGIVTIDALASEVDSIASQCP-------------------SLKTKLLVSDHSRE-------GWLDFRSL 202
Cdd:PRK05605 120 ELEHPFEDHGARVAIVWDKVAPTVERLRRTTPletivsvnmiaampllqrlALRLPIPALRKARAaltgpapGTVPWETL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 203 VKSASP------EHTCVKSKtlDPMVIFFTSGTTGFPKMAKHSHglalqpsfpgsRKLRSLKTSDVSWC--LSDSGWIV- 273
Cdd:PRK05605 200 VDAAIGgdgsdvSHPRPTPD--DVALILYTSGTTGKPKGAQLTH-----------RNLFANAAQGKAWVpgLGDGPERVl 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 274 ----------ATIWTLVEPWTAGCTVFihhLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ------DFTSIRFpAL 337
Cdd:PRK05605 267 aalpmfhaygLTLCLTLAVSIGGELVL---LPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSGVRN-AF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 338 EhcytgGEVVLPKDQ-EEWKRRTGLLLYENYGQSET-------------------------------------------- 372
Cdd:PRK05605 343 S-----GAMALPVSTvELWEKLTGGLLVEGYGLTETspiivgnpmsddrrpgyvgvpfpdtevrivdpedpdetmpdgee 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ---------------GDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESA 437
Cdd:PRK05605 418 gellvrgpqvfkgywNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAA 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828477 438 VVGSPDPIRGEVVKAFIVLTPQfLSHDKDqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK05605 498 VVGLPREDGSEEVVAAVVLEPG-AALDPE----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
81-511 |
3.03e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 138.37 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWsfREMGDLTRRVANVFTQTcGLQQGDH-LALMLPRvPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKA 159
Cdd:PRK07786 40 GNTTTW--RELDDRVAALAGALSRR-GVGFGDRvLILMLNR-TEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTIDALASEVDSIASQCPSLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHS 239
Cdd:PRK07786 116 HVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 240 HGLALQPSFPGSRKLRSLKTSDVSWCLSDSgWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVIIQTLLKYPINHFWGVSS 319
Cdd:PRK07786 196 HANLTGQAMTCLRTNGADINSDVGFVGVPL-FHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 320 IYRMIL------QQDFtSIRF------PA-------LEHCYTGGEVVLPKDQEEWKRRTGLLLYEN-------------- 366
Cdd:PRK07786 275 QWQAVCaeqqarPRDL-ALRVlswgaaPAsdtllrqMAATFPEAQILAAFGQTEMSPVTCMLLGEDairklgsvgkvipt 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 367 ------------YGQSETGD---------------PEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG 419
Cdd:PRK07786 354 vaarvvdenmndVPVGEVGEivyraptlmsgywnnPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 420 PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLT-KELQQHVKSVTAPYKYPRKVEFVSELPKT 498
Cdd:PRK07786 434 CAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN-----DDAALTlEDLAEFLTDRLARYKHPKALEIVDALPRN 508
|
490
....*....|...
gi 578828477 499 ITGKIERKELRKK 511
Cdd:PRK07786 509 PAGKVLKTELRER 521
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
87-438 |
5.47e-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: 135.47 E-value: 5.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPeWWLVAV-GCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTI 165
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSA-ELVVAIlAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 166 DALASEVDSIASQCpslktkLLVSDhsregwLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHG---- 241
Cdd:TIGR01733 80 SALASRLAGLVLPV------ILLDP------LELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRslvn 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 --LALQPSFPGSRKLRSLKTSDVSWCLSdsgwiVATIWTlvePWTAGCTVFI--HHLPQFDTKVIIQTLLKYPINHFWGV 317
Cdd:TIGR01733 148 llAWLARRYGLDPDDRVLQFASLSFDAS-----VEEIFG---ALLAGATLVVppEDEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 318 SSIYRMILQQDFTSirFPALEHCYTGGEVVLPKDQEEWKRRTG-LLLYENYGQSET------------------------ 372
Cdd:TIGR01733 220 PSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETtvwstatlvdpddaprespvpigr 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -------------------------------------GDPEKTAKV---------ECGDFYNTGDRGKMDEEGYICFLGR 406
Cdd:TIGR01733 298 plantrlyvldddlrpvpvgvvgelyiggpgvargylNRPELTAERfvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGR 377
|
410 420 430
....*....|....*....|....*....|..
gi 578828477 407 SDDIINASGYRIGPAEVESALVEHPAVAESAV 438
Cdd:TIGR01733 378 IDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
63-509 |
1.83e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 135.97 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 63 EKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTqTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPAT 142
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 143 ILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKLLVSDHSR---EGWLDFRSLvKSASPEHTC--VKSKT 217
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALpadDGVSSFTQL-KAQQPATLCyaPPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 218 LDPMVIFFTSGTTGFPKMAKHSHGLALqpsFPG--SRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVfihhlp 295
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNLR---FAGyySAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATF------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 296 qfdtkVIIQtllKYPINHFWGVSSIYR--------MILQqdfTSIRFPALE----HCYTGGEVVLP-KDQEE--WKRRTG 360
Cdd:PRK08008 244 -----VLLE---KYSARAFWGQVCKYRatitecipMMIR---TLMVQPPSAndrqHCLREVMFYLNlSDQEKdaFEERFG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 361 LLLYENYGQSET------------------------------------------------------------GDPEKTAK 380
Cdd:PRK08008 313 VRLLTSYGMTETivgiigdrpgdkrrwpsigrpgfcyeaeirddhnrplpageigeicikgvpgktifkeyyLDPKATAK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 381 VECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPq 459
Cdd:PRK08008 393 VLEADgWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE- 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 578828477 460 flshdKDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK08008 472 -----GETLSEEeFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
81-508 |
2.79e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 134.99 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIV---TIDALASEVDSIASQCPSLKTKLL--VSDHSREGWLDfrslvKSASpehtcvksktlDPMVIFFTSGTTGFPKM 235
Cdd:PRK06839 103 VLFvekTFQNMALSMQKVSYVQRVISITSLkeIEDRKIDNFVE-----KNES-----------ASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 236 AKHSHGLALQPSFPGSRKLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHlpQFDTKVIIQTLLKYPINHFW 315
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 316 GVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSET-------------------GDP 375
Cdd:PRK06839 244 GVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfmlseedarrkvgsiGKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 376 ----------EKTAKVECGD-----------------------------FYNTGDRGKMDEEGYICFLGRSDDIINASGY 416
Cdd:PRK06839 323 vlfcdyelidENKNKVEVGEvgellirgpnvmkeywnrpdateetiqdgWLCTGDLARVDEDGFVYIVGRKKEMIISGGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 417 RIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDqltkeLQQHVKSVTAPYKYPRKVEFVSELP 496
Cdd:PRK06839 403 NIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKD-----VIEHCRLFLAKYKIPKEIVFLKELP 477
|
490
....*....|..
gi 578828477 497 KTITGKIERKEL 508
Cdd:PRK06839 478 KNATGKIQKAQL 489
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
214-510 |
8.34e-34 |
|
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: 132.47 E-value: 8.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 214 KSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQpSFPGSrKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHh 293
Cdd:cd05912 73 DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWW-SAIGS-ALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLV- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 294 lPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTsiRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSET- 372
Cdd:cd05912 150 -DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGE--GYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETc 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ------------------------------------------------------GDPEKTAKVECGDFYNTGDRGKMDEE 398
Cdd:cd05912 227 sqivtlspedalnkigsagkplfpvelkieddgqppyevgeillkgpnvtkgylNRPDATEESFENGWFKTGDIGYLDEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 399 GYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlshDKDQLTKELQQHVks 478
Cdd:cd05912 307 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL-- 381
|
330 340 350
....*....|....*....|....*....|..
gi 578828477 479 vtAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05912 382 --AKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
81-510 |
2.34e-33 |
|
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: 132.96 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:COG1021 46 DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTID--------ALASEVdsiASQCPSLKTKLLVSDHsrEGWLDFRSLVKSASPEHTCvkskTLDPM-VIFF--TSGT 229
Cdd:COG1021 125 AYIIPDrhrgfdyrALAREL---QAEVPSLRHVLVVGDA--GEFTSLDALLAAPADLSEP----RPDPDdVAFFqlSGGT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 230 TGFPKMAKHSHglalQP---SFPGSRKLRSLKTSDVSWC---------LSDSGwIVATIWtlvepwtAGCTVFIHHLPQF 297
Cdd:COG1021 196 TGLPKLIPRTH----DDylySVRASAEICGLDADTVYLAalpaahnfpLSSPG-VLGVLY-------AGGTVVLAPDPSP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 298 DT--------KVIIQTLlkypinhfwgVSSIYRMILQQ------DFTSIRF-----------------PALEH------- 339
Cdd:COG1021 264 DTafpliereRVTVTAL----------VPPLALLWLDAaersryDLSSLRVlqvggaklspelarrvrPALGCtlqqvfg 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 340 ------CYT----GGEVVL--------PKDQeewkrrtgLLLYENYGQS----ETG---------------DPEKTAKVE 382
Cdd:COG1021 334 maeglvNYTrlddPEEVILttqgrpisPDDE--------VRIVDEDGNPvppgEVGelltrgpytirgyyrAPEHNARAF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 383 CGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFL 461
Cdd:COG1021 406 TPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPL 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 578828477 462 ShdkdqlTKELQQHVKSV-TAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:COG1021 486 T------LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-509 |
2.39e-33 |
|
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: 129.71 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 219 DPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSlkTSDVSWCLSD-----SGWIVATIWTLvepwTAGCT-VFIH 292
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGL--TEQDRLCIPVplfhcFGSVLGVLACL----THGATmVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 293 hlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ------DFTSIR----------------------FPALEHCY--- 341
Cdd:cd05917 77 --PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHpdfdkfDLSSLRtgimagapcppelmkrvievmnMKDVTIAYgmt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 342 ------------------------------------TGGEVVLPKDQEEWKRRtGLLLYENYGQsetgDPEKTAKVECGD 385
Cdd:cd05917 155 etspvstqtrtddsiekrvntvgrimphteakivdpEGGIVPPVGVPGELCIR-GYSVMKGYWN----DPEKTAEAIDGD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 -FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflsHD 464
Cdd:cd05917 230 gWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL------KE 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578828477 465 KDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:cd05917 304 GAELTEEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
72-508 |
6.27e-33 |
|
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: 130.44 E-value: 6.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 72 PAFWWvngqgDEVKWSFREMGDLTRRVAnVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPatillkakdil 151
Cdd:cd05945 8 PAVVE-----GGRTLTYRELKERADALA-AALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 152 yrlqlskakgivtIDAlASEVDSIASQCPSLKTKLLVSDHSregwldfrslvksaspehtcvksktlDPMVIFFTSGTTG 231
Cdd:cd05945 71 -------------LDA-SSPAERIREILDAAKPALLIADGD--------------------------DNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 232 FPKMAKHSHGlALQ-------PSFPGSRKLRSLKTSDVSWCLSdsgwiVATIW-TLVepwTAGCTVFIHHLPQFDTKVII 303
Cdd:cd05945 111 RPKGVQISHD-NLVsftnwmlSDFPLGPGDVFLNQAPFSFDLS-----VMDLYpALA---SGATLVPVPRDATADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 304 QTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRT-GLLLYENYGQSET-------- 372
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEV-LPHKTaRALQQRFpDARIYNTYGPTEAtvavtyie 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -----------------------------------------------------GDPEKTAKV----ECGDFYNTGDRGKM 395
Cdd:cd05945 261 vtpevldgydrlpigyakpgaklvildedgrpvppgekgelvisgpsvskgylNNPEKTAAAffpdEGQRAYRTGDLVRL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 396 DEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflsHDKDQLTKELQQH 475
Cdd:cd05945 341 EADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP----GAEAGLTKAIKAE 416
|
490 500 510
....*....|....*....|....*....|...
gi 578828477 476 VKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd05945 417 LAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
87-511 |
3.64e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 129.43 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTcGLQQGDHLALML---PRVPEwwlVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIV 163
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 164 TIDALASEVDSIASQCPSLKTKLLV-SDHSREGWLDFRSLVKSASPehTCVKSKTL-DPMviFFTSGTTGFPKMAKhshg 241
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPA--TPIADESLgTDM--LYSSGTTGRPKGIK---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 242 lALQPSFPGSRKLRSLKTSDVSWCLsDSGWIVAT----------IWTLVEPWTAGCTVFIHHlpqFDTKVIIQTLLKYPI 311
Cdd:PRK13391 174 -RPLPEQPPDTPLPLTAFLQRLWGF-RSDMVYLSpaplyhsapqRAVMLVIRLGGTVIVMEH---FDAEQYLALIEEYGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 312 NHFWGVSSIY-RMI-------LQQDFTSIRF---------------------PALEHCYTGGEVVLPK--DQEEWKRRTG 360
Cdd:PRK13391 249 THTQLVPTMFsRMLklpeevrDKYDLSSLEVaihaaapcppqvkeqmidwwgPIIHEYYAATEGLGFTacDSEEWLAHPG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 361 ---------LLLYENYGQ-----------SETG-------DPEKT--AKVECGDFYNTGDRGKMDEEGYICFLGRSDDII 411
Cdd:PRK13391 329 tvgramfgdLHILDDDGAelppgepgtiwFEGGrpfeylnDPAKTaeARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 412 NASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflSHDKDQLTKELQQHVKSVTAPYKYPRKVEF 491
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDG--VDPGPALAAELIAFCRQRLSRQKCPRSIDF 486
|
490 500
....*....|....*....|
gi 578828477 492 VSELPKTITGKIERKELRKK 511
Cdd:PRK13391 487 EDELPRLPTGKLYKRLLRDR 506
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
85-515 |
4.13e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 128.54 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 85 KWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGiifipATIL-----LKAKDILYRLQLSKA 159
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAAL-GVKKGDRVALLMKNGMEMILVIHALQQLG-----AVAVllntrLSREELLWQLDDAEV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTIDALASEVDSIASQcpslktkllvsdhsregwlDFRSLVKSASPEHTCVKSKTLDP-MVIFFTSGTTGFPK---- 234
Cdd:PRK03640 101 KCLITDDDFEAKLIPGISV-------------------KFAELMNGPKEEAEIQEEFDLDEvATIMYTSGTTGKPKgviq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 235 -MAKHSHglalqpSFPGSrklrSLK---TSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHhlPQFDTKVIIQTLLKYP 310
Cdd:PRK03640 162 tYGNHWW------SAVGS----ALNlglTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 311 INhfwgVSSIYRMILQQ---DFTSIRFPALEHCYT--GGEVVLPKdQEEWKRRtGLLLYENYGQSET------------- 372
Cdd:PRK03640 230 VT----IISVVSTMLQRlleRLGEGTYPSSFRCMLlgGGPAPKPL-LEQCKEK-GIPVYQSYGMTETasqivtlspedal 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ------GDP--------------------------------------EKTAKVECGDFYNTGDRGKMDEEGYICFLGRSD 408
Cdd:PRK03640 304 tklgsaGKPlfpcelkiekdgvvvppfeegeivvkgpnvtkgylnreDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 409 DIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlshDKDqltkELQQHVKSVTAPYKYPRK 488
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEV---TEE----ELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|....*..
gi 578828477 489 VEFVSELPKTITGKIERKELRKKETGQ 515
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
65-516 |
7.54e-32 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 129.63 E-value: 7.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 65 EGKRGPNPAFWW-VNGQGDEVKWSFREMGDLTRRVANvFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATI 143
Cdd:PLN02654 99 EAGNGDKIAIYWeGNEPGFDASLTYSELLDRVCQLAN-YLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 144 LLKAKDILYRLQLSKAKGIVTIDALASEVDSI-------ASQCPSLKTKLLV---------SDHSREG--WLDFRSL--- 202
Cdd:PLN02654 178 GFSAESLAQRIVDCKPKVVITCNAVKRGPKTInlkdivdAALDESAKNGVSVgicltyenqLAMKREDtkWQEGRDVwwq 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 203 -VKSASPEHTCVK-SKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLV 280
Cdd:PLN02654 258 dVVPNYPTKCEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 281 EPWTAGCTVFIHH-LPQF-DTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRR 358
Cdd:PLN02654 338 GPMLNGATVLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWF 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 359 TGLL------LYENYGQSETGD----------PEKTAKV---------------------EC------------------ 383
Cdd:PLN02654 418 FNVVgdsrcpISDTWWQTETGGfmitplpgawPQKPGSAtfpffgvqpvivdekgkeiegECsgylcvkkswpgafrtly 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 GD--------------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEV 449
Cdd:PLN02654 498 GDheryettyfkpfagYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQG 577
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 450 VKAFIVLTPQFLShdKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PLN02654 578 IYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 642
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
40-509 |
1.56e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 128.02 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 40 WNDYE---VPEEFNFASY--VLDYWAQKEKegKRGPNPAFwwvNGQGdeVKWSFREMGDLTRRVANVFTQTCGLQQGDHL 114
Cdd:PRK12492 6 WNDKRpagVPSTIDLAAYksVVEVFERSCK--KFADRPAF---SNLG--VTLSYAELERHSAAFAAYLQQHTDLVPGDRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 115 ALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQC--------------P 180
Cdd:PRK12492 79 AVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTgieylieakmgdllP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 181 SLK----------TKLLVSDHSREGWLDFRSLVK-SASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQpsfp 249
Cdd:PRK12492 159 AAKgwlvntvvdkVKKMVPAYHLPQAVPFKQALRqGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 250 gsrklrslKTSDVSWCLSDSGWIVATIW-----TLVEP--------WTAGCTVFI----HHL----PQfDTKVIIQTLLK 308
Cdd:PRK12492 235 --------NMLQVRACLSQLGPDGQPLMkegqeVMIAPlplyhiyaFTANCMCMMvsgnHNVlitnPR-DIPGFIKELGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 309 YPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG-------------- 373
Cdd:PRK12492 306 WRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpvastnpygelarl 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 -------------------------------------------DPEKTAKV-ECGDFYNTGDRGKMDEEGYICFLGRSDD 409
Cdd:PRK12492 386 gtvgipvpgtalkvidddgnelplgergelcikgpqvmkgywqQPEATAEAlDAEGWFKTGDIAVIDPDGFVRIVDRKKD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 410 IINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDkdqltkELQQHVKSVTAPYKYPRKV 489
Cdd:PRK12492 466 LIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE------ELKAYCKENFTGYKVPKHI 539
|
570 580
....*....|....*....|
gi 578828477 490 EFVSELPKTITGKIERKELR 509
Cdd:PRK12492 540 VLRDSLPMTPVGKILRRELR 559
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
83-511 |
5.47e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 126.21 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 83 EVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGI 162
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIDALASEVDSIASQCPslKTKLLVSD--------HSREGWLDFRSLVKSASPEHTCVKSK-TLDPMVIFFTSGTTGFP 233
Cdd:PRK08162 120 IVDTEFAEVAREALALLP--GPKPLVIDvddpeypgGRFIGALDYEAFLASGDPDFAWTLPAdEWDAIALNYTSGTTGNP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 234 K---------------------MAKHSHGLALQPSFPGSrklrslktsdvSWCLsdsgwivatiwtlvePWT----AGCT 288
Cdd:PRK08162 198 KgvvyhhrgaylnalsnilawgMPKHPVYLWTLPMFHCN-----------GWCF---------------PWTvaarAGTN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 289 VFihhLPQFDTKVIIQTLLKYPINHFWGVSSIYRMIL------QQDFT-SIRF-------PA------------LEHCY- 341
Cdd:PRK08162 252 VC---LRKVDPKLIFDLIREHGVTHYCGAPIVLSALInapaewRAGIDhPVHAmvagaapPAaviakmeeigfdLTHVYg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 342 ---TGGEVVLPKDQEEW-----------KRRTGL--LLYE--NYGQSETG--------------------------DPEK 377
Cdd:PRK08162 329 lteTYGPATVCAWQPEWdalplderaqlKARQGVryPLQEgvTVLDPDTMqpvpadgetigeimfrgnivmkgylkNPKA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 378 TAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLt 457
Cdd:PRK08162 409 TEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVEL- 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 458 pqflshdKDQLT---KELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIERKELRKK 511
Cdd:PRK08162 488 -------KDGASateEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
87-510 |
1.39e-30 |
|
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: 123.64 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTid 166
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 alasevdsiasqcPSLktkllvsdhsregwldFRSLVKSASPEHTCVksktldpmvIFFTSGTTGFPKMAKHSHGLALQP 246
Cdd:cd05903 80 -------------PER----------------FRQFDPAAMPDAVAL---------LLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 247 SFPGSRKLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVfiHHLPQFDTKVIIQTLLKYPINHFWGVSS-IYRMIL 325
Cdd:cd05903 122 IRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGATPfLTDLLN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 326 QQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG-------------------------------- 373
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPgavtsitpapedrrlytdgrplpgveikvvdd 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 --------------------------DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESAL 427
Cdd:cd05903 279 tgatlapgvegellsrgpsvflgyldRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 428 VEHPAVAESAVVGSPDPIRGEVVKAFIVL-TPQFLSHDkdqltkELQQHVKSV-TAPYKYPRKVEFVSELPKTITGKIER 505
Cdd:cd05903 359 LGHPGVIEAAVVALPDERLGERACAVVVTkSGALLTFD------ELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
....*
gi 578828477 506 KELRK 510
Cdd:cd05903 433 FRLRE 437
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
42-511 |
4.84e-30 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 123.55 E-value: 4.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 42 DYEVPEEFNFASYVLdywaqkEKEGKRGPNPAFwwVNGQGDEVkWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRV 121
Cdd:PLN02246 16 DIYIPNHLPLHDYCF------ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLHKL-GIRQGDVVMLLLPNC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 122 PEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTidaLASEVDSIASQCPSLKTKLLVSDHSREGWLDFRS 201
Cdd:PLN02246 86 PEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 202 LVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPK--MAKHshglalqpsfpgsrklRSLKTS-----------------DV 262
Cdd:PLN02246 163 LTQADENELPEVEISPDDVVALPYSSGTTGLPKgvMLTH----------------KGLVTSvaqqvdgenpnlyfhsdDV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 263 SWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDT----------KV--------IIQTLLKYPINHFWGVSSIyRMI 324
Cdd:PLN02246 227 ILCVLPMFHIYSLNSVLLCGLRVGAAILI--MPKFEIgalleliqrhKVtiapfvppIVLAIAKSPVVEKYDLSSI-RMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 325 LQ---------QDFTSIRFP---------------ALEHCY----------TG--GEVVLPKDQEEWKRRTGLLLYENYG 368
Cdd:PLN02246 304 LSgaaplgkelEDAFRAKLPnavlgqgygmteagpVLAMCLafakepfpvkSGscGTVVRNAELKIVDPETGASLPRNQP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 369 --------QSETG---DPEKTAK-VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAES 436
Cdd:PLN02246 384 geicirgpQIMKGylnDPEATANtIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADA 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828477 437 AVVGSPDPIRGEVVKAFIVLTPQF-LSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PLN02246 464 AVVPMKDEVAGEVPVAFVVRSNGSeITED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
422-502 |
1.05e-29 |
|
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: 111.10 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 422 EVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITG 501
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 578828477 502 K 502
Cdd:pfam13193 76 K 76
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
207-511 |
1.23e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 122.17 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 207 SPEHTCVKSKTldpmvIFFTSGTTGFPKMAKHshglalqPSFPGSRKLRSLkTSDVSWCLSDSGWIVATI---WTLVEPW 283
Cdd:PRK13382 190 RPEPTGRKGRV-----ILLTSGTTGTPKGARR-------SGPGGIGTLKAI-LDRTPWRAEEPTVIVAPMfhaWGFSQLV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 284 TAG---CTVFIHHlpQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--------QDFTSIRFPAlehcyTGGEVVLPKDQ 352
Cdd:PRK13382 257 LAAslaCTIVTRR--RFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpaevrnrYSGRSLRFAA-----ASGSRMRPDVV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 353 EEWKRRTGLLLYENYGQSETG-----DPEK------TA---------KV------ECGD--------------------- 385
Cdd:PRK13382 330 IAFMDQFGDVIYNNYNATEAGmiataTPADlraapdTAgrpaegteiRIldqdfrEVPTgevgtifvrndtqfdgytsgs 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 -------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP 458
Cdd:PRK13382 410 tkdfhdgFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578828477 459 qflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK13382 490 -----GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
81-508 |
1.72e-29 |
|
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: 121.28 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVtidalasevdsiasqcpslktkllVSDhsREGWLDFRSLVKSaspehtcVKSKTLDPMVIFFTSGTTGFPKMAKHSH 240
Cdd:cd05920 115 AYI------------------------VPD--RHAGFDHRALARE-------LAESIPEVALFLLSGGTTGTPKLIPRTH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 glalqpsfpgSRKLRSLKTSdVSWCLSDSgwivATIWTLVEP----------------WTAGCTVFI------HHLPQFD 298
Cdd:cd05920 162 ----------NDYAYNVRAS-AEVCGLDQ----DTVYLAVLPaahnfplacpgvlgtlLAGGRVVLApdpspdAAFPLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 299 TKVIIQTLLKYPINHFW---------GVSSIyRMI----------------------LQQDF---------TSIRFPALE 338
Cdd:cd05920 227 REGVTVTALVPALVSLWldaaasrraDLSSL-RLLqvggarlspalarrvppvlgctLQQVFgmaegllnyTRLDDPDEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 339 HCYTGGEVVLPKDQ-----EEwkrrtglllYENYGQSETGD---------------PEKTAKVECGD-FYNTGDRGKMDE 397
Cdd:cd05920 306 IIHTQGRPMSPDDEirvvdEE---------GNPVPPGEEGElltrgpytirgyyraPEHNARAFTPDgFYRTGDLVRRTP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 398 EGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLShdkdqlTKELQQHVK 477
Cdd:cd05920 377 DGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPS------AAQLRRFLR 450
|
490 500 510
....*....|....*....|....*....|..
gi 578828477 478 SV-TAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd05920 451 ERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
374-505 |
2.73e-29 |
|
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: 117.76 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRS--DDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVK 451
Cdd:cd17637 205 LPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIK 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578828477 452 AFIVLTP-QFLShdkdqlTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIER 505
Cdd:cd17637 285 AVCVLKPgATLT------ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
219-511 |
3.53e-29 |
|
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: 117.43 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 219 DPMVIFFTSGTTGFPKMAKHSHgLALQPSFPGSRKLRSLKTSDVSWCLSDSGWI--VATIWTLVepWTAGCTVFIHHLPQ 296
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTA-ANLLASAAGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSL--LAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 297 FdtkviIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSETG--- 373
Cdd:cd17630 78 L-----AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETAsqv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ---DPEKTAKVECGDF---------------------------------------YNTGDRGKMDEEGYICFLGRSDDII 411
Cdd:cd17630 152 atkRPDGFGRGGVGVLlpgrelrivedgeiwvggaslamgylrgqlvpefnedgwFTTKDLGELHADGRLTVLGRADNMI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 412 NASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflshDKDQLTKELQQHVKSVTAPYKYPRKVEF 491
Cdd:cd17630 232 ISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGPADPAELRAWLKDKLARFKLPKRIYP 304
|
330 340
....*....|....*....|
gi 578828477 492 VSELPKTITGKIERKELRKK 511
Cdd:cd17630 305 VPELPRTGGGKVDRRALRAW 324
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
85-509 |
4.58e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 119.91 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 85 KWSFREMGDLTRRVANVFtQTCGLQQGDHLA-LMLPRVpewWLVAV--GCMRTGIIFIPATillkakdilYRLQlskakg 161
Cdd:PRK09088 22 RWTYAELDALVGRLAAVL-RRRGCVDGERLAvLARNSV---WLVALhfACARVGAIYVPLN---------WRLS------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 ivtidalASEVDSIASQC-PSLktkLLVSDHSREGWLD------FRSLVKSASPEHTcvksKTLDP---MVIFFTSGTTG 231
Cdd:PRK09088 83 -------ASELDALLQDAePRL---LLGDDAVAAGRTDvedlaaFIASADALEPADT----PSIPPervSLILFTSGTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 232 FPKMAKHSHGLALQPSFPGSRKLRSLKTSdVSWCLSDSGWIVATIwTLVEPWTA-GCTVFIHhlPQFDTKVIIQTL--LK 308
Cdd:PRK09088 149 QPKGVMLSERNLQQTAHNFGVLGRVDAHS-SFLCDAPMFHIIGLI-TSVRPVLAvGGSILVS--NGFEPKRTLGRLgdPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 309 YPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSETG-------------- 373
Cdd:PRK09088 225 LGITHYFCVPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGtvfgmsvdcdvira 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ---------------------------------------------DPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRS 407
Cdd:PRK09088 304 kagaagiptptvqtrvvddqgndcpagvpgelllrgpnlspgywrRPQATARAFTGDgWFRTGDIARRDADGFFWVVDRK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 408 DDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflshdKDQLTKELQQHVKSVTAPYKYPR 487
Cdd:PRK09088 384 KDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-----APLDLERIRSHLSTRLAKYKVPK 458
|
490 500
....*....|....*....|..
gi 578828477 488 KVEFVSELPKTITGKIERKELR 509
Cdd:PRK09088 459 HLRLVDALPRTASGKLQKARLR 480
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
373-509 |
5.25e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 119.71 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGR-SDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVV 450
Cdd:PRK07787 337 NRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRI 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578828477 451 KAFIVltpqflSHDkDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK07787 417 VAYVV------GAD-DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
366-509 |
8.09e-29 |
|
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: 119.02 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 366 NYGQSETGDPEKTA-KVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP 444
Cdd:cd05929 330 GPGFEYTNDPEKTAaARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDE 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578828477 445 IRGEVVKAfiVLTPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:cd05929 410 ELGQRVHA--VVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
67-511 |
1.54e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 119.43 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 67 KRGPNPAFWWVNGqGDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIP--ATIL 144
Cdd:COG1022 23 RFPDRVALREKED-GIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPiyPTSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 145 lkAKDILYRLQLSKAKGIVTID-ALASEVDSIASQCPSLKT-----KLLVSDHSREGWLD--------------FRSLVK 204
Cdd:COG1022 101 --AEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLRHivvldPRGLRDDPRLLSLDellalgrevadpaeLEARRA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 205 SASPEhtcvksktlDPMVIFFTSGTTGFPKMAKHSHG------LALQPSFPgsrklrsLKTSDVSWC---LSdsgWIVAT 275
Cdd:COG1022 179 AVKPD---------DLATIIYTSGTTGRPKGVMLTHRnllsnaRALLERLP-------LGPGDRTLSflpLA---HVFER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 276 IWTLVePWTAGCTVfiHHLPqfDTKVIIQTLLKYPINHFWGV----SSIYRMILQQ------------------------ 327
Cdd:COG1022 240 TVSYY-ALAAGATV--AFAE--SPDTLAEDLREVKPTFMLAVprvwEKVYAGIQAKaeeagglkrklfrwalavgrryar 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 328 -DFTSIRFPA------------------------LEHCYTGGEvVLPKDQEEWKRRTGLLLYENYGQSET---------- 372
Cdd:COG1022 315 aRLAGKSPSLllrlkhaladklvfsklrealggrLRFAVSGGA-ALGPELARFFRALGIPVLEGYGLTETspvitvnrpg 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ------------------------------------GDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDII-NAS 414
Cdd:COG1022 394 dnrigtvgpplpgvevkiaedgeilvrgpnvmkgyyKNPEATAEAFDADgWLHTGDIGELDEDGFLRITGRKKDLIvTSG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 415 GYRIGPAEVESALVEHPAVAESAVVGSPDPirgeVVKAFIVLTPQFLSH----------------DKDQLTKELQQHVKS 478
Cdd:COG1022 474 GKNVAPQPIENALKASPLIEQAVVVGDGRP----FLAALIVPDFEALGEwaeenglpytsyaelaQDPEVRALIQEEVDR 549
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 578828477 479 VT---APYKYPRKVEFvseLPK---------TITGKIERKELRKK 511
Cdd:COG1022 550 ANaglSRAEQIKRFRL---LPKeftiengelTPTLKLKRKVILEK 591
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
89-509 |
1.94e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 118.26 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 89 REMGDLTRRVANVFT--QTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVtid 166
Cdd:PRK12406 12 RSFDELAQRAARAAGglAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQCPSLKTKLLV------------SDHSR---EGWLDFRS-LVKSASPEHTCVKSktldPMVIFFTSGTT 230
Cdd:PRK12406 89 AHADLLHGLASALPAGVTVLSVptppeiaaayriSPALLtppAGAIDWEGwLAQQEPYDGPPVPQ----PQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 231 GFPKMAKHSHGLALQpsfpgsrklrslktsdvswcLSDSGWIVATIWTLVEPWTAGCTVFIHH----------------- 293
Cdd:PRK12406 165 GHPKGVRRAAPTPEQ--------------------AAAAEQMRALIYGLKPGIRALLTGPLYHsapnayglragrlggvl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 294 --LPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--------QDFTSIRF---------------------PALEHCYT 342
Cdd:PRK12406 225 vlQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRHvihaaapcpadvkramiewwgPVIYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 343 GGE--VVLPKDQEEWKRRTGLL-----------LYEN---YGQSETGD----------------PEKTAKVECGDFYNTG 390
Cdd:PRK12406 305 STEsgAVTFATSEDALSHPGTVgkaapgaelrfVDEDgrpLPQGEIGEiysriagnpdftyhnkPEKRAEIDRGGFITSG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 391 DRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAfiVLTPQ---FLSHDkdq 467
Cdd:PRK12406 385 DVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMA--VVEPQpgaTLDEA--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 578828477 468 ltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK12406 460 ---DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
79-509 |
3.12e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 118.23 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 79 GQGDEVKWSFREMGDLTRRVAnVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSK 158
Cdd:PRK13295 49 GTGAPRRFTYRELAALVDRVA-VGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 159 AKGIVTIDAL-----ASEVDSIASQCPSLKTKLLVSDhsrEGWLDFRSLVKSASPE-----HTCVKSKTLDP---MVIFF 225
Cdd:PRK13295 128 SKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVGG---DGADSFEALLITPAWEqepdaPAILARLRPGPddvTQLIY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 226 TSGTTGFPKMAKHSHGLALQPSFPGSRKLRsLKTSDV-------------------------SWCLSDSgWIVATIWTLV 280
Cdd:PRK13295 205 TSGTTGEPKGVMHTANTLMANIVPYAERLG-LGADDVilmaspmahqtgfmyglmmpvmlgaTAVLQDI-WDPARAAELI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 281 E----PWTAGCTVFIHHL-----------PQFDT---------KVII---QTLLKYPINHFWGVSS--IYRMILQQD--- 328
Cdd:PRK13295 283 RtegvTFTMASTPFLTDLtravkesgrpvSSLRTflcagapipGALVeraRAALGAKIVSAWGMTEngAVTLTKLDDpde 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 329 --FTSIRFPalehcYTGGEV--------VLPKDQEEWKRRTGLLLYENYgqseTGDPEKTAKVECGdFYNTGDRGKMDEE 398
Cdd:PRK13295 363 raSTTDGCP-----LPGVEVrvvdadgaPLPAGQIGRLQVRGCSNFGGY----LKRPQLNGTDADG-WFDTGDLARIDAD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 399 GYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSHDKDQLTKELQQHvkS 478
Cdd:PRK13295 433 GYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ--K 509
|
490 500 510
....*....|....*....|....*....|.
gi 578828477 479 VTAPYkYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK13295 510 VAKQY-IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
81-508 |
3.32e-28 |
|
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: 116.93 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTidalasevdsiasqcpslktkllvsdhsreGWLDfrslvksaspehtcvksktlDPMVIFFTSGTTGFPKMAKHSH 240
Cdd:cd05907 80 ALFV------------------------------EDPD--------------------DLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 GLALQPSFPGSRKLRSLKTsDVSWCLSDSGWIVATIWTLVEPWTAGCTvfIHHLPqfDTKVIIQTLLKYPINHFWGVSSI 320
Cdd:cd05907 110 RNILSNALALAERLPATEG-DRHLSFLPLAHVFERRAGLYVPLLAGAR--IYFAS--SAETLLDDLSEVRPTVFLAVPRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 321 YRMI------------LQQDFTSIRFPALEHCYTGGeVVLPKDQEEWKRRTGLLLYENYGQSET---------------- 372
Cdd:cd05907 185 WEKVyaaikvkavpglKRKLFDLAVGGRLRFAASGG-APLPAELLHFFRALGIPVYEGYGLTETsavvtlnppgdnrigt 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ------------------------------GDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDD-IINASGYRIGP 420
Cdd:cd05907 264 vgkplpgvevriaddgeilvrgpnvmlgyyKNPEATAEALDADgWLHTGDLGEIDEDGFLHITGRKKDlIITSGGKNISP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 421 AEVESALVEHPAVAESAVVGSPDPirgeVVKAFIVLTPQFLSHDKDQ----------------LTKELQQHVKSVTA--- 481
Cdd:cd05907 344 EPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEALEAWAEEhgiaytdvaelaanpaVRAEIEAAVEAANArls 419
|
490 500 510
....*....|....*....|....*....|....
gi 578828477 482 PYKYPRKVEFVSElPKTI-------TGKIERKEL 508
Cdd:cd05907 420 RYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-510 |
7.47e-28 |
|
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: 114.50 E-value: 7.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 224 FFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSlKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVII 303
Cdd:cd05944 8 FHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLF-DPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 304 QTLLK----YPINHFWGVSSIYRMILQ----QDFTSIRFPAlehcytGGEVVLPKD-QEEWKRRTGLLLYENYGQSETG- 373
Cdd:cd05944 87 DNFWKlverYRITSLSTVPTVYAALLQvpvnADISSLRFAM------SGAAPLPVElRARFEDATGLPVVEGYGLTEATc 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ------------------------------DPEKTAKVECGD-------------------------------FYNTGDR 392
Cdd:cd05944 161 lvavnppdgpkrpgsvglrlpyarvrikvlDGVGRLLRDCAPdevgeicvagpgvfggylytegnknafvadgWLNTGDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 393 GKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSHDKDQLTKEL 472
Cdd:cd05944 241 GRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG-AVVEEEELLAWA 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 578828477 473 QQHVKSVTApykYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05944 320 RDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
82-508 |
8.17e-28 |
|
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: 116.15 E-value: 8.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEwwLVAV--GCMRTGIIFIPATILLKAKDILYRLQLSKA 159
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPE--LVVAllAVLKAGAAYVPLDPELPAERLAFMLADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTIDALASEVDSiasqcpsLKTKLLVSDHSREGwlDFRSLVKSASPEHTCVksktldpmvIFFTSGTTGFPK--MAK 237
Cdd:cd12117 96 KVLLTDRSLAGRAGG-------LEVAVVIDEALDAG--PAGNPAVPVSPDDLAY---------VMYTSGSTGRPKgvAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 238 HSH--GLALQPSFpgsrklRSLKTSDVSWCLSDSGWIVAT--IWTlvePWTAGCTVFI---HHLpqFDTKVIIQTLLKYP 310
Cdd:cd12117 158 HRGvvRLVKNTNY------VTLGPDDRVLQTSPLAFDASTfeIWG---ALLNGARLVLapkGTL--LDPDALGALIAEEG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 311 INHFWGVSSIYRMILQQD---FTSIRfpaleHCYTGGEVVLPKDQEEWKRRT-GLLLYENYGQSET-------------- 372
Cdd:cd12117 227 VTVLWLTAALFNQLADEDpecFAGLR-----ELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENttfttshvvtelde 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ----------------------------------------------GDPEKTAK--VEC-----GDFYNTGDRGKMDEEG 399
Cdd:cd12117 302 vagsipigrpiantrvyvldedgrpvppgvpgelyvggdglalgylNRPALTAErfVADpfgpgERLYRTGDLARWLPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 400 YICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAV-VGSPDPIRGEVVkAFIVLTPQfLSHDkdqltkELQQHVKS 478
Cdd:cd12117 382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA------ELRAFLRE 453
|
490 500 510
....*....|....*....|....*....|
gi 578828477 479 VTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd12117 454 RLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
389-512 |
8.83e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 116.95 E-value: 8.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 389 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQL 468
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP-----GAALD 505
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578828477 469 TKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 512
Cdd:PRK07788 506 EDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
83-510 |
2.49e-27 |
|
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: 115.32 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 83 EVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGI 162
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIDALASEVDSIASQCPSLKTKLLVSdhSREGWLDFRSL---VKSASPEHTCVKS-------KTLDPMVIFFTSGTTGF 232
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKTIIILD--SKEDYKGYQCLytfITQNLPPGFNEYDfkppsfdRDEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 233 PK---------MAKHSHglALQPSF-----PGSRKLRSLKTSDVSWCLSDSGWIVatiwtlvepwtagCTVFIHHLPQFD 298
Cdd:cd17642 199 PKgvqlthkniVARFSH--ARDPIFgnqiiPDTAILTVIPFHHGFGMFTTLGYLI-------------CGFRVVLMYKFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 299 TKVIIQTLLKYPINHFWGVSSIY------RMILQQDFTSIrfpaleHCYTGGEVVLPKDQEEW-KRRTGL-LLYENYGQS 370
Cdd:cd17642 264 EELFLRSLQDYKVQSALLVPTLFaffaksTLVDKYDLSNL------HEIASGGAPLSKEVGEAvAKRFKLpGIRQGYGLT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 371 ET---------------------------------------------------------GDPEKTAKVECGD-FYNTGDR 392
Cdd:cd17642 338 ETtsailitpegddkpgavgkvvpffyakvvdldtgktlgpnergelcvkgpmimkgyvNNPEATKALIDKDgWLHSGDI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 393 GKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqfLSHDKDQLTKEL 472
Cdd:cd17642 418 AYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV-----LEAGKTMTEKEV 492
|
490 500 510
....*....|....*....|....*....|....*....
gi 578828477 473 QQHVKSVTAPYKYPR-KVEFVSELPKTITGKIERKELRK 510
Cdd:cd17642 493 MDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
81-508 |
2.51e-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: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:cd17646 19 DEGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTIDALAsevdsiasqcPSLKTKLLVSDHSREGWLDFRSlvksASPEhtcVKSKTLDPMVIFFTSGTTGFPK--MAKH 238
Cdd:cd17646 98 VVLTTADLA----------ARLPAGGDVALLGDEALAAPPA----TPPL---VPPRPDNLAYVIYTSGSTGRPKgvMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 239 sHGLA-----LQPSFPGSRKLRSL-KTS---DVSwclsdsgwivatIWTLVEPWTAGCTVFI---------HHLPQFDTK 300
Cdd:cd17646 161 -AGIVnrllwMQDEYPLGPGDRVLqKTPlsfDVS------------VWELFWPLVAGARLVVarpgghrdpAYLAALIRE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 301 VIIQTLlkypinHFwgVSSIYRMILQQDfTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRTGLLLYENYGQSET------- 372
Cdd:cd17646 228 HGVTTC------HF--VPSMLRVFLAEP-AAGSCASLRRVFCSGEA-LPPELaARFLALPGAELHNLYGPTEAaidvthw 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ----------------------------------------------------GDPEKTAKVECGD-------FYNTGDRG 393
Cdd:cd17646 298 pvrgpaetpsvpigrpvpntrlyvlddalrpvpvgvpgelylggvqlargylGRPALTAERFVPDpfgpgsrMYRTGDLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 394 KMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDkdqlTKELQ 473
Cdd:cd17646 378 RWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPD----TAALR 453
|
490 500 510
....*....|....*....|....*....|....*
gi 578828477 474 QHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17646 454 AHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
81-509 |
1.46e-26 |
|
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: 112.44 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTIDALASEVDSIAsqcpslktkllvsdhsREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH 240
Cdd:cd17651 95 LVLTHPALAGELAVEL----------------VAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 G------LALQPSFPGSRKLRSLKTSDVSWCLSdsgwiVATIW-TLVepwTAGCTVFI---------HHLPQFDTKVIIQ 304
Cdd:cd17651 159 RslanlvAWQARASSLGPGARTLQFAGLGFDVS-----VQEIFsTLC---AGATLVLPpeevrtdppALAAWLDEQRISR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 305 TLLKYPINHFWgvssiyrmILQQDFTSIRFPALEHCYTGGE-VVLPKDQEEW-KRRTGLLLYENYGQSET---------- 372
Cdd:cd17651 231 VFLPTVALRAL--------AEHGRPLGVRLAALRYLLTGGEqLVLTEDLREFcAGLPGLRLHNHYGPTEThvvtalslpg 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 --------------------------------------------------GDPEKTAK-------VECGDFYNTGDRGKM 395
Cdd:cd17651 303 dpaawpapppigrpidntrvyvldaalrpvppgvpgelyiggaglargylNRPELTAErfvpdpfVPGARMYRTGDLARW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 396 DEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQQH 475
Cdd:cd17651 383 LPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDP-----EAPVDAAELRAA 457
|
490 500 510
....*....|....*....|....*....|....
gi 578828477 476 VKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:cd17651 458 LATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
84-511 |
3.13e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 112.21 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 84 VKWSFREMGDLTRRVAnvftqtCGL-----QQGDHLALMLPRVPEWWLVAVGCMRTGIIFI---PAtilLKAKDILYRLQ 155
Cdd:PRK08315 42 LRWTYREFNEEVDALA------KGLlalgiEKGDRVGIWAPNVPEWVLTQFATAKIGAILVtinPA---YRLSELEYALN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 156 LSKAKGIVTIDA------------LASEVDSI------ASQCPSLKTKLLVSDHSREGWLDFRSLV---KSASPEHTCVK 214
Cdd:PRK08315 113 QSGCKALIAADGfkdsdyvamlyeLAPELATCepgqlqSARLPELRRVIFLGDEKHPGMLNFDELLalgRAVDDAELAAR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 215 SKTL---DPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRsLKTSD-----------------VSWCLSdSGwivA 274
Cdd:PRK08315 193 QATLdpdDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMK-LTEEDrlcipvplyhcfgmvlgNLACVT-HG---A 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 275 TIWTLVE---PWTA-------GCTV-------FIHHL--PQFDT----------------------KVIIQTllkypinH 313
Cdd:PRK08315 268 TMVYPGEgfdPLATlaaveeeRCTAlygvptmFIAELdhPDFARfdlsslrtgimagspcpievmkRVIDKM-------H 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 314 FWGVSSIYRM------ILQqdfTSIRFP----------ALEHCytggEV--VLPKDQEEWKR-RTGLLLYENYG--QSET 372
Cdd:PRK08315 341 MSEVTIAYGMtetspvSTQ---TRTDDPlekrvttvgrALPHL----EVkiVDPETGETVPRgEQGELCTRGYSvmKGYW 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVK 451
Cdd:PRK08315 414 NDPEKTAEAIDADgWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVC 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828477 452 AFIVLtpqflsHDKDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK08315 494 AWIIL------RPGATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
80-502 |
3.65e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 111.90 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 80 QGDEVkWSFREMGDLTRRVANvFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKA 159
Cdd:PRK07798 24 CGDRR-LTYAELEERANRLAH-YLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTIDALASEVDSIASQCPSLKTKLLVSDHS----REGWLDFRSLVKSASPEHTCVKsKTLDPMVIFFTSGTTGFPKM 235
Cdd:PRK07798 102 VALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDALAAGSPERDFGE-RSPDDLYLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 236 AKHSHGLALQPSFPGSRKLRSLKTSDvSWCLSDSG-------WIV-------ATIWTLVEPWTAGCTVFIHHLPQFDTKV 301
Cdd:PRK07798 181 VMWRQEDIFRVLLGGRDFATGEPIED-EEELAKRAaagpgmrRFPapplmhgAGQWAAFAALFSGQTVVLLPDVRFDADE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 302 IIQTLLKYpinhfwGVSSIY-------RMILQQ-------DFTSIRFPAlehcyTGGEVVLPKDQEEW-KRRTGLLLYEN 366
Cdd:PRK07798 260 VWRTIERE------KVNVITivgdamaRPLLDAleargpyDLSSLFAIA-----SGGALFSPSVKEALlELLPNVVLTDS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 367 YGQSETG---------------------------------------------------------DPEKTAK----VEcGD 385
Cdd:PRK07798 329 IGSSETGfggsgtvakgavhtggprftigprtvvldedgnpvepgsgeigwiarrghiplgyykDPEKTAEtfptID-GV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 FYN-TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSHD 464
Cdd:PRK07798 408 RYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPD 486
|
490 500 510
....*....|....*....|....*....|....*...
gi 578828477 465 KDqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 502
Cdd:PRK07798 487 LA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
82-514 |
1.08e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 110.62 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKG 161
Cdd:PRK06155 43 GGTRWTYAEAARAAAAAAHAL-AAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 IVTIDALASEVDSIASQCPSLKTKLLVSDHSREGW---LDFRSLVKSASPEhTCVKSKTLDPMVIFFTSGTTGFPKMAKH 238
Cdd:PRK06155 122 LVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpagWSTAPLPPLDAPA-PAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 239 SHGlalQPSFPG--SRKLRSLKTSDVSW-CLSDsgWIVATIWTLVEPWTAGCTVFIhhLPQFDTKVIIQTLLKYPINHFW 315
Cdd:PRK06155 201 PHA---QFYWWGrnSAEDLEIGADDVLYtTLPL--FHTNALNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVTY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 316 GVSSIYRMILQQDFT-SIRFPALEHCYTGGevVLPKDQEEWKRRTGLLLYENYGQSET---------------------- 372
Cdd:PRK06155 274 LLGAMVSILLSQPAReSDRAHRVRVALGPG--VPAALHAAFRERFGVDLLDGYGSTETnfviavthgsqrpgsmgrlapg 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ------------------------------------GDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGY 416
Cdd:PRK06155 352 fearvvdehdqelpdgepgelllradepfafatgyfGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 417 RIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSEL 495
Cdd:PRK06155 432 NISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDgTALEPV------ALVRHCEPRLAYFAVPRYVEFVAAL 505
|
490
....*....|....*....
gi 578828477 496 PKTITGKIERKELRkkETG 514
Cdd:PRK06155 506 PKTENGKVQKFVLR--EQG 522
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
223-505 |
1.52e-25 |
|
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: 107.20 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IFFTSGTTGFPK--MAKHSHGLALQPSFPGSRKLRSlktSDVSWCLS--------DSGWIVATIwtlvepwtAGCTVFIH 292
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQTLRAAAAWADCADLTE---DDRYLIINpffhtfgyKAGIVACLL--------TGATVVPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 293 HLpqFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ------DFTSIRFPAlehcyTGGEVVLPkdqEEWKRRTGLLLYEN 366
Cdd:cd17638 74 AV--FDVDAILEAIERERITVLPGPPTLFQSLLDHpgrkkfDLSSLRAAV-----TGAATVPV---ELVRRMRSELGFET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 367 ----YGQSETG------------------------------------------------DPEKTAK-VECGDFYNTGDRG 393
Cdd:cd17638 144 vltaYGLTEAGvatmcrpgddaetvattcgracpgfevriaddgevlvrgynvmqgyldDPEATAEaIDADGWLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 394 KMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSHDKDQLTKELQ 473
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTLTEEDVIAWCR 302
|
330 340 350
....*....|....*....|....*....|..
gi 578828477 474 QHVksvtAPYKYPRKVEFVSELPKTITGKIER 505
Cdd:cd17638 303 ERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
80-509 |
3.21e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 109.06 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 80 QGDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKA 159
Cdd:PRK06164 30 IDEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTIDA-----LASEVDSIA-SQCPSLKTKLLVS-------DHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFT 226
Cdd:PRK06164 109 RWLVVWPGfkgidFAAILAAVPpDALPPLRAIAVVDdaadatpAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 227 -SGTTGFPKMAKHS------HGLALQPSF---PGSRKLRSLKTSDVsWCLSdsgwivatiwTLVEPWTAGCTVfiHHLPQ 296
Cdd:PRK06164 189 tSGTTSGPKLVLHRqatllrHARAIARAYgydPGAVLLAALPFCGV-FGFS----------TLLGALAGGAPL--VCEPV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 297 FDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCytGGEVVLPKDQE--EWKRRTGLLLYENYGQSET-- 372
Cdd:PRK06164 256 FDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPALGElaALARARGVPLTGLYGSSEVqa 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -----------------------------------------------------------GDPEKTAKVECGD-FYNTGDR 392
Cdd:PRK06164 334 lvalqpatdpvsvriegggrpaspearvrardpqdgallpdgesgeieirapslmrgylDNPDATARALTDDgYFRTGDL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 393 GKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpdPIRGE-VVKAFIVLTPqflSHDKDQltKE 471
Cdd:PRK06164 414 GYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTD---GASPDE--AG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 578828477 472 LQQHVKSVTAPYKYPRKVEFVSELPKTITG---KIERKELR 509
Cdd:PRK06164 487 LMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
92-514 |
4.02e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 108.43 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 92 GDLTRRV--ANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKgIVTIDala 169
Cdd:PRK06145 31 AEFHQRIlqAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAK-LLLVD--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 170 SEVDSIasqcPSLKTKLLVSDHSREGwlDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFP 249
Cdd:PRK06145 107 EEFDAI----VALETPKIVIDAAAQA--DSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSID 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 250 GSRKLrSLKTSD---VSWCLSDSGWI----VATIWTlvepwtaGCTVFIHHlpQFDTKVIIQTLLKYPINHFWGVSSIYR 322
Cdd:PRK06145 181 HVIAL-GLTASErllVVGPLYHVGAFdlpgIAVLWV-------GGTLRIHR--EFDPEAVLAAIERHRLTCAWMAPVMLS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 323 MIL------QQDFTSIRFpalehCYTGGEVVLPKDQEEWKRR-TGLLLYENYGQSET----------------------- 372
Cdd:PRK06145 251 RVLtvpdrdRFDLDSLAW-----CIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETcsgdtlmeagreiekigstgral 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -----------------------------------GDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYR 417
Cdd:PRK06145 326 ahveiriadgagrwlppnmkgeicmrgpkvtkgywKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 418 IGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELP 496
Cdd:PRK06145 406 IASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgATLTLE------ALDRHCRQRLASFKVPRQLKVRDELP 479
|
490
....*....|....*...
gi 578828477 497 KTITGKIERKELRKKETG 514
Cdd:PRK06145 480 RNPSGKVLKRVLRDELNG 497
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
87-508 |
5.26e-25 |
|
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: 107.98 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKG-IVTI 165
Cdd:cd05923 30 TYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAaVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 166 DALASEVDSIASQCpslktKLLVSDHSREGWLDfrslvkSASPEHTCVKSKTLDPMVIFFTSGTTGFPK----------- 234
Cdd:cd05923 109 DAQVMDAIFQSGVR-----VLALSDLVGLGEPE------SAGPLIEDPPREPEQPAFVFYTSGTTGLPKgavipqraaes 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 235 ----MA--------KHSHGLALQPSFP--GSRKLRSLKTS-DVSWCLS---DSGWIVATIWTL-VEPWTAGCTVF---IH 292
Cdd:cd05923 178 rvlfMStqaglrhgRHNVVLGLMPLYHviGFFAVLVAALAlDGTYVVVeefDPADALKLIEQErVTSLFATPTHLdalAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 293 HLPQFDTKV------------IIQTLLKY-------PINHFWGVSSIYRMILQQD-----------FTSIRFPALehcyT 342
Cdd:cd05923 258 AAEFAGLKLsslrhvtfagatMPDAVLERvnqhlpgEKVNIYGTTEAMNSLYMRDartgtemrpgfFSEVRIVRI----G 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 343 GGEVVLPKDQEEWK---RRTGLLLYENYgqseTGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG 419
Cdd:cd05923 334 GSPDEALANGEEGElivAAAADAAFTGY----LNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIH 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 420 PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDkdqltkELQQHVK-SVTAPYKYPRKVEFVSELPKT 498
Cdd:cd05923 410 PSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELDQFCRaSELADFKRPRRYFFLDELPKN 483
|
490
....*....|
gi 578828477 499 ITGKIERKEL 508
Cdd:cd05923 484 AMNKVLRRQL 493
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-515 |
6.94e-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: 109.18 E-value: 6.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWwLVAV-GCMRTGIIFIPatilLkakDILY---RLQL- 156
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEM-VVALlAVLKAGAAYVP----L---DPAYpaeRLAYm 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 157 ---SKAKGIVTIDALASEVDSIASQCPSLkTKLLVSDHSREgwldfrSLVKSASPEHTCVksktldpmVIFfTSGTTGFP 233
Cdd:COG1020 569 ledAGARLVLTQSALAARLPELGVPVLAL-DALALAAEPAT------NPPVPVTPDDLAY--------VIY-TSGSTGRP 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 234 KMAKHSHG------LALQPSFPGSRKLRSL-KTS---DVSwclsdsgwiVATIWTlvePWTAGCTVFIhhLPQ---FDTK 300
Cdd:COG1020 633 KGVMVEHRalvnllAWMQRRYGLGPGDRVLqFASlsfDAS---------VWEIFG---ALLSGATLVL--APPearRDPA 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 301 VIIQTLLKYPINHFWGVSSIYRMILQQDFTsiRFPALEHCYTGGEVVLPKDQEEWKRRT-GLLLYENYGQSET------- 372
Cdd:COG1020 699 ALAELLARHRVTVLNLTPSLLRALLDAAPE--ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETtvdstyy 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -----------------------------------------------------GDPEKTAK--VEC-----GD-FYNTGD 391
Cdd:COG1020 777 evtppdadggsvpigrpiantrvyvldahlqpvpvgvpgelyiggaglargylNRPELTAErfVADpfgfpGArLYRTGD 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 392 RGKMDEEGYICFLGRSDD---IinaSGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQL 468
Cdd:COG1020 857 LARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA-----GAAAA 928
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 578828477 469 TKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 515
Cdd:COG1020 929 AALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
375-501 |
1.06e-24 |
|
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: 104.69 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 375 PEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFI 454
Cdd:cd17636 207 PEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIV 286
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578828477 455 VLTP-QFLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITG 501
Cdd:cd17636 287 VLKPgASVTEA------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
81-516 |
1.21e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 106.79 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEVKwSFREMGDLTRRVANVFTQTCGLQQgdHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:PRK07638 23 NDRVL-TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTIDALASEVDSIasqcpslKTKLLVSDHSREgwldfrsLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPK------ 234
Cdd:PRK07638 100 MIVTERYKLNDLPDE-------EGRVIEIDEWKR-------MIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKaflraq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 235 ---------------MAK-----------HSHGL-------------ALQPSFPGSRKLRSLKTSDVSwclsdsgwIVAT 275
Cdd:PRK07638 166 qswlhsfdcnvhdfhMKRedsvliagtlvHSLFLygaistlyvgqtvHLMRKFIPNQVLDKLETENIS--------VMYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 276 IWTLVEPWTAgctvfIHHLPQFDTKVI-------------IQTLLKY-PINHFWGVSSIYRMILQQDFTSIRFP------ 335
Cdd:PRK07638 238 VPTMLESLYK-----ENRVIENKMKIIssgakweaeakekIKNIFPYaKLYEFYGASELSFVTALVDEESERRPnsvgrp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 336 ----ALEHCYTGGEVVLPKDqeewkrrTGLLlYENYGQSETG---DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSD 408
Cdd:PRK07638 313 fhnvQVRICNEAGEEVQKGE-------IGTV-YVKSPQFFMGyiiGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 409 DIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIvltpqflshDKDQLTKELQQHVKSVTAPYKYPRK 488
Cdd:PRK07638 385 NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKE 455
|
490 500
....*....|....*....|....*...
gi 578828477 489 VEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PRK07638 456 WHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
219-505 |
1.65e-24 |
|
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: 104.02 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 219 DPMVIFFTSGTTGFPKMAKHSHGLALQpSFPGSRKLRSLKTSD---VSWCLSDSGWIVATIWTLvepWTAGCtvfIHHLP 295
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIE-SFVCNEDLFNISGEDailAPGPLSHSLFLYGAISAL---YLGGT---FIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 296 QFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIrfpALEHCYTGGEVvLPKDQEEWKRRT--GLLLYENYGQSET- 372
Cdd:cd17633 74 KFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPES---KIKSIFSSGQK-LFESTKKKLKNIfpKANLIEFYGTSELs 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -------GDPEKTAKV---------------------------------ECGDFYN------TGDRGKMDEEGYICFLGR 406
Cdd:cd17633 150 fitynfnQESRPPNSVgrpfpnveieirnadggeigkifvksemvfsgyVRGGFSNpdgwmsVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 407 SDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqflshdKDQLT-KELQQHVKSVTAPYKY 485
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---------GDKLTyKQLKRFLKQKLSRYEI 300
|
330 340
....*....|....*....|
gi 578828477 486 PRKVEFVSELPKTITGKIER 505
Cdd:cd17633 301 PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
388-513 |
2.28e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 105.12 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 388 NTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAfivltpQFLSH---D 464
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVISHeeiD 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578828477 465 KDQLTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIERKELRKKET 513
Cdd:PRK08308 368 PVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGEV 412
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
83-510 |
2.58e-24 |
|
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: 105.98 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 83 EVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKgI 162
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRAL-GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIDalaSEVDSIASQCPSLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKS-KTLDPMVIFFTSGTTGFPKMAKHSH- 240
Cdd:cd05915 100 LLFD---PNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRvPERAACGMAYTTGTTGLPKGVVYSHr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 GLALQPSFPGSRKLRSLKTSDVSWCLSD----SGWivATIWTLvepwTAGCTVFIHHLPQFDTKVIIQTLLKYPINHFWG 316
Cdd:cd05915 177 ALVLHSLAASLVDGTALSEKDVVLPVVPmfhvNAW--CLPYAA----TLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 317 VSSIYRMILQ-QDFTSIRFPALEHCYTGG----EVVLPKDQ-------------------------EEW----------- 355
Cdd:cd05915 251 VPTVWLALADyLESTGHRLKTLRRLVVGGsaapRSLIARFErmgvevrqgygltetspvvvqnfvkSHLeslseeekltl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 356 KRRTGLllyENYGQS-ETGDPE--------KTAKVEC-----------------------GDFYNTGDRGKMDEEGYICF 403
Cdd:cd05915 331 KAKTGL---PIPLVRlRVADEEgrpvpkdgKALGEVQlkgpwitggyygneeatrsaltpDGFFRTGDIAVWDEEGYVEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 404 LGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTpqflshDKDQLTKELQQHVKSVTAPY 483
Cdd:cd05915 408 KDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR------GEKPTPEELNEHLLKAGFAK 481
|
490 500
....*....|....*....|....*...
gi 578828477 484 KY-PRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05915 482 WQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
82-508 |
4.15e-24 |
|
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: 105.05 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQtCGLQQGDHLALMLPRVPEWwLVAV-GCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQ-VVAVlGILAAGAAYVPVDIDQPAARREAILADAGAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTIDALASEVDSIAsqcpslkTKLLVSDHSREGWLDFRSLVKSASpehtcvksktlDPMVIFFTSGTTGFPKMAKHSH 240
Cdd:cd12114 87 LVLTDGPDAQLDVAVF-------DVLILDLDALAAPAPPPPVDVAPD-----------DLAYVIFTSGSTGTPKGVMISH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 G------LALQPSFPGSRKLRSLKTSDVSWCLSdsgwivatIWTLVEPWTAGCT-VFIHHLPQFDTKVIIQTLLKYPINH 313
Cdd:cd12114 149 RaalntiLDINRRFAVGPDDRVLALSSLSFDLS--------VYDIFGALSAGATlVLPDEARRRDPAHWAELIERHGVTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 314 FWGVSSIYRMIL------QQDFTSIR--------------------FPALEHCYTGG-------EVVLPKDQ--EEWK-- 356
Cdd:cd12114 221 WNSVPALLEMLLdvleaaQALLPSLRlvllsgdwipldlparlralAPDARLISLGGateasiwSIYHPIDEvpPDWRsi 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 357 -----------------RR------TGLLLYENYG--QSETGDPEKTAK--VECGD---FYNTGDRGKMDEEGYICFLGR 406
Cdd:cd12114 301 pygrplanqryrvldprGRdcpdwvPGELWIGGRGvaLGYLGDPELTAArfVTHPDgerLYRTGDLGRYRPDGTLEFLGR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 407 SDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPiRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSvtapYKYP 486
Cdd:cd12114 381 RDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPA----YMIP 455
|
490 500
....*....|....*....|..
gi 578828477 487 RKVEFVSELPKTITGKIERKEL 508
Cdd:cd12114 456 SRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
219-510 |
5.83e-24 |
|
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: 104.93 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 219 DPMVIFFTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLK----TSDVSwclsdsgwiVATIWTlvePWTAGCT 288
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHRalstsaLAHGRALGLTSESRVLQfasyTFDVS---------ILEIFT---TLAAGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 289 VFI-------HHLPQFdtkviIQtllKYPINHFWGVSSIYRMILQQDFtsirfPALEHCYTGGEVVLPKDQEEWKRRTGL 361
Cdd:cd05918 175 LCIpseedrlNDLAGF-----IN---RLRVTWAFLTPSVARLLDPEDV-----PSLRTLVLGGEALTQSDVDTWADRVRL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 362 LlyeN-YGQSET----------------------------------------------------------GDPEKTAKV- 381
Cdd:cd05918 242 I---NaYGPAECtiaatvspvvpstdprnigrplgatcwvvdpdnhdrlvpigavgelliegpilargylNDPEKTAAAf 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 382 --------ECGD-----FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGE 448
Cdd:cd05918 319 iedpawlkQEGSgrgrrLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGS 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 449 VVK---AFIVLTPQFLSHDKDQ------------LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05918 399 SSPqlvAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
95-511 |
1.17e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 104.29 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 95 TRRVANVFTqTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDS 174
Cdd:PLN02330 65 TRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 175 IASQCpslktkLLVSDHSREGWLDFRSLVKSAS-PEHTCVKSKTL--DPMVIFFTSGTTGFPK--MAKHSHGLA------ 243
Cdd:PLN02330 144 LGLPV------IVLGEEKIEGAVNWKELLEAADrAGDTSDNEEILqtDLCALPFSSGTTGISKgvMLTHRNLVAnlcssl 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 244 --LQPSFPGSRKLRSLK--------TSDVSWCLSDSGWIVAT----IWTLVEPWTAGCTVFIHHLPQfdtkvIIQTLLKY 309
Cdd:PLN02330 218 fsVGPEMIGQVVTLGLIpffhiygiTGICCATLRNKGKVVVMsrfeLRTFLNALITQEVSFAPIVPP-----IILNLVKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 310 PINHFWGVSsiyRMILQQDFTSI-------------RFPAL---------EH-CYTGGEVVLPKDQEEWKRR-------- 358
Cdd:PLN02330 293 PIVEEFDLS---KLKLQAIMTAAaplapelltafeaKFPGVqvqeaygltEHsCITLTHGDPEKGHGIAKKNsvgfilpn 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 359 ---------TGLLLYENYG-----------QSETGDPEKTAK-VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYR 417
Cdd:PLN02330 370 levkfidpdTGRSLPKNTPgelcvrsqcvmQGYYNNKEETDRtIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 418 IGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLtkelqQHVKSVTAPYKYPRKVEFVSELPK 497
Cdd:PLN02330 450 VAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDIL-----NFVAANVAHYKKVRVVQFVDSIPK 524
|
490
....*....|....
gi 578828477 498 TITGKIERKELRKK 511
Cdd:PLN02330 525 SLSGKIMRRLLKEK 538
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
84-511 |
1.21e-23 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 104.54 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 84 VKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKgIV 163
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSE-VV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 164 TID----ALASEVDSIASQCP--SLKTKLLV--SDHS----------REGWLDFRSLVKSASPEHTCVKSK-TLDPMVIF 224
Cdd:PLN02479 122 MVDqeffTLAEEALKILAEKKksSFKPPLLIviGDPTcdpkslqyalGKGAIEYEKFLETGDPEFAWKPPAdEWQSIALG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 225 FTSGTTGFPKMAKHSHGLALqpsfpgsrkLRSLKTSDVsWCLSDSGwivATIWTL--------VEPWT--AGCTVFIHhL 294
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAY---------LMALSNALI-WGMNEGA---VYLWTLpmfhcngwCFTWTlaALCGTNIC-L 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 295 PQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSET 372
Cdd:PLN02479 268 RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNapKSETILPLPRVVHVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSET 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDP---------------EKTAKVEC------------------------------------------------------ 383
Cdd:PLN02479 347 YGPstvcawkpewdslppEEQARLNArqgvryiglegldvvdtktmkpvpadgktmgeivmrgnmvmkgylknpkaneea 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 --GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFL 461
Cdd:PLN02479 427 faNGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVD 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 578828477 462 SHDKDQLTKELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIERKELRKK 511
Cdd:PLN02479 507 KSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
373-502 |
9.42e-22 |
|
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: 96.68 E-value: 9.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKTAK--VECGD--FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGE 448
Cdd:cd05924 229 GDEAKTAEtfPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 578828477 449 VVKAFIVLTPqflSHDKDQltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 502
Cdd:cd05924 309 EVVAVVQLRE---GAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
82-506 |
1.12e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.42 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKg 161
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGAR- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 IVTIDALA-SEVDSIASQCPSLKTKLLVSDHSREGWLDFrSLVKSASPEHTCVKSKTL--DPMVIFFTSGTTGFPKMAKH 238
Cdd:PRK05852 118 VVLIDADGpHDRAEPTTRWWPLTVNVGGDSGPSGGTLSV-HLDAATEPTPATSTPEGLrpDDAMIMFTGGTTGLPKMVPW 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 239 SHGlalqpSFPGSrkLRSLKTSdvsWCLSDSGWIVAT---------IWTLVEPWTAGCTVFIHHLPQFDTKVIIQTLLKY 309
Cdd:PRK05852 197 THA-----NIASS--VRAIITG---YRLSPRDATVAVmplyhghglIAALLATLASGGAVLLPARGRFSAHTFWDDIKAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 310 PINHFWGVSSIYRMILQ----QDFTSIRfPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSET------------- 372
Cdd:PRK05852 267 GATWYTAVPTIHQILLEraatEPSGRKP-AALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqiegig 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 --------------------------------------------------GDPEKTAKVECGDFYNTGDRGKMDEEGYIC 402
Cdd:PRK05852 346 qtenpvvstglvgrstgaqirivgsdglplpagavgevwlrgttvvrgylGDPTITAANFTDGWLRTGDLGSLSAAGDLS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 403 FLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltPQFLSHDKDQltkELQQHVKSVTAP 482
Cdd:PRK05852 426 IRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERLAA 500
|
490 500
....*....|....*....|....
gi 578828477 483 YKYPRKVEFVSELPKTITGKIERK 506
Cdd:PRK05852 501 FEIPASFQEASGLPHTAKGSLDRR 524
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
375-510 |
1.46e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 97.75 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 375 PEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 453
Cdd:PRK10946 398 PQHNASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAF 477
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578828477 454 IVLtpqflshdKDQL-TKELQQHVKSV-TAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK10946 478 LVV--------KEPLkAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
107-510 |
2.32e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 97.56 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 107 GLQQGDHLALMLPRvPEW---WLVAVGCMrtGIIFIPATillkakdilYRLQLSKAK-GIVTIDALASEVDSIASQ---- 178
Cdd:PLN02860 53 GLRNGDVVAIAALN-SDLyleWLLAVACA--GGIVAPLN---------YRWSFEEAKsAMLLVRPVMLVTDETCSSwyee 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 179 -----CPSLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDP-------MVIFFTSGTTGFPKMAKHSHgLALqp 246
Cdd:PLN02860 121 lqndrLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYawapddaVLICFTSGTTGRPKGVTISH-SAL-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 247 sfpgsrKLRSL-KTSDVSWCLSDS----------GWIVATIWTLVepwTAGCTVFIhhlPQFDTKVIIQTLLKYPINHFW 315
Cdd:PLN02860 198 ------IVQSLaKIAIVGYGEDDVylhtaplchiGGLSSALAMLM---VGACHVLL---PKFDAKAALQAIKQHNVTSMI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 316 GVSSIYRMILQ--------QDFTSIR--------------------FPAL---------EHCYTGGEVVLPKDQEEWKRR 358
Cdd:PLN02860 266 TVPAMMADLISltrksmtwKVFPSVRkilngggslssrllpdakklFPNAklfsaygmtEACSSLTFMTLHDPTLESPKQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 359 TGLLLYENYGQSET-----------------------------------------GDPEKTAKVECGDFY-NTGDRGKMD 396
Cdd:PLN02860 346 TLQTVNQTKSSSVHqpqgvcvgkpaphvelkigldessrvgriltrgphvmlgywGQNSETASVLSNDGWlDTGDIGWID 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 397 EEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKD--------QL 468
Cdd:PLN02860 426 KAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEkenakknlTL 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 578828477 469 TKE-LQQHV--KSVTApYKYPRK-VEFVSELPKTITGKIERKELRK 510
Cdd:PLN02860 506 SSEtLRHHCreKNLSR-FKIPKLfVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
82-508 |
2.80e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 96.99 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQTcGLQQGDhlalmlprvpewwlvAVGCM-RTGIIFIPATI---LLKAKDILYRLQLS 157
Cdd:PRK13383 57 DDGALSYRELQRATESLARRLTRD-GVAPGR---------------AVGVMcRNGRGFVTAVFavgLLGADVVPISTEFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 158 KakgivtiDALASEV-----------DSIASQCPSLKTKLLVSDHSREGWLDFRSLVKSASPEHtcvksktldpmVIFFT 226
Cdd:PRK13383 121 S-------DALAAALrahhistvvadNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGR-----------IVLLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 227 SGTTGFPK----MAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDS---GWIVATIwtlvepwTAGCTVFIHHlpQFDT 299
Cdd:PRK13383 183 SGTTGKPKgvprAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGlglGMLMLTI-------ALGGTVLTHR--HFDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 300 KVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIR--FPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG--- 373
Cdd:PRK13383 254 EAALAQASLHRADAFTAVPVVLARILElPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGiga 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 ---------------------------------DPEKTAKVECG-----DFY-------------NTGDRGKMDEEGYIC 402
Cdd:PRK13383 334 latpadlrdapetvgkpvagcpvrildrnnrpvGPRVTGRIFVGgelagTRYtdgggkavvdgmtSTGDMGYLDNAGRLF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 403 FLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSHDKDQltkeLQQHVKSVTAP 482
Cdd:PRK13383 414 IVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDRVSR 488
|
490 500
....*....|....*....|....*.
gi 578828477 483 YKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:PRK13383 489 FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
78-481 |
3.70e-21 |
|
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: 96.38 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 78 NGQGDEVKWSfrEMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLS 157
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 158 KAKGIVT--IDALASEVDSIASQCPSLKTKLLVSDHSREGWLDfrsLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKM 235
Cdd:cd05932 78 ESKALFVgkLDDWKAMAPGVPEGLISISLPPPSAANCQYQWDD---LIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 236 AKHSHGlalQPSFPGSRKLRSLKTSDVSWCLS-------------DSGWI--------VATIWTLVEPWT-AGCTVFIHh 293
Cdd:cd05932 155 VMLTFG---SFAWAAQAGIEHIGTEENDRMLSylplahvtervfvEGGSLyggvlvafAESLDTFVEDVQrARPTLFFS- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 294 LPQ----FDTKVI-------IQTLLKYPInhfwgVSSIYRMILQQDFtsirfpALEHC--YTGGEVVLPKDQEEWKRRTG 360
Cdd:cd05932 231 VPRlwtkFQQGVQdkipqqkLNLLLKIPV-----VNSLVKRKVLKGL------GLDQCrlAGCGSAPVPPALLEWYRSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 361 LLLYENYG-------------------------------QSETG---------------DPEKTAKVECGD-FYNTGDRG 393
Cdd:cd05932 300 LNILEAYGmtenfayshlnypgrdkigtvgnagpgvevrISEDGeilvrspalmmgyykDPEATAEAFTADgFLRTGDKG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 394 KMDEEGYICFLGRSDDIINAS-GYRIGPAEVESALVEHPAVAESAVVGS--PDPIRGEVVKAFIVltPQFLSHDKDQLTK 470
Cdd:cd05932 380 ELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEAR--LRADAFARAELEA 457
|
490
....*....|.
gi 578828477 471 ELQQHVKSVTA 481
Cdd:cd05932 458 SLRAHLARVNS 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
389-509 |
8.29e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 95.68 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 389 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflshdkDQL 468
Cdd:PLN02574 434 TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STL 507
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578828477 469 TKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PLN02574 508 SQEaVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
108-509 |
1.48e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 95.09 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 108 LQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKgIVTID----ALASEVDSIASQCPSLK 183
Cdd:PLN03102 61 ITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPK-ILFVDrsfePLAREVLHLLSSEDSNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 184 TKLLVSDH---------SREgwLDFRSLVKSASPEHTCVKSKTL-----DPMVIFFTSGTTGFPKMAKHSHglalqpsfp 249
Cdd:PLN03102 140 NLPVIFIHeidfpkrpsSEE--LDYECLIQRGEPTPSLVARMFRiqdehDPISLNYTSGTTADPKGVVISH--------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 250 gsrklRSLKTSDVSWCLsdsGWIVAT----IWTL--------VEPWT----AGCTVFIHHL--PQfdtkvIIQTLLKYPI 311
Cdd:PLN03102 209 -----RGAYLSTLSAII---GWEMGTcpvyLWTLpmfhcngwTFTWGtaarGGTSVCMRHVtaPE-----IYKNIEMHNV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 312 NHFWGVSSIYRMILQQDFT--SIRFPALeHCYTGGE---VVLPKD--------------------------QEEWKR--- 357
Cdd:PLN03102 276 THMCCVPTVFNILLKGNSLdlSPRSGPV-HVLTGGSpppAALVKKvqrlgfqvmhayglteatgpvlfcewQDEWNRlpe 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 358 --------RTGL----LLYENYGQSET--------------------------GDPEKTAKVECGDFYNTGDRGKMDEEG 399
Cdd:PLN03102 355 nqqmelkaRQGVsilgLADVDVKNKETqesvprdgktmgeivikgssimkgylKNPKATSEAFKHGWLNTGDVGVIHPDG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 400 YICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVL--TPQFLSHDKDQL-TKE--LQQ 474
Cdd:PLN03102 435 HVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLvTRErdLIE 514
|
490 500 510
....*....|....*....|....*....|....*
gi 578828477 475 HVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PLN03102 515 YCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
212-510 |
2.12e-20 |
|
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: 93.94 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 212 CVKSKTLDPMVIFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDV---------SWCLSDSGWIvatiwtlveP 282
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHK-NLLANVEQITAIFDPNPEDVvfgalpffhSFGLTGCLWL---------P 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 283 WTAGCTVFIHHLPqFDTKVIIQTLLKYPINHFWGVSSIYRMILQ----QDFTSIRFpalehCYTGGEVVLPKDQEEWKRR 358
Cdd:cd05909 211 LLSGIKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARaahpEDFSSLRL-----VVAGAEKLKDTLRQEFQEK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 359 TGLLLYENYGQSET----------------------------------------------------------GDPEKTAK 380
Cdd:cd05909 285 FGIRILEGYGTTECspvisvntpqspnkegtvgrplpgmevkivsvetheevpigegglllvrgpnvmlgylNEPELTSF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 381 VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEH-PAVAESAVVGSPDPIRGEvvKAFIVLTPQ 459
Cdd:cd05909 365 AFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE--KIVLLTTTT 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828477 460 FLSHDkdqltkELQQHVKSVTAPYKY-PRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05909 443 DTDPS------SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
107-509 |
2.35e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 94.71 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 107 GLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALAsevDSIASQcPSLKTKL 186
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALR---DRFQPS-RVAEAAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 187 LVSDHSREGWLDFRSLVKSASPEHTcvksktldpmvifFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWC- 265
Cdd:PRK06060 127 LMSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCs 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 266 --------LSDSGWIvatiwtlvePWTAGCTVFIHHLPqFDTKVIIQTLLKYPINHFWGVSSIYRMILQ----QDFTSIR 333
Cdd:PRK06060 194 armyfaygLGNSVWF---------PLATGGSAVINSAP-VTPEAAAILSARFGPSVLYGVPNFFARVIDscspDSFRSLR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 334 F---------PALEHCYTG----------------GEVVLPKDQEEWKRRT-GLLL--YE-------------------- 365
Cdd:PRK06060 264 CvvsagealeLGLAERLMEffggipildgigstevGQTFVSNRVDEWRLGTlGRVLppYEirvvapdgttagpgvegdlw 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 366 ----NYGQSETGDPEKTakVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGS 441
Cdd:PRK06060 344 vrgpAIAKGYWNRPDSP--VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAV 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828477 442 PDPIRGEVVKAFIVltPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK06060 422 RESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
219-505 |
2.87e-20 |
|
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: 91.94 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 219 DPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTV--------- 289
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVtggenttyk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 290 -FIHHLPQFD--TKVIIQTLLKYPINHF---------------------------------------WGVSSIYRMI-LQ 326
Cdd:cd17635 82 sLFKILTTNAvtTTCLVPTLLSKLVSELksanatvpslrligyggsraiaadvrfieatgltntaqvYGLSETGTALcLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 327 QDFTSIRFPALEHCYTGGEVVL--------PKDQEE--WKRRTGLLL--YENygqsetgdPEKTAKVECGDFYNTGDRGK 394
Cdd:cd17635 162 TDDDSIEINAVGRPYPGVDVYLaatdgiagPSASFGtiWIKSPANMLgyWNN--------PERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 395 MDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqfLSHDKDQLTKELQQ 474
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV-----ASAELDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|..
gi 578828477 475 H-VKSVTAPYKYPRKVEFVSELPKTITGKIER 505
Cdd:cd17635 309 HtIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
223-509 |
6.07e-20 |
|
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: 92.43 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRsLKTSDVSWCLSDSGWIVAtIWTLVEPWTAGCTVFIHHLPQFDTKVI 302
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG-LTPGDRELQFASFNFDGA-HEQLLPPLICGACVVLRPDELWASADE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 303 IQTLL-KYPINhfwgVSSIYRMILQQ------DFTSIRFPALEHCYTGGEVVLPKDQEEWkRRTGLLLYENYGQSET--- 372
Cdd:cd17649 177 LAEMVrELGVT----VLDLPPAYLQQlaeeadRTGDGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEAtvt 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ----------------------------------------------------------GDPEKTAK--------VECGDF 386
Cdd:cd17649 252 plvwkceagaaragasmpigrplggrsayildadlnpvpvgvtgelyiggeglargylGRPELTAErfvpdpfgAPGSRL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVkAFIVL-TPQFLSHDK 465
Cdd:cd17649 332 YRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAAAAQPELR 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578828477 466 DQltkeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:cd17649 411 AQ----LRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
387-508 |
8.33e-20 |
|
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: 92.00 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLShdkd 466
Cdd:cd12115 331 YRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG---- 406
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578828477 467 qLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd12115 407 -LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
81-508 |
1.13e-19 |
|
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: 91.62 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 81 GDEvKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAK 160
Cdd:cd17655 19 EDQ-TLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 161 GIVTIDALASEVDSIasqcpslKTKLLVSDHSregwldfrslVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPK--MAKH 238
Cdd:cd17655 97 ILLTQSHLQPPIAFI-------GLIDLLDEDT----------IYHEESENLEPVSKSDDLAYVIYTSGSTGKPKgvMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 239 sHGL-----ALQPSFPGSRKLRSLKTSDVSWclsDsgwivATIWTLVEPWTAGCTVFIH-HLPQFDTKVIIQTLLKYPIN 312
Cdd:cd17655 160 -RGVvnlveWANKVIYQGEHLRVALFASISF---D-----ASVTEIFASLLSGNTLYIVrKETVLDGQALTQYIRQNRIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 313 HFWGVSSIYRMILQQDFTSirFPALEHCYTGGEVVLPKDQEEWKRRTGL--LLYENYGQSET------------------ 372
Cdd:cd17655 231 IIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETtvdasiyqyepetdqqvs 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ---------------------------------GD---------PEKTAK-------VECGDFYNTGDRGKMDEEGYICF 403
Cdd:cd17655 309 vpigkplgntriyildqygrpqpvgvagelyigGEgvargylnrPELTAEkfvddpfVPGERMYRTGDLARWLPDGNIEF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 404 LGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqflsHDKDQLTKELQQHVKSVTAPY 483
Cdd:cd17655 389 LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-------SEKELPVAQLREFLARELPDY 461
|
490 500
....*....|....*....|....*
gi 578828477 484 KYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17655 462 MIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
63-508 |
1.50e-19 |
|
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: 91.08 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 63 EKEGKRGPNPAFWWVNGQgdevKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPAT 142
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ----SLTYKQLNEKANQLARHL-RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 143 ILLKAKDILYRLQLSKAKgivtidalasevdsiasqcpslktkLLVSDhsregwldfrslvksasPEhtcvksktlDPMV 222
Cdd:cd17645 80 PDYPGERIAYMLADSSAK-------------------------ILLTN-----------------PD---------DLAY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IFFTSGTTGFPK--MAKHSHGLAL----QPSFPGSRKLRSLKTSDVSWclsdsgwiVATIWTLVEPWTAGCTVfiHHLPQ 296
Cdd:cd17645 109 VIYTSGSTGLPKgvMIEHHNLVNLcewhRPYFGVTPADKSLVYASFSF--------DASAWEIFPHLTAGAAL--HVVPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 297 fDTKVIIQTLLKYPINHFWGVSSIYRMILQQdFTSIRFPALEHCYTGGEVVlpkdqeewKR--RTGLLLYENYGQSE--- 371
Cdd:cd17645 179 -ERRLDLDALNDYFNQEGITISFLPTGAAEQ-FMQLDNQSLRVLLTGGDKL--------KKieRKGYKLVNNYGPTEntv 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 372 ---------------------------------------TGD---------------PEKTAKVECGD-------FYNTG 390
Cdd:cd17645 249 vatsfeidkpyanipigkpidntrvyildealqlqpigvAGElciageglargylnrPELTAEKFIVHpfvpgerMYRTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 391 DRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVlTPQFLSHDkdqltk 470
Cdd:cd17645 329 DLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-APEEIPHE------ 401
|
490 500 510
....*....|....*....|....*....|....*...
gi 578828477 471 ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17645 402 ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
374-510 |
6.29e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 89.74 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 453
Cdd:PRK07867 370 DPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAA 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 454 IVLTPQfLSHDKDQLTKELqqHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK07867 450 LVLAPG-AKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
389-510 |
1.14e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 88.51 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 389 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDkdql 468
Cdd:PRK07445 328 TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE---- 403
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578828477 469 tkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK07445 404 --ELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
82-508 |
1.66e-18 |
|
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: 88.12 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKG 161
Cdd:cd12116 9 DDRSLSYAELDERANRLAARL-RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 IVTIDALAsevDSIASQCPslktklLVSDHSREGWLDFRSLVKSASPEhtcvksktlDPMVIFFTSGTTGFPK--MAKHS 239
Cdd:cd12116 88 VLTDDALP---DRLPAGLP------VLLLALAAAAAAPAAPRTPVSPD---------DLAYVIYTSGSTGRPKgvVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 240 ------HGLALQPSF-PGSRKLrSLKTS--DVSwclsdsgwivatIWTLVEPWTAGCTVFIhhLP---QFDTKVIIQTLL 307
Cdd:cd12116 150 nlvnflHSMRERLGLgPGDRLL-AVTTYafDIS------------LLELLLPLLAGARVVI--APretQRDPEALARLIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 308 KYPINHFWGVSSIYRMILQQDFTSIR-FPALehCytGGEVvLPKDQEEWKRRTGLLLYENYGQSET-------------- 372
Cdd:cd12116 215 AHSITVMQATPATWRMLLDAGWQGRAgLTAL--C--GGEA-LPPDLAARLLSRVGSLWNLYGPTETtiwstaarvtaaag 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -------------------------------------------GDPEKTAKV--------ECGDFYNTGDRGKMDEEGYI 401
Cdd:cd12116 290 pipigrplantqvyvldaalrpvppgvpgelyiggdgvaqgylGRPALTAERfvpdpfagPGSRLYRTGDLVRRRADGRL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 402 CFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVkAFIVLtPQFLSHDKDQLTKELQQHVKSvta 481
Cdd:cd12116 370 EYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRATLPA--- 444
|
490 500
....*....|....*....|....*..
gi 578828477 482 pYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd12116 445 -YMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
87-510 |
3.67e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 87.53 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWW--LVAVGCMrtGIIFIPATILLKAKDILYRLQLSKAKGIVT 164
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 165 IDALASEVDSIASQCPSLKTKLLVSD----------------HSREGWLDFRSLVKS--ASPEHTcvksktldPMVIFFT 226
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPsdadsaaahmpegikvYSYEALLDGRSTVYDwpELDETT--------AAAICYS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 227 SGTTGFPKMAKHSH-GLALQPsfpgsrklRSLKTSD-------------------VSWCLSDSGWI-------------- 272
Cdd:PRK05620 190 TGTTGAPKGVVYSHrSLYLQS--------LSLRTTDslavthgesflccvpiyhvLSWGVPLAAFMsgtplvfpgpdlsa 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 273 -----------------VATIWTlvepwtagcTVFIHHLPQFDTKVIIQTLL----------------KYPIN--HFWGV 317
Cdd:PRK05620 262 ptlakiiatamprvahgVPTLWI---------QLMVHYLKNPPERMSLQEIYvggsavppilikaweeRYGVDvvHVWGM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 318 SSI--------------------YRMilqqdfTSIRFPA-LEH-CYTGGEVVLPKD--QEEWKRRtGLLLYENYGQSETG 373
Cdd:PRK05620 333 TETspvgtvarppsgvsgearwaYRV------SQGRFPAsLEYrIVNDGQVMESTDrnEGEIQVR-GNWVTASYYHSPTE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 DPEKTA------KVECGD-------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVG 440
Cdd:PRK05620 406 EGGGAAstfrgeDVEDANdrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578828477 441 SPDPIRGEVVKAFIVLTP--QFLSHDKDQLTKELQQHVKSVTAPYKYprkvEFVSELPKTITGKIERKELRK 510
Cdd:PRK05620 486 YPDDKWGERPLAVTVLAPgiEPTRETAERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
80-505 |
5.39e-18 |
|
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: 86.34 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 80 QGDEVKWSFREMGDLTRRVANvFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKA 159
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KgivtidalasevdsiasqcpslktKLLVSDHSregwldfrslvksaspehtcvksktlDPMVIFFTSGTTGFPK--MAK 237
Cdd:cd05914 81 K------------------------AIFVSDED--------------------------DVALINYTSGTTGNSKgvMLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 238 HSHglaLQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTV-FIHHLP--------QFDTKVIIQTLLK 308
Cdd:cd05914 111 YRN---IVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVvFLDKIPsakiialaFAQVTPTLGVPVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 309 YPINHF------------WGVSSIYRMILQQDFTSIRFPALEHCYTG-------GEVVLPKDQEEWKRRTGLLLYENYGQ 369
Cdd:cd05914 188 LVIEKIfkmdiipkltlkKFKFKLAKKINNRKIRKLAFKKVHEAFGGnikefviGGAKINPDVEEFLRTIGFPYTIGYGM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 370 SETG----------------------------------------------------DPEKTAKV--ECGDFYnTGDRGKM 395
Cdd:cd05914 268 TETApiisysppnrirlgsagkvidgvevridspdpatgegeiivrgpnvmkgyykNPEATAEAfdKDGWFH-TGDLGKI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 396 DEEGYICFLGRSDD-IINASGYRIGPAEVESALVEHPAVAESAVVgspdpIRGEVVKAFIVLTPQFL-------SHDKDQ 467
Cdd:cd05914 347 DAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFLdvkalkqRNIIDA 421
|
490 500 510
....*....|....*....|....*....|....*....
gi 578828477 468 LTKELQQHVKSVTAPYKYPRKVEFV-SELPKTITGKIER 505
Cdd:cd05914 422 IKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
387-508 |
5.80e-18 |
|
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: 86.15 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKD 466
Cdd:cd17652 319 YRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAA 393
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578828477 467 QLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17652 394 PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
198-509 |
6.69e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 86.62 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 198 DFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKlRSLKTSDVSWC---LSDS----- 269
Cdd:PRK13388 130 AYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTER-FGLTRDDVCYVsmpLFHSnavma 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 270 GWIVATiwtlvepwTAGCTVFIHhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-------DFTsirfpaLEHCYt 342
Cdd:PRK13388 209 GWAPAV--------ASGAAVALP--AKFSASGFLDDVRRYGATYFNYVGKPLAYILATperpddaDNP------LRVAF- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 343 GGEVVlPKDQEEWKRRTGLLLYENYGQSETG------------------------DPEktAKVEC--------------- 383
Cdd:PRK13388 272 GNEAS-PRDIAEFSRRFGCQVEDGYGSSEGAvivvrepgtppgsigrgapgvaiyNPE--TLTECavarfdahgallnad 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 ------------GDF---YN---------------TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAV 433
Cdd:PRK13388 349 eaigelvntagaGFFegyYNnpeataermrhgmywSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 434 AESAVVGSPDPIRGEVVKAFIVLTP----------QFLSHDKDQLTKelqqhvksvtapyKYPRKVEFVSELPKTITGKI 503
Cdd:PRK13388 429 NRVAVYAVPDERVGDQVMAALVLRDgatfdpdafaAFLAAQPDLGTK-------------AWPRYVRIAADLPSTATNKV 495
|
....*.
gi 578828477 504 ERKELR 509
Cdd:PRK13388 496 LKRELI 501
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
87-510 |
1.48e-17 |
|
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: 85.05 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPatillkakdilyrlqlskakgiVTID 166
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP----------------------LDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALASEVDSIASQCPSlktKLLVSDhsregwldfrslvksASPEhtcvksktlDPMVIFFTSGTTGFPKMAKHSHG----L 242
Cdd:cd17653 81 LPSARIQAILRTSGA---TLLLTT---------------DSPD---------DLAYIIFTSGSTGIPKGVMVPHRgvlnY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 243 ALQPSF-----PGSRKLRSLKTS-DVSW-----CLSDSGwivatiwTLV-----EPWTA---GCTVFIHhlpqfdTKVII 303
Cdd:cd17653 134 VSQPPArldvgPGSRVAQVLSIAfDACIgeifsTLCNGG-------TLVladpsDPFAHvarTVDALMS------TPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 304 QTLlkypinhfwgvssiyrmilqqdfTSIRFPALEHCYTGGEVVLPKDQEEWK-RRTgllLYENYGQSET---------- 372
Cdd:cd17653 201 STL-----------------------SPQDFPNLKTIFLGGEAVPPSLLDRWSpGRR---LYNAYGPTECtisstmtell 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ----------------------------------------------GDPEKTAK--VECGD-----FYNTGDRGKMDEEG 399
Cdd:cd17653 255 pgqpvtigkpipnstcyildadlqpvpegvvgeicisgvqvargylGNPALTASkfVPDPFwpgsrMYRTGDYGRWTEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 400 YICFLGRSDDIINASGYRIG-PAEVESALVEHPAVAESAVVGSpdpirGEVVKAFIvlTPQflSHDKDQLTKELQQHVKS 478
Cdd:cd17653 335 GLEFLGREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAIVV-----NGRLVAFV--TPE--TVDVDGLRSELAKHLPS 405
|
490 500 510
....*....|....*....|....*....|..
gi 578828477 479 vtapYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd17653 406 ----YAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
50-503 |
1.89e-17 |
|
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: 85.40 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 50 NFASYVLdywaqkekEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEwwlVAV 129
Cdd:cd05943 71 NYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAGYLPNIPE---AVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 130 GCMRT---GIIFIPATILLKAKDILYRLQLSKAKGIVTIDA---------LASEVDSIASQCPSLKTKLLVSDHSREGWL 197
Cdd:cd05943 139 AMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLAVVVVPYTVAAGQP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 198 DFRSLVKSASPEHTCVKSKTL----------DPMVIFFTSGTTGFPKMAKHSHG---------LALQpsfpgsrklRSLK 258
Cdd:cd05943 219 DLSKIAKALTLEDFLATGAAGelefeplpfdHPLYILYSSGTTGLPKCIVHGAGgtllqhlkeHILH---------CDLR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 259 TSDVSWCLSDSGWIvatIWT-LVEPWTAGCTVFIHHLPQF--DTKVIIQTLLKYPINHFwGVSSIYRMILQQ-DFTsirf 334
Cdd:cd05943 290 PGDRLFYYTTCGWM---MWNwLVSGLAVGATIVLYDGSPFypDTNALWDLADEEGITVF-GTSAKYLDALEKaGLK---- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 335 PALEHCYTGGEVV------LPKDQEEW---KRRTGLLLYENYGQS-----------------------------ETGDPE 376
Cdd:cd05943 362 PAETHDLSSLRTIlstgspLKPESFDYvydHIKPDVLLASISGGTdiiscfvggnpllpvyrgeiqcrglgmavEAFDEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 377 KTAKV-ECGD-------------FYNT--------------------GDRGKMDEEGYICFLGRSDDIINASGYRIGPAE 422
Cdd:cd05943 442 GKPVWgEKGElvctkpfpsmpvgFWNDpdgsryraayfakypgvwahGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 423 VESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlshdkdQLTKELQQHVKSVTA----PYKYPRKVEFVSELPKT 498
Cdd:cd05943 522 IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGV------ELDDELRKRIRSTIRsalsPRHVPAKIIAVPDIPRT 595
|
....*
gi 578828477 499 ITGKI 503
Cdd:cd05943 596 LSGKK 600
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
375-515 |
2.11e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 83.56 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 375 PEKTAKVECGDFyNTGDRGKMDEeGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFI 454
Cdd:PRK07824 225 VDPDPFAEPGWF-RTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828477 455 VLTPqflsHDKDQLTkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 515
Cdd:PRK07824 303 VGDG----GPAPTLE-ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
387-508 |
2.40e-17 |
|
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: 84.28 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflshdKD 466
Cdd:cd17643 334 YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AA 408
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578828477 467 QLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17643 409 ADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
223-516 |
2.98e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.78 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IFFTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLKTSDVSWCLSDSGWIvatiwtlvEPWTAGCTVFIHHLPQ 296
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGslvnhlHATGERYELTPDDRVLQFMSFSFDGSHEGLY--------HPLINGASVVIRDDSL 4770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 297 FDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEE-WKRRTGLLLYENYGQSET--- 372
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETtvt 4850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 --------GDPEKTAKV---------------------------------EC-------------------------GDF 386
Cdd:PRK12316 4851 vllwkardGDACGAAYMpigtplgnrsgyvldgqlnplpvgvagelylggEGvargylerpaltaerfvpdpfgapgGRL 4930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKD 466
Cdd:PRK12316 4931 YRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEA 5010
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828477 467 Q--LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PRK12316 5011 QaeLRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLL 5062
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
129-514 |
2.20e-16 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 81.87 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 129 VGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIasqcPSLKTKLLVSDHSREGWLDFRSLVKSAsp 208
Cdd:PRK04813 70 LGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGI----PVITLDELKDIFATGNPYDFDHAVKGD-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 209 ehtcvksktlDPMVIFFTSGTTGFPKMAKHSH--------------GLALQPSF----PGSRKLrslktSDVSW--CLSD 268
Cdd:PRK04813 144 ----------DNYYIIFTSGTTGKPKGVQISHdnlvsftnwmledfALPEGPQFlnqaPYSFDL-----SVMDLypTLAS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 269 SGwivaTIWTLVEPWTAgctvfihhlpqfDTKVIIQTLLKYPINhFWgVS--SIYRM-ILQQDFTSIRFPALEHCYTGGE 345
Cdd:PRK04813 209 GG----TLVALPKDMTA------------NFKQLFETLPQLPIN-VW-VStpSFADMcLLDPSFNEEHLPNLTHFLFCGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 346 VVLPKDQEEWKRR-TGLLLYENYGQSET---------------------------------------------------- 372
Cdd:PRK04813 271 ELPHKTAKKLLERfPSATIYNTYGPTEAtvavtsieitdemldqykrlpigyakpdsplliideegtklpdgeqgeivis 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ---------GDPEKTAKVecgdF--------YNTGDRGKMDEeGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAE 435
Cdd:PRK04813 351 gpsvskgylNNPEKTAEA----FftfdgqpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVES 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 436 SAVVgspdPI-RGEVVK---AFIVLTPQflSHDKD-QLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK04813 426 AVVV----PYnKDHKVQyliAYVVPKEE--DFEREfELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
....
gi 578828477 511 KETG 514
Cdd:PRK04813 500 EVNK 503
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
220-510 |
1.15e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 79.79 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 220 PMVIFFTSGTTGFPKMAKHSHG-----LALQPSFPGSRK--LRSLKTSDVSWcLSDSGWIVATI---WTLVEpWTAGCTV 289
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGphlvgLKYYWRSIIEKDipTVVFSHSSIGW-VSFHGFLYGSLslgNTFVM-FEGGIIK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 290 FIHHLPQFdtkviIQTLLKYPINHFWGVSSIYRMILQQD--FTSIR----FPALEHCYTGGEVVLPKDQEEWKRRTGLLL 363
Cdd:PTZ00237 334 NKHIEDDL-----WNTIEKHKVTHTLTLPKTIRYLIKTDpeATIIRskydLSNLKEIWCGGEVIEESIPEYIENKLKIKS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 364 YENYGQSETG-------------------------------DPEKTAKVECGD--------------------------- 385
Cdd:PTZ00237 409 SRGYGQTEIGitylycyghinipynatgvpsifikpsilseDGKELNVNEIGEvafklpmppsfattfykndekfkqlfs 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 ----FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFL 461
Cdd:PTZ00237 489 kfpgYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQS 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 578828477 462 SH--DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PTZ00237 569 NQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
223-516 |
1.69e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.21 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDvSWCLSDSGWIVATIWTLVEPWTAGCTVFI-----HHLPQF 297
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHG-ALVNRLCATQEAYQLSAAD-VVLQFTSFAFDVSVWELFWPLINGARLVIappgaHRDPEQ 1800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 298 dtkvIIQTLLKYPIN--HFwgVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG-LLLYENYGQSET-- 372
Cdd:PRK12467 1801 ----LIQLIERQQVTtlHF--VPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETav 1874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ---------GDPEKTAKVECGD---------------------------------------------------------- 385
Cdd:PRK12467 1875 dvthwtcrrKDLEGRDSVPIGQpianlstyildaslnpvpigvagelylggvglargylnrpaltaerfvadpfgtvgsr 1954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpDPIRGEVVKAFIV-LTPQFLSHD 464
Cdd:PRK12467 1955 LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDD 2033
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578828477 465 KDQLT--KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PRK12467 2034 EAQVAlrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASEL 2087
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
386-508 |
9.28e-15 |
|
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: 76.32 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 386 FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltPQFlshDK 465
Cdd:cd17644 347 LYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PHY---EE 421
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578828477 466 DQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17644 422 SPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
385-511 |
9.95e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 76.71 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 385 DFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshD 464
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----G 484
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578828477 465 KDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:PRK06018 485 ETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-515 |
1.04e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.69 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 40 WNdyEVPEEFNFASYVLDYWAQKEKEGKRGPNPAFwwvngqgDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLP 119
Cdd:PRK12316 500 WN--ATAAEYPLQRGVHRLFEEQVERTPEAPALAF-------GEETLDYAELNRRANRLAHAL-IERGVGPDVLVGVAME 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 120 RVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDsiasqcpsLKTKLLVSDHSREG-WLD 198
Cdd:PRK12316 570 RSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP--------LAAGVQVLDLDRPAaWLE 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 199 FRS---LVKSASPEHtcvksktldPMVIFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVaT 275
Cdd:PRK12316 642 GYSeenPGTELNPEN---------LAYVIYTSGSTGKPKGAGNRHR-ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDV-S 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 276 IWTLVEPWTAGCTvfIHHLPQ---FDTKVIIQTLLKYPINHFWGVSSIYRMILQ----QDFTSIRFPALehcytGGEVvL 348
Cdd:PRK12316 711 VWEFFWPLMSGAR--LVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQdedvASCTSLRRIVC-----SGEA-L 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 349 PKDQEE--WKRRTGLLLYENYGQSET------------------------------------------------------ 372
Cdd:PRK12316 783 PADAQEqvFAKLPQAGLYNLYGPTEAaidvthwtcveeggdsvpigrpianlacyildanlepvpvgvlgelylagrgla 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ----GDPEKTAK-------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGs 441
Cdd:PRK12316 863 rgyhGRPGLTAErfvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA- 941
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578828477 442 pdpIRGEVVKAFIVLTpqflshDKDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 515
Cdd:PRK12316 942 ---VDGKQLVGYVVLE------SEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
384-512 |
1.07e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.51 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVkAFIVLTPQFLSH 463
Cdd:PRK12467 889 GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGA 967
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578828477 464 DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 512
Cdd:PRK12467 968 EHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPD 1016
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
389-509 |
5.40e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 74.36 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 389 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlshdkdQL 468
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA------EV 486
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578828477 469 TK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 509
Cdd:PRK07008 487 TReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
50-503 |
8.91e-14 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 74.06 E-value: 8.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 50 NFASYVLdywaqkekEGKRGPNPAFWWVNGQGDEVKWSFREmgdLTRRVANV--FTQTCGLQQGDHLALMLPRVPEwwlv 127
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAE---LRRQVAALaaALRALGVGPGDRVAAYLPNIPE---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 128 avgcmrTGIIFIpATILLKA-----------KDILYRLQLSKAKGIVTIDA---------LASEVDSIASQCPSLKtKLL 187
Cdd:PRK03584 152 ------TVVAML-ATASLGAiwsscspdfgvQGVLDRFGQIEPKVLIAVDGyryggkafdRRAKVAELRAALPSLE-HVV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 188 VSDHSREG-----------WLDFRSLVKSASPEHTCVKSKtlDPMVIFFTSGTTGFPKMAKHSHG---------LALQPS 247
Cdd:PRK03584 224 VVPYLGPAaaaaalpgallWEDFLAPAEAAELEFEPVPFD--HPLWILYSSGTTGLPKCIVHGHGgillehlkeLGLHCD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 248 F-PGSRklrslktsdVSWcLSDSGWIVatiW-TLVEPWTAGCTVFIhhlpqFD-------TKVIIQTLLKYPINHFwGVS 318
Cdd:PRK03584 302 LgPGDR---------FFW-YTTCGWMM---WnWLVSGLLVGATLVL-----YDgspfypdPNVLWDLAAEEGVTVF-GTS 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 319 SIYRMILQQ---------DFTSIRfpALehCYTGGevVLPKDQEEWkrrtgllLYENYGQS----------------ETG 373
Cdd:PRK03584 363 AKYLDACEKaglvpgethDLSALR--TI--GSTGS--PLPPEGFDW-------VYEHVKADvwlasisggtdicscfVGG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 DPEKT------------AKVECGD-------------------------FYNT--------------------GDRGKMD 396
Cdd:PRK03584 430 NPLLPvyrgeiqcrglgMAVEAWDedgrpvvgevgelvctkpfpsmplgFWNDpdgsryrdayfdtfpgvwrhGDWIEIT 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 397 EEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLShdkDQLTKELQQH 475
Cdd:PRK03584 510 EHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEgVTLD---DALRARIRTT 586
|
570 580
....*....|....*....|....*...
gi 578828477 476 VKSVTAPYKYPRKVEFVSELPKTITGKI 503
Cdd:PRK03584 587 IRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-502 |
1.41e-13 |
|
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: 73.09 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEW---W--LVAVGCMrtgIIFIPATIllKAKDILYRLQLSKAKG 161
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWlgLAKLGCP---VAFLNTNI--RSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 IVTIDALASEVDSIasqCPSLKTK-----LLVSDHSREGWLDFRSLVKSASPE------HTCVKSKTldPMVIFFTSGTT 230
Cdd:cd05938 82 LVVAPELQEAVEEV---LPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEpvpaslRAHVTIKS--PALYIYTSGTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 231 GFPKMAKHSHGLALQPSFPGSrkLRSLKTSDVSW-CLS---DSGWIV---------ATIwTLVEPWTAGCtvFIHHLPQF 297
Cdd:cd05938 157 GLPKAARISHLRVLQCSGFLS--LCGVTADDVIYiTLPlyhSSGFLLgiggcielgATC-VLKPKFSASQ--FWDDCRKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 298 DTKVI--IQTLLKY----P----------------------------------INHFWG--------------------V 317
Cdd:cd05938 232 NVTVIqyIGELLRYlcnqPqspndrdhkvrlaignglradvwreflrrfgpirIREFYGstegnigffnytgkigavgrV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 318 SSIYRMILQQDFtsIRF------P---ALEHCytggeVVLPKDQeewkrrTGLLLYENYGQSE----TGDPEKTAK---- 380
Cdd:cd05938 312 SYLYKLLFPFEL--IKFdvekeePvrdAQGFC-----IPVAKGE------PGLLVAKITQQSPflgyAGDKEQTEKkllr 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 381 --VECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP-IRGEVVKAFIVL 456
Cdd:cd05938 379 dvFKKGDvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKL 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 578828477 457 TPqflSHDKDQltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 502
Cdd:cd05938 459 KP---GHEFDG--KKLYQHVREYLPAYARPRFLRIQDSLEITGTFK 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
368-516 |
1.57e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.66 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 368 GQSETGDPEKTAKV-------ECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAvV 439
Cdd:PRK05691 4077 GRGYVGDPLRTALAfvphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-V 4155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 440 GSPDPIRGEVVKAFIVLTPQFLSHdkDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PRK05691 4156 AVQEGVNGKHLVGYLVPHQTVLAQ--GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQL 4230
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
85-508 |
1.74e-13 |
|
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: 72.51 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 85 KWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVT 164
Cdd:cd17656 13 KLTYRELNERSNQLARFL-REKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 165 idalasevdsiasqCPSLKTKLlvSDHSREGWLDFRSLVKSASPEHTCVKSKTlDPMVIFFTSGTTGFPK--MAKHSHGL 242
Cdd:cd17656 92 --------------QRHLKSKL--SFNKSTILLEDPSISQEDTSNIDYINNSD-DLLYIIYTSGTTGKPKgvQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 243 AL-QPSFPGSRKLRSLKTSDVSWCLSDSGW--IVATiwtlvepWTAGCTVFI-HHLPQFDTKVIIQTLLKYPINHFWGVS 318
Cdd:cd17656 155 NLlHFEREKTNINFSDKVLQFATCSFDVCYqeIFST-------LLSGGTLYIiREETKRDVEQLFDLVKRHNIEVVFLPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 319 SIYRMILQQDFTSIRFP-ALEHCYTGGE-VVLPKDQEEWKRRTGLLLYENYGQSET--------------------GDPE 376
Cdd:cd17656 228 AFLKFIFSEREFINRFPtCVKHIITAGEqLVITNEFKEMLHEHNVHLHNHYGPSEThvvttytinpeaeipelppiGKPI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 377 KTAKV----------ECG------------------------------------DFYNTGDRGKMDEEGYICFLGRSDDI 410
Cdd:cd17656 308 SNTWIyildqeqqlqPQGivgelyisgasvargylnrqeltaekffpdpfdpneRMYRTGDLARYLPDGNIEFLGRADHQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 411 INASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTpQFLShdkdqlTKELQQHVKSVTAPYKYPRKVE 490
Cdd:cd17656 388 VKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME-QELN------ISQLREYLAKQLPEYMIPSFFV 460
|
490
....*....|....*...
gi 578828477 491 FVSELPKTITGKIERKEL 508
Cdd:cd17656 461 PLDQLPLTPNGKVDRKAL 478
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
118-513 |
6.11e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 71.00 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 118 LPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASE------VDSIASQCPSLKTKLLVSDH 191
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 192 S-----REGWLDFRSLVKSASPEHtCVKSKTLDPMV--------IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLK 258
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQG-SVGGNEYSPVYapvesvtnILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 259 TSDVSWClSDSGWIVATiWTLVEPWTAGCTVFIHH-------LPQF--DTKVIIQTLLKyPINHFWGVSSIYRMILQqDF 329
Cdd:PLN03051 160 GDVVCWP-TNLGWMMGP-WLLYSAFLNGATLALYGgaplgrgFGKFvqDAGVTVLGLVP-SIVKAWRHTGAFAMEGL-DW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 330 TSIRF------------------------PALEHC--------YTGGEVVLPKDQEEWKRR---TGLLLYENYGQSETGD 374
Cdd:PLN03051 236 SKLRVfastgeasavddvlwlssvrgyykPVIEYCggtelasgYISSTLLQPQAPGAFSTAslgTRFVLLNDNGVPYPDD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 375 PEKTAKVEC-------------GDFYNT------------------GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEV 423
Cdd:PLN03051 316 QPCVGEVALappmlgasdrllnADHDKVyykgmpmygskgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 424 ESALVE-HPAVAESAVVGSPDPIRGE----VVKAFIVLTPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKT 498
Cdd:PLN03051 396 ERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRN 475
|
490
....*....|....*...
gi 578828477 499 ITGKIERKELR---KKET 513
Cdd:PLN03051 476 ASNKLLRRVLRdqlKKEL 493
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
87-514 |
6.13e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 71.61 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTID 166
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 167 ALA---SEVDSIASQCPSlkTKLLVSDHsregwldfRSLVKSAsPEHTCVksktldpmvIFFTSGTTGFPK--MAKH--- 238
Cdd:PRK10252 564 DQLprfADVPDLTSLCYN--APLAPQGA--------APLQLSQ-PHHTAY---------IIFTSGSTGRPKgvMVGQtai 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 239 -SHGLALQPSFPGSRKLRSL-KTS---DVSwclsdsgwivatIWTLVEPWTAGCTVFI-----HHLPQFDTKVI----IQ 304
Cdd:PRK10252 624 vNRLLWMQNHYPLTADDVVLqKTPcsfDVS------------VWEFFWPFIAGAKLVMaepeaHRDPLAMQQFFaeygVT 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 305 TLlkypinHFwgVSSIYRMILQQ---DFTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRTGLLLYENYGQSET-------- 372
Cdd:PRK10252 692 TT------HF--VPSMLAAFVASltpEGARQSCASLRQVFCSGEA-LPADLcREWQQLTGAPLHNLYGPTEAavdvswyp 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -------------------------------------------------------GDPEKTAK-------VECGDFYNTG 390
Cdd:PRK10252 763 afgeelaavrgssvpigypvwntglrildarmrpvppgvagdlyltgiqlaqgylGRPDLTASrfiadpfAPGERMYRTG 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 391 DRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHP----AVAESAVVGSPDPIRGEVVKAFIVLTPQF-LSHDK 465
Cdd:PRK10252 843 DVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQLVGYLVSQSgLPLDT 922
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 578828477 466 DQltkeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETG 514
Cdd:PRK10252 923 SA----LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELK 967
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
82-508 |
9.13e-13 |
|
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: 70.19 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 82 DEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKg 161
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAK- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 162 ivtidalasevdsiasqcpslktkLLVSDhsregwldfrslvksasPEhtcvksktlDPMVIFFTSGTTGFPK--MAKHS 239
Cdd:cd17650 87 ------------------------LLLTQ-----------------PE---------DLAYVIYTSGTTGKPKgvMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 240 H------------GLALQPsfpgsrkLRSLKTSDVSWCLSDSGWIVATiwtlvepwTAGCTVFIhhLPQ---FDTKVIIQ 304
Cdd:cd17650 117 NvahaahawrreyELDSFP-------VRLLQMASFSFDVFAGDFARSL--------LNGGTLVI--CPDevkLDPAALYD 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 305 TLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG--LLLYENYGQSET--------- 372
Cdd:cd17650 180 LILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIINSYGVTEAtidstyyee 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ----------------------------------------------------GDPEKTAK-------VECGDFYNTGDRG 393
Cdd:cd17650 260 grdplgdsanvpigrplpntamyvlderlqpqpvgvagelyiggagvargylNRPELTAErfvenpfAPGERMYRTGDLA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 394 KMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPiRGEV-VKAFIVltpqfLSHDKDqlTKEL 472
Cdd:cd17650 340 RWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEArLCAYVV-----AAATLN--TAEL 411
|
490 500 510
....*....|....*....|....*....|....*.
gi 578828477 473 QQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17650 412 RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
223-515 |
1.50e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 223 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVAtIWTLVEPWTAGCTVFIHHLPQF-DTKV 301
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIRHS-ALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVF-VEELFWPLMSGARVVLAGPEDWrDPAL 3278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 302 IIQTLLKYPINHFWGVSSIYRMILQqDFTSIRFPALEHCYTGGEVVLPKDQEEWKrrTGLLLYENYGQSET--------- 372
Cdd:PRK12316 3279 LVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEAtitvthwqc 3355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 -------------------------------------------------GDPEKTAK-------VECGDFYNTGDRGKMD 396
Cdd:PRK12316 3356 veegkdavpigrpianracyildgslepvpvgalgelylggeglargyhNRPGLTAErfvpdpfVPGERLYRTGDLARYR 3435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 397 EEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGspdpIRGEVVKAFIVLTPQflshdKDQLTKELQQHV 476
Cdd:PRK12316 3436 ADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE-----AGDLREALKAHL 3506
|
330 340 350
....*....|....*....|....*....|....*....
gi 578828477 477 KSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 515
Cdd:PRK12316 3507 KASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
387-508 |
4.24e-12 |
|
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: 68.20 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVV------GSPDPIRGEVVkAFIVLTPQF 460
Cdd:cd17648 332 YKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedasQAQSRIQKYLV-GYYLPEPGH 410
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578828477 461 LSHdkdqltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17648 411 VPE------SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
384-516 |
6.37e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.83 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpDPIRGEVVKAFIVltPQFLSH 463
Cdd:PRK12316 2380 ERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PDDAAE 2456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578828477 464 DkdqLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 516
Cdd:PRK12316 2457 D---LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
373-508 |
9.34e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 67.34 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKA 452
Cdd:PRK05857 390 NNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGL 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578828477 453 FIVLTPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:PRK05857 470 AVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
384-513 |
2.00e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpDPIRGEVVKAFIVltPQFLSH 463
Cdd:PRK12467 3470 GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVV--PADPQG 3546
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 578828477 464 DkdqLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKET 513
Cdd:PRK12467 3547 D---WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA 3593
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
55-510 |
2.69e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 66.05 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 55 VLDYWAQKekegkRGPNPAFwwvngQGDEVKWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRT 134
Cdd:PRK08279 42 VFEEAAAR-----HPDRPAL-----LFEDQSISYAELNARANRYAHWA-AARGVGKGDVVALLMENRPEYLAAWLGLAKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 135 GIIfipATIL---LKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKLLVSD---HSREGWLDFRSLVKSASP 208
Cdd:PRK08279 111 GAV---VALLntqQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 209 EHTCVKSKTL--DPMVIFFTSGTTGFPKMAKHSHG---LALQpSFPGSRKLRSlktSD---------------VSWC--L 266
Cdd:PRK08279 188 TNPASRSGVTakDTAFYIYTSGTTGLPKAAVMSHMrwlKAMG-GFGGLLRLTP---DDvlycclplyhntggtVAWSsvL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 267 SDSGWIV-------ATIWTLVEPWtaGCTVFI--------------------HHL-------------PQFDTKVIIQTL 306
Cdd:PRK08279 264 AAGATLAlrrkfsaSRFWDDVRRY--RATAFQyigelcryllnqppkptdrdHRLrlmignglrpdiwDEFQQRFGIPRI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 307 LKypinhFWGVS----SIYRmILQQDFTSIRFPAL--------EHCYTGGEVVlpKDQEEWKRR-----TGLLL------ 363
Cdd:PRK08279 342 LE-----FYAASegnvGFIN-VFNFDGTVGRVPLWlahpyaivKYDVDTGEPV--RDADGRCIKvkpgeVGLLIgritdr 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 364 --YENYgqsetGDPEKTAKV------ECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVA 434
Cdd:PRK08279 414 gpFDGY-----TDPEASEKKilrdvfKKGDaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVE 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828477 435 ESAVVGSPDP-IRGEVVKAFIVLtpqflsHDKDQLT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK08279 489 EAVVYGVEVPgTDGRAGMAAIVL------ADGAEFDlAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
85-462 |
2.75e-11 |
|
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: 65.91 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 85 KWSFREMGDLTRRVANVFtQTCGLQQGDHLALMLPRVPEWWLV-----AVGCMRTGIIfipATILlkAKDILYRLQLSKA 159
Cdd:cd17641 11 EFTWADYADRVRAFALGL-LALGVGRGDVVAILGDNRPEWVWAelaaqAIGALSLGIY---QDSM--AEEVAYLLNYTGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 160 KGIVTIDAlaSEVD---SIASQCPSLKtKLLVSD--------HSREGWLD----------------FRSLVKSASPEHTC 212
Cdd:cd17641 85 RVVIAEDE--EQVDkllEIADRIPSVR-YVIYCDprgmrkydDPRLISFEdvvalgraldrrdpglYEREVAAGKGEDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 213 VKSktldpmvifFTSGTTGFPKMAKHSHG---------LALQPSFPGSRKLRSLKTSdvswclsdsgWIVATIWTLVEPW 283
Cdd:cd17641 162 VLC---------TTSGTTGKPKLAMLSHGnflghcaayLAADPLGPGDEYVSVLPLP----------WIGEQMYSVGQAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 284 TAGCTV-FIHHL-----------PQF-----------DTKVIIQTLLKYPINHF---WGVSSIYRMILQQD--------- 328
Cdd:cd17641 223 VCGFIVnFPEEPetmmedlreigPTFvllpprvwegiAADVRARMMDATPFKRFmfeLGMKLGLRALDRGKrgrpvslwl 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 329 -----------FTSIR----FPALEHCYTGGEVVLPkDQEEWKRRTGLLLYENYGQSET---------GD---------- 374
Cdd:cd17641 303 rlaswladallFRPLRdrlgFSRLRSAATGGAALGP-DTFRFFHAIGVPLKQLYGQTELagaytvhrdGDvdpdtvgvpf 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 375 ---------------------------PEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIIN-ASGYRIGPAEVES 425
Cdd:cd17641 382 pgtevridevgeilvrspgvfvgyyknPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIEN 461
|
490 500 510
....*....|....*....|....*....|....*..
gi 578828477 426 ALVEHPAVAESAVVGSPDPIrgevVKAFIVLTPQFLS 462
Cdd:cd17641 462 KLKFSPYIAEAVVLGAGRPY----LTAFICIDYAIVG 494
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
384-508 |
6.79e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSH 463
Cdd:PRK05691 2567 GRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDE 2646
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578828477 464 DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:PRK05691 2647 AQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
67-510 |
1.93e-10 |
|
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: 63.07 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 67 KRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANvFTQTCGLQQGDHLALMLPR----VPEWWlvavGCMRTGIIFIPAT 142
Cdd:cd05906 21 ERGPTKGITYIDADGSEEFQSYQDLLEDARRLAA-GLRQLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 143 I----------LLKAKDIlyRLQLSKAKgIVTIDALASEVDSIASQCPSLKTKLLVSdhsregwldfrSLVKSASPEHTC 212
Cdd:cd05906 96 VpptydepnarLRKLRHI--WQLLGSPV-VLTDAELVAEFAGLETLSGLPGIRVLSI-----------EELLDTAADHDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 213 VKSKTLDPMVIFFTSGTTGFPKMAKHSHG---------LALQPSFPGSRKL----------------RSL---------K 258
Cdd:cd05906 162 PQSRPDDLALLMLTSGSTGFPKAVPLTHRnilarsagkIQHNGLTPQDVFLnwvpldhvgglvelhlRAVylgcqqvhvP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 259 TSDVswcLSDS----GWI----VATIWT----------LVE-----PWTAGCT-VFIHHLPQFDTKVIIQTL-----LKY 309
Cdd:cd05906 242 TEEI---LADPlrwlDLIdryrVTITWApnfafallndLLEeiedgTWDLSSLrYLVNAGEAVVAKTIRRLLrllepYGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 310 PINHF---WGVS-----SIY-RMILQQDFT-SIRFPALEHCYTGGEV--------VLPKDQEEWKRRTGLLLYENYgqse 371
Cdd:cd05906 319 PPDAIrpaFGMTetcsgVIYsRSFPTYDHSqALEFVSLGRPIPGVSMrivddegqLLPEGEVGRLQVRGPVVTKGY---- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 372 TGDPEKTAKVECGD-FYNTGDRGKMDeEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAES--AVVGSPDPIRGE 448
Cdd:cd05906 395 YNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAET 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578828477 449 VVKAFIVLTPQFLSHDKDQLTKELQQHVK---SVTAPYKYPRKVEfvsELPKTITGKIERKELRK 510
Cdd:cd05906 474 EELAIFFVPEYDLQDALSETLRAIRSVVSrevGVSPAYLIPLPKE---EIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
200-508 |
3.27e-10 |
|
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: 62.10 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 200 RSLVKSASPEHTCVKSKTLDPMV-IFFTSGTTGFPKMAKHSHGlALQPSFPGSRK-----------LRSLKTSDVSwcls 267
Cdd:cd17654 99 DNAPLSFTPEHRHFNIRTDECLAyVIHTSGTTGTPKIVAVPHK-CILPNIQHFRSlfnitsedilfLTSPLTFDPS---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 268 dsgwIVATIWTLvepwTAGCTVFI---------HHLPQ-FDTKVIIQTLLKYP--INHFwGVSSIYRMILQQDfTSIRFP 335
Cdd:cd17654 174 ----VVEIFLSL----SSGATLLIvptsvkvlpSKLADiLFKRHRITVLQATPtlFRRF-GSQSIKSTVLSAT-SSLRVL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 336 ALehcytGGEVvLPKDQEEWKRRTGLL---LYENYGQSET------------------GDPEKTAKVE------------ 382
Cdd:cd17654 244 AL-----GGEP-FPSLVILSSWRGKGNrtrIFNIYGITEVscwalaykvpeedspvqlGSPLLGTVIEvrdqngsegtgq 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 383 ---------C----------GDFYNTGDRGKMdEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPD 443
Cdd:cd17654 318 vflgglnrvCilddevtvpkGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578828477 444 pirgEVVKAFIVLTPQflshdKDQLTKELQQHVKSvtaPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:cd17654 397 ----QRLIAFIVGESS-----SSRIHKELQLTLLS---SHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
107-510 |
3.31e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 63.06 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 107 GLQQGDHLALMLPRVPEWWLVAVGCMRTGiiFIPATILLKA--KDILYRLQLSKAKGIVTIDA------LASEVDSIASQ 178
Cdd:PRK06814 678 NTPPGENVGVMLPNANGAAVTFFALQSAG--RVPAMINFSAgiANILSACKAAQVKTVLTSRAfiekarLGPLIEALEFG 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 179 cpslkTKLLVSDHSREG---WLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLr 255
Cdd:PRK06814 756 -----IRIIYLEDVRAQiglADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI- 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 256 SLKTSDVSWC---LSDS-GWIVATIWTLVepwtAGCTVFIHHLPqFDTKVIIQtlLKYPINhfwgvSSI----------Y 321
Cdd:PRK06814 830 DFSPEDKVFNalpVFHSfGLTGGLVLPLL----SGVKVFLYPSP-LHYRIIPE--LIYDTN-----ATIlfgtdtflngY 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 322 -RMILQQDFTSIRFpalehCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGdP------------------------- 375
Cdd:PRK06814 898 aRYAHPYDFRSLRY-----VFAGAEKVKEETRQTWMEKFGIRILEGYGVTETA-Pvialntpmhnkagtvgrllpgieyr 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 376 -EKTAKVECG----------------------------DFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESA 426
Cdd:PRK06814 972 lEPVPGIDEGgrlfvrgpnvmlgylraenpgvleppadGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEEL 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 427 LVEHPAVAESAVVGSPDPIRGEVVkafIVLTPQflshdKDQLTKELQQHVKSVTAPYKY-PRKVEFVSELPKTITGKIER 505
Cdd:PRK06814 1052 AAELWPDALHAAVSIPDARKGERI---ILLTTA-----SDATRAAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKIDY 1123
|
....*
gi 578828477 506 KELRK 510
Cdd:PRK06814 1124 VAVTK 1128
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
86-511 |
5.41e-10 |
|
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: 61.68 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 86 WSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEW---W--LVAVGCmrtgiifIPATIL--LKAKDILYRLQLSK 158
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFvflWlgLWSIGA-------APAFINynLSGDPLIHCLKLSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 159 AKG-IVTIDALA-----SEVDSIASQCPSLKTKLLVSDHSREGWLdfrslvksaspeHTCVKSKTLDPMVIFF-TSGTTG 231
Cdd:cd05937 79 SRFvIVDPDDPAiliytSGTTGLPKAAAISWRRTLVTSNLLSHDL------------NLKNGDRTYTCMPLYHgTAAFLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 232 FPKMAKHSHGLALQPSFPGSRKLRSLKTSD-----------------------------VSWC--LSDSGWI-------- 272
Cdd:cd05937 147 ACNCLMSGGTLALSRKFSASQFWKDVRDSGatiiqyvgelcryllstppspydrdhkvrVAWGngLRPDIWErfrerfnv 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 273 ------------VATIWTL-VEPWTAGCTVF----IHHLPQFDtkviiQTLLKYPINHfwgvssiyRMILQQDFT--SIR 333
Cdd:cd05937 227 peigefyaategVFALTNHnVGDFGAGAIGHhgliRRWKFENQ-----VVLVKMDPET--------DDPIRDPKTgfCVR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 334 FPALEhcytGGEVV--LPKDQEEwkrrtgllLYENYGQSETGDPEKTAK--VECGD-FYNTGDRGKMDEEGYICFLGRSD 408
Cdd:cd05937 294 APVGE----PGEMLgrVPFKNRE--------AFQGYLHNEDATESKLVRdvFRKGDiYFRTGDLLRQDADGRWYFLDRLG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 409 DIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP-IRGEVVKAFIVLTPQflSHDKDQLTK-ELQQHVKSVTAPYKYP 486
Cdd:cd05937 362 DTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEES--SAVPTEFTKsLLASLARKNLPSYAVP 439
|
490 500
....*....|....*....|....*
gi 578828477 487 RKVEFVSELPKTITGKIERKELRKK 511
Cdd:cd05937 440 LFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
85-510 |
7.00e-09 |
|
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: 58.21 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 85 KWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVT 164
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 165 idalasevdsiasqcpSLKTKLLvsdhsregwldfrslvkSASPEH--TCVKSKTLDPMVIFFTSGTTGFPKMA--KHSH 240
Cdd:cd05939 82 ----------------NLLDPLL-----------------TQSSTEppSQDDVNFRDKLFYIYTSGTTGLPKAAviVHSR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 241 GLALQpsfPGSRKLRSLKTSDVSW-CLsdsgwivatiwtlvePW--TAGCTVFIHHLPQFDTKVIIQTllKYPINHFWG- 316
Cdd:cd05939 129 YYRIA---AGAYYAFGMRPEDVVYdCL---------------PLyhSAGGIMGVGQALLHGSTVVIRK--KFSASNFWDd 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 317 -----------VSSIYRMILQQdftSIRFPALEHC--YTGGEVVLPKDQEEWKRRTGLL-LYENYGQSE----------- 371
Cdd:cd05939 189 cvkynctivqyIGEICRYLLAQ---PPSEEEQKHNvrLAVGNGLRPQIWEQFVRRFGIPqIGEFYGATEgnsslvnidnh 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 372 -------------------------TGDPEKTAKVEC------------------------------------------- 383
Cdd:cd05939 266 vgacgfnsrilpsvypirlikvdedTGELIRDSDGLCipcqpgepgllvgkiiqndplrrfdgyvnegatnkkiardvfk 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 384 -GD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP-IRGEVVKAFIVLTPQF 460
Cdd:cd05939 346 kGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAGMAAIVDPERK 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 578828477 461 LshDKDQLTKELQqhvkSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05939 426 V--DLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
387-508 |
1.60e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.87 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVgspdpIRGEVVKAFIVltpQFLSHDK- 465
Cdd:PRK05691 1507 YRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLV---GYYTGEAg 1578
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578828477 466 -DQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 508
Cdd:PRK05691 1579 qEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
85-510 |
1.84e-08 |
|
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: 56.59 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 85 KWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIfiPATI--LLKAKDILYRLQLSKAKGI 162
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VtidalasevdsiasqcpslktkllvsdhsregwldfrslvksaspehtcvksktLDPMVIFFTSGTTGFPKMAKHSHGL 242
Cdd:cd05940 80 V------------------------------------------------------VDAALYIYTSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 243 ALQPSFPGSRKLRSLKTSDVSWCLS---DSGWIV---------ATI-----------WTLVEPWTAGCTVFIHHL----- 294
Cdd:cd05940 106 AWRGGAFFAGSGGALPSDVLYTCLPlyhSTALIVgwsaclasgATLvirkkfsasnfWDDIRKYQATIFQYIGELcryll 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 295 --PQFDT------KVIIQTLLKYPI-----------------------NHFWGVSSIYRMI-----LQQDFTSIRFPALE 338
Cdd:cd05940 186 nqPPKPTerkhkvRMIFGNGLRPDIweefkerfgvpriaefyaategnSGFINFFGKPGAIgrnpsLLRKVAPLALVKYD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 339 HcyTGGEVVLPKD---QEEWKRRTGLLLYE-NYGQSETG--DPEKTAKV------ECGD-FYNTGDRGKMDEEGYICFLG 405
Cdd:cd05940 266 L--ESGEPIRDAEgrcIKVPRGEPGLLISRiNPLEPFDGytDPAATEKKilrdvfKKGDaWFNTGDLMRLDGEGFWYFVD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 406 RSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP-IRGEVVKAFIVLTPqflSHDKDqlTKELQQHVKSVTAPYK 484
Cdd:cd05940 344 RLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQP---NEEFD--LSALAAHLEKNLPGYA 418
|
490 500
....*....|....*....|....*.
gi 578828477 485 YPRKVEFVSELPKTITGKIERKELRK 510
Cdd:cd05940 419 RPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
63-511 |
4.02e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 55.86 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 63 EKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTR---RVANVFtQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFI 139
Cdd:PLN03052 183 PKPSKTDDSIAIIWRDEGSDDLPVNRMTLSELRSqvsRVANAL-DALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 140 PATILLKAKDILYRLQLSKAKGIVT-----------------IDALASEVDSIASQCPSLKTKLLVSDHSregWLDFRSL 202
Cdd:PLN03052 262 SIADSFAPSEIATRLKISKAKAIFTqdvivrggksiplysrvVEAKAPKAIVLPADGKSVRVKLREGDMS---WDDFLAR 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 203 VK--SASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHglaLQPsfpgsrklrsLKTSDVSWCLSDS----------- 269
Cdd:PLN03052 339 ANglRRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQ---LTP----------LRAAADAWAHLDIrkgdivcwptn 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 270 -GWIVATiWTLVEPWTAGCTVFIHH-------LPQF--DTKVIIQTLlkypinhfwgVSSIYRM------ILQQDFTSIR 333
Cdd:PLN03052 406 lGWMMGP-WLVYASLLNGATLALYNgsplgrgFAKFvqDAKVTMLGT----------VPSIVKTwkntncMAGLDWSSIR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 334 F-----------------------PALEHC--------YTGGEVVLPKDQEEWKR---RTGLLLYENYGQSETGDPEKTA 379
Cdd:PLN03052 475 CfgstgeassvddylwlmsragykPIIEYCggtelgggFVTGSLLQPQAFAAFSTpamGCKLFILDDSGNPYPDDAPCTG 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 380 kvECG---------------DFYNT----------------GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVE---- 424
Cdd:PLN03052 555 --ELAlfplmfgasstllnaDHYKVyfkgmpvfngkilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcn 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 425 SAlveHPAVAESAVVGSPDPIRG--EVVKAFIVLTPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 502
Cdd:PLN03052 633 AA---DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNK 709
|
....*....
gi 578828477 503 IERKELRKK 511
Cdd:PLN03052 710 VMRRVLRQQ 718
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
379-510 |
6.45e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.16 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 379 AKVECGDFYNTGDRGKM-DEEGYICflGRSDDIINASGYRIGPAEVESALVEHPAVAESAVV--GSPDpirgEVVKAFIV 455
Cdd:PRK05851 390 APIDPDDWFPTGDLGYLvDGGLVVC--GRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVavGTGE----GSARPGLV 463
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 456 LTPQFLSHDKDQLTKELQQHVKSVTApyKYPRKVEFVS--ELPKTITGKIERKELRK 510
Cdd:PRK05851 464 IAAEFRGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
373-510 |
4.99e-07 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 52.62 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKTAKV----ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALveHPAVAES----AVVGSPDP 444
Cdd:PRK08633 1003 GDPEKTAEVikdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDE 1080
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828477 445 IRGEVVkafIVLTPQflshdKDQLTKELQQHVKSVTAP--YKyPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK08633 1081 KKGEKL---VVLHTC-----GAEDVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
374-511 |
8.36e-07 |
|
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: 51.59 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 374 DPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINAS-GYRIGPAEVESALVEHPAVAESAVVGSPDPIRGevvk 451
Cdd:cd17640 308 NPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG---- 383
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 452 AFIVltPqflshDKDQLTKELQQhvksvtapykypRKVEFVSELPKTITGKIERKELRKK 511
Cdd:cd17640 384 ALIV--P-----NFEELEKWAKE------------SGVKLANDRSQLLASKKVLKLYKNE 424
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
373-475 |
2.79e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.90 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKT--AKVE--CGDFYN-TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPirG 447
Cdd:PRK09274 403 NRPEATrlAKIPdgQGDVWHrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--G 480
|
90 100
....*....|....*....|....*...
gi 578828477 448 EVVKAFIVLTPQFLSHDKDQLTKELQQH 475
Cdd:PRK09274 481 AQRPVLCVELEPGVACSKSALYQELRAL 508
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
366-508 |
7.29e-06 |
|
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: 48.67 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 366 NYGQSETGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP 444
Cdd:cd17647 352 NYLDKDNNEPWRQFWLGPRDrLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 445 IRGEVVKAFIVltPQFLSHDKD------------------------QLTKELQQHVKSVTAPYKYPRKVEFVSELPKTIT 500
Cdd:cd17647 432 DEEPTLVSYIV--PRFDKPDDEsfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPN 509
|
....*...
gi 578828477 501 GKIERKEL 508
Cdd:cd17647 510 GKVDKPKL 517
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
78-440 |
2.63e-05 |
|
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: 46.97 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 78 NGQGDEVKWSFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIF--IPATIllKAKDILYRLQ 155
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKL-GLERFHGVGILGFNSPEWFIAAVGAIFAGGIAvgIYTTN--SPEACQYVAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 156 LSKAKGIVTIDA-LASEVDSIASQCPSLKTKLLVSDHSRE------GWLDFRSLVKSASPEHTCVKSKTLDP---MVIFF 225
Cdd:cd05933 78 TSEANILVVENQkQLQKILQIQDKLPHLKAIIQYKEPLKEkepnlySWDEFMELGRSIPDEQLDAIISSQKPnqcCTLIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 226 TSGTTGFPK--MAKH----------SHGLALQPSFPGSRKLRS--------LKTSDVSWCLSDSGWIV-----ATIWTLV 280
Cdd:cd05933 158 TSGTTGMPKgvMLSHdnitwtakaaSQHMDLRPATVGQESVVSylplshiaAQILDIWLPIKVGGQVYfaqpdALKGTLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 281 E-------------PWT------------AGCTVFIHHLPQFDTKVIIQTLLKYP---INHFWGvssiYRMILQQDFTSI 332
Cdd:cd05933 238 KtlrevrptafmgvPRVwekiqekmkavgAKSGTLKRKIASWAKGVGLETNLKLMggeSPSPLF----YRLAKKLVFKKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 333 R-FPALEHC---YTGGeVVLPKDQEEWKRRTGLLLYENYGQSET------------------------------------ 372
Cdd:cd05933 314 RkALGLDRCqkfFTGA-APISRETLEFFLSLNIPIMELYGMSETsgphtisnpqayrllscgkalpgcktkihnpdadgi 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 ---------------GDPEKTA-KVECGDFYNTGDRGKMDEEGYICFLGRSDD-IINASGYRIGPAEVESAL-VEHPAVA 434
Cdd:cd05933 393 geicfwgrhvfmgylNMEDKTEeAIDEDGWLHSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVkKELPIIS 472
|
....*.
gi 578828477 435 ESAVVG 440
Cdd:cd05933 473 NAMLIG 478
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
365-511 |
3.47e-05 |
|
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: 46.33 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 365 ENYGQSETGDPEKTAKVECGD-FYNTGDRGKM-DEEGYIcfLGRSDDIINASGYRIGPAEVESALVEHPAV--AESAVVG 440
Cdd:cd05908 348 KNVTPGYYNNPEATAKVFTDDgWLKTGDLGFIrNGRLVI--TGREKDIIFVNGQNVYPHDIERIAEELEGVelGRVVACG 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828477 441 SPDP-IRGEVVKAFIVltpqflsHDKDQ-----LTKELQQHVKSVTApyKYPRKVEFVSELPKTITGKIERKELRKK 511
Cdd:cd05908 426 VNNSnTRNEEIFCFIE-------HRKSEddfypLGKKIKKHLNKRGG--WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
373-510 |
4.00e-05 |
|
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: 46.08 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKTAKVEC-------GDFYNTGDRGKM-DEEGYICflGRSDDIINASGYRIGPAEVESALVE-HPAVAES--AVVGS 441
Cdd:cd05931 398 GRPEATAETFGalaatdeGGWLRTGDLGFLhDGELYIT--GRLKDLIIVRGRNHYPQDIEATAEEaHPALRPGcvAAFSV 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828477 442 PDPIRGEVVkAFIVLTPQFLSHDKDQLTKELQQHVKS---VTapykyPRKVEFVS--ELPKTITGKIERKELRK 510
Cdd:cd05931 476 PDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
387-505 |
1.15e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 44.60 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 387 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAV-AESAV-VGSPDPIRGEvvkAFIVLTPQFLSHD 464
Cdd:PRK07768 416 LDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE---GFAVAVESNAFED 492
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578828477 465 KDQLTKELQQHVKSVTAPYKY-PRKVEFVS--ELPKTITGKIER 505
Cdd:PRK07768 493 PAEVRRIRHQVAHEVVAEVGVrPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
360-510 |
1.49e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 44.70 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 360 GLLLYENYGQSETGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVV 439
Cdd:PRK08043 566 GYLRVEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATA 645
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828477 440 GSPDPIRGEvvkAFIVLTPqflshDKdQLTKE-LQQHVKSVTAP-YKYPRKVEFVSELPKTITGKIERKELRK 510
Cdd:PRK08043 646 IKSDASKGE---ALVLFTT-----DS-ELTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKS 709
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
87-254 |
7.26e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 42.19 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 87 SFREMGDLTRRVANVFTQTcGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIfipaTILLKA----KDILYRLQLSKAKGI 162
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAV----PVLVDPgmgiKNLKQCLAEAQPDAF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 163 VTIdALASevdsIASQ-----CPSLKTKLLVSDhsREGW----LDfRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFP 233
Cdd:PRK09274 118 IGI-PKAH----LARRlfgwgKPSVRRLVTVGG--RLLWggttLA-TLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTP 189
|
170 180 190
....*....|....*....|....*....|
gi 578828477 234 KMAKHSHGL------ALQPSF---PGSRKL 254
Cdd:PRK09274 190 KGVVYTHGMfeaqieALREDYgiePGEIDL 219
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
373-510 |
7.61e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 42.30 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828477 373 GDPEKTAKVECGDFYNTGDRGKMdEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAV--AESAVVGSPDPIRGEVV 450
Cdd:PRK09192 427 RDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQENGEKIV 505
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828477 451 kafiVLTPQFLS--HDKDQLTKELQQHVKSVTApykYPRKVEFVS--ELPKTITGKIERKELRK 510
Cdd:PRK09192 506 ----LLVQCRISdeERRGQLIHALAALVRSEFG---VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
389-440 |
8.72e-04 |
|
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: 41.68 E-value: 8.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 578828477 389 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVG 440
Cdd:cd05910 335 MGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
|
| |
