|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
101-623 |
0e+00 |
|
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: 850.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI 180
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 181 FggemvaavaevsghlgkslikfcsgdlgpegilpdtHLLDPLLKEASTAPLAQIPsKGMDDRLFYIYTSGTTGLPKAAI 260
Cdd:cd05939 81 F------------------------------------NLLDPLLTQSSTEPPSQDD-VNFRDKLFYIYTSGTTGLPKAAV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTIngvrhcr 340
Cdd:cd05939 124 IVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTI------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 341 llclvVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGF 420
Cdd:cd05939 197 -----VQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGF 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 421 NSRILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSVFSKGDSAY 500
Cdd:cd05939 272 NSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 501 LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAI 580
Cdd:cd05939 352 LSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRF 431
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 768002382 581 YQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 623
Cdd:cd05939 432 SAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
42-656 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 673.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 42 RFLRIVCKTARRDLFGLSVLIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFR 121
Cdd:PRK08279 3 TLMDLAARLPRRLPDLPGILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQS--ISYAELNARANRYAHWAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 122 QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLI 201
Cdd:PRK08279 81 ARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 202 KFCSGDlgPEGILPDTHL-LDPLLKEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-MAAFGHhAYRM 279
Cdd:PRK08279 161 LWVAGG--DTLDDPEGYEdLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKaMGGFGG-LLRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 280 QAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTingvrhcrllclVVQYIGEICRYLLKQ 359
Cdd:PRK08279 238 TPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRAT------------AFQYIGELCRYLLNQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 360 PVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHvyPIRLVKVNED 439
Cdd:PRK08279 306 PPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVKYDVD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 440 TMELLRDAQGLCIPCQAGEPGLLVGQINqqdPLRRFDGYVSESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDR 519
Cdd:PRK08279 384 TGEPVRDADGRCIKVKPGEVGLLIGRIT---DRGPFDGYTDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 520 SGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAA-VADPHSLLDPNAIYQELQKVLAPYARPIFLR 598
Cdd:PRK08279 461 LGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAiVLADGAEFDLAALAAHLYERLPAYAVPLFVR 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 768002382 599 LLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAF 656
Cdd:PRK08279 541 LVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKF 598
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
101-623 |
0e+00 |
|
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: 642.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI 180
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 181 FggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmdDRLFYIYTSGTTGLPKAAI 260
Cdd:cd05940 81 V------------------------------------------------------------DAALYIYTSGTTGLPKAAI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTIngvrhcr 340
Cdd:cd05940 101 ISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATI------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 341 llclvVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGF 420
Cdd:cd05940 174 -----FQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 421 NSRILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINqqdPLRRFDGYVSESATSKKIAHSVFSKGDSAY 500
Cdd:cd05940 249 NPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 501 LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSL-LDPNA 579
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEeFDLSA 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 768002382 580 IYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 623
Cdd:cd05940 406 LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
101-648 |
0e+00 |
|
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: 590.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 101 GECWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAL 179
Cdd:cd05938 3 GETYTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 180 IFGGEMVAAVAEVSGHLGKSLIK--FCSGDLGPEGIlpdTHLLDpLLKEASTAPLAQ---IPSKGMDDRLfYIYTSGTTG 254
Cdd:cd05938 83 VVAPELQEAVEEVLPALRADGVSvwYLSHTSNTEGV---ISLLD-KVDAASDEPVPAslrAHVTIKSPAL-YIYTSGTTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 255 LPKAAIVVHSRYYRMAAFgHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTin 334
Cdd:cd05938 158 LPKAARISHLRVLQCSGF-LSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVT-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 335 gvrhcrllclVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGK 414
Cdd:cd05938 235 ----------VIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 415 VGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPlrrFDGYV-SESATSKKIAHSVF 493
Cdd:cd05938 305 IGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAgDKEQTEKKLLRDVF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 494 SKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAV--ADP 571
Cdd:cd05938 382 KKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVklKPG 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 572 HSlLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVY 648
Cdd:cd05938 462 HE-FDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
101-623 |
6.64e-135 |
|
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: 403.74 E-value: 6.64e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 101 GECWTFAQLDAYSNAVANLFR-QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAL 179
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 180 IfggemvaavaevsghlgkslikfcsgdlgpegilpdthlLDPllkeastaplaqipskgmDDRLFYIYTSGTTGLPKAA 259
Cdd:cd05937 83 I---------------------------------------VDP------------------DDPAILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 260 IVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTIngvrhc 339
Cdd:cd05937 106 AISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATI------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 340 rllclvVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANM---DGKVG 416
Cdd:cd05937 180 ------IQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnvgDFGAG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 417 SCGFNSRILPHVY--PIRLVKVNEDTMELLRDAQ-GLCIPCQAGEPGLLVGQINQqDPLRRFDGYV-SESATSKKIAHSV 492
Cdd:cd05937 254 AIGHHGLIRRWKFenQVVLVKMDPETDDPIRDPKtGFCVRAPVGEPGEMLGRVPF-KNREAFQGYLhNEDATESKLVRDV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 493 FSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVA-DP 571
Cdd:cd05937 333 FRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITlEE 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 572 HSLLDPNAIYQELQKV----LAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 623
Cdd:cd05937 413 SSAVPTEFTKSLLASLarknLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
78-619 |
6.06e-86 |
|
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: 276.69 E-value: 6.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 78 IPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAAL 157
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGG--RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 158 LNVNLRREPLAFCLGTSGAKALIFggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqips 237
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 238 kgmddrLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKF 317
Cdd:COG0318 103 ------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 318 SASRFWDDCIKYNCTIngvrhcrlLCLVvqyiGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRqI 395
Cdd:COG0318 177 DPERVLELIERERVTV--------LFGV----PTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-I 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 396 GEFYGATECNCSIA-----NMDGKVGSCGfnsRILPHVyPIRLVkvnedtmellrDAQGlcIPCQAGEPGLLVGQINQQd 470
Cdd:COG0318 244 VEGYGLTETSPVVTvnpedPGERRPGSVG---RPLPGV-EVRIV-----------DEDG--RELPPGEVGEIVVRGPNV- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 471 plrrFDGYV-SESATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDV 549
Cdd:COG0318 306 ----MKGYWnDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEA 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 550 AVYGVAVPgVEGKAGMAAV-ADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 619
Cdd:COG0318 375 AVVGVPDE-KWGERVVAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
101-617 |
5.26e-84 |
|
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: 270.70 E-value: 5.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI 180
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 181 fggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeASTAPLaqipskgmddrlfyIYTSGTTGLPKAAI 260
Cdd:cd05934 81 ----------------------------------------------VDPASI--------------LYTSGTTGPPKGVV 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTIngvrhcr 340
Cdd:cd05934 101 ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATV------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 341 llclvVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATECNCSIAN---MDGKVGS 417
Cdd:cd05934 174 -----TNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGprdEPRRPGS 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 418 CGfnsrilphvYPIRLVKVnedtmeLLRDAQGLciPCQAGEPGLLVgqINQQDPLRRFDGYVS-ESATSKKIAHSVFSKG 496
Cdd:cd05934 248 IG---------RPAPGYEV------RIVDDDGQ--ELPAGEPGELV--IRGLRGWGFFKGYYNmPEATAEAMRNGWFHTG 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 497 DSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLD 576
Cdd:cd05934 309 DLGY-------RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD 381
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 768002382 577 PNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 617
Cdd:cd05934 382 PEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
74-629 |
5.48e-78 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 258.53 E-value: 5.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 74 AGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM 153
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGGTR--WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 154 EAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkslikfcsgDLGPEGiLPDTHLLDPLLKEASTAPLA 233
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA--------------DPGDLP-LPAVWLLDAPASVSVPAGWS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 234 QIPSKGMD-----------DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHS-AGNIIGv 301
Cdd:PRK06155 162 TAPLPPLDapapaaavqpgDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTnALNAFF- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 302 gQCLIYGLTVVLRKKFSASRFWDDCIKYNCTingvrhcrllclVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPA 381
Cdd:PRK06155 241 -QALLAGATYVLEPRFSASGFWPAVRRHGAT------------VTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 382 IWEEFTERFGVRQIgEFYGATECNCSIANM--DGKVGSCGfnsRILPHvYPIRLVkvnedtmellrDAQGLCIPcqAGEP 459
Cdd:PRK06155 308 LHAAFRERFGVDLL-DGYGSTETNFVIAVThgSQRPGSMG---RLAPG-FEARVV-----------DEHDQELP--DGEP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 460 GLLVGQINQqdPLRRFDGYVSESATSkkiahsVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGV 539
Cdd:PRK06155 370 GELLLRADE--PFAFATGYFGMPEKT------VEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQV 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 540 LSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 619
Cdd:PRK06155 442 LLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
570
....*....|
gi 768002382 620 GFDPrQTSDR 629
Cdd:PRK06155 522 GVTA-DTWDR 530
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
242-612 |
1.31e-61 |
|
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: 208.68 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLRKKFSASR 321
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 322 FWDDCIKYNCTIngvrhcrlLCLVVQYIgeicRYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRqIGEFY 399
Cdd:cd04433 80 ALELIEREKVTI--------LLGVPTLL----ARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 400 GATECNCSIA-----NMDGKVGSCGfnsRILPHVYpIRLVkvNEDTmellrdaqglcIPCQAGEPGLLVGQINQqdplrR 474
Cdd:cd04433 147 GLTETGGTVAtgppdDDARKPGSVG---RPVPGVE-VRIV--DPDG-----------GELPPGEIGELVVRGPS-----V 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 475 FDGYVsesatsKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 554
Cdd:cd04433 205 MKGYW------NNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGV 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 555 AVPgVEGKAGMAAV-ADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQ 612
Cdd:cd04433 279 PDP-EWGERVVAVVvLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-527 |
8.29e-61 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 209.09 E-value: 8.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 82 FQAVVQRQPERLALVDaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:pfam00501 1 LERQAARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 162 LRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPegilPDTHLLDPLLKEASTAPLAQIPSKGMD 241
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVH----SRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKF 317
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 318 SA---SRFWDDCIKYNCTIngvrhcrlLCLVvqyiGEICRYLLKQPVREAERRHRVR--LAVGNGLRPAIWEEFTERFGv 392
Cdd:pfam00501 236 PAldpAALLELIERYKVTV--------LYGV----PTLLNMLLEAGAPKRALLSSLRlvLSGGAPLPPELARRFRELFG- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 393 RQIGEFYGATECNCSIANMD------GKVGSCGfnsRILPHVypiRLVKVNEDTMELLRDaqglcipcqaGEPG-LLVGQ 465
Cdd:pfam00501 303 GALVNGYGLTETTGVVTTPLpldedlRSLGSVG---RPLPGT---EVKIVDDETGEPVPP----------GEPGeLCVRG 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768002382 466 INQqdplrrFDGYV-SESATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 527
Cdd:pfam00501 367 PGV------MKGYLnDPELTAEAF------DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
86-622 |
4.73e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 188.31 E-value: 4.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALvdaGTGEC-WTFAQLDAYSNAVANLFRQLGFAPGDV-VAIFLEGRPEFVgLWLGLAKAGmEAALLNVNLR 163
Cdd:PRK13388 11 DRAGDDTIAV---RYGDRtWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEML-FWLAAAALG-GYVLVGLNTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 164 REplafclgtsgakalifGGEMVAAVAEVSGHL------GKSLIKfcsgDLGpegiLPDTHLLD---PLLKE--ASTAPL 232
Cdd:PRK13388 86 RR----------------GAALAADIRRADCQLlvtdaeHRPLLD----GLD----LPGVRVLDvdtPAYAElvAAAGAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 233 AQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAA-----FGHHayrmqAADVLYDCLPLYHSAGNIIGVGQCLIY 307
Cdd:PRK13388 142 TPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRalterFGLT-----RDDVCYVSMPLFHSNAVMAGWAPAVAS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 308 GLTVVLRKKFSASRFWDDCIKYNCTIngvrhcrllclvVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFT 387
Cdd:PRK13388 217 GAAVALPAKFSASGFLDDVRRYGATY------------FNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 388 ERFGVrQIGEFYGATECNCSIANMDGK-VGSCGfnsRILPHVypirlVKVNEDTMEllrdaqgLCIPCQAGEPGLL---- 462
Cdd:PRK13388 285 RRFGC-QVEDGYGSSEGAVIVVREPGTpPGSIG---RGAPGV-----AIYNPETLT-------ECAVARFDAHGALlnad 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 463 --VGQINQQDPLRRFDGYVS-ESATSKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGV 539
Cdd:PRK13388 349 eaIGELVNTAGAGFFEGYYNnPEATAERMRHGMYWSGDLAYRDAD-------GWIYFAGRTADWMRVDGENLSAAPIERI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 540 LSRLLGQTDVAVYGVAVPGVeGKAGMAAV--ADPHSlLDPNAIYQEL--QKVLAPYARPIFLRLLPQVDTTGTFKIQKTR 615
Cdd:PRK13388 422 LLRHPAINRVAVYAVPDERV-GDQVMAALvlRDGAT-FDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRE 499
|
....*..
gi 768002382 616 LQREGFD 622
Cdd:PRK13388 500 LIAQGWA 506
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
241-622 |
1.98e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 180.65 E-value: 1.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 241 DDRLFYIYTSGTTGLPKAAIVVHSRYY---RMAA--FGHhayrmQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRK 315
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVAsagVMLAqrFGL-----GPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 316 KFSASRFWDDCIKYNCTingvrhcrllclVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQI 395
Cdd:PRK07867 227 KFSASGFLPDVRRYGAT------------YANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 396 gEFYGATECNCSIANM-DGKVGSCGfnsrilPHVYPIRLVkvNEDTMELlrdaqglCIPCQAGEPGLL-----VGQ-INQ 468
Cdd:PRK07867 295 -DGFGSTEGGVAITRTpDTPPGALG------PLPPGVAIV--DPDTGTE-------CPPAEDADGRLLnadeaIGElVNT 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 469 QDPlRRFDGYVS-ESATSKKIAHSVFSKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQT 547
Cdd:PRK07867 359 AGP-GGFEGYYNdPEADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768002382 548 DVAVYGVAVPGVeGKAGMAAVA-DPHSLLDPNAIYQEL--QKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFD 622
Cdd:PRK07867 431 EVAVYAVPDPVV-GDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
77-619 |
3.47e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 176.92 E-value: 3.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 77 TIPRIFQAVVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYF--DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGksLIKFC--SGDLGPEGILPDTHLLDPLLKEASTAPLAq 234
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLP--TVRTVivEGDGPAAPLAPEVGEYEELLAAASDTFDF- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 235 iPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGniIGVG-QCLIYGLTVVL 313
Cdd:PRK06187 162 -PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPyLALMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 314 RKKFSASRFWDDCIKYNCTIngvrhcrLLClvvqyIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFG 391
Cdd:PRK06187 239 PRRFDPENLLDLIETERVTF-------FFA-----VPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 392 VRQIgEFYGATECnCSIA----------NMDGKVGSCGfnsRILPHVYpIRLvkVNEDTMELlrdaqglciPCQAGEPGL 461
Cdd:PRK06187 307 IDLV-QGYGMTET-SPVVsvlppedqlpGQWTKRRSAG---RPLPGVE-ARI--VDDDGDEL---------PPDGGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 462 LV--GQINQQdplrrfdGYVS-ESATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEG 538
Cdd:PRK06187 370 IIvrGPWLMQ-------GYWNrPEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELED 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 539 VLSRLLGQTDVAVYGVAVPgvegKAGMAAVA----DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKT 614
Cdd:PRK06187 436 ALYGHPAVAEVAVIGVPDE----KWGERPVAvvvlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKR 511
|
....*
gi 768002382 615 RLqRE 619
Cdd:PRK06187 512 VL-RE 515
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
86-627 |
1.57e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 176.07 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALV---DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNL 162
Cdd:COG0365 19 AEGRGDKVALIwegEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 163 RREPLAFCLGTSGAKALI------FGGEMV---AAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEAS-TAPL 232
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglRGGKVIdlkEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASaEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 233 AQIPSkgmDDRLFYIYTSGTTGLPKAaiVVHS-RYY--RMAAFGHHAYRMQAADVLYdCLP----LYHsAGNIIgVGQcL 305
Cdd:COG0365 179 EPTDA---DDPLFILYTSGTTGKPKG--VVHThGGYlvHAATTAKYVLDLKPGDVFW-CTAdigwATG-HSYIV-YGP-L 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 306 IYGLTVVL---RKKF-SASRFWDDCIKYNCTIngvrhcrlLCLVVQYIgeicRYLLKQPVREAERRHRVRL----AVGNG 377
Cdd:COG0365 250 LNGATVVLyegRPDFpDPGRLWELIEKYGVTV--------FFTAPTAI----RALMKAGDEPLKKYDLSSLrllgSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 378 LRPAIWEEFTERFGVrQIGEFYGATECNCSIAN----MDGKVGSCGFnsrilphvyPIRLVKVnedtmELLrDAQGlcIP 453
Cdd:COG0365 318 LNPEVWEWWYEAVGV-PIVDGWGQTETGGIFISnlpgLPVKPGSMGK---------PVPGYDV-----AVV-DEDG--NP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 454 CQAGEPGLLVgqINQQDP--LRRF----DGYVSesatskkiahSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 527
Cdd:COG0365 380 VPPGEEGELV--IKGPWPgmFRGYwndpERYRE----------TYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 528 GENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAA--VADPHSLLDPnAIYQELQ----KVLAPYARP---IFLR 598
Cdd:COG0365 448 GHRIGTAEIESALVSHPAVAEAAV--VGVPDEIRGQVVKAfvVLKPGVEPSD-ELAKELQahvrEELGPYAYPreiEFVD 524
|
570 580 590
....*....|....*....|....*....|.
gi 768002382 599 LLPqvdTTGTFKIQKTRLQR--EGFDPRQTS 627
Cdd:COG0365 525 ELP---KTRSGKIMRRLLRKiaEGRPLGDTS 552
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
75-617 |
6.25e-45 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 167.94 E-value: 6.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 75 GHTIPRIFQAVVQRQPERLALV---DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKA 151
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIfesSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 152 GMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGpEGILPDTHLLDPLLKEAStAP 231
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVA-LPADDGVSSFTQLKAQQP-AT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 232 LAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRMAAFGHHAY---RMQAADVLYDCLPLYHSAGNIIGVGQCLIYG 308
Cdd:PRK08008 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 309 LTVVLRKKFSASRFWDDCIKYNCTINgvrHCrllclvvqyIGEICRYLLKQPVREAERRHRVR-----LAVGNGLRpaiw 383
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRATIT---EC---------IPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 384 EEFTERFGVRQIGEfYGATEcncSIAnmdGKVGSCGFNSRILPHV------YPIRlvkvnedtmelLRDAQGLCIP---- 453
Cdd:PRK08008 305 DAFEERFGVRLLTS-YGMTE---TIV---GIIGDRPGDKRRWPSIgrpgfcYEAE-----------IRDDHNRPLPagei 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 454 ---CQAGEPGLLVGQINQQDPlrrfdgyvseSATSKKI-AHSVFSKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGE 529
Cdd:PRK08008 367 geiCIKGVPGKTIFKEYYLDP----------KATAKVLeADGWLHTGDTGY-------VDEEGFFYFVDRRCNMIKRGGE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 530 NVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVA-DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGT 608
Cdd:PRK08008 430 NVSCVELENIIATHPKIQDIVVVGIKDS-IRDEAIKAFVVlNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCS 508
|
....*....
gi 768002382 609 FKIQKTRLQ 617
Cdd:PRK08008 509 GKIIKKNLK 517
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
94-612 |
1.62e-44 |
|
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: 165.85 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 94 ALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGT 173
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 174 SGAKALIFGGEMVAAVAEVSGHLG-KSLIkFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKgmDDRLFYIYTSGT 252
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGpKDKI-IVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGK--DDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 253 TGLPKAAIVVHSRYYRMA--AFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGqCLIYGLTVVLRKKFSASRFWDDCIKYN 330
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLA-SLLNGATVIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 331 CTIngvrhcrllCLVVQYIGEIcryLLKQPVREAERRHRVR-LAVGNG-LRPAIWEEFTERFGVRQIGEFYGATECNCSI 408
Cdd:cd05911 237 ITF---------LYLVPPIAAA---LAKSPLLDKYDLSSLRvILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 409 A---NMDGKVGSCGfnsRILPHVypiRLVKVNEDTMELLRDaqglcipcqaGEPG-LLV--GQInqqdplrrFDGYVS-E 481
Cdd:cd05911 305 TvnpDGDDKPGSVG---RLLPNV---EAKIVDDDGKDSLGP----------NEPGeICVrgPQV--------MKGYYNnP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 482 SATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEG 561
Cdd:cd05911 361 EATKETFDE------DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 562 KAGMAAVA-DPHSLLDPNAIYQELQKVLAPY----ARPIFLRLLPQvdtTGTFKIQ 612
Cdd:cd05911 434 ELPRAYVVrKPGEKLTEKEVKDYVAKKVASYkqlrGGVVFVDEIPK---SASGKIL 486
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
86-613 |
4.01e-44 |
|
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: 163.94 E-value: 4.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:cd17631 5 ARRHPDRTALVFGG--RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 PLAFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmDDRLF 245
Cdd:cd17631 83 EVAYILADSGAKVLF------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 246 YIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAG-NIIGVGQcLIYGLTVVLRKKFSASRFWD 324
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGlGVFTLPT-LLRGGTVVILRKFDPETVLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 325 DCIKYnctinGVRHCRLLCLVVQyigeicrYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFtERFGVRqIGEFYGAT 402
Cdd:cd17631 182 LIERH-----RVTSFFLVPTMIQ-------ALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGVK-FVQGYGMT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 403 ECNCSIANMD-----GKVGSCGfnsRILPHVyPIRLVKVNEDtmellrdaqglciPCQAGEpgllVGQINQQDPLrRFDG 477
Cdd:cd17631 248 ETSPGVTFLSpedhrRKLGSAG---RPVFFV-EVRIVDPDGR-------------EVPPGE----VGEIVVRGPH-VMAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 478 YVS-ESATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaV 556
Cdd:cd17631 306 YWNrPEATAAAFR-------DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--V 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 557 PGVE-GKAGMAAVA-DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQK 613
Cdd:cd17631 377 PDEKwGEAVVAVVVpRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
77-617 |
1.07e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 158.53 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 77 TIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAA 156
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGD--QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--AV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNVNLRREP--LAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLkeASTAPLAQ 234
Cdd:PRK07656 82 VVPLNTRYTAdeAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFL--AAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 235 IPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMA-AFGHHAyRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL 313
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAaDWAEYL-GLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 314 RKKFSASRFWDDCIKYNCTI-NGVRhcrllclvvqyigEICRYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERF 390
Cdd:PRK07656 239 LPVFDPDEVFRLIETERITVlPGPP-------------TMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 391 GVRQIGEFYGATECnCSIANM-----DGKV--GSCGfnsRILPHVyPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLV 463
Cdd:PRK07656 306 GVDIVLTGYGLSEA-SGVTTFnrlddDRKTvaGTIG---TAIAGV-ENKIV-----------NELGEEVP--VGEVGELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 464 gqinqqdpLRRFD---GYVS-ESATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGV 539
Cdd:PRK07656 368 --------VRGPNvmkGYYDdPEATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 540 LSRLLGQTDVAVYGVAVPGVeGKAGMA-AVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPqVDTTGtfKIQKTR 615
Cdd:PRK07656 434 LYEHPAVAEAAVIGVPDERL-GEVGKAyVVLKPGAELTEEELIAYCREHLAKYKVPrsiEFLDELP-KNATG--KVLKRA 509
|
..
gi 768002382 616 LQ 617
Cdd:PRK07656 510 LR 511
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
78-617 |
1.41e-41 |
|
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: 157.34 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 78 IPRIFQAVVQRQPERLALVdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAAL 157
Cdd:cd05936 1 LADLLEEAARRFPDKTALI--FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 158 LNVNLRREPLAFCLGTSGAKALIfggemvaavaevsghlgkSLIKFCSgdlgpegilpdthlldpLLKEASTAPLAQIPS 237
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALI------------------VAVSFTD-----------------LLAAGAPLGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 238 KgmDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMAAFGHHAYRMQaaDVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL 313
Cdd:cd05936 124 P--EDVAVLQYTSGTTGVPKGAMLTHrnlvANALQIKAWLEDLLEGD--DVVLAALPLFHVFGLTVALLLPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 314 RKKFSASRFWDDCIKYNCTI-NGVRhcrllclvVQYIGeicryLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERF 390
Cdd:cd05936 200 IPRFRPIGVLKEIRKHRVTIfPGVP--------TMYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 391 GVRqIGEFYGATECNCSIA-N-MDG--KVGSCGFnsrILPHVYpirlVKVnedtmellRDAQGLCIPCqaGEPGLLVgqi 466
Cdd:cd05936 267 GVP-IVEGYGLTETSPVVAvNpLDGprKPGSIGI---PLPGTE----VKI--------VDDDGEELPP--GEVGELW--- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 467 nqqdpLR---RFDGYVS-ESATSKkiahsVFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSR 542
Cdd:cd05936 326 -----VRgpqVMKGYWNrPEETAE-----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYE 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 543 LLGQTDVAVYGVAVP--GVEGKAgmAAVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLQ 617
Cdd:cd05936 394 HPAVAEAAVVGVPDPysGEAVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPrqvEFRDELPK-SAVG--KILRRELR 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
69-621 |
2.57e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 152.01 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 69 RRHQRAG-HTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLG 147
Cdd:PRK08316 3 ERSTRARrQTIGDILRRSARRYPDKTALVFGD--RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 148 LAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVA---AVAEVSGHLGKSLIKFCSGDLGPEGILPdthLLDPLL 224
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPtaeAALALLPVDTLILSLVLGGREAPGGWLD---FADWAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 225 KEASTAPLAQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSryyrmaAFGH------HAYRMQAADVLYDCLPLYHSAGNI 298
Cdd:PRK08316 158 AGSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHR------ALIAeyvsciVAGDMSADDIPLHALPLYHCAQLD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 299 IGVGQCLIYGLTVVLRKKFSASRFWDdcikyncTINGVRHCRLLCLVVQYIGeicryLLKQPVREaerrhRVRLAvgnGL 378
Cdd:PRK08316 229 VFLGPYLYVGATNVILDAPDPELILR-------TIEAERITSFFAPPTVWIS-----LLRHPDFD-----TRDLS---SL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 379 RPA----------IWEEFTERFGVRQIGEFYGATEcncsIA---------NMDGKVGSCG---FN--SRILphvypirlv 434
Cdd:PRK08316 289 RKGyygasimpveVLKELRERLPGLRFYNCYGQTE----IAplatvlgpeEHLRRPGSAGrpvLNveTRVV--------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 435 kvnedtmellrDAQGLCIPcqAGEPGLLVGQINQQdplrrFDGYV-SESATSKKIAHSVFSkgdsaylSGDVLVMDELGY 513
Cdd:PRK08316 356 -----------DDDGNDVA--PGEVGEIVHRSPQL-----MLGYWdDPEKTAEAFRGGWFH-------SGDLGVMDEEGY 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 514 MYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV-------AVPGVegkagmaAVADPHSLLDPNAIYQELQK 586
Cdd:PRK08316 411 ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLpdpkwieAVTAV-------VVPKAGATVTEDELIAHCRA 483
|
570 580 590
....*....|....*....|....*....|....*...
gi 768002382 587 VLAPYARP---IFLRLLPQvDTTGtfKIQKTRLqREGF 621
Cdd:PRK08316 484 RLAGFKVPkrvIFVDELPR-NPSG--KILKREL-RERY 517
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
81-613 |
1.03e-37 |
|
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: 147.64 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 81 IFQAVVQRQPERLALV---DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAAL 157
Cdd:cd05970 22 VVDAMAKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 158 LNVNLRREPLAFCLGTSGAKALIFGGE--MVAAVAEVSGHLGKSLIKFCSGDLGPEGILPdthlLDPLLKEAS---TAPL 232
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWVGDPVPEGWID----FRKLIKNASpdfERPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 233 AQIPSKGMDDRLFYiYTSGTTGLPKaaIVVHSRYYRMaafGHHAYRMQAADVLYDCLplyHSAGNIIGVGQCL---IYG- 308
Cdd:cd05970 178 ANSYPCGEDILLVY-FSSGTTGMPK--MVEHDFTYPL---GHIVTAKYWQNVREGGL---HLTVADTGWGKAVwgkIYGq 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 309 ------LTVVLRKKFSASRFWDDCIKYNCTIngvrhcrlLCLVVQyigeICRYLLKQPVRE---AERRHRVrlAVGNGLR 379
Cdd:cd05970 249 wiagaaVFVYDYDKFDPKALLEKLSKYGVTT--------FCAPPT----IYRFLIREDLSRydlSSLRYCT--TAGEALN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 380 PAIWEEFTERFGVrQIGEFYGATECNCSIAN---MDGKVGSCGfnsRILPHvYPIRLVKVNEDtmellrdaqglciPCQA 456
Cdd:cd05970 315 PEVFNTFKEKTGI-KLMEGFGQTETTLTIATfpwMEPKPGSMG---KPAPG-YEIDLIDREGR-------------SCEA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 457 GEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEV 536
Cdd:cd05970 377 GEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWH------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 537 EGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVADPHSLLDPNAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQ 612
Cdd:cd05970 451 ESALIQHPAVLECAVTGVPDP-IRGQVVKATIVLAKGYEPSEELKKELQdhvkKVTAPYKYPRIVEFVDELPKTISGKIR 529
|
.
gi 768002382 613 K 613
Cdd:cd05970 530 R 530
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
90-616 |
3.27e-37 |
|
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: 145.53 E-value: 3.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIkfcsgDLGPEGILPDTHLLD---PLLKEASTAPLAQIPSKGMDDRLFy 246
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAIL-----ELALDVGVLIRAPSAeslSNLLADKKNAKSEGVPLPDDLALI- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 247 IYTSGTTGLPKAAIVVHSryyRMAAFGHH---AYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFW 323
Cdd:cd05926 155 LHTSGTTGRPKGVPLTHR---NLAASATNitnTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 324 DDCIKYNCTINGVrhcrllclvvqyIGEICRYLLKQPVREAERRH---RVRLAVGNGLRPAIWEEFTERFGVRQIgEFYG 400
Cdd:cd05926 232 PDVRDYNATWYTA------------VPTIHQILLNRPEPNPESPPpklRFIRSCSASLPPAVLEALEATFGAPVL-EAYG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 401 ATE------CNCSIANMDgKVGSCGfnsriLPHVYPIRLvkVNEDtmellrdaqGLciPCQAGEpgllVGQINQQDPlRR 474
Cdd:cd05926 299 MTEaahqmtSNPLPPGPR-KPGSVG-----KPVGVEVRI--LDED---------GE--ILPPGV----VGEICLRGP-NV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 475 FDGYVSESATSKKIAhsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 554
Cdd:cd05926 355 TRGYLNNPEANAEAA-----FKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGV 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 555 AVPgVEGKA-GMAAVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRL 616
Cdd:cd05926 430 PDE-KYGEEvAAAVVLREGASVTEEELRAFCRKHLAAFKVPkkvYFVDELPK---TATGKIQRRKV 491
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
104-616 |
2.59e-36 |
|
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: 141.32 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGG 183
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 184 EmvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmdDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05972 81 E---------------------------------------------------------DPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 264 SryyrmAAFGHHAYR-----MQAADVLY---DCLPLYHSAGNIIGVgqcLIYGLTVVL--RKKFSASRFWDDCIKYNCTI 333
Cdd:cd05972 104 S-----YPLGHIPTAaywlgLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 334 ngvrhcrLLCLVVQYigeicRYLLKQPVrEAERRHRVRLAVGNG--LRPAIWEEFTERFGVrQIGEFYGATECNCSIAN- 410
Cdd:cd05972 176 -------FCGPPTAY-----RMLIKQDL-SSYKFSHLRLVVSAGepLNPEVIEWWRAATGL-PIRDGYGQTETGLTVGNf 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 411 --MDGKVGSCGfnsrilphvYPIRLVKVnedtmELLRDAQGLCIPcqaGEPGLLVGQINqqdPLRRFDGYVS-ESATSKK 487
Cdd:cd05972 242 pdMPVKPGSMG---------RPTPGYDV-----AIIDDDGRELPP---GEEGDIAIKLP---PPGLFLGYVGdPEKTEAS 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 488 IahsvfskGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAA 567
Cdd:cd05972 302 I-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVKAF 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 768002382 568 VADPHSLLDPNAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd05972 374 VVLTSGYEPSEELAEELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
105-617 |
1.84e-31 |
|
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: 127.58 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 185 MVAavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmddrlFYIYTSGTTGLPKAAIVVHS 264
Cdd:cd05919 92 DIA---------------------------------------------------------YLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 265 RYYRMA-AFGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIYGL----TVVLrkkFSASRFWDdcikyNCTINGVRHC 339
Cdd:cd05919 115 DPLLFAdAMAREALGLTPGDRVFSSAKMFFG----YGLGNSLWFPLavgaSAVL---NPGWPTAE-----RVLATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 340 RLlclVVQYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVrQIGEFYGATEC-NCSIANMDGKV- 415
Cdd:cd05919 183 PT---VLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGG-PILDGIGATEVgHIFLSNRPGAWr 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 416 -GSCGfnsRILPHvYPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLVGQINQQDPlrrfdGYVSESATSKKiahsvfS 494
Cdd:cd05919 259 lGSTG---RPVPG-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWNNPEKSRA------T 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 495 KGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAAVADPHSL 574
Cdd:cd05919 311 FNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAFVVLKSP 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 768002382 575 LDPN-----AIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 617
Cdd:cd05919 389 AAPQeslarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
90-616 |
2.26e-31 |
|
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: 128.26 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDaGTGECWtFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd05959 18 GDKTAFID-DAGSLT-YAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIFGGEMVAAVAEVSG---HLGKSLIKfcSGDLGPEGILPD-THLLD---PLLKEASTAPlaqipskgmDD 242
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAALTkseHTLVVLIV--SGGAGPEAGALLlAELVAaeaEQLKPAATHA---------DD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 243 RLFYIYTSGTTGLPKAAIVVHSRYYRMA-AFGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIY----GLTVVLRKKF 317
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFA----YGLGNSLTFplsvGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 318 -SASRFWDdcikyncTINGVRHCRLLCLVVQYIGeicryLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVrQ 394
Cdd:cd05959 241 pTPAAVFK-------RIRRYRPTVFFGVPTLYAA-----MLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-D 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 395 IGEFYGATEC-NCSIANMDGKV--GSCGfnsRILPHvYPIRLVkvNEDTMELlrdaqglcipcQAGEPGLL--------V 463
Cdd:cd05959 308 ILDGIGSTEMlHIFLSNRPGRVryGTTG---KPVPG-YEVELR--DEDGGDV-----------ADGEPGELyvrgpssaT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 464 GQINQQDPLRR-FDGYvsesatskkiahsvfskgdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLsr 542
Cdd:cd05959 371 MYWNNRDKTRDtFQGE--------------------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL-- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 543 llgQTDVAVYGVAVPGVEGKAGM---AAVADPHSLLDPNAIYQE-----LQKVLAPYARP---IFLRLLPQvdtTGTFKI 611
Cdd:cd05959 429 ---VQHPAVLEAAVVGVEDEDGLtkpKAFVVLRPGYEDSEALEEelkefVKDRLAPYKYPrwiVFVDELPK---TATGKI 502
|
....*
gi 768002382 612 QKTRL 616
Cdd:cd05959 503 QRFKL 507
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
42-605 |
8.02e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 127.35 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 42 RFLRIVCKTARRDLFGLSVLIRVRLELRRHQRAGhtipRIFQAVVQRQPERLALVD-AGTgecWTFAQLDAYSNAVANLF 120
Cdd:PRK07788 19 HYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFA----GLVAHAARRAPDRAALIDeRGT---LTYAELDEQSNALARGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 121 RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSL 200
Cdd:PRK07788 92 LALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 201 IKFCSGDLGPEGIlPDTHLLDPLLKEASTAPLAQIPSKGMddrlFYIYTSGTTGLPKAAivVHSRYYRMAAFGHHAYRM- 279
Cdd:PRK07788 172 AWGGNPDDDEPSG-STDETLDDLIAGSSTAPLPKPPKPGG----IVILTSGTTGTPKGA--PRPEPSPLAPLAGLLSRVp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 280 -QAADVLYDCLPLYHSagniIGVGQCLI---YGLTVVLRKKFSASRFWDDCIKYNCTIngvrhcrllcLVVQYIgeicry 355
Cdd:PRK07788 245 fRAGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEATLEDIAKHKATA----------LVVVPV------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 356 LLKQPVREAE--------RRHRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATECN-CSIANMD------GKVGScgf 420
Cdd:PRK07788 305 MLSRILDLGPevlakydtSSLKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAfATIATPEdlaeapGTVGR--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 421 nsrilphvyPIRLVKVnedtmELLrDAQGLCIPcqAGEPG-LLVGQINQqdplrrFDGYVseSATSKKIAHSVFSKGDSA 499
Cdd:PRK07788 381 ---------PPKGVTV-----KIL-DENGNEVP--RGVVGrIFVGNGFP------FEGYT--DGRDKQIIDGLLSSGDVG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 500 YLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVEGKAGMAA--VADPHSLLDP 577
Cdd:PRK07788 436 YF-------DEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEEFGQRLRAfvVKAPGAALDE 506
|
570 580 590
....*....|....*....|....*....|.
gi 768002382 578 NAIYQELQKVLAPYARP---IFLRLLPQVDT 605
Cdd:PRK07788 507 DAIKDYVRDNLARYKVPrdvVFLDELPRNPT 537
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
99-618 |
9.44e-30 |
|
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: 122.54 E-value: 9.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 99 GTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKA 178
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 179 LIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipSKGMDDRLFYIYTSGTTGLPKA 258
Cdd:cd05971 82 LV--------------------------------------------------------TDGSDDPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 259 AIvvhsryyrmaafghHAYR--MQAADVLYDCLPLYHSAGN----------IIGVGQCLI----YGLTVVLRK--KFSAS 320
Cdd:cd05971 106 AL--------------HAHRvlLGHLPGVQFPFNLFPRDGDlywtpadwawIGGLLDVLLpslyFGVPVLAHRmtKFDPK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 321 RFWDDCIKYnctinGVRHCRLLCLVVQYIGEicryllkqpVREAERRHRVRL-AVGNGLRPAIWEEF---TERFGVrQIG 396
Cdd:cd05971 172 AALDLMSRY-----GVTTAFLPPTALKMMRQ---------QGEQLKHAQVKLrAIATGGESLGEELLgwaREQFGV-EVN 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 397 EFYGATECNCSIAN----MDGKVGSCGfnsRILP-HVYPIrlvkVNEDTMELLRDAQG-LCipcqagepgllvgqINQQD 470
Cdd:cd05971 237 EFYGQTECNLVIGNcsalFPIKPGSMG---KPIPgHRVAI----VDDNGTPLPPGEVGeIA--------------VELPD 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 471 PLrRFDGYV-SESATSKKIAHSVFskgdsayLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDV 549
Cdd:cd05971 296 PV-AFLGYWnNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMA 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768002382 550 AVYGVAVPgVEGKAGMAAVADPHSLLDPNAIYQELQKV----LAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 618
Cdd:cd05971 368 AVVGIPDP-IRGEIVKAFVVLNPGETPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
97-651 |
1.24e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 125.60 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 97 DAGTGECW-------TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNlrrEPLAF 169
Cdd:PRK07868 459 DAPKGEFLlfdgrvhTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPD---TDLAA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIFGGEMVAAVAEVSGH---LGKSLIKFCSGDLGPEGIlpDTHLLDPllkEASTAPLAQIPSKGMDDRLFY 246
Cdd:PRK07868 536 AVRLGGVTEIITDPTNLEAARQLPGRvlvLGGGESRDLDLPDDADVI--DMEKIDP---DAVELPGWYRPNPGLARDLAF 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 247 IYTSGTTGLPKAAIVVHSRYyRMAAFG-HHAYRMQAADVLYdCL-PLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWD 324
Cdd:PRK07868 611 IAFSTAGGELVAKQITNYRW-ALSAFGtASAAALDRRDTVY-CLtPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQ 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 325 DCIKYNCTingvrhcrllclVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATEC 404
Cdd:PRK07868 689 EVRQYGVT------------VVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDG 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 405 NCSIANMDG-KVGSCGfnsRILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGqinqqdplrRFDGYVSESA 483
Cdd:PRK07868 757 QAVLANVSGaKIGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLA---------RARGPIDPTA 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 484 TSKKiahSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRlLGQTDVAV-YGVAVPGVEgk 562
Cdd:PRK07868 825 SVKR---GVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGR-IGGVDLAVtYGVEVGGRQ-- 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 563 AGMAAVA-DPHSLLDPNAIYQELQKvLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFdPRqTSDRLFFLDLKQGHYL 641
Cdd:PRK07868 899 LAVAAVTlRPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PK-PGRQAWYFDPETNRYR 975
|
570
....*....|
gi 768002382 642 PLNEAVYTRI 651
Cdd:PRK07868 976 RLTPAVRAEL 985
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
94-627 |
6.94e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 120.78 E-value: 6.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 94 ALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGT 173
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 174 SGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPdthlLDPLLKEASTAPLA-QIPSKGMddrlfyIYTSGT 252
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRS----YEEALAAQPDTPIAdETAGADM------LYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 253 TGLPKA------AIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGvGQCLIYGLTVVLRKKFSASRFWDDC 326
Cdd:PRK08276 152 TGRPKGikrplpGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFG-MSALALGGTVVVMEKFDAEEALALI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 327 IKYNCTingvrhcrllclVVQYIGEICRYLLKQPvreAERRHR-----VRLAVGNG--LRPAIWEEFTERFGvRQIGEFY 399
Cdd:PRK08276 231 ERYRVT------------HSQLVPTMFVRMLKLP---EEVRARydvssLRVAIHAAapCPVEVKRAMIDWWG-PIIHEYY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 400 GATECN----CSIANMDGKVGSCGfnsriLPHVYPIRLVkvnedtmellrDAQGlcIPCQAGEPGLLVGQINQQDplrrF 475
Cdd:PRK08276 295 ASSEGGgvtvITSEDWLAHPGSVG-----KAVLGEVRIL-----------DEDG--NELPPGEIGTVYFEMDGYP----F 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 476 DGYVSESATSK-KIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGv 554
Cdd:PRK08276 353 EYHNDPEKTAAaRNPHGWVTVGDVGYL-------DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG- 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 555 aVPGVEGKAGMAAVADPHSLLDPN-AIYQEL----QKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLqREGFDPRQT 626
Cdd:PRK08276 425 -VPDEEMGERVKAVVQPADGADAGdALAAELiawlRGRLAHYKCPrsiDFEDELPR-TPTG--KLYKRRL-RDRYWEGRQ 499
|
.
gi 768002382 627 S 627
Cdd:PRK08276 500 R 500
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
86-619 |
1.50e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 119.68 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:PRK03640 12 AFLTPDRTAIEFEE--KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 PLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkslikfCSGDLGPegiLPDTHLLDPLLKEasTAPLAQIPSkgmddrlf 245
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPG-----------ISVKFAE---LMNGPKEEAEIQE--EFDLDEVAT-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 246 YIYTSGTTGLPKAAivvhsryyrMAAFGHHAYR---------MQAADVLYDCLPLYHSAGNIIGVGQcLIYGLTVVLRKK 316
Cdd:PRK03640 146 IMYTSGTTGKPKGV---------IQTYGNHWWSavgsalnlgLTEDDCWLAAVPIFHISGLSILMRS-VIYGMRVVLVEK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 317 FSASRFWDDCIKYNCTINGvrhcrllclVVQyigeicrYLLKQPVREAERRH-----RVRLAVGNGLRPAIWEEFTER-F 390
Cdd:PRK03640 216 FDAEKINKLLQTGGVTIIS---------VVS-------TMLQRLLERLGEGTypssfRCMLLGGGPAPKPLLEQCKEKgI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 391 GVRQIgefYGATECNCSIANMD-----GKVGSCG---FNSRIlphvypirlvKVNEDTMEllrdaqglCIPCQAGE---- 458
Cdd:PRK03640 280 PVYQS---YGMTETASQIVTLSpedalTKLGSAGkplFPCEL----------KIEKDGVV--------VPPFEEGEivvk 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 459 -PGLLVGQINQqdplrrfdgyvsESATSKKIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVE 537
Cdd:PRK03640 339 gPNVTKGYLNR------------EDATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 538 GVLSRLLGQTDVAVYGVAvpgvEGKAGMAAVAD--PHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQ 612
Cdd:PRK03640 400 EVLLSHPGVAEAGVVGVP----DDKWGQVPVAFvvKSGEVTEEELRHFCEEKLAKYKVPkrfYFVEELPR---NASGKLL 472
|
....*..
gi 768002382 613 KTRLQRE 619
Cdd:PRK03640 473 RHELKQL 479
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
86-555 |
5.16e-28 |
|
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: 118.00 E-value: 5.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:cd05923 11 ASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 PLAFClgtsgakalIFGGEMVAAVAEVsGHLGKSLIKFCSGDLGPEGILPDTHLLDpllkeaSTAPLAQIPSKGMDDRLF 245
Cdd:cd05923 91 ELAEL---------IERGEMTAAVIAV-DAQVMDAIFQSGVRVLALSDLVGLGEPE------SAGPLIEDPPREPEQPAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 246 YIYTSGTTGLPKAAIVVH-SRYYRMAAFGHHA-YRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRfw 323
Cdd:cd05923 155 VFYTSGTTGLPKGAVIPQrAAESRVLFMSTQAgLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPAD-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 324 ddcikyncTINGVRHCRLLCL--VVQYIGEICRYLLKQPVREAERRHrVRLAvGNGLRPAIWEEFTERFGVRQIgEFYGA 401
Cdd:cd05923 233 --------ALKLIEQERVTSLfaTPTHLDALAAAAEFAGLKLSSLRH-VTFA-GATMPDAVLERVNQHLPGEKV-NIYGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 402 TECNCSIANMDGKVGSC---GFNSRilphvypIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDplrrfdgy 478
Cdd:cd05923 302 TEAMNSLYMRDARTGTEmrpGFFSE-------VRIVRIGGSPDEALANGEEGELIVAAAADAAFTGYLNQPE-------- 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 479 vsesATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVA 555
Cdd:cd05923 367 ----ATAKKLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
88-618 |
1.99e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 117.75 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 88 RQPERLAL---VDAG---TGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeAALLNVN 161
Cdd:PRK07529 37 RHPDAPALsflLDADpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI-ANPINPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 162 LRREPLAFCLGTSGAKALI-----FGGEMVAAVAEVSGHL--GKSLIKFCSGDLGPegilPDTHLLDPLLKEASTAP--- 231
Cdd:PRK07529 116 LEPEQIAELLRAAGAKVLVtlgpfPGTDIWQKVAEVLAALpeLRTVVEVDLARYLP----GPKRLAVPLIRRKAHARild 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 232 -LAQIpSKGMDDRLF------------YIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNI 298
Cdd:PRK07529 192 fDAEL-ARQPGDRLFsgrpigpddvaaYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 299 IGVGQCLIYGLTVVL------RKKFSASRFWDDCIKYNCTIngvrhcrllclvvqYIGEICRY--LLKQPVrEAERRHRV 370
Cdd:PRK07529 271 VTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINF--------------LSGVPTVYaaLLQVPV-DGHDISSL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 371 RLAVGNG--LRPAIWEEFTERFGVRqIGEFYGATECNC--SIANMDG--KVGSCGFNsriLPHVYpIRLVKVNEDTmELL 444
Cdd:PRK07529 336 RYALCGAapLPVEVFRRFEAATGVR-IVEGYGLTEATCvsSVNPPDGerRIGSVGLR---LPYQR-VRVVILDDAG-RYL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 445 RDaqglcipCQAGEPGLLVgqinQQDPlRRFDGYVSEsatskkiAHSVFSKGDSAYL-SGDVLVMDELGYMYFRDRSGDT 523
Cdd:PRK07529 410 RD-------CAVDEVGVLC----IAGP-NVFSGYLEA-------AHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 524 FRWRGENVSTTEVEGVLSRLLGQTDVAVYG--------VAVPGVEGKAGmaAVADPHSLLDPNAiyqelQKVLAPYARPI 595
Cdd:PRK07529 471 IIRGGHNIDPAAIEEALLRHPAVALAAAVGrpdahageLPVAYVQLKPG--ASATEAELLAFAR-----DHIAERAAVPK 543
|
570 580
....*....|....*....|...
gi 768002382 596 FLRLLPQVDTTGTFKIQKTRLQR 618
Cdd:PRK07529 544 HVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
90-621 |
2.36e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 116.13 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALvDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:PRK07514 16 RDAPFI-ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKfcsgDLGPEGIlpdthllDPLLKEASTAPLAQIP-SKGMDDRLFYIY 248
Cdd:PRK07514 95 FIGDAEPALVVCDPANFAWLSKIAAAAGAPHVE----TLDADGT-------GSLLEAAAAAPDDFETvPRGADDLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 249 TSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRfwddcik 328
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDA------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 329 yncTINGVRHCRLLCLVVQYigeicrY--LLKQPV--REAERrhRVRLAVgNGLRPAIWE---EFTERFGVRqIGEFYGA 401
Cdd:PRK07514 237 ---VLALMPRATVMMGVPTF------YtrLLQEPRltREAAA--HMRLFI-SGSAPLLAEthrEFQERTGHA-ILERYGM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 402 TECNCSIAN-MDGK--VGSCGFNsriLPHVyPIRLvkVNEDTMEllrdaqglciPCQAGEpgllVGQINQQDPlRRFDGY 478
Cdd:PRK07514 304 TETNMNTSNpYDGErrAGTVGFP---LPGV-SLRV--TDPETGA----------ELPPGE----IGMIEVKGP-NVFKGY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 479 --VSEsatskKIAHSVfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAV 556
Cdd:PRK07514 363 wrMPE-----KTAEEF--RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPH 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 557 PGVeGKAGMAA-VADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLqREGF 621
Cdd:PRK07514 436 PDF-GEGVTAVvVPKPGAALDEAAILAALKGRLARFKQPkrvFFVDELPR-NTMG--KVQKNLL-REQY 499
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
86-584 |
2.92e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 115.94 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 PLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFcsgDLGPEGILPDTHLLDPLLKEASTAPLAQiPSKGMDdrlf 245
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEAVAGLPATPIAD-ESLGTD---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 246 YIYTSGTTGLPKAAivvhsryYR------------MAAFGHHAYRMQAADVLYDCLPLYHSA-GNIIGVGQCLiyGLTVV 312
Cdd:PRK13391 159 MLYSSGTTGRPKGI-------KRplpeqppdtplpLTAFLQRLWGFRSDMVYLSPAPLYHSApQRAVMLVIRL--GGTVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 313 LRKKFSASRFWDDCIKYnctinGVRHcrllclvVQYIGEICRYLLKQPvREAERRHRVrlavgNGLRPAIW--------- 383
Cdd:PRK13391 230 VMEHFDAEQYLALIEEY-----GVTH-------TQLVPTMFSRMLKLP-EEVRDKYDL-----SSLEVAIHaaapcppqv 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 384 -EEFTERFGvRQIGEFYGATECNcsianmdgkvGSCGFNSR-ILPHvyPIRLVKVNEDTMELLRDAQGlciPCQAGEPgl 461
Cdd:PRK13391 292 kEQMIDWWG-PIIHEYYAATEGL----------GFTACDSEeWLAH--PGTVGRAMFGDLHILDDDGA---ELPPGEP-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 462 lvGQI--NQQDPLRRF-DGYVSESATSkkiAHSVFSKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEG 538
Cdd:PRK13391 354 --GTIwfEGGRPFEYLnDPAKTAEARH---PDGTWST------VGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAEN 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 768002382 539 VLSRLLGQTDVAVYGvaVPGVEGKAGMAAVADPHSLLDPN-AIYQEL 584
Cdd:PRK13391 423 LLITHPKVADAAVFG--VPNEDLGEEVKAVVQPVDGVDPGpALAAEL 467
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
90-618 |
6.58e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.96 E-value: 6.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVdaGTGECWTFAQLDAYSNAVANLFR-QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLA 168
Cdd:PRK06839 16 PDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 169 FCLGTSGAKALIFGGEMVAAVAEVSGHLGkslikfcsgdlgpegILPDTHLLDPllKEASTAPLAQIPSKGMDDRLFYIY 248
Cdd:PRK06839 94 FQLKDSGTTVLFVEKTFQNMALSMQKVSY---------------VQRVISITSL--KEIEDRKIDNFVEKNESASFIICY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 249 TSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIK 328
Cdd:PRK06839 157 TSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 329 YNCTingvrhcrllclVVQYIGEICRYLLKQPVREAERRHRVRLAVgNGLRPA---IWEEFTERfGVRqIGEFYGATECN 405
Cdd:PRK06839 237 HKVT------------VVMGVPTIHQALINCSKFETTNLQSVRWFY-NGGAPCpeeLMREFIDR-GFL-FGQGFGMTETS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 406 CS---IANMDG--KVGSCGfnsrilphvypiRLVKVNEdtMELLRDAQGLCIPcqaGEpgllVGQINQQDPLRRFDGYVS 480
Cdd:PRK06839 302 PTvfmLSEEDArrKVGSIG------------KPVLFCD--YELIDENKNKVEV---GE----VGELLIRGPNVMKEYWNR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 481 ESATSKKIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVE 560
Cdd:PRK06839 361 PDATEETIQDGWLCTGDLARV-------DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 561 GKAGMAAVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLQR 618
Cdd:PRK06839 434 EIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPkeiVFLKELPK-NATG--KIQKAQLVN 491
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
82-617 |
1.23e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 114.13 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 82 FQAvvQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:PRK09088 3 FHA--RLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 162 LrreplafclgtsgakalifggemvaAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGMD 241
Cdd:PRK09088 81 L-------------------------SASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAA-FGHHAyRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSAS 320
Cdd:PRK09088 136 RVSLILFTSGTSGQPKGVMLSERNLQQTAHnFGVLG-RVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 321 R----FWDDCIkynctinGVRHcrllclvvqYIG--EICRYLLKQPVREAER-RHRVRLAVGNGLRPAI----WEE---- 385
Cdd:PRK09088 215 RtlgrLGDPAL-------GITH---------YFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHAAEdilgWLDdgip 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 386 FTERFGVRQIGEFYGATeCNCSIanMDGKVGSCGFNSrilPHVYpIRLVkvnedtmellrDAQGLciPCQAGEPG--LLV 463
Cdd:PRK09088 279 MVDGFGMSEAGTVFGMS-VDCDV--IRAKAGAAGIPT---PTVQ-TRVV-----------DDQGN--DCPAGVPGelLLR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 464 GQinqqdplRRFDGYVSESATSKKiahsVFSkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRL 543
Cdd:PRK09088 339 GP-------NLSPGYWRRPQATAR----AFT-GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADH 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002382 544 LGQTDVAVYGVAVPGvEGKAG-MAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 617
Cdd:PRK09088 407 PGIRECAVVGMADAQ-WGEVGyLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
75-619 |
3.01e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 113.33 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 75 GHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGme 154
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 155 AALLNVN--LRREPLAFCLGTSGAKALIF-----GGEMVAAVAEvsghLGKSLIKFCSGDLGPE-----------GILPD 216
Cdd:PRK12583 95 AILVNINpaYRASELEYALGQSGVRWVICadafkTSDYHAMLQE----LLPGLAEGQPGALACErlpelrgvvslAPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 217 THLL--DPLLKEA---STAPLAQI-PSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLP 290
Cdd:PRK12583 171 PGFLawHELQARGetvSREALAERqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 291 LYHSAGNIIGVGQCLIYGLTVVL-RKKFSASRFWDDCIKYNCT-INGVRhcrllclvVQYIGEicrylLKQPVREAERRH 368
Cdd:PRK12583 251 LYHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTaLYGVP--------TMFIAE-----LDHPQRGNFDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 369 RVRLAV--GNGLRPAIWEEFTERFGVRQIGEFYGATECN------CSIANMDGKVGSCGfnsRILPHVYpirlVK-VNED 439
Cdd:PRK12583 318 SLRTGImaGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSpvslqtTAADDLERRVETVG---RTQPHLE----VKvVDPD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 440 TMELLRDAQG-LCIpcqagePGLLVGQINQQDPlrrfdgyvseSATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRD 518
Cdd:PRK12583 391 GATVPRGEIGeLCT------RGYSVMKGYWNNP----------EATAESI------DEDGWMHTGDLATMDEQGYVRIVG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 519 RSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAvpgvEGKAGMAAVA----DPHSLLDPNAIYQELQKVLAPYARP 594
Cdd:PRK12583 449 RSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVP----DEKYGEEIVAwvrlHPGHAASEEELREFCKARIAHFKVP 524
|
570 580
....*....|....*....|....*
gi 768002382 595 IFLRLLPQVDTTGTFKIQKTRLqRE 619
Cdd:PRK12583 525 RYFRFVDEFPMTVTGKVQKFRM-RE 548
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
87-621 |
9.26e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.79 E-value: 9.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 87 QRQPERLALVDAGTGECWtfAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREP 166
Cdd:PRK07786 28 LMQPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 167 LAFCLGTSGAKALIFGG---EMVAAVAEVSGHLGKSLIkfcSGDLGPEGILPdthlLDPLLKEASTA-PLAQIPSkgmDD 242
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAalaPVATAVRDIVPLLSTVVV---AGGSSDDSVLG----YEDLLAEAGPAhAPVDIPN---DS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 243 RLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQ-AADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLR--KKFSA 319
Cdd:PRK07786 176 PALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADiNSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 320 SRFWDdcikyncTINGVRHCRLLCLVVQYIGeICRyllKQPVREAERRHRVrlaVGNGLRPA---IWEEFTERFGVRQIG 396
Cdd:PRK07786 255 GQLLD-------VLEAEKVTGIFLVPAQWQA-VCA---EQQARPRDLALRV---LSWGAAPAsdtLLRQMAATFPEAQIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 397 EFYGATECNCSIANMDG-----KVGSCGfnsRILPHVYpirlVKVNEDTMELLrdAQGlcipcQAGE-----PGLLVGQI 466
Cdd:PRK07786 321 AAFGQTEMSPVTCMLLGedairKLGSVG---KVIPTVA----ARVVDENMNDV--PVG-----EVGEivyraPTLMSGYW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 467 NqqdplrrfdgyvSESATSKKIAHSVFSkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQ 546
Cdd:PRK07786 387 N------------NPEATAEAFAGGWFH-------SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDI 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 547 TDVAVYGVAVPG-VEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLqREGF 621
Cdd:PRK07786 448 VEVAVIGRADEKwGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL-RERY 522
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
59-619 |
9.86e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 111.68 E-value: 9.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 59 SVLIRVRLElrRHQRAGH----TIPRIFQAVVQRQPERLALVD--AGTGEC--WTFAQLDAYSNAVANLFRQLGFAPGDV 130
Cdd:PRK13295 5 AVLLPPRRA--ASIAAGHwhdrTINDDLDACVASCPDKTAVTAvrLGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 131 VAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI----FGG----EMVAAVAEVSGHLGKslIK 202
Cdd:PRK13295 83 VSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVvpktFRGfdhaAMARRLRPELPALRH--VV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 203 FCSGDlGPEGIlpDTHLLDPLLKEASTAP-LAQIPSKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRMAAFGHHAYRMQ- 280
Cdd:PRK13295 161 VVGGD-GADSF--EALLITPAWEQEPDAPaILARLRPGPDDVTQLIYTSGTTGEPKG--VMHTANTLMANIVPYAERLGl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 281 -AADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWD----DCIKYncTINGVRHCRLLCLVVQYIGeicry 355
Cdd:PRK13295 236 gADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTF--TMASTPFLTDLTRAVKESG----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 356 llkQPVreaeRRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEfYGATECNC-----------SIANMDGkvgscgfnsRI 424
Cdd:PRK13295 309 ---RPV----SSLRTFLCAGAPIPGALVERARAALGAKIVSA-WGMTENGAvtltklddpdeRASTTDG---------CP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 425 LPHVyPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLV--GQINqqdplrrFDGYVSESATSKKIAHSVFSKGDSAYLS 502
Cdd:PRK13295 372 LPGV-EVRVV-----------DADGAPLP--AGQIGRLQvrGCSN-------FGGYLKRPQLNGTDADGWFDTGDLARID 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 503 GDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAI-- 580
Cdd:PRK13295 431 AD-------GYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMve 503
|
570 580 590
....*....|....*....|....*....|....*....
gi 768002382 581 YQELQKVLAPYArPIFLRLLPQVDTTGTFKIQKTRLQRE 619
Cdd:PRK13295 504 FLKAQKVAKQYI-PERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
90-616 |
1.17e-25 |
|
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: 110.31 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNLR--REPL 167
Cdd:cd05930 1 PDAVAVVDGD--QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAG--AAYVPLDPSypAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 168 AFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeasTAPlaqipskgmdDRLFY- 246
Cdd:cd05930 77 AYILEDSGAKLVL------------------------------------------------TDP----------DDLAYv 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYdclpLYHSAGNIIGVGQ---CLIYGLTVVLRKK---FSAS 320
Cdd:cd05930 99 IYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVL----QFTSFSFDVSVWEifgALLAGATLVVLPEevrKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 321 RFWDDCIKYNCTingvrhcrLLCLVVQYIgeicRYLLKQPvrEAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIGEF 398
Cdd:cd05930 175 ALADLLAEEGIT--------VLHLTPSLL----RLLLQEL--ELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 399 YGATEcnCSIANMDGKVGSCGFNSRILPHVYPIRLVKVnedtmeLLRDAQGLCIPcqAGEPG-LLVG--QINQqdplrrf 475
Cdd:cd05930 241 YGPTE--ATVDATYYRVPPDDEEDGRVPIGRPIPNTRV------YVLDENLRPVP--PGVPGeLYIGgaGLAR------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 476 dGYV-SESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygV 554
Cdd:cd05930 304 -GYLnRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV--V 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768002382 555 AVPGVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd05930 381 AREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-611 |
7.94e-25 |
|
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: 108.59 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 82 FQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:cd17651 1 FERQAARTPDAPALVAEGR--RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 162 LRREPLAFCLGTSGAKAlifggemVAAVAEVsghlgkslikfcSGDLGPEGILPdthLLDPLLKEASTAPLAQIPSKGMD 241
Cdd:cd17651 79 YPAERLAFMLADAGPVL-------VLTHPAL------------AGELAVELVAV---TLLDQPGAAAGADAEPDPALDAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVHSR-----YYRMAAFGHHAYR--MQAADVLYDClplyhSAGNIIGVgqcLIYGLTVVLR 314
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPHRSlanlvAWQARASSLGPGArtLQFAGLGFDV-----SVQEIFST---LCAGATLVLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 315 K---KFSASRFWDDCIKYnctinGVRHCRLLCLVVQYIGEICRyllKQPVREAERRHRV----RLAVGNGLRpaiweEFT 387
Cdd:cd17651 209 PeevRTDPPALAAWLDEQ-----RISRVFLPTVALRALAEHGR---PLGVRLAALRYLLtggeQLVLTEDLR-----EFC 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 388 ERFGVRQIGEFYGATEcncsiaNMDGKVGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQglciPCQAGEPG-LLVGqi 466
Cdd:cd17651 276 AGLPGLRLHNHYGPTE------THVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALR----PVPPGVPGeLYIG-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 467 nqQDPLRRfdGYVSESA-TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLG 545
Cdd:cd17651 344 --GAGLAR--GYLNRPElTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPG 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768002382 546 QTDVAVygVAVPGVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKI 611
Cdd:cd17651 420 VREAVV--LAREDRPGEKRLVAyvVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
86-593 |
1.07e-24 |
|
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: 108.09 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN-VNLRR 164
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 165 EpLAFCLGTSGAKaLIFggeMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPllkeaSTAPLAQIPSkgmDDRL 244
Cdd:cd05904 95 E-IAKQVKDSGAK-LAF---TTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADE-----AEPPVVVIKQ---DDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 245 FYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAA--DVLYDCLPLYHSAG-NIIGVGQcLIYGLTVVLRKKFSASR 321
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDseDVFLCVLPMFHIYGlSSFALGL-LRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 322 FWDDCIKYNCTIngvrhcrLLC---LVVQyigeicryLLKQPVREAERRHRVRlAVGNG---LRPAIWEEFTERFGVRQI 395
Cdd:cd05904 241 LLAAIERYKVTH-------LPVvppIVLA--------LVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 396 GEFYGATECNCSIANMD------GKVGSCGfnsRILPHVYpirlVK-VNEDTMELLRdaqglciPCQAGE-----PGLLV 463
Cdd:cd05904 305 GQGYGMTESTGVVAMCFapekdrAKYGSVG---RLVPNVE----AKiVDPETGESLP-------PNQTGElwirgPSIMK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 464 GQINqqdplrrfdgyvSESATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRL 543
Cdd:cd05904 371 GYLN------------NPEATAATI------DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSH 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 768002382 544 LGQTDVAVygVAVPGVE-GKAGMA-AVADPHSLLDPNAIYQELQKVLAPYAR 593
Cdd:cd05904 433 PEILDAAV--IPYPDEEaGEVPMAfVVRKPGSSLTEDEIMDFVAKQVAPYKK 482
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
87-617 |
1.52e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 108.20 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 87 QRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREP 166
Cdd:PRK06178 44 RERPQRPAIIFYGH--VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 167 LAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCS-GDLGPEGI---LPDTHLLDPLLKE----------ASTAPl 232
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSlADVLPAEPtlpLPDSLRAPRLAAAgaidllpalrACTAP- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 233 AQIPSKGMDDRLFYIYTSGTTGLPKAaiVVHSR---YYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGL 309
Cdd:PRK06178 201 VPLPPPALDALAALNYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 310 TVVLRKKFSASRFWDDCIKYNCTINGvrhcrllcLVVQYIGEICRY---------LLKQP-----VRE--AERRHRVRLA 373
Cdd:PRK06178 279 TLVLLARWDAVAFMAAVERYRVTRTV--------MLVDNAVELMDHprfaeydlsSLRQVrvvsfVKKlnPDYRQRWRAL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 374 VGNGLRPAIW--------EEFTERFgvrQIGEFygatecncsiaNMDGKVGSCGfnsriLPhVYPIRLVKVNEDTMELLr 445
Cdd:PRK06178 351 TGSVLAEAAWgmtethtcDTFTAGF---QDDDF-----------DLLSQPVFVG-----LP-VPGTEFKICDFETGELL- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 446 daqglciPC-QAGE-----PGLLVGQINQQDplrrfdgyvsesATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDR 519
Cdd:PRK06178 410 -------PLgAEGEivvrtPSLLKGYWNKPE------------ATAEALR-------DGWLHTGDIGKIDEQGFLHYLGR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 520 SGDTFRWRGENVSTTEVEGvlsrLLGQTDvAVYGVAVPGV--EGKaGMAAVA----DPHSLLDPNAIYQELQKVLAPYAR 593
Cdd:PRK06178 464 RKEMLKVNGMSVFPSEVEA----LLGQHP-AVLGSAVVGRpdPDK-GQVPVAfvqlKPGADLTAAALQAWCRENMAVYKV 537
|
570 580
....*....|....*....|....
gi 768002382 594 PIfLRLLPQVDTTGTFKIQKTRLQ 617
Cdd:PRK06178 538 PE-IRIVDALPMTATGKVRKQDLQ 560
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-616 |
1.58e-24 |
|
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: 106.99 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 91 ERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGF-APGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd05941 1 DRIAIVDDG--DSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmdDRLFYIYT 249
Cdd:cd05941 79 VITDSEPSLVL-------------------------------------------------------------DPALILYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 250 SGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKY 329
Cdd:cd05941 98 SGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 330 NCTI-NGVR--HCRLLclvvQYigeicrYLLKQPVREAERR---HRVRLAV-GNG-LRPAIWEEFTERFGVRqIGEFYGA 401
Cdd:cd05941 178 SITVfMGVPtiYTRLL----QY------YEAHFTDPQFARAaaaERLRLMVsGSAaLPVPTLEEWEAITGHT-LLERYGM 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 402 TECNCSIAN-MDG--KVGSCGFNsriLPHVyPIRLVKvNEDTMELLRDAQG-LCIpcqAGePGLlvgqinqqdplrrFDG 477
Cdd:cd05941 247 TEIGMALSNpLDGerRPGTVGMP---LPGV-QARIVD-EETGEPLPRGEVGeIQV---RG-PSV-------------FKE 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 478 YVSE-SATSKKIAhsvfskGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVA 555
Cdd:cd05941 305 YWNKpEATKEEFT------DDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVP 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768002382 556 VPgVEGKAGMAAVA--DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd05941 379 DP-DWGERVVAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
76-324 |
1.81e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 107.66 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 76 HTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeA 155
Cdd:PRK07798 3 WNIADLFEAVADAVPDRVALVCGD--RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 156 ALLNVNLR--REPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLA 233
Cdd:PRK07798 79 VPVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 234 QIPSKgmDDrLFYIYTSGTTGLPKAAIVVHSRYYRmAAFG--------------HHAYRMQAAD--VLYDCLPLYHSAGn 297
Cdd:PRK07798 159 GERSP--DD-LYLLYTGGTTGMPKGVMWRQEDIFR-VLLGgrdfatgepiedeeELAKRAAAGPgmRRFPAPPLMHGAG- 233
|
250 260
....*....|....*....|....*....
gi 768002382 298 IIGVGQCLIYGLTVVL--RKKFSASRFWD 324
Cdd:PRK07798 234 QWAAFAALFSGQTVVLlpDVRFDADEVWR 262
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-311 |
9.70e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 105.95 E-value: 9.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 74 AGHTIPRIFQAVVQRQPERLALV--DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKA 151
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALRekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 152 GmeaaLLNV----NLRREPLAFCLGTSGAKALIFGG-EMVAAVAEVSGHLGkSLIKFCSGDLGPEGILPDTHLLDPLLKE 226
Cdd:COG1022 89 G----AVTVpiypTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELP-SLRHIVVLDPRGLRDDPRLLSLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 227 ASTAPL-----AQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGV 301
Cdd:COG1022 164 GREVADpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSY 243
|
250
....*....|
gi 768002382 302 GqCLIYGLTV 311
Cdd:COG1022 244 Y-ALAAGATV 252
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
80-618 |
1.69e-23 |
|
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: 103.54 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 80 RIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN 159
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLG--GSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 160 VNLRREPLAFCLGTSGAKALIFggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeaSTAPlaqipskg 239
Cdd:cd17653 79 AKLPSARIQAILRTSGATLLLT----------------------------------------------TDSP-------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 240 mDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHayRM---------QAADVLYDClplyhSAGNIIGvgqCLIYGLT 310
Cdd:cd17653 105 -DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPA--RLdvgpgsrvaQVLSIAFDA-----CIGEIFS---TLCNGGT 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 311 VVLRkkfSASRFWDDCIkynctingvRHCRLLCLVVQYIGEIcryllkqPVREAERRHRVRLAvGNGLRPAIWEEFTERf 390
Cdd:cd17653 174 LVLA---DPSDPFAHVA---------RTVDALMSTPSILSTL-------SPQDFPNLKTIFLG-GEAVPPSLLDRWSPG- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 391 gvRQIGEFYGATECNCSIAnmdgkvgscgfNSRILPHV-----YPIRLVKV---NEDTMELLRDAQG-LCIpcqAGePGL 461
Cdd:cd17653 233 --RRLYNAYGPTECTISST-----------MTELLPGQpvtigKPIPNSTCyilDADLQPVPEGVVGeICI---SG-VQV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 462 LVGQINQqdplrrfdgyvsESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLS 541
Cdd:cd17653 296 ARGYLGN------------PALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVL 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 542 RLLGQtdvaVYGVAVPGVEGKagMAAVADPHSlLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 618
Cdd:cd17653 364 QSQPE----VTQAAAIVVNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
85-620 |
1.97e-23 |
|
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: 104.54 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 85 VVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRR 164
Cdd:TIGR02262 14 VVEGRGGKTAFID--DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 165 EPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDlGPEGILPDTHLL---DPLLKEASTAPlaqipskgmD 241
Cdd:TIGR02262 92 DDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLateSEQFKPAATQA---------D 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAA-FGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIY----GLTVVLR-K 315
Cdd:TIGR02262 162 DPAFWLYSSGSTGMPKGVVHTHSNPYWTAElYARNTLGIREDDVCFSAAKLFFA----YGLGNALTFpmsvGATTVLMgE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 316 KFSASRFWDDCIKYNCTIngvrhcrLLCLVVQYIGeicryLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVr 393
Cdd:TIGR02262 238 RPTPDAVFDRLRRHQPTI-------FYGVPTLYAA-----MLADPNLPSEDQVRLRLCTsaGEALPAEVGQRWQARFGV- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 394 QIGEFYGATEC-NCSIANMDGKV--GSCGfnsrilphvypirlVKVNEDTMELLRDAQGlciPCQAGEPGLL-------- 462
Cdd:TIGR02262 305 DIVDGIGSTEMlHIFLSNLPGDVryGTSG--------------KPVPGYRLRLVGDGGQ---DVADGEPGELlisgpssa 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 463 VGQINQQDPLRR-FDGYVSESatskkiahsvfskgdsaylsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLs 541
Cdd:TIGR02262 368 TMYWNNRAKSRDtFQGEWTRS--------------------GDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESAL- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 542 rllgqtdvavygVAVPGVEgKAGMAAVADPHSLLDPNA----------IYQELQK----VLAPYARPIFLRLLPQVDTTG 607
Cdd:TIGR02262 427 ------------IQHPAVL-EAAVVGVADEDGLIKPKAfvvlrpgqtaLETELKEhvkdRLAPYKYPRWIVFVDDLPKTA 493
|
570
....*....|...
gi 768002382 608 TFKIQKTRLqREG 620
Cdd:TIGR02262 494 TGKIQRFKL-REG 505
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
87-593 |
1.21e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 102.01 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 87 QRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLWLGLaKAGMEAALLNVNLRRE 165
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 PLAFCLGTSGAKALIFGGEMVAAVAEVSGHL------GKSLIKFCSGDLGPEGILPdthlldpllkeastaPLAQIPSKG 239
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGADLplrlsfGGEIDGFGSFEAALAGAGP---------------RLTEQPCGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 240 MddrlfYIYTSGTTGLPKA------AIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAgNIIGVGQCLIYGLTVVL 313
Cdd:PRK13390 152 V-----MLYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA-PLRWCSMVHALGGTVVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 314 RKKFSASRFWDDCIKYNCTingvrhcrllclVVQYIGEICRYLLKQpvrEAERRHRVRLAvgnGLRPAIWEEFTERFGVR 393
Cdd:PRK13390 226 AKRFDAQATLGHVERYRIT------------VTQMVPTMFVRLLKL---DADVRTRYDVS---SLRAVIHAAAPCPVDVK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 394 Q---------IGEFYGATECNcSIANMD-----GKVGSCGFNSRILPHVypirlvkVNEDTMELlrdaqglcipcQAGEP 459
Cdd:PRK13390 288 HamidwlgpiVYEYYSSTEAH-GMTFIDspdwlAHPGSVGRSVLGDLHI-------CDDDGNEL-----------PAGRI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 460 GLLVgqiNQQDPLR-RFDGYVSESATSKKIAHSVFSKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEG 538
Cdd:PRK13390 349 GTVY---FERDRLPfRYLNDPEKTAAAQHPAHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETEN 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 539 VLSRLLGQTDVAVYGVAVP--GVEGKAGMAAVADphslLDPNaiyQELQKVLAPYAR 593
Cdd:PRK13390 420 ALTMHPAVHDVAVIGVPDPemGEQVKAVIQLVEG----IRGS---DELARELIDYTR 469
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
86-619 |
5.13e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 100.21 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALVDaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:PRK06087 33 ARAMPDKIAVVD-NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 PLAFCLGTSGAKALIFGG--------EMVAAVAEVSGHLGKSLIkfcSGDLGPEgilpdthLLDPLLKE--ASTAPLAQI 235
Cdd:PRK06087 112 ELVWVLNKCQAKMFFAPTlfkqtrpvDLILPLQNQLPQLQQIVG---VDKLAPA-------TSSLSLSQiiADYEPLTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 236 PSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYrmaaFGHHAY----RMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTV 311
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL----ASERAYcarlNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 312 VLRKKFSAsrfwDDCI----KYNCTingvrhCR---------LLCLVVQYIGEI--CRYLL-------KQPVREAERRHr 369
Cdd:PRK06087 258 VLLDIFTP----DACLalleQQRCT------CMlgatpfiydLLNLLEKQPADLsaLRFFLcggttipKKVARECQQRG- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 370 VRLAvgnglrpaiweefterfgvrqigEFYGATE-CNCSIANMDGKVGSCGFNSRILPHVYPIRLvkVNEDTMELLRDAQ 448
Cdd:PRK06087 327 IKLL-----------------------SVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKV--VDEARKTLPPGCE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 449 GLciPCQAGePGLLVGQINQQDplrrfdgyvsesATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRG 528
Cdd:PRK06087 382 GE--EASRG-PNVFMGYLDEPE------------LTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGG 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 529 ENVSTTEVEGVLSRLLGQTDVAVygVAVP----GvEGKAGMAAVADPH---SLLDPNAIYQElqKVLAPYARPIFLRLLP 601
Cdd:PRK06087 441 ENISSREVEDILLQHPKIHDACV--VAMPderlG-ERSCAYVVLKAPHhslTLEEVVAFFSR--KRVAKYKYPEHIVVID 515
|
570
....*....|....*...
gi 768002382 602 QVDTTGTFKIQKTRLQRE 619
Cdd:PRK06087 516 KLPRTASGKIQKFLLRKD 533
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
105-616 |
6.74e-22 |
|
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: 98.99 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI---- 180
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVvper 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 181 FGGEMVAAvaevsghlgkslikfcsgdlgpegiLPDThlldpllkeastapLAQIpskgmddrlfyIYTSGTTGLPKAai 260
Cdd:cd05903 83 FRQFDPAA-------------------------MPDA--------------VALL-----------LFTSGTTGEPKG-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 261 VVHSRYYRMAAFGHHAYRMQA--ADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSAsrfwDDCIKYnctingVRH 338
Cdd:cd05903 111 VMHSHNTLSASIRQYAERLGLgpGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDP----DKALAL------MRE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 339 CRLLCLV--VQYIGEICRYLLKQPvrEAERRHRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATECNcsianmdGKVG 416
Cdd:cd05903 181 HGVTFMMgaTPFLTDLLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECP-------GAVT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 417 SC---------GFNSRILPHVYpirlVKVNEDTMELLRdaqglciPCQAGE-----PGLLVGQINQQDPLRRFDgyvses 482
Cdd:cd05903 251 SItpapedrrlYTDGRPLPGVE----IKVVDDTGATLA-------PGVEGEllsrgPSVFLGYLDRPDLTADAA------ 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 483 atskkiahsvfskGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPgvEGK 562
Cdd:cd05903 314 -------------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV--VALP--DER 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 563 AGMAAVA-----DPHSL-LDPNAIYQELQKVlAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd05903 377 LGERACAvvvtkSGALLtFDELVAYLDRQGV-AKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
87-619 |
1.02e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 99.19 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 87 QRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNLR--R 164
Cdd:PRK06145 13 RRTPDRAALVYRD--QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLG--AVFLPINYRlaA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 165 EPLAFCLGTSGAKALIFGGEMVAAVAEVSghlgkslikfcsgdlgPEGILPDTHLLDPLLKEASTAPLAQIPSKGMDDRL 244
Cdd:PRK06145 89 DEVAYILGDAGAKLLLVDEEFDAIVALET----------------PKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 245 FYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHsagniigVGQCLIYGLTVVLRKKFSasrfwd 324
Cdd:PRK06145 153 RLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYH-------VGAFDLPGIAVLWVGGTL------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 325 dCIKYN----CTINGVRHCRLLCLVVQYIgeICRYLLKQPVREAERRHRVRLAVGNGLR-PAI-WEEFTERFGVRQIGEF 398
Cdd:PRK06145 220 -RIHREfdpeAVLAAIERHRLTCAWMAPV--MLSRVLTVPDRDRFDLDSLAWCIGGGEKtPESrIRDFTRVFTRARYIDA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 399 YGATECNCSIANMDG-----KVGSCGfnsRILPHVypirlvkvnedTMELLRDAQGLCIPCQAGEPGLLVGQINQqdplr 473
Cdd:PRK06145 297 YGLTETCSGDTLMEAgreieKIGSTG---RALAHV-----------EIRIADGAGRWLPPNMKGEICMRGPKVTK----- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 474 rfdGYVSEsatSKKIAHSVFskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYG 553
Cdd:PRK06145 358 ---GYWKD---PEKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIG 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 554 VAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 619
Cdd:PRK06145 429 VHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
68-563 |
1.09e-21 |
|
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: 99.49 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 68 LRRHQRAGHTiprifQAVVQRQPERlalvdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLG 147
Cdd:cd05968 67 LDKWLADTRT-----RPALRWEGED------GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 148 LAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSghLGKSLIKFCSGDLGPEGILPDTHLLDPLLK-- 225
Cdd:cd05968 136 VARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVN--LKEEADKACAQCPTVEKVVVVRHLGNDFTPak 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 226 -------EASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG-HHAYRMQAADVLYDCLPLYHSAGN 297
Cdd:cd05968 214 grdlsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDmYFQFDLKPGDLLTWFTDLGWMMGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 298 IIGVGQcLIYGLTVVLRKKF----SASRFWDDCIKYNCTINGVRHcrllCLVVQYIGEICRYLlkqpvrEAERRHRVRLA 373
Cdd:cd05968 294 WLIFGG-LILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSP----TLIRALKPRGDAPV------NAHDLSSLRVL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 374 VGNG--LRPAIWEEFTERFGVRQ--IGEFYGATECNCSI--ANMDGKVGSCGFNSrILPHVYPIRLvkvnedtmellrDA 447
Cdd:cd05968 363 GSTGepWNPEPWNWLFETVGKGRnpIINYSGGTEISGGIlgNVLIKPIKPSSFNG-PVPGMKADVL------------DE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 448 QGLCIPCQAGE-------PGLLVGqiNQQDPLRRFDGYvsesatskkiahsvFSKGDSAYLSGDVLVMDELGYMYFRDRS 520
Cdd:cd05968 430 SGKPARPEVGElvllapwPGMTRG--FWRDEDRYLETY--------------WSRFDNVWVHGDFAYYDEEGYFYILGRS 493
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 768002382 521 GDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKA 563
Cdd:cd05968 494 DDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP-VKGEA 535
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
74-404 |
1.13e-21 |
|
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: 100.70 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 74 AGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGm 153
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVFGD--QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 154 eAAL--LNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLgkslikfcsgdlgpegILPDTHLLDPllkEASTAP 231
Cdd:COG1020 551 -AAYvpLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPV----------------LALDALALAA---EPATNP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 232 LAQIPSkgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVlydcLPLYHSAGNIIGVGQ---CLIY 307
Cdd:COG1020 611 PVPVTP----DDLAYvIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDR----VLQFASLSFDASVWEifgALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 308 GLTVVLRKK---FSASRFWDDCIKYNCTIngvrhcrlLCLVVQYIGEICRYLLKQPvreaerrHRVRLAV--GNGLRPAI 382
Cdd:COG1020 683 GATLVLAPPearRDPAALAELLARHRVTV--------LNLTPSLLRALLDAAPEAL-------PSLRLVLvgGEALPPEL 747
|
330 340
....*....|....*....|..
gi 768002382 383 WEEFTERFGVRQIGEFYGATEC 404
Cdd:COG1020 748 VRRWRARLPGARLVNLYGPTET 769
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
86-589 |
1.21e-21 |
|
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: 99.19 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:cd17634 63 LRENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 162 LRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkSLIKFCSGDLGPEGILPDTHLL------------------DPL 223
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGGVRAGRSV------PLKKNVDDALNPNVTSVEHVIVlkrtgsdidwqegrdlwwRDL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 224 LKEAStaPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG-HHAYRMQAADVLYDCLPLYHSAGNIIGVG 302
Cdd:cd17634 217 IAKAS--PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIYWCTADVGWVTGHSYLLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 303 QCLIYGLTVVLRKKF----SASRFWDDCIKYnctinGVRHCRLLCLVVqyigeicRYLLKQPVREAERRHRVRL----AV 374
Cdd:cd17634 295 GPLACGATTLLYEGVpnwpTPARMWQVVDKH-----GVNILYTAPTAI-------RALMAAGDDAIEGTDRSSLrilgSV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 375 GNGLRPAIWEEFTERFGVRQigefygatecnCSIANMDGKVGSCGFNSRILPHVYPIR----LVKVNEDTMELLrDAQGL 450
Cdd:cd17634 363 GEPINPEAYEWYWKKIGKEK-----------CPVVDTWWQTETGGFMITPLPGAIELKagsaTRPVFGVQPAVV-DNEGH 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 451 ciPCQAGEPGLLV------GQINQ--QDPLRRFDGYvsesatskkiahsvFSKGDSAYLSGDVLVMDELGYMYFRDRSGD 522
Cdd:cd17634 431 --PQPGGTEGNLVitdpwpGQTRTlfGDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDD 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 523 TFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVADPHSLLDPNAIYQELQKVLA 589
Cdd:cd17634 495 VINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
104-618 |
2.29e-21 |
|
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: 97.03 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKalifgg 183
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 184 emvaavaevsghlgkslikfcsgdlgpegiLPDTHLLdpllkeastaplaqipskgmddrlfyIYTSGTTGLPKAAIVvh 263
Cdd:cd05912 76 ------------------------------LDDIATI--------------------------MYTSGTTGKPKGVQQ-- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 264 sryyrmaAFGHHAYRMQAADV---LYD------CLPLYHSAGNIIGVGQcLIYGLTVVLRKKFSASRFWDDCIKYNCTIN 334
Cdd:cd05912 98 -------TFGNHWWSAIGSALnlgLTEddnwlcALPLFHISGLSILMRS-VIYGMTVYLVDKFDAEQVLHLINSGKVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 335 GVRHCRLLCLVVQYiGEICRYLLkqpvreaerrhRVRLAVGNGLRPAIWEEFTER-FGVRQIgefYGATE-----CNCSI 408
Cdd:cd05912 170 SVVPTMLQRLLEIL-GEGYPNNL-----------RCILLGGGPAPKPLLEQCKEKgIPVYQS---YGMTEtcsqiVTLSP 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 409 ANMDGKVGSCGfnsRILPHVYpirlvkvnedtmelLRDAQGLCIPCQAGE-----PGLLVGQINQQDplrrfdgyvsesA 483
Cdd:cd05912 235 EDALNKIGSAG---KPLFPVE--------------LKIEDDGQPPYEVGEillkgPNVTKGYLNRPD------------A 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 484 TSKKIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPgvEGKA 563
Cdd:cd05912 286 TEESFENGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV--VGIP--DDKW 354
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 564 GMAAVA--DPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRLQR 618
Cdd:cd05912 355 GQVPVAfvVSERPISEEELIAYCSEKLAKYKVPkkiYFVDELPR---TASGKLLRHELKQ 411
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
72-618 |
3.32e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.52 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 72 QRAGHTIPRIFQAVVQRQPERLALVD-AGTgecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAK 150
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLIDeLGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 151 AGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAevsghlgksliKFCSGDLGPEGILPDTHLLDPLLKEA-ST 229
Cdd:PRK13382 116 IGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVD-----------RALADCPQATRIVAWTDEDHDLTVEVlIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 230 APLAQ-IPSKGMDDRLFyIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAgniiGVGQCLIYG 308
Cdd:PRK13382 185 AHAGQrPEPTGRKGRVI-LLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAW----GFSQLVLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 309 L---TVVLRKKFSASRFWDDCIKYNCTIngvrhcrlLCLVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEE 385
Cdd:PRK13382 260 SlacTIVTRRRFDPEATLDLIDRHRATG--------LAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 386 FTERFGvRQIGEFYGATECN-CSIANMDgkvgscgfNSRILPHVYPirlvKVNEDTMELLRDAQGLCIPcqAGEpgllVG 464
Cdd:PRK13382 332 FMDQFG-DVIYNNYNATEAGmIATATPA--------DLRAAPDTAG----RPAEGTEIRILDQDFREVP--TGE----VG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 465 QINQQDPLrRFDGYVseSATSKKIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLL 544
Cdd:PRK13382 393 TIFVRNDT-QFDGYT--SGSTKDFHDGFMASGDVGYL-------DENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768002382 545 GQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 618
Cdd:PRK13382 463 DVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-594 |
1.43e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 95.72 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 79 PRIF---QAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEA 155
Cdd:PRK05852 16 PRIAdlvEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 156 ALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFcSGDLGPEGILPDTHLLDpllkEASTAPLAQI 235
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNV-GGDSGPSGGTLSVHLDA----ATEPTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 236 PSKGMDDRLFYIYTSGTTGLPKAAIVVHSryyRMAAFGHH---AYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK05852 171 PEGLRPDDAMIMFTGGTTGLPKMVPWTHA---NIASSVRAiitGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 313 L--RKKFSASRFWDDCIKYNCTIngvrhcrllclvVQYIGEICRYLLKQPVREAERRHRVRL----AVGNGLRPAIWEEF 386
Cdd:PRK05852 248 LpaRGRFSAHTFWDDIKAVGATW------------YTAVPTIHQILLERAATEPSGRKPAALrfirSCSAPLTAETAQAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 387 TERFGVRQIgEFYGATECNCSIANMDGKVGSCGFNSRILPHVypirlvkVNEDTMELLRDAQGLCIPCQAGEpgllVGQI 466
Cdd:PRK05852 316 QTEFAAPVV-CAFGMTEATHQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRIVGSDGLPLPAGA----VGEV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 467 NQQDP--LRrfdGYVSESA-TSKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRL 543
Cdd:PRK05852 384 WLRGTtvVR---GYLGDPTiTAANFTDGWLRTGDLGSLSAA-------GDLSIRGRIKELINRGGEKISPERVEGVLASH 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 768002382 544 LGQTDVAVYGVAvPGVEGKAgMAAVADPHSLLDPNA--IYQELQKVLAPYARP 594
Cdd:PRK05852 454 PNVMEAAVFGVP-DQLYGEA-VAAVIVPRESAPPTAeeLVQFCRERLAAFEIP 504
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
75-312 |
1.62e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 95.65 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 75 GHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGme 154
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIG-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 155 AALLNVN--LRREPLAFCLGTSGAKALIFGG--------EMVAAVA-----EVSGHLG-------KSLIKFcsGDLGPEG 212
Cdd:PRK08315 93 AILVTINpaYRLSELEYALNQSGCKALIAADgfkdsdyvAMLYELApelatCEPGQLQsarlpelRRVIFL--GDEKHPG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 213 ILPDTHLLDpLLKEASTAPLAQIPSK-GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPL 291
Cdd:PRK08315 171 MLNFDELLA-LGRAVDDAELAARQATlDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL 249
|
250 260
....*....|....*....|.
gi 768002382 292 YHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK08315 250 YHCFGMVLGNLACVTHGATMV 270
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
106-616 |
2.67e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 94.77 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 106 FAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEM 185
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 186 VAAVAevsGHLGKSlIKFCSGDLGPEGI----LPDTHL--------LDPLLK--EASTAPLAQIPSKgmddrlfYIYTSG 251
Cdd:PRK12406 94 LHGLA---SALPAG-VTVLSVPTPPEIAaayrISPALLtppagaidWEGWLAqqEPYDGPPVPQPQS-------MIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 252 TTGLPK-----AAIVVHSRYY-RMAAfghHAYRMQAADVLYDCLPLYHSAGNIIGVgQCLIYGLTVVLRKKFSASRFWDD 325
Cdd:PRK12406 163 TTGHPKgvrraAPTPEQAAAAeQMRA---LIYGLKPGIRALLTGPLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 326 CIKYNCTingvrhcRLLCLVVQYIgeicrYLLKQPvreAERRHRVRL----AVGNGLRPA---IWEEFTERFG-VrqIGE 397
Cdd:PRK12406 239 IERHRIT-------HMHMVPTMFI-----RLLKLP---EEVRAKYDVsslrHVIHAAAPCpadVKRAMIEWWGpV--IYE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 398 FYGATE------CNCSIA-NMDGKVGscgfnsRILPHVypiRLVKVNEDTMELlrdaqglcipcQAGEPGLLVGQInQQD 470
Cdd:PRK12406 302 YYGSTEsgavtfATSEDAlSHPGTVG------KAAPGA---ELRFVDEDGRPL-----------PQGEIGEIYSRI-AGN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 471 PLRRFDGYVSESATSKKiahsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVA 550
Cdd:PRK12406 361 PDFTYHNKPEKRAEIDR---------GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCA 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768002382 551 VYGvaVPGVE-GKAGMAAV-ADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:PRK12406 432 VFG--IPDAEfGEALMAVVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
99-619 |
2.88e-20 |
|
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: 94.84 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 99 GTGE--CWTFAQLDAYSNAVANLFRQL-GFAPGDVVAIFLEGRPEFvglWLgLAKAGMEAALL----NVNLRREPLAFCL 171
Cdd:cd05928 35 GKGDevKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEW---WL-VNVACIRTGLVfipgTIQLTAKDILYRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 172 GTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPdthlLDPLLKEASTAPLAqIPSKGMDDRLFYiYTSG 251
Cdd:cd05928 111 QASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLN----FKELLNEASTEHHC-VETGSQEPMAIY-FTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 252 TTGLPKAAIVVHSRY-YRMAAFGHHAYRMQAADVLYdCLPLYHSAGNIIG-VGQCLIYGLTVVLRK--KFSASRFWDDCI 327
Cdd:cd05928 185 TTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMW-NTSDTGWIKSAWSsLFEPWIQGACVFVHHlpRFDPLVILKTLS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 328 KYNCTIngvrhcrlLCLVvqyiGEICRYLLKQPVREAERRH-RVRLAVGNGLRPAIWEEFTERFGVrQIGEFYGATECNC 406
Cdd:cd05928 264 SYPITT--------FCGA----PTVYRMLVQQDLSSYKFPSlQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 407 SIANMDG---KVGSCGFNSriLPhvYPIRLVKVNEDTMEllrdaqglciPCQAGEPGLlvgQINQQDPLRRFDGYVSE-S 482
Cdd:cd05928 331 ICANFKGmkiKPGSMGKAS--PP--YDVQIIDDNGNVLP----------PGTEGDIGI---RVKPIRPFGLFSGYVDNpE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 483 ATSKKIahsvfsKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGK 562
Cdd:cd05928 394 KTAATI------RGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGE 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768002382 563 AGMAAV--ADPHSLLDPNAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 619
Cdd:cd05928 466 VVKAFVvlAPQFLSHDPEQLTKELQqhvkSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
113-611 |
3.32e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 94.04 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 113 SNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAlifGGEMVAAVAEV 192
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADA---GGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 193 SGHLGKSLIKFCSGD--LGPEGILPDTHLLDpllkeastaplAQIPSKgmDDRLFYIYTSGTTGLPKAAIVVHsRYYRMA 270
Cdd:cd05922 80 ADRLRDALPASPDPGtvLDADGIRAARASAP-----------AHEVSH--EDLALLLYTSGSTGSPKLVRLSH-QNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 271 AFGHHAY-RMQAADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLRKKFSASR-FWDDCIKYNCT-INGvrhcrllclvVQ 347
Cdd:cd05922 146 ARSIAEYlGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATgLAG----------VP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 348 YIGEICRYLLKQPVREAERRHRVRlaVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDG-----KVGSCGfns 422
Cdd:cd05922 215 STYAMLTRLGFDPAKLPSLRYLTQ--AGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPerileKPGSIG--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 423 RILPhvypirlvkvnEDTMELLRDAQGLCIPcqaGEPGLLVgqinQQDPLRRFDGYVSESATSKKIAhsvfsKGDSAYlS 502
Cdd:cd05922 290 LAIP-----------GGEFEILDDDGTPTPP---GEPGEIV----HRGPNVMKGYWNDPPYRRKEGR-----GGGVLH-T 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 503 GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEgkaGMAAVADPHSLLDPNAIYQ 582
Cdd:cd05922 346 GDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPDKIDPKDVLR 422
|
490 500
....*....|....*....|....*....
gi 768002382 583 ELQKVLAPYARPIFLRLLPQVDTTGTFKI 611
Cdd:cd05922 423 SLAERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
87-624 |
6.14e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 93.57 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 87 QRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLWlglAKAGMEAALLNVNLRRE 165
Cdd:PRK07470 18 RRFPDRIALVWGD--RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMF---AAFRLGAVWVPTNFRQT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 P--LAFCLGTSGAKALIFGG---EMVAAVAEVSGHLgKSLIKFCSGDLGPEgilpdthlLDPLLKEASTAPlAQIPSKGM 240
Cdd:PRK07470 93 PdeVAYLAEASGARAMICHAdfpEHAAAVRAASPDL-THVVAIGGARAGLD--------YEALVARHLGAR-VANAAVDH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 241 DDRLFYIYTSGTTGLPKAAIVVHSryyRMaAF---GHHAYRMQA---ADVLYDCLPLYHSAGniigvgqclIYGLTVVLR 314
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTHG---QM-AFvitNHLADLMPGtteQDASLVVAPLSHGAG---------IHQLCQVAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 315 ---------KKFSASRFWDdcikynctingvrhcrllcLVVQY-------IGEICRYLLKQPVREAERRHRVRLAVGNGl 378
Cdd:PRK07470 230 gaatvllpsERFDPAEVWA-------------------LVERHrvtnlftVPTILKMLVEHPAVDRYDHSSLRYVIYAG- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 379 rPAIWEEFTERfGVRQIG----EFYGATECNCSIANM--------DG---KVGSCGFnsrilphvypirlvkvnEDT-ME 442
Cdd:PRK07470 290 -APMYRADQKR-ALAKLGkvlvQYFGLGEVTGNITVLppalhdaeDGpdaRIGTCGF-----------------ERTgME 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 443 L-LRDAQGLciPCQAGEpgllVGQINQQDPlRRFDGYVSES-ATSKKIAHSVFSKGDSAYlsgdvlvMDELGYMYFRDRS 520
Cdd:PRK07470 351 VqIQDDEGR--ELPPGE----TGEICVIGP-AVFAGYYNNPeANAKAFRDGWFRTGDLGH-------LDARGFLYITGRA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 521 GDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAA-VADPHSLLDPNAIYQELQKVLAPYARP---IF 596
Cdd:PRK07470 417 SDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPkrfFF 495
|
570 580
....*....|....*....|....*...
gi 768002382 597 LRLLPQvdtTGTFKIQKtRLQREGFDPR 624
Cdd:PRK07470 496 WDALPK---SGYGKITK-KMVREELEER 519
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
243-611 |
7.87e-20 |
|
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: 90.93 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 243 RLFYI-YTSGTTGLPKAaivvhsrYYR-----MAAF--GHHAYRMQAADVLYDCLPLYHSaGNIIGVGQCLIYGLTVVLR 314
Cdd:cd17633 1 NPFYIgFTSGTTGLPKA-------YYRserswIESFvcNEDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 315 KKFSASRFWDDCIKYNCTIngvrhcrlLCLVVQyigeicryLLKQPVREAERRHRVR--LAVGNGLRPAIWEEFTERFGV 392
Cdd:cd17633 73 RKFNPKSWIRKINQYNATV--------IYLVPT--------MLQALARTLEPESKIKsiFSSGQKLFESTKKKLKNIFPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 393 RQIGEFYGATECNCSIANMDG---KVGSCGfnsRILPHVyPIRLvkvnedtmellRDAQGlcipcqaGEPGLLVGQINQq 469
Cdd:cd17633 137 ANLIEFYGTSELSFITYNFNQesrPPNSVG---RPFPNV-EIEI-----------RNADG-------GEIGKIFVKSEM- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 470 dplrRFDGYVSESATSKkiaHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDV 549
Cdd:cd17633 194 ----VFSGYVRGGFSNP---DGWMSVGDIGYV-------DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEA 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002382 550 AVYGvaVPGVEGKAGMAAVADPHSLLDPNaIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKI 611
Cdd:cd17633 260 IVVG--IPDARFGEIAVALYSGDKLTYKQ-LKRFLKQKLSRYEIPkkiIFVDSLPY---TSSGKI 318
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
83-616 |
8.91e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 93.27 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 83 QAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNL 162
Cdd:PRK06164 17 DAHARARPDAVALIDEDR--PLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 163 RREPLAFCLGTSGAKALI----FGG----EMVAAVAEVSGHLGKSLIKFCSG-DLGPEGILPDTHLLDPLlkEASTAPLA 233
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVvwpgFKGidfaAILAAVPPDALPPLRAIAVVDDAaDATPAPAPGARVQLFAL--PDPAPPAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 234 QIPSKGMDDRLFYIY-TSGTTGLPKaaIVVHsryyRMAAFGHH------AYRMQAADVLYDCLPLYHSAGnIIGVGQCLI 306
Cdd:PRK06164 173 AGERAADPDAGALLFtTSGTTSGPK--LVLH----RQATLLRHaraiarAYGYDPGAVLLAALPFCGVFG-FSTLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 307 YGLTVVLRKKFSASRfwddcikyncTINGVRHCRllclVVQYIG--EICRYLLKQPVREAERRHRVRLAVGNgLRPAiWE 384
Cdd:PRK06164 246 GGAPLVCEPVFDAAR----------TARALRRHR----VTHTFGndEMLRRILDTAGERADFPSARLFGFAS-FAPA-LG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 385 EFTERfgVRQIGE----FYGATECncsIANMDGKVGSCGFNSRILPHVYPIR---LVKVnedtmellRDAQ--GLCIPCQ 455
Cdd:PRK06164 310 ELAAL--ARARGVpltgLYGSSEV---QALVALQPATDPVSVRIEGGGRPASpeaRVRA--------RDPQdgALLPDGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 456 AGE-----PGLLVGQINQQDPLRRF---DGYvsesatskkiahsvFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWR 527
Cdd:PRK06164 377 SGEieiraPSLMRGYLDNPDATARAltdDGY--------------FRTGDLGYTRGD-------GQFVYQTRMGDSLRLG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 528 GENVSTTEVEGVLSRLLGQTDVAVYGVAvpgVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPY---ARPIFLRLLPQ 602
Cdd:PRK06164 436 GFLVNPAEIEHALEALPGVAAAQVVGAT---RDGKTVPVAfvIPTDGASPDEAGLMAACREALAGFkvpARVQVVEAFPV 512
|
570
....*....|....
gi 768002382 603 VDTTGTFKIQKTRL 616
Cdd:PRK06164 513 TESANGAKIQKHRL 526
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
101-616 |
1.46e-19 |
|
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: 91.77 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 101 GECWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGtsgaKAL 179
Cdd:cd05958 8 EREWTYRDLLALANRIANvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 180 IfggemvaAVAevsghlgkslikfcsgdlgpegilpdthlldpLLKEASTAplaqipskgMDDRLFYIYTSGTTGLPKAA 259
Cdd:cd05958 84 I-------TVA--------------------------------LCAHALTA---------SDDICILAFTSGTTGAPKAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 260 IVVHSRYYRMA-AFGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIY----GLTVVLRKKFSASRFWDDCIKYNCTIn 334
Cdd:cd05958 116 MHFHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLLLSAIARYKPTV- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 335 gvrhcrLLCLVVQYigeicRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIgEFYGATEC-NCSIANM 411
Cdd:cd05958 191 ------LFTAPTAY-----RAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPII-DGIGSTEMfHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 412 DG--KVGSCGfnsRILPHvYPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLVgqinqqdplrrfdgyvsesATSKKIA 489
Cdd:cd05958 259 PGdaRPGATG---KPVPG-YEAKVV-----------DDEGNPVP--DGTIGRLA-------------------VRGPTGC 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 490 HSVFSKGDSAYL------SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVP--GVEG 561
Cdd:cd05958 303 RYLADKRQRTYVqggwniTGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDEsrGVVV 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 562 KAGMaaVADPHSLLDPnAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd05958 383 KAFV--VLRPGVIPGP-VLARELQdhakAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
104-557 |
3.53e-19 |
|
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: 90.64 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIfgg 183
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 184 emvaavaevsghlgkslikfcsgdlgpegilpdTHlldPLLKEASTaplaqipskgMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05969 78 ---------------------------------TT---EELYERTD----------PEDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 264 SRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRK-KFSASRFWDDCIKYNCTingvrhcrll 342
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVT---------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 343 clvVQYIGEIC-RYLLK---QPVREAERRH-RVRLAVGNGLRPAI--WEEftERFGVRqIGEFYGATECNC-SIAN---M 411
Cdd:cd05969 182 ---VWYTAPTAiRMLMKegdELARKYDLSSlRFIHSVGEPLNPEAirWGM--EVFGVP-IHDTWWQTETGSiMIANypcM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 412 DGKVGSCGfnsRILPHVypiRLVKVNEDTMELLRDAQGLcIPCQAGEPGLLVGQINQQDplrRFDGYvsesatskkiahs 491
Cdd:cd05969 256 PIKPGSMG---KPLPGV---KAAVVDENGNELPPGTKGI-LALKPGWPSMFRGIWNDEE---RYKNS------------- 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 492 vFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVP 557
Cdd:cd05969 313 -FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP 375
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
80-616 |
8.21e-19 |
|
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: 89.95 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 80 RIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLN 159
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRS--LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAG--AAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 160 VNLR--REPLAFCLGTSGAKALIFGGEMVAAVAEvsghlgkslikfcsgdlgpegiLPDTHLLDPLLKEASTAPLAQIPS 237
Cdd:cd12117 77 LDPElpAERLAFMLADAGAKVLLTDRSLAGRAGG----------------------LEVAVVIDEALDAGPAGNPAVPVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 238 KgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAyRMQAADVLYDCLPLyhsagniigvgqcliygltvvlrkKF 317
Cdd:cd12117 135 P--DDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPL------------------------AF 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 318 SASRF--WddcikyNCTINGvrhcrlLCLVVQYIGEIcryLLKQPVREAERRHRVR-LAVGNGLRPAIWEEFTERF-GVR 393
Cdd:cd12117 188 DASTFeiW------GALLNG------ARLVLAPKGTL---LDPDALGALIAEEGVTvLWLTAALFNQLADEDPECFaGLR 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 394 QI---GE---------------------FYGATE-----CNCSIANMDGKVGScgfnsriLPHVYPIRlvkvneDTMELL 444
Cdd:cd12117 253 ELltgGEvvspphvrrvlaacpglrlvnGYGPTEnttftTSHVVTELDEVAGS-------IPIGRPIA------NTRVYV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 445 RDAQGlcIPCQAGEPG-LLVGqinqQDPLRRfdGYVS-ESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGD 522
Cdd:cd12117 320 LDEDG--RPVPPGVPGeLYVG----GDGLAL--GYLNrPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDD 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 523 TFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAA--VADPhsLLDPNAIYQELQKVLAPYARPIFLRLL 600
Cdd:cd12117 392 QVKIRGFRIELGEIEAALRAHPGVREAVV--VVREDAGGDKRLVAyvVAEG--ALDAAELRAFLRERLPAYMVPAAFVVL 467
|
570
....*....|....*.
gi 768002382 601 PQVDTTGTFKIQKTRL 616
Cdd:cd12117 468 DELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
105-551 |
2.03e-18 |
|
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: 88.09 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFA-PGDVVAIFLEGRPEFVGLWLGLAKAGmeAA--LLNVNLRREPLAFCLGTSGAKALIF 181
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAG--AAyvPLDPAYPAERLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 182 GGEMVAAVAevsghlgkslikfcsgDLGPEGILPDThLLDPLLKEASTAPLAQIPSKGmDDRLFYIYTSGTTGLPKAAIV 261
Cdd:TIGR01733 79 DSALASRLA----------------GLVLPVILLDP-LELAALDDAPAPPPPDAPSGP-DDLAYVIYTSGSTGRPKGVVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 262 VH----------SRYY------RMAAFGHHAYRMQAADVLydcLPLYHsagniigvGQCLIYGLTVVLRKKFSASRFWDD 325
Cdd:TIGR01733 141 THrslvnllawlARRYgldpddRVLQFASLSFDASVEEIF---GALLA--------GATLVVPPEDEERDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 326 ciKYNCTIngvrhcrlLCLVVQYIGeicryLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECN 405
Cdd:TIGR01733 210 --EHPVTV--------LNLTPSLLA-----LLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 406 csianmdgkVGSCGFnsrILPHVYPIRLVKVN-----EDTMELLRDAQGLciPCQAGEPG-LLVGQINqqdpLRRfdGYV 479
Cdd:TIGR01733 275 ---------VWSTAT---LVDPDDAPRESPVPigrplANTRLYVLDDDLR--PVPVGVVGeLYIGGPG----VAR--GYL 334
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002382 480 S-ESATSKKIAHSVFSKGDSA--YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 551
Cdd:TIGR01733 335 NrPELTAERFVPDPFAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-554 |
2.17e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 88.89 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 71 HQRAGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEfvglwlglAK 150
Cdd:PRK06188 7 LLHSGATYGHLLVSALKRYPDRPALVLGDTR--LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE--------VL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 151 AGMEAALLnVNLRREPL---------AFCLGTSGAKALIF--------GGEMVAAVAEVSGHLGkslikfcsgdLGPEGI 213
Cdd:PRK06188 77 MAIGAAQL-AGLRRTALhplgslddhAYVLEDAGISTLIVdpapfverALALLARVPSLKHVLT----------LGPVPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 214 LPDthlldpLLKEASTAPLAQIPSKGMDDRLFYI-YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLY 292
Cdd:PRK06188 146 GVD------LLAAAAKFGPAPLVAAALPPDIAGLaYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 293 HSAGNIIGVGqcLIYGLTVVLRKKFSASRFWDDCIKYNCTINgvrhcrllCLVVQYIgeicrY-LLKQP-VREAERRHRV 370
Cdd:PRK06188 220 HAGGAFFLPT--LLRGGTVIVLAKFDPAEVLRAIEEQRITAT--------FLVPTMI-----YaLLDHPdLRTRDLSSLE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 371 RLAVG-NGLRPAIWEEFTERFGvrQI-GEFYGATECNCSIANMD---------GKVGSCGFnsrilphvyPIRLVKVned 439
Cdd:PRK06188 285 TVYYGaSPMSPVRLAEAIERFG--PIfAQYYGQTEAPMVITYLRkrdhdpddpKRLTSCGR---------PTPGLRV--- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 440 tmELLrDAQGLCIPcqAGEPgllvGQINQQDPLrRFDGYVSE-SATSKkiahsVFSKGdsaYL-SGDVLVMDELGYMYFR 517
Cdd:PRK06188 351 --ALL-DEDGREVA--QGEV----GEICVRGPL-VMDGYWNRpEETAE-----AFRDG---WLhTGDVAREDEDGFYYIV 412
|
490 500 510
....*....|....*....|....*....|....*..
gi 768002382 518 DRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 554
Cdd:PRK06188 413 DRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
77-594 |
2.61e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 88.90 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 77 TIPRIFQAVVQRQPERLALVDAGTGEcwTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNVNLRREPLAFCLGTSGAKALIFGgEMVAAVAE-----------VSGHLGKSL--------------IKFCSGDL--G 209
Cdd:PRK05605 111 EHNPLYTAHELEHPFEDHGARVAIVW-DKVAPTVErlrrttpletiVSVNMIAAMpllqrlalrlpipaLRKARAALtgP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 210 PEGILPDTHLLD-PLLKEASTAPLaqiPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHH--------AYRMQ 280
Cdd:PRK05605 190 APGTVPWETLVDaAIGGDGSDVSH---PRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvpglgdgPERVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 281 AAdvlydcLPLYHsagniigvgqclIYGLTVVLrkKFSASrfwddcikynctINGvrhcRLLCLVVQYIGEICRYLLKQP 360
Cdd:PRK05605 267 AA------LPMFH------------AYGLTLCL--TLAVS------------IGG----ELVLLPAPDIDLILDAMKKHP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 361 -------------VREAERRHRVRLavgNGLRPAI-------------WEEFTERFGVrqigEFYGATECN----CSIAN 410
Cdd:PRK05605 311 ptwlpgvpplyekIAEAAEERGVDL---SGVRNAFsgamalpvstvelWEKLTGGLLV----EGYGLTETSpiivGNPMS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 411 MDGKVGSCGfnsriLPhvYP---IRLVkvNEDTMELLRDaqglciPCQAGEpgLLVgqinqQDPlRRFDGYVSESATSKK 487
Cdd:PRK05605 384 DDRRPGYVG-----VP--FPdteVRIV--DPEDPDETMP------DGEEGE--LLV-----RGP-QVFKGYWNRPEETAK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 488 IAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAA 567
Cdd:PRK05605 441 SFL------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV--VGLPREDGSEEVVA 512
|
570 580
....*....|....*....|....*....
gi 768002382 568 --VADPHSLLDPNAIYQELQKVLAPYARP 594
Cdd:PRK05605 513 avVLEPGAALDPEGLRAYCREHLTRYKVP 541
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-625 |
8.12e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 38 SGGWR-FLRIVCKTARRDLFGLSVLIRV--RLELRRHQRAGHTIPR------IFQAVVQRQPERLALVdAGtGECWTFAQ 108
Cdd:PRK12316 1956 DRHLLhLLEQMAEDAQAALGELALLDAGerQRILADWDRTPEAYPRgpgvhqRIAEQAARAPEAIAVV-FG-DQHLSYAE 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 109 LDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAkALIFGGEMVAA 188
Cdd:PRK12316 2034 LDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGA-ALLLTQRHLLE 2112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 189 VAEVSGHLgKSLikfcsgDLGPEGILPDThlldpllkeASTAPLAQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR 268
Cdd:PRK12316 2113 RLPLPAGV-ARL------PLDRDAEWADY---------PDTAPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 269 MAAFGHHAYRMQAADVLYDCLPLYHSAgniiGVGQC---LIYGLTVVLR--KKFSASRFWDDCIKYNCTIngvrhcrlLC 343
Cdd:PRK12316 2174 HCQAAGERYELSPADCELQFMSFSFDG----AHEQWfhpLLNGARVLIRddELWDPEQLYDEMERHGVTI--------LD 2241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 344 LVVQYIgeicrYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIGEFYGATEcncsiANMDGKVGSCGFN 421
Cdd:PRK12316 2242 FPPVYL-----QQLAEHAERDGRPPAVRVYCfgGEAVPAASLRLAWEALRPVYLFNGYGPTE-----AVVTPLLWKCRPQ 2311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 422 SRILPHVYPI------RLVKVNEDTMELLrdAQGLCIPCQAGEPGLLVGQINQQdplrrfdGYVSESATSKKIAHSvfsk 495
Cdd:PRK12316 2312 DPCGAAYVPIgralgnRRAYILDADLNLL--APGMAGELYLGGEGLARGYLNRP-------GLTAERFVPDPFSAS---- 2378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 496 GDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMA-AVADPHSL 574
Cdd:PRK12316 2379 GERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAyVVPDDAAE 2456
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 768002382 575 LDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQ 625
Cdd:PRK12316 2457 DLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR 2507
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
241-557 |
8.68e-18 |
|
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: 86.62 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 241 DDRLFYIYTSGTTGLPKAAIVVHSRYY--RMAAFGHhaYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFS 318
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI--FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 319 ASRFWDDCI-KYNCTIngvrhcrlLCLVVQYIGEICRYllKQPvreaERRHRVRLAV--GNGLRPAIWEEFTERFGVRqI 395
Cdd:cd05909 225 DYKKIPELIyDKKATI--------LLGTPTFLRGYARA--AHP----EDFSSLRLVVagAEKLKDTLRQEFQEKFGIR-I 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 396 GEFYGATEC----NCSIANMDGKVGSCGfnsRILPHVyPIRLVKVnedtmellrdaQGLCiPCQAGEPGLLVGQINQqdp 471
Cdd:cd05909 290 LEGYGTTECspviSVNTPQSPNKEGTVG---RPLPGM-EVKIVSV-----------ETHE-EVPIGEGGLLLVRGPN--- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 472 lrRFDGYVSESatskkiAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQtDVAV 551
Cdd:cd05909 351 --VMLGYLNEP------ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEV 421
|
....*.
gi 768002382 552 YGVAVP 557
Cdd:cd05909 422 AVVSVP 427
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
91-554 |
1.81e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 86.10 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 91 ERLAL--VDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLeGR-PEFVGLWLGLAKAGMEAALLNVNLRREPL 167
Cdd:PRK04319 59 DKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFM-PRiPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 168 AFCLGTSGAKALIFGGEMVA-AVAEVSGHLGKSLIkfcSGDLGPEGilPDTHLLDPLLKEASTAplAQIPSKGMDDRLFY 246
Cdd:PRK04319 138 RDRLEDSEAKVLITTPALLErKPADDLPSLKHVLL---VGEDVEEG--PGTLDFNALMEQASDE--FDIEWTDREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 247 IYTSGTTGLPKAAIVVHSryyrmAAFGHHA---YRM--QAADVlYDCL---------------PLYHSAGNIIGVGqcli 306
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHN-----AMLQHYQtgkYVLdlHEDDV-YWCTadpgwvtgtsygifaPWLNGATNVIDGG---- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 307 ygltvvlrkKFSASRFWDDCIKYNCTingvrhcrllclvVQYIGEIC-RYLLKQPVREAERRH----RVRLAVGNGLRP- 380
Cdd:PRK04319 281 ---------RFSPERWYRILEDYKVT-------------VWYTAPTAiRMLMGAGDDLVKKYDlsslRHILSVGEPLNPe 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 381 AI-WEEftERFGVRqIGEFYGATECNCS-IAN---MDGKVGSCGfnsRILPHVYpIRLVKVNEDtmELLRDAQG-LCIpc 454
Cdd:PRK04319 339 VVrWGM--KVFGLP-IHDNWWMTETGGImIANypaMDIKPGSMG---KPLPGIE-AAIVDDQGN--ELPPNRMGnLAI-- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 455 QAGEPGLLVGQINQQDplrRFDGYvsesatskkiahsvFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 534
Cdd:PRK04319 408 KKGWPSMMRGIWNNPE---KYESY--------------FAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPF 468
|
490 500
....*....|....*....|
gi 768002382 535 EVEgvlSRLLGQTDVAVYGV 554
Cdd:PRK04319 469 EVE---SKLMEHPAVAEAGV 485
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
105-611 |
4.02e-17 |
|
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: 84.07 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 185 mvaavaevsghlgkslikfcsgdlgpegiLPDthlldpllkeastapLAQIPskgmddrlfyiYTSGTTGLPKAAIVVHS 264
Cdd:cd05935 83 -----------------------------LDD---------------LALIP-----------YTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 265 RYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTingvrhcrllcl 344
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVT------------ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 345 VVQYIGEICRYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRQIgEFYGATEcNCSIANMDgkvgscgfns 422
Cdd:cd05935 176 FWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTGLRFV-EGYGLTE-TMSQTHTN---------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 423 rilPHVYPIR--LVKVNEDTMELLRDAQGLcIPCQAGEpgllVGQINQQDPlRRFDGYVS-ESATSKKIahsVFSKGDSA 499
Cdd:cd05935 244 ---PPLRPKLqcLGIP*FGVDARVIDIETG-RELPPNE----VGEIVVRGP-QIFKGYWNrPEETEESF---IEIKGRRF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 500 YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADP--HSLLDP 577
Cdd:cd05935 312 FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyRGKVTE 391
|
490 500 510
....*....|....*....|....*....|....*..
gi 768002382 578 NAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKI 611
Cdd:cd05935 392 EDIIEWAREQMAAYKYPrevEFVDELPR---SASGKI 425
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
248-617 |
5.15e-17 |
|
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: 83.10 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 248 YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL-RKKFSASRFWDDC 326
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 327 IKYNCT-INGVRhcrllclvVQYIGEicrylLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIGEFYGATE 403
Cdd:cd05917 89 EKEKCTaLHGVP--------TMFIAE-----LEHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 404 CNCSIAN------MDGKVGSCGfnsRILPHVYpirlVK-VNEDTMELL-RDAQG-LCIpcqagePGLLVGQINQQDPLRr 474
Cdd:cd05917 156 TSPVSTQtrtddsIEKRVNTVG---RIMPHTE----AKiVDPEGGIVPpVGVPGeLCI------RGYSVMKGYWNDPEK- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 475 fdgyvsesaTSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 554
Cdd:cd05917 222 ---------TAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 555 AvpgvEGKAGMAAVA----DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 617
Cdd:cd05917 287 P----DERYGEEVCAwirlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
69-257 |
1.03e-16 |
|
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: 83.66 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 69 RRHQRAGH----TIPRIFQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGL 144
Cdd:COG1021 14 ARYREAGYwrgeTLGDLLRRRAERHPDRIAVVDGER--RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 145 WLGLAKAGmeaaLLNVNL-----RREPLAFClGTSGAKALI----FGG----EMVAAVAEVSGHLGKSLIkfcSGDLGPE 211
Cdd:COG1021 92 FFALFRAG----AIPVFAlpahrRAEISHFA-EQSEAVAYIipdrHRGfdyrALARELQAEVPSLRHVLV---VGDAGEF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768002382 212 gilpdtHLLDPLLKEASTAPLAQIPSkgmDDRLFYIYTSGTTGLPK 257
Cdd:COG1021 164 ------TSLDALLAAPADLSEPRPDP---DDVAFFQLSGGTTGLPK 200
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
80-616 |
1.39e-16 |
|
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: 82.60 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 80 RIFQAVVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN 159
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 160 VNLRREPLAFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipsKG 239
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILL---------------------------------------------------------TN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 240 MDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAAD--VLYDCLPLYHSAGNIIgvgQCLIYGLTV-VLRkk 316
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSFDASAWEIF---PHLTAGAALhVVP-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 317 fSASRFwdDCIKYN--CTINGVRhcrllclvvqyIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFterfgvrQ 394
Cdd:cd17645 178 -SERRL--DLDALNdyFNQEGIT-----------ISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGY-------K 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 395 IGEFYGATECN--CSIANMDGKVGScgfnsriLPHVYPIRLVKV---NED-TMELLRDAQGLCIpcqAGEpGLLVGQINQ 468
Cdd:cd17645 237 LVNNYGPTENTvvATSFEIDKPYAN-------IPIGKPIDNTRVyilDEAlQLQPIGVAGELCI---AGE-GLARGYLNR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 469 QDplrrfdgyvsesATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTD 548
Cdd:cd17645 306 PE------------LTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768002382 549 VAVygVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd17645 374 AAV--LAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-626 |
3.71e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.90 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 61 LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE 140
Cdd:PRK12467 497 RELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGE--QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 141 FVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAkALIFGGEMVAAVAEVsghlgkslikfcsgdlgPEGI--LPDTH 218
Cdd:PRK12467 575 MVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV-RLLLTQSHLLAQLPV-----------------PAGLrsLCLDE 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 219 LLDPLLKEASTAP-LAQIPskgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYdclpLYHSAG 296
Cdd:PRK12467 637 PADLLCGYSGHNPeVALDP-----DNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSML----MVSTFA 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 297 NIIGVGQ---CLIYGLTVVLRKK---FSASRFWDDCIKYNCTIngvrhcrlLCLVVQYIGEICryllkQPVREAERRHRV 370
Cdd:PRK12467 708 FDLGVTElfgALASGATLHLLPPdcaRDAEAFAALMADQGVTV--------LKIVPSHLQALL-----QASRVALPRPQR 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 371 RLAVG------NGLRPaiWEEFteRFGVRQIgEFYGATEcncsiANMDGKVGSCGFNSRILPHVyPIRLVKVNEDTMELL 444
Cdd:PRK12467 775 ALVCGgealqvDLLAR--VRAL--GPGARLI-NHYGPTE-----TTVGVSTYELSDEERDFGNV-PIGQPLANLGLYILD 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 445 RDAQglciPCQAGEPG-LLVGqinqQDPLRRfdGYVSESA-TSKKIAHSVFS-KGDSAYLSGDVLVMDELGYMYFRDRSG 521
Cdd:PRK12467 844 HYLN----PVPVGVVGeLYIG----GAGLAR--GYHRRPAlTAERFVPDPFGaDGGRLYRTGDLARYRADGVIEYLGRMD 913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 522 DTFRWRGENVSTTEVEgvlSRLLGQTDV--AVYgVAVPGVEGK--------AGMAAVADPHSLLDpnAIYQELQKVLAPY 591
Cdd:PRK12467 914 HQVKIRGFRIELGEIE---ARLLAQPGVreAVV-LAQPGDAGLqlvaylvpAAVADGAEHQATRD--ELKAQLRQVLPDY 987
|
570 580 590
....*....|....*....|....*....|....*.
gi 768002382 592 ARPIFLRLLPQVDTTGTFKIQKTRL-QREGFDPRQT 626
Cdd:PRK12467 988 MVPAHLLLLDSLPLTPNGKLDRKALpKPDASAVQAT 1023
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-618 |
1.16e-15 |
|
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: 79.87 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIfgge 184
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 185 mvaavaevsghlgkslikfCSGDlgpegilpDTHLLDpllkeastaplaqipskgmDDRLFYIYTSGTTGLPKaAIVVHS 264
Cdd:cd05973 78 -------------------TDAA--------NRHKLD-------------------SDPFVMMFTSGTTGLPK-GVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 265 RYyrMAAFghHAYRMQAADVLYDclplyHSAGNIIGVGQCliYGL-------------TVVLRKKFSASRFWDDCIKYNC 331
Cdd:cd05973 111 RA--LAAF--GAYLRDAVDLRPE-----DSFWNAADPGWA--YGLyyaitgplalghpTILLEGGFSVESTWRVIERLGV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 332 TingvrhcRLLCLVVQYigeicRYLLKQPVrEAERRHRVRLAV----GNGLRPAIWEEFTERFGVrQIGEFYGATECNCS 407
Cdd:cd05973 180 T-------NLAGSPTAY-----RLLMAAGA-EVPARPKGRLRRvssaGEPLTPEVIRWFDAALGV-PIHDHYGQTELGMV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 408 IANMDG-----KVGSCGFnsrILPHvypIRLVKVNEDTMELLrdaqglcipcqAGEPGLLVGQINQQdPLRRFDGYvses 482
Cdd:cd05973 246 LANHHAlehpvHAGSAGR---AMPG---WRVAVLDDDGDELG-----------PGEPGRLAIDIANS-PLMWFRGY---- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 483 atskkiahsvFSKGDSA-----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVP 557
Cdd:cd05973 304 ----------QLPDTPAidggyYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDP 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002382 558 gVEGKAGMAAVADPHSLLDPNAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 618
Cdd:cd05973 374 -ERTEVVKAFVVLRGGHEGTPALADELQlhvkKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
78-618 |
1.72e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.89 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 78 IPRIFQAvvQRQPERLALVDAGTGECWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PLN02574 43 VSFIFSH--HNHNGDTALIDSSTGFSISYSELQPLVKSMAAgLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNvnlrrePLAfclgtsgakALifgGEMVAAVAEVSGHLGKSLIKfCSGDLGPEGI----LPDTHLLDPLLKEAST--- 229
Cdd:PLN02574 121 TMN------PSS---------SL---GEIKKRVVDCSVGLAFTSPE-NVEKLSPLGVpvigVPENYDFDSKRIEFPKfye 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 230 ------APLAQiPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAA----FGHHAYRMQAADVLY-DCLPLYHSAGNI 298
Cdd:PLN02574 182 likedfDFVPK-PVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrFEASQYEYPGSDNVYlAALPMFHIYGLS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 299 IGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTINGVRHCRLLCLV--VQYIGEICRYLLKQpvreaerrhrvrlaVGN 376
Cdd:PLN02574 261 LFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTkkAKGVCGEVLKSLKQ--------------VSC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 377 GLRPA---IWEEFTERFGVRQIGEFYGATEcncSIAnmdgkVGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQGLCIP 453
Cdd:PLN02574 327 GAAPLsgkFIQDFVQTLPHVDFIQGYGMTE---STA-----VGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 454 CQAGE-----PGLLVGQINqqdplrrfdgyvSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRG 528
Cdd:PLN02574 399 GNCGElwiqgPGVMKGYLN------------NPKATQSTIDK------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 529 ENVSTTEVEGVLSRLLGQTDVAVYGVavpgVEGKAGMAAVA----DPHSLLDPNAIYQELQKVLAPYA---RPIFLRLLP 601
Cdd:PLN02574 461 FQIAPADLEAVLISHPEIIDAAVTAV----PDKECGEIPVAfvvrRQGSTLSQEAVINYVAKQVAPYKkvrKVVFVQSIP 536
|
570
....*....|....*..
gi 768002382 602 QvdtTGTFKIQKTRLQR 618
Cdd:PLN02574 537 K---SPAGKILRRELKR 550
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-332 |
3.06e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 78.85 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 87 QRQPERLALVDAGTGecWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAgmEAALLNVN--LR 163
Cdd:PRK08314 21 RRYPDKTAIVFYGRA--ISYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRA--NAVVVPVNpmNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 164 REPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGDL---GPEGILPD----THLLDPL-------LKEAS 228
Cdd:PRK08314 97 EEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRlRHVIVAQYSDYlpaEPEIAVPAwlraEPPLQALapggvvaWKEAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 229 TAPLAQIPSK-GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIY 307
Cdd:PRK08314 177 AAGLAPPPHTaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYA 256
|
250 260 270
....*....|....*....|....*....|.
gi 768002382 308 GLTVVLrkkfsASRfWD-----DCI-KYNCT 332
Cdd:PRK08314 257 GATVVL-----MPR-WDreaaaRLIeRYRVT 281
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
79-616 |
4.39e-15 |
|
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: 78.09 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 79 PRIFQAVVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALL 158
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAG--AAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 159 NVN--LRREPLAFCLGTSGAKALIFGGEMVAAvaevsghlgkslikfcsgdlgPEGILPDTHLLDPLLKEASTAPLAQIP 236
Cdd:cd17646 77 PLDpgYPADRLAYMLADAGPAVVLTTADLAAR---------------------LPAGGDVALLGDEALAAPPATPPLVPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 237 skGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMaafgHHAYRMQAADVLYDCLPLyhsaGNIIGVGQC---LIYGL 309
Cdd:cd17646 136 --RPDNLAYVIYTSGSTGRPKGVMVTHagivNRLLWM----QDEYPLGPGDRVLQKTPL----SFDVSVWELfwpLVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 310 TVVLRK-------KFSASRFWDDCIKynctingvrhcrllclVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAI 382
Cdd:cd17646 206 RLVVARpgghrdpAYLAALIREHGVT----------------TCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPEL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 383 WEEFTERFGVRqIGEFYGATEcnCSIANMDGKVgSCGFNSRILPHVYPI---RLVKVNEDtmelLRdaqglciPCQAGEP 459
Cdd:cd17646 270 AARFLALPGAE-LHNLYGPTE--AAIDVTHWPV-RGPAETPSVPIGRPVpntRLYVLDDA----LR-------PVPVGVP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 460 G-LLVGQInqqdPLRRfdGYVSESA-TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 537
Cdd:cd17646 335 GeLYLGGV----QLAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 538 GVLSRLLGQTDVAVygVAVPGVEGKAGMAA---VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKT 614
Cdd:cd17646 409 AALAAHPAVTHAVV--VARAAPAGAARLVGyvvPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
..
gi 768002382 615 RL 616
Cdd:cd17646 487 AL 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-646 |
5.29e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.23 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 80 RIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN 159
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGE--QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 160 VNLRREPLAFCLGTSGAKALIfggemvaavaeVSGHLGkslikfcsgdlgpegiLPDTHLLDPLLKEASTAPLAQ--IPS 237
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLL-----------SQSHLR----------------LPLAQGVQVLDLDRGDENYAEanPAI 3191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 238 KGMDDRLFY-IYTSGTTGLPKAAIVVHsryyrmAAFGHHAYRM-QAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRK 315
Cdd:PRK12316 3192 RTMPENLAYvIYTSGSTGKPKGVGIRH------SALSNHLCWMqQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 316 KFSASRFWDDCIKYNCTINgvrhcRLLCLVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPaiwEEFTERFGVRQI 395
Cdd:PRK12316 3266 VLAGPEDWRDPALLVELIN-----SEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPA---DLQQQVFAGLPL 3337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 396 GEFYGATEcncsiANMDGKVGSCgfnsrILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRf 475
Cdd:PRK12316 3338 YNLYGPTE-----ATITVTHWQC-----VEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNR- 3406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 476 dgyvsESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEgvlSRLLGQTdvAVYGVA 555
Cdd:PRK12316 3407 -----PGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE---ARLLEHP--WVREAV 3476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 556 VPGVEGKAGMAAVADPHSLLD-PNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLqregfdPRQTSDrlfflD 634
Cdd:PRK12316 3477 VLAVDGRQLVAYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL------PRPDAA-----L 3545
|
570
....*....|..
gi 768002382 635 LKQGHYLPLNEA 646
Cdd:PRK12316 3546 LQQDYVAPVNEL 3557
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
90-557 |
7.61e-15 |
|
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: 77.34 E-value: 7.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNLRREP--L 167
Cdd:cd12118 18 PDRTSIVYGDRR--YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAG--AVLNALNTRLDAeeI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 168 AFCLGTSGAKALIFGGEmvaavaevsgHLGKSLIKfcSGDLGPEGILPDThlldpllkEASTAPLAqipskgmddrlfyi 247
Cdd:cd12118 94 AFILRHSEAKVLFVDRE----------FEYEDLLA--EGDPDFEWIPPAD--------EWDPIALN-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 248 YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGniigvgQCLIYGLT------VVLRKkFSASR 321
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG------WCFPWTVAavggtnVCLRK-VDAKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 322 FWDDCIKYnctinGVRHcrlLCLVVQYIGEICRYllkQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGA 401
Cdd:cd12118 213 IYDLIEKH-----KVTH---FCGAPTVLNMLANA---PPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFD-VTHVYGL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 402 TECNcsianmdGKVGSCGFN--SRILPhvypirlvkvnEDTMELLRDAQGLCIPcqaGEPGLLVGQINQQDPLRRfDG-- 477
Cdd:cd12118 281 TETY-------GPATVCAWKpeWDELP-----------TEERARLKARQGVRYV---GLEEVDVLDPETMKPVPR-DGkt 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 478 ---------------YVSESATSKKIAHSVFskgdsayLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSR 542
Cdd:cd12118 339 igeivfrgnivmkgyLKNPEATAEAFRGGWF-------HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYK 411
|
490
....*....|....*
gi 768002382 543 LLGQTDVAVygVAVP 557
Cdd:cd12118 412 HPAVLEAAV--VARP 424
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
86-313 |
2.38e-14 |
|
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: 76.12 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGfAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALL--- 158
Cdd:cd05931 3 AAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 159 --NVNLRRepLAFCLGTSGAKALIFGGEMVAAVAEVSghlgkslikfcsgdLGPEGILPDTHLLDPLLkEASTAPLAQIP 236
Cdd:cd05931 82 tpGRHAER--LAAILADAGPRVVLTTAAALAAVRAFA--------------ASRPAAGTPRLLVVDLL-PDTSAADWPPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 237 SKGMDDRLFYIYTSGTTGLPKAAIVVHsryyrmAAFGH------HAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLT 310
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
...
gi 768002382 311 VVL 313
Cdd:cd05931 219 SVL 221
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
83-619 |
2.98e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 75.84 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 83 QAVVQRQPERLALvdAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNL 162
Cdd:PRK06710 31 EQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 163 RREPLAFCLGTSGAKALIFGGEMVAAVAEV-SGHLGKSLIKFCSGDLGP---EGILP-----------------DTHLLD 221
Cdd:PRK06710 109 TERELEYQLHDSGAKVILCLDLVFPRVTNVqSATKIEHVIVTRIADFLPfpkNLLYPfvqkkqsnlvvkvseseTIHLWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 222 PLLKEASTAplAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG-HHAYR-MQAADVLYDCLPLYHSAGNII 299
Cdd:PRK06710 189 SVEKEVNTG--VEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGvQWLYNcKEGEEVVLGVLPFFHVYGMTA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 300 GVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTIngvrhcrllclvvqYIGEICRY--LLKQPVREAERRHRVRLAV-GN 376
Cdd:PRK06710 267 VMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTL--------------FPGAPTIYiaLLNSPLLKEYDISSIRACIsGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 377 GLRPAIWEEFTERFGVRQIGEFYGATECN-CSIANM--DGKV-GSCGfnsriLPhvYPirlvkvnedtmellrDAQGLCI 452
Cdd:PRK06710 333 APLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFlwEKRVpGSIG-----VP--WP---------------DTEAMIM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 453 PCQAGE---PGlLVGQINQQDPlRRFDGYVSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 529
Cdd:PRK06710 391 SLETGEalpPG-EIGEIVVKGP-QIMKGYWNKPEETAAVLQ------DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 530 NVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTF 609
Cdd:PRK06710 463 NVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVG 542
|
570
....*....|
gi 768002382 610 KIQKTRLQRE 619
Cdd:PRK06710 543 KILRRVLIEE 552
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
90-263 |
6.62e-14 |
|
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: 74.61 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNL-----RR 164
Cdd:cd12114 1 PDATAVICGD--GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAG--AAYVPVDIdqpaaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 165 EPLafcLGTSGAKALIfggemvaavaevsghlgkslikFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPskGMDDRL 244
Cdd:cd12114 77 EAI---LADAGARLVL----------------------TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDV--APDDLA 129
|
170
....*....|....*....
gi 768002382 245 FYIYTSGTTGLPKAAIVVH 263
Cdd:cd12114 130 YVIFTSGSTGTPKGVMISH 148
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
69-616 |
8.51e-14 |
|
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: 74.29 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 69 RRHQRAGHTIPRIFQAV----VQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGL 144
Cdd:cd05920 4 RRYRAAGYWQDEPLGDLlarsAARHPDRIAVVDGDRR--LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 145 WLGLAKAGMEAAL-LNVNLRREPLAFClGTSGAKALIfggemvaavaevsghlgkslikfcsgdlGPEGILPDTHLldPL 223
Cdd:cd05920 82 FFALLRLGAVPVLaLPSHRRSELSAFC-AHAEAVAYI----------------------------VPDRHAGFDHR--AL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 224 LKEAstapLAQIPskgmdDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYH----SAGNII 299
Cdd:cd05920 131 AREL----AESIP-----EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplACPGVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 300 GVgqcLIYGLTVVLrkkfSASRFWDDCIKyncTI--NGVRHCRLL-CLVVQYIGEICRYllkqpvREAERRHRVRLAVGN 376
Cdd:cd05920 202 GT---LLAGGRVVL----APDPSPDAAFP---LIerEGVTVTALVpALVSLWLDAAASR------RADLSSLRLLQVGGA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 377 GLRPAIWEEFTERFGVrQIGEFYGATE--CNCS--------IANMDGKVGSCGFNSRILphvypirlvkvnedtmellrD 446
Cdd:cd05920 266 RLSPALARRVPPVLGC-TLQQVFGMAEglLNYTrlddpdevIIHTQGRPMSPDDEIRVV--------------------D 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 447 AQGLCIPcqAGEPGLLvgqinqqdpLRR----FDGYV-SESATSKkiahsVFSKgDSAYLSGDVLVMDELGYMYFRDRSG 521
Cdd:cd05920 325 EEGNPVP--PGEEGEL---------LTRgpytIRGYYrAPEHNAR-----AFTP-DGFYRTGDLVRRTPDGYLVVEGRIK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 522 DTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAAVADPHsllDPNAIYQELQKVL-----APYARPIF 596
Cdd:cd05920 388 DQINRGGEKIAAEEVENLLLRHPAVHDAAV--VAMPDELLGERSCAFVVLR---DPPPSAAQLRRFLrerglAAYKLPDR 462
|
570 580
....*....|....*....|
gi 768002382 597 LRLLPQVDTTGTFKIQKTRL 616
Cdd:cd05920 463 IEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
90-619 |
2.90e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.67 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGTGECWtfAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAAL--LNVNLRREPL 167
Cdd:PRK08162 32 PDRPAVIHGDRRRTW--AETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAG--AVLntLNTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 168 AFCLGTSGAKALI----FGGEMVAAVAEVSGhlgksLIKFCSGDLGPEgiLPDTHLLDPLLKEASTA----PLAQIPSKG 239
Cdd:PRK08162 108 AFMLRHGEAKVLIvdteFAEVAREALALLPG-----PKPLVIDVDDPE--YPGGRFIGALDYEAFLAsgdpDFAWTLPAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 240 MDDRLFYIYTSGTTGLPKAaIVVHSR-YYRMAA-------FGHHAyrmqaadVLYDCLPLYHSagNiigvGQC------L 305
Cdd:PRK08162 181 EWDAIALNYTSGTTGNPKG-VVYHHRgAYLNALsnilawgMPKHP-------VYLWTLPMFHC--N----GWCfpwtvaA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 306 IYGLTVVLRKkFSASRFWDDCIKYnctinGVRHcrlLC--LVVQYIgeicryLLKQPvrEAERR---HRVRLAVGNGLRP 380
Cdd:PRK08162 247 RAGTNVCLRK-VDPKLIFDLIREH-----GVTH---YCgaPIVLSA------LINAP--AEWRAgidHPVHAMVAGAAPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 381 AIWEEFTERFGVRqIGEFYGATECNcsianmdGKVGSCGFNS--RILPHvypirlvkvneDTMELLRDAQGLCIPCQAG- 457
Cdd:PRK08162 310 AAVIAKMEEIGFD-LTHVYGLTETY-------GPATVCAWQPewDALPL-----------DERAQLKARQGVRYPLQEGv 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 458 --------EP----GLLVGQInqqdpLRR----FDGYV-SESATSKKIAHSVFSKGDSAylsgdvlVMDELGYMYFRDRS 520
Cdd:PRK08162 371 tvldpdtmQPvpadGETIGEI-----MFRgnivMKGYLkNPKATEEAFAGGWFHTGDLA-------VLHPDGYIKIKDRS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 521 GDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPG----------VEGKAGMAAVADphslldpnAIYQELQKVLAP 590
Cdd:PRK08162 439 KDIIISGGENISSIEVEDVLYRHPAVLVAAV--VAKPDpkwgevpcafVELKDGASATEE--------EIIAHCREHLAG 508
|
570 580 590
....*....|....*....|....*....|.
gi 768002382 591 YARP--IFLRLLPQvdtTGTFKIQKTRLQRE 619
Cdd:PRK08162 509 FKVPkaVVFGELPK---TSTGKIQKFVLREQ 536
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-618 |
3.13e-13 |
|
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: 72.22 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEfvgLWlglakagmEAALLNVNLRreplafclgtsgakalifgge 184
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVE---LW--------EAMLAAMKLG--------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 185 mvaAVaevsghlgkslikfcsgdlgpegILPDTHLLDP-----LLKEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKaa 259
Cdd:cd05974 50 ---AV-----------------------VIPATTLLTPddlrdRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPK-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 260 IVVHSryYRMAAFGHHAYR----MQAADVLYDClplyHSAGNIIGVGQCLI----YGLTVVL--RKKFSASRFWDDCIKY 329
Cdd:cd05974 102 LVEHT--HRSYPVGHLSTMywigLKPGDVHWNI----SSPGWAKHAWSCFFapwnAGATVFLfnYARFDAKRVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 330 NCTIngvrhcrlLCLVVQyigeICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGvRQIGEFYGATECNCSIA 409
Cdd:cd05974 176 GVTT--------LCAPPT----VWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETTALVG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 410 NMDGKVGSCGFNSRILPHvYPIRLVkvnedtmellrDAQGLciPCQAGEPGLLVGQINqqdPLRRFDGYVSESAtskKIA 489
Cdd:cd05974 243 NSPGQPVKAGSMGRPLPG-YRVALL-----------DPDGA--PATEGEVALDLGDTR---PVGLMKGYAGDPD---KTA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 490 HSVfskGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYG------VAVPgvegKA 563
Cdd:cd05974 303 HAM---RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPspdpvrLSVP----KA 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 564 GMAAVA----DPHSLLDpnaIYQELQKVLAPY--ARPIFLRLLPQvdtTGTFKIQKTRLQR 618
Cdd:cd05974 376 FIVLRAgyepSPETALE---IFRFSRERLAPYkrIRRLEFAELPK---TISGKIRRVELRR 430
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
90-333 |
3.23e-13 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 72.71 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:PLN02246 37 SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIfggEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLdpllkEASTAPLAQIpSKGMDDRLFYIYT 249
Cdd:PLN02246 117 QAKASGAKLII---TQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELT-----QADENELPEV-EISPDDVVALPYS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 250 SGTTGLPKAAIVVH-----SRYYRMAAFGHHAYrMQAADVLYDCLPLYH--SAGNIIGVGqcLIYGLTVVLRKKFSASRF 322
Cdd:PLN02246 188 SGTTGLPKGVMLTHkglvtSVAQQVDGENPNLY-FHSDDVILCVLPMFHiySLNSVLLCG--LRVGAAILIMPKFEIGAL 264
|
250
....*....|.
gi 768002382 323 WDDCIKYNCTI 333
Cdd:PLN02246 265 LELIQRHKVTI 275
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
242-618 |
5.79e-13 |
|
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: 70.44 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIgVGQCLIYGLTVVLRKKFSASR 321
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 322 fwddcikYNCTINGVRHCRLLCLVVQYIgeicryLLKQPVREAERRHRVRLaVGNGlrpAIWEEFTERFGVRQIGEF--Y 399
Cdd:cd17630 80 -------EDLAPPGVTHVSLVPTQLQRL------LDSGQGPAALKSLRAVL-LGGA---PIPPELLERAADRGIPLYttY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 400 GATE---CNCSIANMDGKVGSCGfnsRILPHVypirlvkvnedtmELLRDAQGlCIpcQAGEPGLLVGQINQQDPLRRFD 476
Cdd:cd17630 143 GMTEtasQVATKRPDGFGRGGVG---VLLPGR-------------ELRIVEDG-EI--WVGGASLAMGYLRGQLVPEFNE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 477 GyvsesatskkiahSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAV 556
Cdd:cd17630 204 D-------------GWFTTKDLGELHAD-------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPD 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768002382 557 PgvegKAGMAAVA--DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 618
Cdd:cd17630 264 E----ELGQRPVAviVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
90-616 |
7.82e-13 |
|
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: 70.80 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNLR--REPL 167
Cdd:cd17643 1 PEAVAVVDED--RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG--GAYVPIDPAypVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 168 AFCLGTSGAKALIFGGEMVAAVaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmddrlfyI 247
Cdd:cd17643 77 AFILADSGPSLLLTDPDDLAYV---------------------------------------------------------I 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 248 YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYdclpLYHSAG------NIIGVgqcLIYGLTVVLRKKF---S 318
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWGA---LLHGGRLVVVPYEvarS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 319 ASRFWddcikynctingvrhcRLLC----LVVQYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGV 392
Cdd:cd17643 173 PEDFA----------------RLLRdegvTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 393 R--QIGEFYGATECNC-------SIANMDGKVGS-CGfnsRILPHvYPIRLVkvnedtmellrDAQGLCIPcqAGEPG-L 461
Cdd:cd17643 237 DrpQLVNMYGITETTVhvtfrplDAADLPAAAASpIG---RPLPG-LRVYVL-----------DADGRPVP--PGVVGeL 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 462 LVG--QINQqdplrrfdGYVSESA--TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 537
Cdd:cd17643 300 YVSgaGVAR--------GYLGRPEltAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIE 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 538 GVLSRLLGQTDVAVygVAVPGVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTR 615
Cdd:cd17643 372 AALATHPSVRDAAV--IVREDEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAA 449
|
.
gi 768002382 616 L 616
Cdd:cd17643 450 L 450
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
90-616 |
8.40e-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: 70.96 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17650 1 PDAIAVSDATRQ--LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALifggemvaavaevsghlgkslikfcsgdlgpegilpdthLLDPllkeastaplaqipskgmDDRLFYIYT 249
Cdd:cd17650 79 MLEDSGAKLL---------------------------------------LTQP------------------EDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 250 SGTTGLPKAAIVVHS----------RYYRMAAFGHHAyrMQAADVLYDClplyhSAGNIIgvgQCLIYGLTVVL---RKK 316
Cdd:cd17650 102 SGTTGKPKGVMVEHRnvahaahawrREYELDSFPVRL--LQMASFSFDV-----FAGDFA---RSLLNGGTLVIcpdEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 317 FSASRFWDDCIKYNCTIngvrhcrllclvVQYIGEICRYLLKQPVREAERRHRVR-LAVGNGLRPAIW-EEFTERFGVR- 393
Cdd:cd17650 172 LDPAALYDLILKSRITL------------MESTPALIRPVMAYVYRNGLDLSAMRlLIVGSDGCKAQDfKTLAARFGQGm 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 394 QIGEFYGATECN-------------CSIANMdgKVGSCGFNSRIL---PHVYPIRLVKVNEdtmellrdaqgLCIpcqaG 457
Cdd:cd17650 240 RIINSYGVTEATidstyyeegrdplGDSANV--PIGRPLPNTAMYvldERLQPQPVGVAGE-----------LYI----G 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 458 EPGLLVGQINQQDplrrfdgyvsesATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 537
Cdd:cd17650 303 GAGVARGYLNRPE------------LTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIE 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 538 GVLSRLLGQTDVAVygVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd17650 371 SQLARHPAIDEAVV--AVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
74-291 |
1.29e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 74 AGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEF-VGLwLGLAKAG 152
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALVWDG--GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLlVGL-LAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 153 MEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGhlgkslikFCSGDLgpegilpDTHLLDPLlkeASTAPL 232
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEG--------VSAIAL-------DSLHLDSW---PSQAPG 1267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 233 AQIpskgMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPL 291
Cdd:PRK05691 1268 LHL----HGDNLAYvIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI 1323
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
247-613 |
1.98e-12 |
|
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: 68.68 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFsasrfwdDC 326
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVF-------DV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 327 IKYNCTINGVRhcrllCLVVQYIGEICRYLLKQPVREAERRHRVRLAV-GNGLRPAIW-EEFTERFGVRQIGEFYGATEC 404
Cdd:cd17638 79 DAILEAIERER-----ITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELvRRMRSELGFETVLTAYGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 405 NC-----------SIANMDGKvGSCGFNSRIlphvypirlvkvnEDTMELLrdAQGlcipcqagePGLLVGQINqqDPlr 473
Cdd:cd17638 154 GVatmcrpgddaeTVATTCGR-ACPGFEVRI-------------ADDGEVL--VRG---------YNVMQGYLD--DP-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 474 rfdgyvseSATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYG 553
Cdd:cd17638 205 --------EATAEAI------DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 554 VAVPGVeGKAGMA-AVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQK 613
Cdd:cd17638 271 VPDERM-GEVGKAfVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
105-619 |
3.22e-12 |
|
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: 69.20 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 185 MVAAVAEVSGHL--GKSLIKFCSGDLGPEGILPDTHLLDPLLkeASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKA---- 258
Cdd:cd12119 107 FLPLLEAIAPRLptVEHVVVMTDDAAMPEPAGVGVLAYEELL--AAESPEYDWPDFDENTAAAICYTSGTTGNPKGvvys 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 259 --AIVVHSryyrMAAFGHHAYRMQAADVLYDCLPLYHsaGNIIGVG-QCLIYGLTVVLRKKFSASRFWDDCIK-YNCTI- 333
Cdd:cd12119 185 hrSLVLHA----MAALLTDGLGLSESDVVLPVVPMFH--VNAWGLPyAAAMVGAKLVLPGPYLDPASLAELIErEGVTFa 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 334 NGVRhcrllclvvqyigEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERfGVRQIgEFYGATE-CNCSIAN 410
Cdd:cd12119 259 AGVP-------------TVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEER-GVRVI-HAWGMTEtSPLGTVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 411 -----MDGKVGSCGFNSRILPHvYPIRLVK---VNEDTMELLRDAQglcipcQAGE-----PGLLVGQINQQDPLRRF-- 475
Cdd:cd12119 324 rppseHSNLSEDEQLALRAKQG-RPVPGVElriVDDDGRELPWDGK------AVGElqvrgPWVTKSYYKNDEESEALte 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 476 DGYVSesatskkiahsvfskgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVA 555
Cdd:cd12119 397 DGWLR---------------------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVP 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 556 VPgvegKAG---MA-AVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRLqRE 619
Cdd:cd12119 456 HP----KWGerpLAvVVLKEGATVTAEELLEFLADKVAKWWLPddvVFVDEIPK---TSTGKIDKKAL-RE 518
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
90-616 |
3.41e-12 |
|
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: 68.93 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLwLGLAKAGMEAALLNVNLRREPLA 168
Cdd:cd17649 1 PDAVALVFGD--QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEmVVAL-LAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 169 FCLGTSGAKALIfggemvaavaevsGHLGKSLIkfcsgdlgpegilpdthlldpllkeastaplaqipskgmddrlFYIY 248
Cdd:cd17649 78 YMLEDSGAGLLL-------------THHPRQLA-------------------------------------------YVIY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 249 TSGTTGLPKAAIVVHsryyrmAAFGHHA------YRMQAADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLRkkfsASRF 322
Cdd:cd17649 102 TSGSTGTPKGVAVSH------GPLAAHCqataerYGLTPGDRELQFASFNFDGA-HEQLLPPLICGACVVLR----PDEL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 323 WDDCIKYnCTIngVRHCR--LLCLVVQYIGEICRYLLKQPVReaeRRHRVRLAV--GNGLRPAIWEEfTERFGVRQIGEf 398
Cdd:cd17649 171 WASADEL-AEM--VRELGvtVLDLPPAYLQQLAEEADRTGDG---RPPSLRLYIfgGEALSPELLRR-WLKAPVRLFNA- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 399 YGATEcncsiANMDGKVGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQglciPCQAGEPG-LLVGqinqQDPLRRfdG 477
Cdd:cd17649 243 YGPTE-----ATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN----PVPVGVTGeLYIG----GEGLAR--G 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 478 YVSESATSKK--IAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVA 555
Cdd:cd17649 308 YLGRPELTAErfVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAV--VA 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768002382 556 VPGVEGK---AGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd17649 386 LDGAGGKqlvAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
104-602 |
3.51e-12 |
|
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: 68.78 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGG 183
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 184 emvaavaevsghlgkslikfcsgdlgpegilPDThlldpllkeastapLAQIpskgmddrlfyIYTSGTTGLPKAAIVVH 263
Cdd:cd05907 86 -------------------------------PDD--------------LATI-----------IYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 264 SRYyrMAAFGHHAYRMQAA--DVLYDCLPLYHSAGNIIGVGQCLIYGLTVV-----------LRKK-----FSASRFWDd 325
Cdd:cd05907 110 RNI--LSNALALAERLPATegDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetllddLSEVrptvfLAVPRVWE- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 326 cikynctingvRHCrlLCLVVQYIGEICRYLLKQPVREaerrhRVRLAVGNG--LRPAIwEEFTERFGVrQIGEFYGATE 403
Cdd:cd05907 187 -----------KVY--AAIKVKAVPGLKRKLFDLAVGG-----RLRFAASGGapLPAEL-LHFFRALGI-PVYEGYGLTE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 404 CnCSIANM----DGKVGSCGfnsrilpHVYPIRLVKVNEDtmellrdaqglcipcqaGEpgLLV-GQINqqdplrrFDGY 478
Cdd:cd05907 247 T-SAVVTLnppgDNRIGTVG-------KPLPGVEVRIADD-----------------GE--ILVrGPNV-------MLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 479 VSESATSKKIAhsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR-GENVSTTEVEGVL--SRLLGQtdVAVYGVA 555
Cdd:cd05907 293 YKNPEATAEAL-----DADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALkaSPLISQ--AVVIGDG 365
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 556 VPGV-------------EGKAGMAAVADPHSLLDPNAIYQELQKV-------LAPYARPIFLRLLPQ 602
Cdd:cd05907 366 RPFLvalivpdpealeaWAEEHGIAYTDVAELAANPAVRAEIEAAveaanarLSRYEQIKKFLLLPE 432
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
241-618 |
4.30e-12 |
|
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: 67.89 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL------R 314
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 315 KKFSASRFWDDCIKYNCTingvrhcrllclVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVrQ 394
Cdd:cd05944 82 NPGLFDNFWKLVERYRIT------------SLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGL-P 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 395 IGEFYGATECNCSIA----NMDGKVGSCGFNsriLPHVYpIRLVKVNEDTMELLRDAQGLCIP-CQAGePGLLVGQINQQ 469
Cdd:cd05944 149 VVEGYGLTEATCLVAvnppDGPKRPGSVGLR---LPYAR-VRIKVLDGVGRLLRDCAPDEVGEiCVAG-PGVFGGYLYTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 470 DPLRRF--DGYVSesatskkiahsvfskgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSR----- 542
Cdd:cd05944 224 GNKNAFvaDGWLN---------------------TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRhpava 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 543 ---LLGQTDVAVYGVAVPGVEGKAGmaAVADPHSLLDPNAiyqelQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 618
Cdd:cd05944 283 fagAVGQPDAHAGELPVAYVQLKPG--AVVEEEELLAWAR-----DHVPERAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
107-616 |
5.81e-12 |
|
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: 68.17 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 107 AQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaaLLNVNLRREPLAFCLGTSGAKALIFGGEMV 186
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIY---LINSILTVFAAAAAWKCGACPAYKSSRAPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 187 AAVAEVSGHLGKSLIkfCSGDLGPEGilpdthlLDPLlkEASTAPLAQIPSKGMDDRLFY---IYTSGTTGLPKA----- 258
Cdd:cd05929 79 AEACAIIEIKAAALV--CGLFTGGGA-------LDGL--EDYEAAEGGSPETPIEDEAAGwkmLYSGGTTGRPKGikrgl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 259 -AIVVHSRYYRMAAFGhhaYRMQAADVLYDCLPLYHSAGNIIGVGqCLIYGLTVVLRKKFSASRFWDDCIKYnctinGVR 337
Cdd:cd05929 148 pGGPPDNDTLMAAALG---FGPGADSVYLSPAPLYHAAPFRWSMT-ALFMGGTLVLMEKFDPEEFLRLIERY-----RVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 338 HcrllclvVQYIGEICRYLLKQP--VREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRqIGEFYGATECNcsianmdg 413
Cdd:cd05929 219 F-------AQFVPTMFVRLLKLPeaVRNAYDLSSLKRVIHAAapCPPWVKEQWIDWGGPI-IWEYYGGTEGQ-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 414 kvGSCGFNS-RILPHvyPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGqinqqDPLRRFDGYVSESATSKKiaHSV 492
Cdd:cd05929 283 --GLTIINGeEWLTH--PGSVGRAVLGKVHILDEDGNEVPPGEIGEVYFANG-----PGFEYTNDPEKTAAARNE--GGW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 493 FSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAVaDP 571
Cdd:cd05929 352 STLGDVGYL-------DEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVV-QP 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 768002382 572 HSLLDPNAIYQE-----LQKVLAPYARP---IFLRLLPQVDTTgtfKIQKTRL 616
Cdd:cd05929 422 APGADAGTALAEeliafLRDRLSRYKCPrsiEFVAELPRDDTG---KLYRRLL 471
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
69-557 |
6.12e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.18 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 69 RRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECwTFAQLDAYSNAVANLFRQLgFAPGDVVAIFLegrPEFVG---LW 145
Cdd:PRK08633 608 KSRKEALPPLAEAWIDTAKRNWSRLAVADSTGGEL-SYGKALTGALALARLLKRE-LKDEENVGILL---PPSVAgalAN 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 146 LGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAlIFGGEMVAAVAEVSGHLGKSLIKfcSGDLGPEGILPDTHLLDPLLK 225
Cdd:PRK08633 683 LALLLAGKVPVNLNYTASEAALKSAIEQAQIKT-VITSRKFLEKLKNKGFDLELPEN--VKVIYLEDLKAKISKVDKLTA 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 226 --EASTAPLAQI-----PSKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRMAAFGH--HAYRMQAADVLYDCLPLYHSag 296
Cdd:PRK08633 760 llAARLLPARLLkrlygPTFKPDDTATIIFSSGSEGEPKG--VMLSHHNILSNIEQisDVFNLRNDDVILSSLPFFHS-- 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 297 niigvgqcliYGLTV----VLRKKFSASRFWDD---------CIKYNCTIngvrhcrlLCLVVQYigeiCRYLLKQPVRE 363
Cdd:PRK08633 836 ----------FGLTVtlwlPLLEGIKVVYHPDPtdalgiaklVAKHRATI--------LLGTPTF----LRLYLRNKKLH 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 364 AERRHRVRLAVGNG--LRPAIWEEFTERFGVRqIGEFYGATEC------NCSIANMDG-------KVGSCGfnsRILPHV 428
Cdd:PRK08633 894 PLMFASLRLVVAGAekLKPEVADAFEEKFGIR-ILEGYGATETspvasvNLPDVLAADfkrqtgsKEGSVG---MPLPGV 969
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 429 yPIRLvkVNEDTMEllrdaqglciPCQAGEPGL-LVGQINqqdplrRFDGYVS-ESATSKKIAHsvfSKGDSAYLSGDVL 506
Cdd:PRK08633 970 -AVRI--VDPETFE----------ELPPGEDGLiLIGGPQ------VMKGYLGdPEKTAEVIKD---IDGIGWYVTGDKG 1027
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 768002382 507 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVP 557
Cdd:PRK08633 1028 HLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVP 1078
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
80-616 |
9.34e-12 |
|
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: 67.74 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 80 RIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLwLGLAKAGMEAALL 158
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED--QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEmIVGI-LGILKAGGAYLPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 159 NVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEvsghlgkslIKFCsgdlgpegilpdTHLLDPLLKEASTAPLAqIPSK 238
Cdd:cd17655 78 DPDYPEERIQYILEDSGADILLTQSHLQPPIAF---------IGLI------------DLLDEDTIYHEESENLE-PVSK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 239 GmDDRLFYIYTSGTTGLPKAAIVVHSryyrmaafGHHAYRMQAADVLY----DCLPLYHSAGNIIGVGQ---CLIYGLTV 311
Cdd:cd17655 136 S-DDLAYVIYTSGSTGKPKGVMIEHR--------GVVNLVEWANKVIYqgehLRVALFASISFDASVTEifaSLLSGNTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 312 VLRKKFSASR---FWDDCIKYNCTIngvrhCRLLCLVVQYIGEIcRYLLKQPVReaerrhrvRLAV-GNGLRPAIWEEFT 387
Cdd:cd17655 207 YIVRKETVLDgqaLTQYIRQNRITI-----IDLTPAHLKLLDAA-DDSEGLSLK--------HLIVgGEALSTELAKKII 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 388 ERFGV-RQIGEFYGATEC--NCSIANMDGKvgscgfnSRILPHVyPIRLVKVNedTMELLRDAQGLCIPcqAGEPG-LLV 463
Cdd:cd17655 273 ELFGTnPTITNAYGPTETtvDASIYQYEPE-------TDQQVSV-PIGKPLGN--TRIYILDQYGRPQP--VGVAGeLYI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 464 GqinqQDPLRRfdGYVS-ESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSR 542
Cdd:cd17655 341 G----GEGVAR--GYLNrPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQ 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 543 LLGQTDVAVygVAVPGVEGKAGMAA--VADPHslLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd17655 415 HPDIKEAVV--IARKDEQGQNYLCAyiVSEKE--LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
77-625 |
1.41e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 67.35 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 77 TIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaA 156
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKA--ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGY--V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNVNLRREP--LAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGD-LGPEGI-----------------LP 215
Cdd:PRK07059 100 VVNVNPLYTPreLEHQLKDSGAEAIVVLENFATTVQQVLAKTAvKHVVVASMGDlLGFKGHivnfvvrrvkkmvpawsLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 216 DTHLLDPLLKEASTAPLAQiPSKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMAAFGHHAYRMQAAD--VLYDC- 288
Cdd:PRK07059 180 GHVRFNDALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPRPdqLNFVCa 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 289 LPLYHsagniigvgqclIYGLTVvlrkkfsasrfwddcikynCTINGVRHCRLLCLVVQ------YIGEICRY------- 355
Cdd:PRK07059 259 LPLYH------------IFALTV-------------------CGLLGMRTGGRNILIPNprdipgFIKELKKYqvhifpa 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 356 -------LLKQPVREAERRHRVRLAVGNGLrpAIWEEFTERFGVRQ---IGEFYGATECN----CSIANMDGKVGSCGFn 421
Cdd:PRK07059 308 vntlynaLLNNPDFDKLDFSKLIVANGGGM--AVQRPVAERWLEMTgcpITEGYGLSETSpvatCNPVDATEFSGTIGL- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 422 srilphvyPIRLVKVNedtmelLRDAQGLCIPC-QAGE-----PGLLVGQINQQDplrrfdgyvsesATSKKIAHSVFSK 495
Cdd:PRK07059 385 --------PLPSTEVS------IRDDDGNDLPLgEPGEicirgPQVMAGYWNRPD------------ETAKVMTADGFFR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 496 gdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvavpgvegkagmaaVADPHS-- 573
Cdd:PRK07059 439 ------TGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVG--------------VPDEHSge 498
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768002382 574 ---LL----DPNAIYQELQKV----LAPYARPIFLRLLPQVDTTGTFKIqktrLQREGFDPRQ 625
Cdd:PRK07059 499 avkLFvvkkDPALTEEDVKAFckerLTNYKRPKFVEFRTELPKTNVGKI----LRRELRDGKA 557
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-279 |
1.43e-11 |
|
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: 67.18 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 81 IFQAVVQRQPERLAlVDAGTGEcWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAA--LL 158
Cdd:cd05918 4 LIEERARSQPDAPA-VCAWDGS-LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG--GAfvPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 159 NVNLRREPLAFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeASTAplaqipsk 238
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVL----------------------------------------------TSSP-------- 105
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768002382 239 gmDDRLFYIYTSGTTGLPKAAIVVHSRYyrMAAFGHHAYRM 279
Cdd:cd05918 106 --SDAAYVIFTSGSTGKPKGVVIEHRAL--STSALAHGRAL 142
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
122-554 |
2.21e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 66.75 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 122 QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEV-SGHLGKSL 200
Cdd:PLN02860 51 RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELqNDRLPSLM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 201 IKFCSGDLGPEGILPDTHLL--DPLLKEASTAPLAQiPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYY-----RMAAFG 273
Cdd:PLN02860 131 WQVFLESPSSSVFIFLNSFLttEMLKQRALGTTELD-YAWAPDDAVLICFTSGTTGRPKGVTISHSALIvqslaKIAIVG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 274 HhayrmQAADVLYDCLPLYH-----SAGNIIGVGQCLiygltvVLRKKFSASRFWdDCIKYNCTINgvrhcrlLCLVVQY 348
Cdd:PLN02860 210 Y-----GEDDVYLHTAPLCHigglsSALAMLMVGACH------VLLPKFDAKAAL-QAIKQHNVTS-------MITVPAM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 349 IGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHV 428
Cdd:PLN02860 271 MADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 429 YPIRLVKVNEdtmellrdAQGLCIpcqaGEP------------GLLVGQINQQDP--LRRFDGYVSESATSKKiahsvfs 494
Cdd:PLN02860 351 NQTKSSSVHQ--------PQGVCV----GKPaphvelkigldeSSRVGRILTRGPhvMLGYWGQNSETASVLS------- 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 495 kgDSAYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 554
Cdd:PLN02860 412 --NDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-588 |
3.57e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.90 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 74 AGHTIPRIFQAVVQRQPERLALVdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM 153
Cdd:PRK12316 4549 ATRCVHQLVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 154 EAALLNVNLRREPLAFCLGTSGAKALIfggemvaavaeVSGHLGKSLIKfcsgdlgPEGIlpDTHLLDPlLKEASTAPLA 233
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLL-----------TQSHLLQRLPI-------PDGL--ASLALDR-DEDWEGFPAH 4685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 234 QIPSKGMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPlYHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK12316 4686 DPAVRLHPDNLAYvIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 313 LRKkfsaSRFWDDciKYNCTINGVRHCRLLCLVVQYIgeicRYLLKQPVREAE-RRHRVRLAVGNGLRPAIWEEFTERFG 391
Cdd:PRK12316 4765 IRD----DSLWDP--ERLYAEIHEHRVTVLVFPPVYL----QQLAEHAERDGEpPSLRVYCFGGEAVAQASYDLAWRALK 4834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 392 VRQIGEFYGATECNCSIANMDGKVGS-CGfnsrilPHVYPIRLVKVNEDTMeLLRDAQGLCIPCQAGEpgLLVGqinqQD 470
Cdd:PRK12316 4835 PVYLFNGYGPTETTVTVLLWKARDGDaCG------AAYMPIGTPLGNRSGY-VLDGQLNPLPVGVAGE--LYLG----GE 4901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 471 PLRRfdGYVSESA-TSKKIAHSVFSK-GDSAYLSGDVL------VMDELGymyfrdRSGDTFRWRGENVSTTEVEgvlSR 542
Cdd:PRK12316 4902 GVAR--GYLERPAlTAERFVPDPFGApGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIE---AR 4970
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 768002382 543 LLGQTDV--AVYgVAVPGVEGKAGMAAV--ADPHsLLDPNAIYQELQKVL 588
Cdd:PRK12316 4971 LREHPAVreAVV-IAQEGAVGKQLVGYVvpQDPA-LADADEAQAELRDEL 5018
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
90-554 |
4.36e-11 |
|
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: 65.63 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKaLIF----GGEMVAAVAEVSGHLGKSLIKFCSGDLGpeGILPD----THLLDPLLKEASTAPlaqiPSKGMD 241
Cdd:cd17642 111 SLNISKPT-IVFcskkGLQKVLNVQKKLKIIKTIIILDSKEDYK--GYQCLytfiTQNLPPGFNEYDFKP----PSFDRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYI-YTSGTTGLPKAAIVVHSRYyrMAAFGH-----HAYRMQAADVLYDCLPLYHSAGNIIGVGQcLIYGLTVVLRK 315
Cdd:cd17642 184 EQVALImNSSGSTGLPKGVQLTHKNI--VARFSHardpiFGNQIIPDTAILTVIPFHHGFGMFTTLGY-LICGFRVVLMY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 316 KFSASRFWDDCIKYNCTingvrhcrllclVVQYIGEICRYLLKQP-VREAERRHRVRLAVGNG-LRPAIWEEFTERFGVR 393
Cdd:cd17642 261 KFEEELFLRSLQDYKVQ------------SALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 394 QIGEFYGATECNCSI---ANMDGKVGSCGfnsRILPHVYpirlVKV-NEDTMELLRdaqglciPCQAGE-----PGLLVG 464
Cdd:cd17642 329 GIRQGYGLTETTSAIlitPEGDDKPGAVG---KVVPFFY----AKVvDLDTGKTLG-------PNERGElcvkgPMIMKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 465 QINqqdplrrfdgyvSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLL 544
Cdd:cd17642 395 YVN------------NPEATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHP 456
|
490
....*....|
gi 768002382 545 GQTDVAVYGV 554
Cdd:cd17642 457 KIFDAGVAGI 466
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
74-625 |
5.32e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.34 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 74 AGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM 153
Cdd:PRK12467 1572 LARLVHQLIEDQAAATPEAVALVFGE--QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGG 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 154 EAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHlgKSLikfcsgdlgpegilpdthLLDPLLKEASTAPLA 233
Cdd:PRK12467 1650 AYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGL--RSL------------------VLDQEDDWLEGYSDS 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 234 QIPSKGMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPlYHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK12467 1710 NPAVNLAPQNLAYvIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 313 LRkKFSASRFWDDCIKYNCTingvRHCRLLCLVVQYIgeicRYLLKQPVREAE-RRHRVRLAVGNGLRPAIWEEFTERFG 391
Cdd:PRK12467 1789 IA-PPGAHRDPEQLIQLIER----QQVTTLHFVPSML----QQLLQMDEQVEHpLSLRRVVCGGEALEVEALRPWLERLP 1859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 392 VRQIGEFYGATEC-------NCSIANMDGKVGScgfnsrilphvyPIRLVKVNEDTMELlrDAQGLCIPCQ-AGEpgLLV 463
Cdd:PRK12467 1860 DTGLFNLYGPTETavdvthwTCRRKDLEGRDSV------------PIGQPIANLSTYIL--DASLNPVPIGvAGE--LYL 1923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 464 GqinqQDPLRRfdGYVSESA-TSKKIAHSVFSKGDS-AYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEgvlS 541
Cdd:PRK12467 1924 G----GVGLAR--GYLNRPAlTAERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE---A 1994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 542 RLLGQTDVAvyGVAVPGVEGKAGMAAVA-----DPHSLLDPNAIY-------QELQKVLAPYARPIFLRLLPQVDTTGTF 609
Cdd:PRK12467 1995 RLREQGGVR--EAVVIAQDGANGKQLVAyvvptDPGLVDDDEAQValrailkNHLKASLPEYMVPAHLVFLARMPLTPNG 2072
|
570
....*....|....*.
gi 768002382 610 KIQKTRLQREgfDPRQ 625
Cdd:PRK12467 2073 KLDRKALPAP--DASE 2086
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
81-554 |
5.69e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 65.46 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 81 IFQAVVQRQPERLALVDagTGECWTFAQLDAYSNA-VANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAalLN 159
Cdd:PRK08974 28 MFEQAVARYADQPAFIN--MGEVMTFRKLEERSRAfAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIV--VN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 160 VNLRREP--LAFCLGTSGAKALI----FGG--EMVAAVAEVsghlgKSLIKFCSGDL--GPEGIL------------PDT 217
Cdd:PRK08974 104 VNPLYTPreLEHQLNDSGAKAIVivsnFAHtlEKVVFKTPV-----KHVILTRMGDQlsTAKGTLvnfvvkyikrlvPKY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 218 HLLDPL-LKEA-STAPLAQI--PSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYrmaafghhAYRMQA----ADVLYD-- 287
Cdd:PRK08974 179 HLPDAIsFRSAlHKGRRMQYvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNML--------ANLEQAkaayGPLLHPgk 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 288 -----CLPLYHsagniigvgqclIYGLTVvlrkkfsasrfwdDCIKY------NCTINGVRHcrllclVVQYIGEICRY- 355
Cdd:PRK08974 251 elvvtALPLYH------------IFALTV-------------NCLLFielggqNLLITNPRD------IPGFVKELKKYp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 356 ---------LLKQPVREAERRH----RVRLAVGNGL--RPAI---WEEFTerfGVRQIgEFYGATECN----CSIANMDG 413
Cdd:PRK08974 300 ftaitgvntLFNALLNNEEFQEldfsSLKLSVGGGMavQQAVaerWVKLT---GQYLL-EGYGLTECSplvsVNPYDLDY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 414 KVGSCGFnsrilPhvYPIRLVKVNEDTMELLrdAQGlcipcQAGE-----PGLLVGQINQQDplrrfdgyvsesATSKki 488
Cdd:PRK08974 376 YSGSIGL-----P--VPSTEIKLVDDDGNEV--PPG-----EPGElwvkgPQVMLGYWQRPE------------ATDE-- 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 489 ahsVFSKGdsaYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 554
Cdd:PRK08974 428 ---VIKDG---WLAtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
78-292 |
7.24e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 64.92 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 78 IPRIFQAVVQRQPERLALVDAGTGECW--------TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLA 149
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADgklaydelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 150 KAGMEAALLNVNLRREPLAFCLGTSGAKALIfgGEMVAAVAEVSGHLGKSLIKF---CSGDLGPEGILPDTHLLDPLLKE 226
Cdd:PRK09274 88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI--GIPKAHLARRLFGWGKPSVRRlvtVGGRLLWGGTTLATLLRDGAAAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 227 ASTAPLAQipskgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLY 292
Cdd:PRK09274 166 FPMADLAP------DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF 225
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-616 |
9.74e-11 |
|
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: 64.19 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALVdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:cd05945 1 AAANPDRPAVV--EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 166 PLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGK---------SLIKFCsgdlgpEGILPDThLLDPLLKEASTAPLAqip 236
Cdd:cd05945 79 RIREILDAAKPALLIADGDDNAYIIFTSGSTGRpkgvqishdNLVSFT------NWMLSDF-PLGPGDVFLNQAPFS--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 237 skgMDDRLFYIYTSGTTGlpkAAIVVHSRyyrmaafghhayrmqaaDVLYDCLPLYHSAGNiigvgqcliYGLTVVlrkk 316
Cdd:cd05945 149 ---FDLSVMDLYPALASG---ATLVPVPR-----------------DATADPKQLFRFLAE---------HGITVW---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 317 FSASRFWDDCIKY-NCTINGVRHCR--LLClvvqyiGEICryllkqPVREAERRHrvrlavgnglrpaiweeftERFGVR 393
Cdd:cd05945 193 VSTPSFAAMCLLSpTFTPESLPSLRhfLFC------GEVL------PHKTARALQ-------------------QRFPDA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 394 QIGEFYGATECNCSIANMdgkvgscgfnsRILPHVY------PIRLVKVNEDTMelLRDAQGLCIPcqAGEPG--LLVGQ 465
Cdd:cd05945 242 RIYNTYGPTEATVAVTYI-----------EVTPEVLdgydrlPIGYAKPGAKLV--ILDEDGRPVP--PGEKGelVISGP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 466 inqqdplRRFDGYVSESATSKKIAHSVfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLG 545
Cdd:cd05945 307 -------SVSKGYLNNPEKTAAAFFPD--EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPG 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768002382 546 QTDVAVygVAVPGVEGKAGMAAVADPH---SLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd05945 378 VKEAVV--VPKYKGEKVTELIAFVVPKpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
90-264 |
1.07e-10 |
|
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: 64.23 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd12116 1 PDATAVRDDD--RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIFGGEMVAAVAevsghlgkslikfcsgdlgpeGILPDTHLLDPLLKEASTAPLAQIPskgmDDRLFY-IY 248
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLP---------------------AGLPVLLLALAAAAAAPAAPRTPVS----PDDLAYvIY 133
|
170
....*....|....*.
gi 768002382 249 TSGTTGLPKAAIVVHS 264
Cdd:cd12116 134 TSGSTGRPKGVVVSHR 149
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
90-616 |
1.25e-10 |
|
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: 64.03 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17656 2 PDAVAVVF--ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALifggemvaaVAEVSghlgkslikfCSGDLGPEGILpdTHLLDPLLKEASTaplAQIPSKGMDDRLFY-IY 248
Cdd:cd17656 80 IMLDSGVRVV---------LTQRH----------LKSKLSFNKST--ILLEDPSISQEDT---SNIDYINNSDDLLYiIY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 249 TSGTTGLPKAAIVVHSryyRMAAFGHHAYRMQAADVLYDCLplyhsagniigvgQCLIYGLTVVLRKKFSASRFWDDC-I 327
Cdd:cd17656 136 TSGTTGKPKGVQLEHK---NMVNLLHFEREKTNINFSDKVL-------------QFATCSFDVCYQEIFSTLLSGGTLyI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 328 KYNCTINGVRhcRLLCLVVQYIGEICRY---LLKQPVREAERRHR----VRLAVGNGLRPAIWEEFTERFGVRQIG--EF 398
Cdd:cd17656 200 IREETKRDVE--QLFDLVKRHNIEVVFLpvaFLKFIFSEREFINRfptcVKHIITAGEQLVITNEFKEMLHEHNVHlhNH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 399 YGATECNCsianmdgkVGSCGFNSRI-LPHVYPIRLVKVNEDTmeLLRDAQGLCIPCqaGEPG-LLVGQINqqdpLRRfd 476
Cdd:cd17656 278 YGPSETHV--------VTTYTINPEAeIPELPPIGKPISNTWI--YILDQEQQLQPQ--GIVGeLYISGAS----VAR-- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 477 GYVS-ESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVA 555
Cdd:cd17656 340 GYLNrQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVV--LD 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 556 VPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:cd17656 418 KADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
83-264 |
2.63e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 63.66 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 83 QAVVQRQPERLALVDAG-TGE--CWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeaALLN 159
Cdd:PRK03584 91 NLLRHRRDDRPAIIFRGeDGPrrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLG---AIWS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 160 VnlrreplafC---LGTSGA---------KALI------FGG---EMVAAVAEVSGHLgKSLIKFCS----GDLGPEGIL 214
Cdd:PRK03584 168 S---------CspdFGVQGVldrfgqiepKVLIavdgyrYGGkafDRRAKVAELRAAL-PSLEHVVVvpylGPAAAAAAL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768002382 215 PDTHLLDPLLKEASTAPL--AQIPskgMDDRLFYIYTSGTTGLPKAaiVVHS 264
Cdd:PRK03584 238 PGALLWEDFLAPAEAAELefEPVP---FDHPLWILYSSGTTGLPKC--IVHG 284
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
89-617 |
3.95e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 62.49 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 89 QPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPgDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLA 168
Cdd:PRK07638 14 QPNKIAIKE--NDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 169 FCLGTSGAkalifggEMVaaVAEvsghlgksliKFCSGDL-GPEGILPDTHLLDPLLKEASTAPLaqiPSKGMDDRLFYI 247
Cdd:PRK07638 91 ERLAISNA-------DMI--VTE----------RYKLNDLpDEEGRVIEIDEWKRMIEKYLPTYA---PIENVQNAPFYM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 248 -YTSGTTGLPKAAIVVHSRYyrMAAF--GHHAYRMQAADVLYDCLPLYHSAgNIIGVGQCLIYGLTVVLRKKFSASrfwd 324
Cdd:PRK07638 149 gFTSGSTGKPKAFLRAQQSW--LHSFdcNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKFIPN---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 325 DCIKYNCTINgvrhcrllcLVVQYIgeiCRYLLKQPVREAERRHRVRLAVGNGlrpAIW-----EEFTERFGVRQIGEFY 399
Cdd:PRK07638 222 QVLDKLETEN---------ISVMYT---VPTMLESLYKENRVIENKMKIISSG---AKWeaeakEKIKNIFPYAKLYEFY 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 400 GATECNCSIANMDGkvgscgfNSRILPHVY--PIRLVKVNedtmelLRDAQGlcIPCQAGEpgllVGQINQQDPLRrFDG 477
Cdd:PRK07638 287 GASELSFVTALVDE-------ESERRPNSVgrPFHNVQVR------ICNEAG--EEVQKGE----IGTVYVKSPQF-FMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 478 YVSESATSKKIAhsvfskgDSAYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAV 556
Cdd:PRK07638 347 YIIGGVLARELN-------ADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768002382 557 PgvegKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 617
Cdd:PRK07638 420 S----YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
69-616 |
7.37e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.95 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 69 RRHQRAGHTIPRIFQAVV---QRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLW 145
Cdd:PRK05857 4 KKFQAMPQLPSTVLDRVFeqaRQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 146 LGLAKAGMEAALLNVNLRREPLA-FCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSG-DLGPEGILPDThlldpl 223
Cdd:PRK05857 84 LACAKLGAIAVMADGNLPIAAIErFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAaVTRESEHSLDA------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 224 lkeastAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR----MAAFGHHAYRMQAADVLYDCLPLYHsAGNII 299
Cdd:PRK05857 158 ------ASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdiLQKEGLNWVTWVVGETTYSPLPATH-IGGLW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 300 GVGQCLIYGLTVVLRKKFSASrfwddcIKYNCTINGVRHCrllCLVVQyigeicryLLKQPVREAERRHRV----RLAVG 375
Cdd:PRK05857 231 WILTCLMHGGLCVTGGENTTS------LLEILTTNAVATT---CLVPT--------LLSKLVSELKSANATvpslRLVGY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 376 NGLRpAIWEE--FTERFGVRQiGEFYGATECNC----------SIANMD-GKVGscgfnsRILP--HVYpirlvkvnedt 440
Cdd:PRK05857 294 GGSR-AIAADvrFIEATGVRT-AQVYGLSETGCtalclptddgSIVKIEaGAVG------RPYPgvDVY----------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 441 melLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFdGYVSESATSKKIAhsvfskGDSAYLSGDVLVMDELGYMYFRDRS 520
Cdd:PRK05857 355 ---LAATDGIGPTAPGAGPSASFGTLWIKSPANML-GYWNNPERTAEVL------IDGWVNTGDLLERREDGFFYIKGRS 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 521 GDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVadPHSLLDPNAIYQELQKVLAPY-------AR 593
Cdd:PRK05857 425 SEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV--ASAELDESAARALKHTIAARFrresepmAR 502
|
570 580
....*....|....*....|...
gi 768002382 594 PIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:PRK05857 503 PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
70-284 |
8.26e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 62.37 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 70 RHQRAGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEgRPEFVGLWL-GL 148
Cdd:PRK10252 452 AVEIPETTLSALVAQQAAKTPDAPALADARYQ--FSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLALhAI 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 149 AKAGmeAALLNVNLRR--EPLAFCLGTSGAKALIfggemvaAVAEVSGHlgkslikfcsgdlgpegiLPDTHLLDPLLKE 226
Cdd:PRK10252 529 VEAG--AAWLPLDTGYpdDRLKMMLEDARPSLLI-------TTADQLPR------------------FADVPDLTSLCYN 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002382 227 ASTAPlAQIPSKGM---DDRLFYIYTSGTTGLPKAAIVVH----SRYYRMaafgHHAYRMQAADV 284
Cdd:PRK10252 582 APLAP-QGAAPLQLsqpHHTAYIIFTSGSTGRPKGVMVGQtaivNRLLWM----QNHYPLTADDV 641
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
86-615 |
1.40e-09 |
|
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: 61.04 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 86 VQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAK---------AG 152
Cdd:cd05966 63 LKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARigavhsvvfAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 153 MEAallnvnlrrEPLAFCLGTSGAKALIF------GGEMV-------AAVAE--------VSGHLGKSlIKFCSG-DLgp 210
Cdd:cd05966 143 FSA---------ESLADRINDAQCKLVITadggyrGGKVIplkeivdEALEKcpsvekvlVVKRTGGE-VPMTEGrDL-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 211 egilpdthLLDPLLKEASTaplaQIPSKGMD--DRLFYIYTSGTTGLPKAaiVVHSR--YYRMAAFGHH---AYRMQ--- 280
Cdd:cd05966 211 --------WWHDLMAKQSP----ECEPEWMDseDPLFILYTSGSTGKPKG--VVHTTggYLLYAATTFKyvfDYHPDdiy 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 281 --AADVlydclplyhsaGNIIG----VGQCLIYGLTVVLrkkF-------SASRFWDDCIKYNCTI-----NGVRhcrll 342
Cdd:cd05966 277 wcTADI-----------GWITGhsyiVYGPLANGATTVM---FegtptypDPGRYWDIVEKHKVTIfytapTAIR----- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 343 clvvqyigeicryLLKQPVREAERRH-----RVRLAVGNGLRPAIWEEFTERFGVRQ--IGEFYGATEC-NCSIANMDG- 413
Cdd:cd05966 338 -------------ALMKFGDEWVKKHdlsslRVLGSVGEPINPEAWMWYYEVIGKERcpIVDTWWQTETgGIMITPLPGa 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 414 ---KVGSCGFNsriLPHVYPirlVKVNEDTMELLRDAQG-LCIpcQAGEPGLLVGQINqqDPLRRFDGYvsesatskkia 489
Cdd:cd05966 405 tplKPGSATRP---FFGIEP---AILDEEGNEVEGEVEGyLVI--KRPWPGMARTIYG--DHERYEDTY----------- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 490 hsvFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLsrllgqtdvavygVAVPGVegkAGMAAVA 569
Cdd:cd05966 464 ---FSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL-------------VAHPAV---AEAAVVG 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 570 DPHSlLDPNAIY----------------QEL----QKVLAPYARP---IFLRLLPqvdttgtfkiqKTR 615
Cdd:cd05966 525 RPHD-IKGEAIYafvtlkdgeepsdelrKELrkhvRKEIGPIATPdkiQFVPGLP-----------KTR 581
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-263 |
1.43e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 72 QRAGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKA 151
Cdd:PRK05691 2184 ARLDQTLHGLFAAQAARTPQAPALTFAG--QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 152 GMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEvsghLGKSLIKFCSGDLGPegilpdthlldpLLKEASTAP 231
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGE----LPAGVARWCLEDDAA------------ALAAYSDAP 2325
|
170 180 190
....*....|....*....|....*....|..
gi 768002382 232 LAQIpsKGMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:PRK05691 2326 LPFL--SLPQHQAYLIYTSGSTGKPKGVVVSH 2355
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
242-613 |
1.59e-09 |
|
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: 59.97 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVHSRYYrmAAFGH---HAYRMQAADVLYDCLPLYHSaGNIIGVGQCLIY-GLTVVLRKKF 317
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFF--AVPDIlqkEGLNWVVGDVTYLPLPATHI-GGLWWILTCLIHgGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 318 SASRFWDDCIKYNCTIngvrhcrlLCLVVQYIGEICRyLLKQPVREAERrhrVRLAVGNGLRP-AIWEEFTERFGVRQIG 396
Cdd:cd17635 79 TYKSLFKILTTNAVTT--------TCLVPTLLSKLVS-ELKSANATVPS---LRLIGYGGSRAiAADVRFIEATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 397 EFYGATECN--CSIANMDG--KVGSCGfnsrilpHVYPIRLVKVnedtmellRDAQGLCIPcqAGEPGLLVGQINqqdpl 472
Cdd:cd17635 147 QVYGLSETGtaLCLPTDDDsiEINAVG-------RPYPGVDVYL--------AATDGIAGP--SASFGTIWIKSP----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 473 RRFDGYVSESA-TSKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 551
Cdd:cd17635 205 ANMLGYWNNPErTAEVLIDGWVNTGDLGERRED-------GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAC 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002382 552 YgvAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKV---LAPYARPIFLRLLPQVDTTGTFKIQK 613
Cdd:cd17635 278 Y--EISDEEFGELVGLAVVASAELDENAIRALKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-264 |
1.85e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.51 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 78 IPRIFQAVVQRQPERLALVdagTGE-CWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALA---FGEeTLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNVNLRREPLAFCLGTSGAKALIfggemvaavaeVSGHLGKSLikfcSGDLGPEGILPDThlLDPLLKEASTAPlaqiP 236
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDSGVQLLL-----------SQSHLGRKL----PLAAGVQVLDLDR--PAAWLEGYSEEN----P 648
|
170 180 190
....*....|....*....|....*....|
gi 768002382 237 SKGMD-DRLFY-IYTSGTTGLPKAAIVVHS 264
Cdd:PRK12316 649 GTELNpENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
90-557 |
4.55e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 59.26 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGTGECWTfAQLDAYSNAVANLFrQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:PLN03102 28 PNRTSIIYGKTRFTWP-QTYDRCCRLAASLI-SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIFGGEMVAAVAEVSghlgkSLIKFCSGDLGPEGILpdTHLLD----PLLKEASTAPLAQI--PSKGMDDR 243
Cdd:PLN03102 106 ILRHAKPKILFVDRSFEPLAREVL-----HLLSSEDSNLNLPVIF--IHEIDfpkrPSSEELDYECLIQRgePTPSLVAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 244 LFYI----------YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL 313
Cdd:PLN03102 179 MFRIqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 314 RKKFSASrfwddcIKYNCTINGVRHcrlLCLVvqyiGEICRYLLK-QPVREAERRHRVRLAVGNGLRPAIWEEFTERFGV 392
Cdd:PLN03102 259 RHVTAPE------IYKNIEMHNVTH---MCCV----PTVFNILLKgNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 393 rQIGEFYGATECNcsianmdGKVGSCGFNSRI--LPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEP--GLLVGQINQ 468
Cdd:PLN03102 326 -QVMHAYGLTEAT-------GPVLFCEWQDEWnrLPENQQMELKARQGVSILGLADVDVKNKETQESVPrdGKTMGEIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 469 QDPLrRFDGYVSE-SATSKKIAHSVFSkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQT 547
Cdd:PLN03102 398 KGSS-IMKGYLKNpKATSEAFKHGWLN-------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVL 469
|
490
....*....|
gi 768002382 548 DVAVygVAVP 557
Cdd:PLN03102 470 ETAV--VAMP 477
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
104-617 |
4.67e-09 |
|
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: 59.40 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALiFGG 183
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL-FVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 184 EMVAAVAEVSGhLGKSLIkfcSGDLGPEGILPDTHLLDPLLKEAstAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05932 86 KLDDWKAMAPG-VPEGLI---SISLPPPSAANCQYQWDDLIAQH--PPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 264 SRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTV------------VLRKK----FSASRFWddcI 327
Cdd:cd05932 160 GSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlfFSVPRLW---T 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 328 KYNCTIN---GVRHCRLLcLVVQYIGEicryLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFtERFGVrQIGEFYGAT 402
Cdd:cd05932 237 KFQQGVQdkiPQQKLNLL-LKIPVVNS----LVKRKVLKGLGLDQCRLAGCGSapVPPALLEWY-RSLGL-NILEAYGMT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 403 EcNCSIANM----DGKVGSCGFNsrilphvYPIRLVKVNEDTMELLRdaqglcipcqagEPGLLVGQinqqdplrrfdgY 478
Cdd:cd05932 310 E-NFAYSHLnypgRDKIGTVGNA-------GPGVEVRISEDGEILVR------------SPALMMGY------------Y 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 479 VSESATSkkiahSVFSKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEGVLSR--------LLGQTDV 549
Cdd:cd05932 358 KDPEATA-----EAFTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEhdrvemvcVIGSGLP 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768002382 550 AVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQ---VDT---TGTFKIQKTRLQ 617
Cdd:cd05932 432 APLALVVLSEEARLRADAFARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDpwsIDNgilTPTLKIKRNVLE 505
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
87-341 |
6.11e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 58.73 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 87 QRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREP 166
Cdd:PRK09029 14 QVRPQAIALRLND--EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 167 LafclgtsgakalifggemvaavAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAP--LAQIpskgmddrl 244
Cdd:PRK09029 92 L----------------------EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPqrLATM--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 245 fyIYTSGTTGLPKAaiVVHSryyrmaafgHHAYRMQAADVL----YDC-------LPLYHSAGNIIgVGQCLIYGLTVVL 313
Cdd:PRK09029 141 --TLTSGSTGLPKA--AVHT---------AQAHLASAEGVLslmpFTAqdswllsLPLFHVSGQGI-VWRWLYAGATLVV 206
|
250 260
....*....|....*....|....*...
gi 768002382 314 RKKfsaSRFWDDcikynctINGVRHCRL 341
Cdd:PRK09029 207 RDK---QPLEQA-------LAGCTHASL 224
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
90-271 |
1.24e-08 |
|
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: 57.65 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17652 1 PDAPAVVFGD--ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 170 CLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeasTAPlaqipskgmdDRLFY-IY 248
Cdd:cd17652 79 MLADARPALLL------------------------------------------------TTP----------DNLAYvIY 100
|
170 180
....*....|....*....|...
gi 768002382 249 TSGTTGLPKAAIVVHSRYYRMAA 271
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLAA 123
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
76-554 |
1.38e-08 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 57.96 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 76 HTIPRIFQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMe 154
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYHSFGK--TITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 155 aALLNVNLRREP--LAFCLGTSGAKALI----FGGEMVAAVAEVSGhlgKSLIKFCSGDL--GPEGIL------------ 214
Cdd:PRK08751 102 -TVVNVNPLYTPreLKHQLIDSGASVLVvidnFGTTVQQVIADTPV---KQVITTGLGDMlgFPKAALvnfvvkyvkklv 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 215 PDTHLLDPL-LKEA------STAPLAQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHH-----AYRMQAA 282
Cdd:PRK08751 178 PEYRINGAIrFREAlalgrkHSMPTLQIEP---DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagtGKLEEGC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 283 DVLYDCLPLYH----SAGNII--GVGQC--LIY------GLTVVLRK-KFSAsrfwddCIKYNCTINGvrhcrllclvvq 347
Cdd:PRK08751 255 EVVITALPLYHifalTANGLVfmKIGGCnhLISnprdmpGFVKELKKtRFTA------FTGVNTLFNG------------ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 348 yigeicryLLKQPVREAERRHRVRLAVGNGL--RPAIWEEFTERFGVRQIgEFYGATECNCSIA----NMDGKVGSCGFn 421
Cdd:PRK08751 317 --------LLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTGLTLV-EAYGLTETSPAACinplTLKEYNGSIGL- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 422 srilphvyPIrlvkvnEDTMELLRDAQGLCIPcqAGEpgllVGQINQQDPlRRFDGYVSESATSKKIAHSvfskgDSAYL 501
Cdd:PRK08751 387 --------PI------PSTDACIKDDAGTVLA--IGE----IGELCIKGP-QVMKGYWKRPEETAKVMDA-----DGWLH 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 768002382 502 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 554
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGV 493
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
101-571 |
1.54e-08 |
|
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: 57.45 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALi 180
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 181 fggemvaavaevsghlgkslikFCSgdlgpegilpdthllDPllkeastaplaqipskgmDDRLFYIYTSGTTGLPKAAI 260
Cdd:cd05914 84 ----------------------FVS---------------DE------------------DDVALINYTSGTTGNSKGVM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFwDDCIKYNCTIN-GVrhC 339
Cdd:cd05914 109 LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI-IALAFAQVTPTlGV--P 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 340 RLLCLVVQYIGEIC--------RYLLKQPVREAERRHRVRLAV--------------GNGLRPAIwEEFTERFGVRQIgE 397
Cdd:cd05914 186 VPLVIEKIFKMDIIpkltlkkfKFKLAKKINNRKIRKLAFKKVheafggnikefvigGAKINPDV-EEFLRTIGFPYT-I 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 398 FYGATECN---CSIANMDGKVGSCGFnsrilphvyPIRLVKVNEDtmellrdaqglcipcqAGEPGLLVGQINQQDPLRR 474
Cdd:cd05914 264 GYGMTETApiiSYSPPNRIRLGSAGK---------VIDGVEVRID----------------SPDPATGEGEIIVRGPNVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 475 FDGYVSESATSkkiahSVFSKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEgvlSRLLGQTDVAVYG 553
Cdd:cd05914 319 KGYYKNPEATA-----EAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIE---AKINNMPFVLESL 389
|
490
....*....|....*...
gi 768002382 554 VAVpgVEGKAGMAAVADP 571
Cdd:cd05914 390 VVV--QEKKLVALAYIDP 405
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
105-264 |
2.02e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 57.29 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 185 MVAAVAEVSGHLG-KSLIKFCSGDLgPEG-------ILPDTHLLDPLLKEASTAPLAqIPSKGmDDRLFYIYTSGTTGLP 256
Cdd:PTZ00216 203 NVPNLLRLMKSGGmPNTTIIYLDSL-PASvdtegcrLVAWTDVVAKGHSAGSHHPLN-IPENN-DDLALIMYTSGTTGDP 279
|
....*...
gi 768002382 257 KAaiVVHS 264
Cdd:PTZ00216 280 KG--VMHT 285
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
535-610 |
2.46e-08 |
|
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: 51.39 E-value: 2.46e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768002382 535 EVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMA-AVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFK 610
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
106-296 |
4.94e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.17 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 106 FAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVnlrrePLAF------------CLGT 173
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL-----PMGFggresyiaqlrgMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 174 SGAKALIFGGEMVAAVAEVSGHLGkslikfcsgdlGPEGILPDthllDPLLKEASTAPLAQI-PskgmDDRLFYIYTSGT 252
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHGNP-----------LLHVLSHA----WFKALPEADVALPRPtP----DDIAYLQYSSGS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768002382 253 TGLPKAAIVVHSRYyrMA---AFGHHAYRMQAADVLYDCLPLYHSAG 296
Cdd:PRK09192 188 TRFPRGVIITHRAL--MAnlrAISHDGLKVRPGDRCVSWLPFYHDMG 232
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
78-619 |
5.17e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 55.92 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 78 IPRIFQAVVQRQPERLALvdAGTGECWTFAQLDAYSNAVANLFRQL-GFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaA 156
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAF--SNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGL--I 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNVN---LRREpLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGDLG-------------------PEGI 213
Cdd:PRK05677 102 VVNTNplyTARE-MEHQFNDSGAKALVCLANMAHLAEKVLPKTGvKHVIVTEVADMLpplkrllinavvkhvkkmvPAYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 214 LPDTHLLDPLLKEASTAPLAQIPSKGmDDRLFYIYTSGTTGLPKAAIVVHSRyyrMAAFGHHAYRMQAADVLYDC----- 288
Cdd:PRK05677 181 LPQAVKFNDALAKGAGQPVTEANPQA-DDVAVLQYTGGTTGVAKGAMLTHRN---LVANMLQCRALMGSNLNEGCeilia 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 289 -LPLYH--------SAGNIIGVGQCLIY------GLTVVLRK-KFSASRFWDDCIKYNCTINGVRHCRLLCLVVQYIGEI 352
Cdd:PRK05677 257 pLPLYHiyaftfhcMAMMLIGNHNILISnprdlpAMVKELGKwKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGM 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 353 CrylLKQPVreAERrhrvrlavgnglrpaiWEEFTerfGVrQIGEFYGATECN--CSIANMDG-KVGSCGfnsriLPhvY 429
Cdd:PRK05677 337 A---LQLAT--AER----------------WKEVT---GC-AICEGYGMTETSpvVSVNPSQAiQVGTIG-----IP--V 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 430 PIRLVKV-NEDTMELLRDAQG-LCIPcqagEPGLLVGQINQQDplrrfdgyvsesATSKKIAHSVFSKgdsaylSGDVLV 507
Cdd:PRK05677 385 PSTLCKViDDDGNELPLGEVGeLCVK----GPQVMKGYWQRPE------------ATDEILDSDGWLK------TGDIAL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 508 MDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAvpgvEGKAGMA----AVADPHSLLDPNAIYQE 583
Cdd:PRK05677 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSGEAikvfVVVKPGETLTKEQVMEH 518
|
570 580 590
....*....|....*....|....*....|....*.
gi 768002382 584 LQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 619
Cdd:PRK05677 519 MRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
85-601 |
7.34e-08 |
|
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: 55.40 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 85 VVQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNV 160
Cdd:cd05967 60 VEAGRGDQIALIydspVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 161 NLRREPLAFCLGTSGAKALI---FGGE---------MVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLL-DPLLKEA 227
Cdd:cd05967 140 GFAAKELASRIDDAKPKLIVtasCGIEpgkvvpykpLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDLDwSELLAKA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 228 STAPLAQIPSkgmDDRLFYIYTSGTTGLPKAaiVV-----HS--RYYRMAafghHAYRMQAADVLYdclplyhsAGNIIG 300
Cdd:cd05967 220 EPVDCVPVAA---TDPLYILYTSGTTGKPKG--VVrdnggHAvaLNWSMR----NIYGIKPGDVWW--------AASDVG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 301 --VGQCLI-YG------LTVVLRKKFS----ASRFWDDCIKYnctinGVRHcrLLCLVVQYigeicRYLLKQPVREAE-R 366
Cdd:cd05967 283 wvVGHSYIvYGpllhgaTTVLYEGKPVgtpdPGAFWRVIEKY-----QVNA--LFTAPTAI-----RAIRKEDPDGKYiK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 367 RH-----RVRLAVGNGLRPAIWEEFTERFGVRQIgEFYGATE------CNCS-IANMDGKVGSCGfnsriLPhvYPIRLV 434
Cdd:cd05967 351 KYdlsslRTLFLAGERLDPPTLEWAENTLGVPVI-DHWWQTEtgwpitANPVgLEPLPIKAGSPG-----KP--VPGYQV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 435 KVNEDTMEllrdaqglciPCQAGEPGLLV-------GQINQ--QDPLRRFDGYvsesatskkiahsvFSKGDSAYLSGDV 505
Cdd:cd05967 423 QVLDEDGE----------PVGPNELGNIViklplppGCLLTlwKNDERFKKLY--------------LSKFPGYYDTGDA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 506 LVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVaVPGVEGKAGMA-AVADPHSLLDPNAIYQEL 584
Cdd:cd05967 479 GYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGV-RDELKGQVPLGlVVLKEGVKITAEELEKEL 557
|
570 580
....*....|....*....|....
gi 768002382 585 QKV----LAPYARP---IFLRLLP 601
Cdd:cd05967 558 VALvreqIGPVAAFrlvIFVKRLP 581
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
47-616 |
1.28e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 54.62 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 47 VCKTARRDLFGLSVLI----RVRLELRRHQRAGHTIPRIFQAVVQ-RQPERLALVDAGTGecWTFAQLDAYSNAVANLFR 121
Cdd:PRK13383 1 VAPTAARALVRSGLLNppspRAVLRLLREASRGGTNPYTLLAVTAaRWPGRTAIIDDDGA--LSYRELQRATESLARRLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 122 QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlGKSLI 201
Cdd:PRK13383 79 RDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGA----DDAVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 202 KfcsgdlgpegILPDTHLLDPLLKEASTAPLAQIpskgmddrlfYIYTSGTTGLPKAaivVHSRYYRMAAFG-----HHA 276
Cdd:PRK13383 155 V----------IDPATAGAEESGGRPAVAAPGRI----------VLLTSGTTGKPKG---VPRAPQLRSAVGvwvtiLDR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 277 YRMQAADVLYDCLPLYHSagniIGVGQCLI---YGLTVVLRKKFSASrfwddcikynCTINGVRHCRLLCLVVQYIgeIC 353
Cdd:PRK13383 212 TRLRTGSRISVAMPMFHG----LGLGMLMLtiaLGGTVLTHRHFDAE----------AALAQASLHRADAFTAVPV--VL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 354 RYLLKQPVREAERRH----RVRLAVGNGLRPAIWEEFTERFGvRQIGEFYGATECNcsianmdgkVGSCGfnsrilphvy 429
Cdd:PRK13383 276 ARILELPPRVRARNPlpqlRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVG---------IGALA---------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 430 pirlvkvnedTMELLRDAqglciPCQAGEPglLVGQinqqdPLRRFDGY---VSESATSK-----KIAHSVFSKG----- 496
Cdd:PRK13383 336 ----------TPADLRDA-----PETVGKP--VAGC-----PVRILDRNnrpVGPRVTGRifvggELAGTRYTDGggkav 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 497 -DSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLL 575
Cdd:PRK13383 394 vDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGV 473
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 768002382 576 DPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 616
Cdd:PRK13383 474 DAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
76-296 |
1.62e-07 |
|
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: 54.21 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 76 HTIPRIFQAVVQRQPERLALV------DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFV-GLWlGL 148
Cdd:cd05906 6 EGAPRTLLELLLRAAERGPTKgityidADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIpAFW-AC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 149 AKAGMEAALLNV-------NLRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkslikfcsgdLGPEGILPDTHLLD 221
Cdd:cd05906 85 VLAGFVPAPLTVpptydepNARLRKLRHIWQLLGSPVVLTDAELVAEFAGL---------------ETLSGLPGIRVLSI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002382 222 PLLKEasTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAG 296
Cdd:cd05906 150 EELLD--TAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
116-553 |
1.73e-07 |
|
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: 54.36 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 116 VANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAaVAEVSGH 195
Cdd:cd05915 37 LMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLP-LVEAIRG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 196 LGKSLIKFCSGDLGPEGILPDTHLLDPLLKeastaplaqiPSKGMD--DRLFYIYTSGTTGLPKAAIVVH-SRYYRMAAF 272
Cdd:cd05915 116 ELKTVQHFVVMDEKAPEGYLAYEEALGEEA----------DPVRVPerAACGMAYTTGTTGLPKGVVYSHrALVLHSLAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 273 GHHAYRMQAADVLYDC-LPLYHSAGniigvgQCLIY------GLTVVLRKKFSASRFWDDCIKYNCTINGvrhcrllclv 345
Cdd:cd05915 186 SLVDGTALSEKDVVLPvVPMFHVNA------WCLPYaatlvgAKQVLPGPRLDPASLVELFDGEGVTFTA---------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 346 vqyiGEICRYLLKQPVREAERRH---RVRLAVGNGLRPAIWEEFtERFGVRQIGEFYGATEcncsianMDGKVGSCGFNS 422
Cdd:cd05915 250 ----GVPTVWLALADYLESTGHRlktLRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTE-------TSPVVVQNFVKS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 423 R--ILPHVYPIRLVKvnEDTMELLRDAQGLCIPCQAGEPGllVGQINQQDPLRR---FDGYVSESATSKKIAhsvFSKGd 497
Cdd:cd05915 318 HleSLSEEEKLTLKA--KTGLPIPLVRLRVADEEGRPVPK--DGKALGEVQLKGpwiTGGYYGNEEATRSAL---TPDG- 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 768002382 498 sAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYG 553
Cdd:cd05915 390 -FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
83-335 |
2.27e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 83 QAVVQR---QPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGfAPGDVVAIFLEGRPEFVGLWLGLAKAGMEA 155
Cdd:PRK05691 13 QALQRRaaqTPDRLALRfladDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 156 A---------------LLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAevsghlgkslikfcsgdlgPEGILPDThlL 220
Cdd:PRK05691 92 VpayppesarrhhqerLLSIIADAEPRLLLTVADLRDSLLQMEELAAANA-------------------PELLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 221 DPLLKEASTAPlaQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAA--DVLYDCLPLYHSAGNI 298
Cdd:PRK05691 151 DPALAEAWQEP--ALQP---DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLI 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 768002382 299 IGVGQCLIYGLTVVLrkkFSASRF------WDDCI-KYNCTING 335
Cdd:PRK05691 226 GGLLQPIFSGVPCVL---MSPAYFlerplrWLEAIsEYGGTISG 266
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
105-294 |
3.62e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 53.22 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 185 MVAAVAEVSGHLG--KSLIKFCSGDLGPEGILPDTHLLDPLLKEAStaplAQIPSKGMDDRLF--YIYTSGTTGLPKAAI 260
Cdd:PRK06018 121 FVPILEKIADKLPsvERYVVLTDAAHMPQTTLKNAVAYEEWIAEAD----GDFAWKTFDENTAagMCYTSGTTGDPKGVL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768002382 261 ------VVHSryyrMAAFGHHAYRMQAADVLYDCLPLYHS 294
Cdd:PRK06018 197 yshrsnVLHA----LMANNGDALGTSAADTMLPVVPLFHA 232
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
81-436 |
9.72e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 52.28 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 81 IFQAVVQ----RQPERLALVDAGTGECwTFAQLDAYSNAVANLFRQlGFAPGDVVAIFLegrPEFVGL---WLGLAKAGM 153
Cdd:PRK06814 633 LFEALIEaakiHGFKKLAVEDPVNGPL-TYRKLLTGAFVLGRKLKK-NTPPGENVGVML---PNANGAavtFFALQSAGR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 154 EAALLN-----VNLrrepLAFC-------LGTSgaKALIFGGEMVAAVAEVSGHLgkSLIKFcsgdlgpEGILPDTHLLD 221
Cdd:PRK06814 708 VPAMINfsagiANI----LSACkaaqvktVLTS--RAFIEKARLGPLIEALEFGI--RIIYL-------EDVRAQIGLAD 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 222 PLL-KEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMAA---FGhhayrmqAADVLYDCLPLYH 293
Cdd:PRK06814 773 KIKgLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAAridFS-------PEDKVFNALPVFH 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 294 SAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIkY--NCTI--------NG---VRHcrllclvvQYIGEICRYLL--K 358
Cdd:PRK06814 846 SFGLTGGLVLPLLSGVKVFLYPSPLHYRIIPELI-YdtNATIlfgtdtflNGyarYAH--------PYDFRSLRYVFagA 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 359 QPVREAERRhrvrlavgnglrpaIWeefTERFGVRqIGEFYGATECNCSIA-N--MDGKVGSCGfnsRILPHVYPiRLVK 435
Cdd:PRK06814 917 EKVKEETRQ--------------TW---MEKFGIR-ILEGYGVTETAPVIAlNtpMHNKAGTVG---RLLPGIEY-RLEP 974
|
.
gi 768002382 436 V 436
Cdd:PRK06814 975 V 975
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
105-293 |
1.34e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 51.45 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGF--APGDVVAIFLEGRPEfvglWLGLAKAGMEAALLNVnlrrePLafcLGTSGAKALIFg 182
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPE----WIISELACYAYSLVTV-----PL---YDTLGPEAIEY- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 183 gemVAAVAEVSghlgkslIKFCSGDLgpegilpDTHLLDPLLKEASTAPLAQIPSKGMDdrLFYI-YTSGTTGLPKAAIV 261
Cdd:cd05927 74 ---ILNHAEIS-------IVFCDAGV-------KVYSLEEFEKLGKKNKVPPPPPKPED--LATIcYTSGTTGNPKGVML 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 768002382 262 VH----SRYYRMAAFGHHAYRMQAADVLYDCLPLYH 293
Cdd:cd05927 135 THgnivSNVAGVFKILEILNKINPTDVYISYLPLAH 170
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
247-620 |
1.46e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 51.14 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 247 IYTSGTTGLPKAaiVVHSRyyRMAAFG----HHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRF 322
Cdd:PRK07787 134 VYTSGTTGPPKG--VVLSR--RAIAADldalAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 323 WDDCIKYNCTINGV-----RhcrllclvvqyigeicrylLKQPVREAERRHRVRLAV-GNGLRPA-IWEEFTERFGVRQI 395
Cdd:PRK07787 210 AQALSEGGTLYFGVptvwsR-------------------IAADPEAARALRGARLLVsGSAALPVpVFDRLAALTGHRPV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 396 gEFYGATEC--NCSI-ANMDGKVGSCGFnsrilphvyPIRLVKVNedtmelLRDAQGLCIPCQaGEPgllVGQINQQDPL 472
Cdd:PRK07787 271 -ERYGMTETliTLSTrADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD-GET---VGELQVRGPT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 473 rRFDGYVSE-SATSkkiahSVFSkGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEGVlsrLLGQTDVA 550
Cdd:PRK07787 331 -LFDGYLNRpDATA-----AAFT-ADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETA---LLGHPGVR 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768002382 551 vyGVAVPGVE----GKAGMAAVAdPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREG 620
Cdd:PRK07787 401 --EAAVVGVPdddlGQRIVAYVV-GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
241-618 |
2.12e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 51.05 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 241 DDRLFYIYTSGTTGLPKAAIVVHSRY--YRMAAFgHHAYRMQAADVLY---DClplyhsaGNIIGVGQC----LIYGLTV 311
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmvYTATTF-KYAFDYKPTDVYWctaDC-------GWITGHSYVtygpMLNGATV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 312 VLRKKF----SASRFWDDCIKYNCTIngvrhcrlLCLVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFT 387
Cdd:PLN02654 347 LVFEGApnypDSGRCWDIVDKYKVTI--------FYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 388 ERFGvrqigefygatECNCSIANMDGKVGSCGFNSRILPHVYP------------IRLVKVNEDTMELLRDAQG-LCIpc 454
Cdd:PLN02654 419 NVVG-----------DSRCPISDTWWQTETGGFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEIEGECSGyLCV-- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 455 QAGEPGL---LVGQINQQDP--LRRFDGYvsesatskkiahsvfskgdsaYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 529
Cdd:PLN02654 486 KKSWPGAfrtLYGDHERYETtyFKPFAGY---------------------YFSGDGCSRDKDGYYWLTGRVDDVINVSGH 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 530 NVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVadphSLLDPNAIYQELQKVL--------APYARPIFLRLLP 601
Cdd:PLN02654 545 RIGTAEVESALVSHPQCAEAAVVGIEHE-VKGQGIYAFV----TLVEGVPYSEELRKSLiltvrnqiGAFAAPDKIHWAP 619
|
410
....*....|....*..
gi 768002382 602 QVDTTGTFKIQKTRLQR 618
Cdd:PLN02654 620 GLPKTRSGKIMRRILRK 636
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
247-568 |
2.68e-06 |
|
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: 49.96 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGniIGVGQCLIY--GLTVVLRKkFSASRFWD 324
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 325 DCIKYNCTingvrhcrllclvvqYIGE---ICRYLLkqpvrEAERRHRVRLAvgnGLR-------PAIWEEFTERFGvrq 394
Cdd:cd17637 83 LIEEEKVT---------------LMGSfppILSNLL-----DAAEKSGVDLS---SLRhvlgldaPETIQRFEETTG--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 395 iGEF---YGATECNC--SIANMDGKVGSCGfnsRILPHVyPIRLVKVNEDtmellrdaqglciPCQAGEPGllvgQINQQ 469
Cdd:cd17637 137 -ATFwslYGQTETSGlvTLSPYRERPGSAG---RPGPLV-RVRIVDDNDR-------------PVPAGETG----EIVVR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 470 DPLRrFDGYVSESATSkkiAHSvFSKGdsAYLSGDVLVMDELGYMYFRDRSG--DTFRWRGENVSTTEVEGVLSRLLGQT 547
Cdd:cd17637 195 GPLV-FQGYWNLPELT---AYT-FRNG--WHHTGDLGRFDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIA 267
|
330 340
....*....|....*....|.
gi 768002382 548 DVAVYGvaVPGVEGKAGMAAV 568
Cdd:cd17637 268 EVCVIG--VPDPKWGEGIKAV 286
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
242-554 |
5.47e-06 |
|
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: 48.92 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG--------------HHAYRMQAADVLYDCLPLYHSAGNIIGVGQcLIY 307
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGadfgtgeftpsedaHKAAAAAAGTVMFPAPPLMHGTGSWTAFGG-LLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 308 GLTVVL-RKKFSASRFWDDCIKYNCTingvrhcrllclVVQYIGEIcrylLKQPVREAERRHRVR-----LAVGNG---L 378
Cdd:cd05924 83 GQTVVLpDDRFDPEEVWRTIEKHKVT------------SMTIVGDA----MARPLIDALRDAGPYdlsslFAISSGgalL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 379 RPAIWEEFTERFGVRQIGEFYGATEC-NCSIANMDGKVGSCGFNSRILPhvypiRLVKVNEDTMELLRDAQGlcipcqag 457
Cdd:cd05924 147 SPEVKQGLLELVPNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP-----DTVVLDDDGRVVPPGSGG-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 458 epgllVGQINQQD--PLrrfdGYVSEsatSKKIAHSVFSKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 534
Cdd:cd05924 214 -----VGWIARRGhiPL----GYYGD---EAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPE 281
|
330 340
....*....|....*....|
gi 768002382 535 EVEGVLSRLLGQTDVAVYGV 554
Cdd:cd05924 282 EVEEALKSHPAVYDVLVVGR 301
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
81-293 |
1.24e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 48.28 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 81 IFQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQ-LGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaALLN 159
Cdd:PRK12492 29 VFERSCKKFADRPAFSNLGV--TLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGL--IVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 160 VN---LRREpLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGDLGP--------------EGILPDTHL-- 219
Cdd:PRK12492 105 TNplyTARE-MRHQFKDSGARALVYLNMFGKLVQEVLPDTGiEYLIEAKMGDLLPaakgwlvntvvdkvKKMVPAYHLpq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 220 ---LDPLLKEASTAPLAQIPsKGMDDRLFYIYTSGTTGLPKAAIVVHSR--------YYRMAAFGHHAYRM--QAADVLY 286
Cdd:PRK12492 184 avpFKQALRQGRGLSLKPVP-VGLDDIAVLQYTGGTTGLAKGAMLTHGNlvanmlqvRACLSQLGPDGQPLmkEGQEVMI 262
|
....*..
gi 768002382 287 DCLPLYH 293
Cdd:PRK12492 263 APLPLYH 269
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
78-272 |
1.62e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 48.14 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 78 IPRIFQAVVQRQPERLALVDAGTGEC-------WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAK 150
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVETPSFLDpssktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 151 AGmeaALLNVNLRREPLA---FCLGTSGAKALIfggemvaaVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDP----- 222
Cdd:TIGR03443 318 AG---ATFSVIDPAYPPArqtIYLSVAKPRALI--------VIEKAGTLDQLVRDYIDKELELRTEIPALALQDDgslvg 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 223 -LLKEASTAPLAQIPSK---------GMDDRLFYIYTSGTTGLPKAaivVHSRYYRMAAF 272
Cdd:TIGR03443 387 gSLEGGETDVLAPYQALkdtptgvvvGPDSNPTLSFTSGSEGIPKG---VLGRHFSLAYY 443
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
73-299 |
5.76e-05 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 46.29 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 73 RAGHTIPRIFQAVVQRQPERLAL--------VDAGTG----------ECWTFAQLDAYSNAVANLFR-QLGFAPGDVVAI 133
Cdd:cd17632 19 RPGLRLAQIIATVMTGYADRPALgqratelvTDPATGrttlrllprfETITYAELWERVGAVAAAHDpEQPVRPGDFVAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 134 FLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMV-AAVAEVSGHLG-KSLIKFcsgDLGPE 211
Cdd:cd17632 99 LGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLdLAVEAVLEGGTpPRLVVF---DHRPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 212 GilpDTH-------------------LLDPLLKEASTAPLAQIPSKGMD-DRL-FYIYTSGTTGLPKAAIVVHSRYYRM- 269
Cdd:cd17632 176 V---DAHraalesarerlaavgipvtTLTLIAVRGRDLPPAPLFRPEPDdDPLaLLIYTSGSTGTPKGAMYTERLVATFw 252
|
250 260 270
....*....|....*....|....*....|.
gi 768002382 270 -AAFGHHAYRMQAADVLyDCLPLYHSAGNII 299
Cdd:cd17632 253 lKVSSIQDIRPPASITL-NFMPMSHIAGRIS 282
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
496-611 |
9.33e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 45.41 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 496 GDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVADPHSLl 575
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDP-VAGERVKAKVISHEEI- 366
|
90 100 110
....*....|....*....|....*....|....*.
gi 768002382 576 DPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKI 611
Cdd:PRK08308 367 DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
88-263 |
1.13e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.49 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 88 RQPERLALvdaGTGECWTFAQ-LDAYSNAVANLFrQLGFAPGDVVAIFLEGRPEfvglWLGLAKAGMEAALLNV----NL 162
Cdd:PLN02387 94 RKFEKLHL---GEYEWITYGQvFERVCNFASGLV-ALGHNKEERVAIFADTRAE----WLIALQGCFRQNITVVtiyaSL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 163 RREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG--KSLIkfCSGDLGPEGILPDTHL-------LDPLLKEASTAPL- 232
Cdd:PLN02387 166 GEEALCHSLNETEVTTVICDSKQLKKLIDISSQLEtvKRVI--YMDDEGVDSDSSLSGSsnwtvssFSEVEKLGKENPVd 243
|
170 180 190
....*....|....*....|....*....|.
gi 768002382 233 AQIPSKgmDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:PLN02387 244 PDLPSP--NDIAVIMYTSGSTGLPKGVMMTH 272
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
89-264 |
1.92e-04 |
|
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: 44.57 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 89 QPERLALVDAGTGEC--WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM----------EAA 156
Cdd:cd05943 82 ADDPAAIYAAEDGERteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAiwsscspdfgVPG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 157 LLNVNLRREP--LAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKS-LIKFCSGDLGPE-GILPDTHLLDPLLKEASTAPL 232
Cdd:cd05943 162 VLDRFGQIEPkvLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVvVVPYTVAAGQPDlSKIAKALTLEDFLATGAAGEL 241
|
170 180 190
....*....|....*....|....*....|....
gi 768002382 233 --AQIPskgMDDRLFYIYTSGTTGLPKAaiVVHS 264
Cdd:cd05943 242 efEPLP---FDHPLYILYSSGTTGLPKC--IVHG 270
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
104-293 |
1.96e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 44.70 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 104 W-TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEfvglWLGLAKAGMEAALLNVnlrrePLAFCLGTSGAKALIFG 182
Cdd:PLN02736 78 WmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPE----WLIVDHACSAYSYVSV-----PLYDTLGPDAVKFIVNH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 183 GEmVAAVAEVSGHLgKSLIKFCSgDL----------GPEGILPDTHL--------LDPLLKEASTAPLAQIPSKGmDDRL 244
Cdd:PLN02736 149 AE-VAAIFCVPQTL-NTLLSCLS-EIpsvrlivvvgGADEPLPSLPSgtgveivtYSKLLAQGRSSPQPFRPPKP-EDVA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768002382 245 FYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYH 293
Cdd:PLN02736 225 TICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH 273
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
84-540 |
2.44e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 44.06 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 84 AVVQrqPERLALVDAGTGECW--TFAQLDAYSNAVANlfRQLGfaPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:PLN02479 30 AVVH--PTRKSVVHGSVRYTWaqTYQRCRRLASALAK--RSIG--PGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 162 LRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKS---------LIKFCSGDLGPEGIlpdTHLL-------DPLLK 225
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKkkssfkpplLIVIGDPTCDPKSL---QYALgkgaieyEKFLE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 226 EASTApLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCL 305
Cdd:PLN02479 181 TGDPE-FAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 306 IYGLTVVLRKkFSASRFWDDCIKYnctinGVRHcrlLCLVVQYIGEIcrylLKQPVREA--ERRHRVRLAVGNGLRPAIW 383
Cdd:PLN02479 260 LCGTNICLRQ-VTAKAIYSAIANY-----GVTH---FCAAPVVLNTI----VNAPKSETilPLPRVVHVMTAGAAPPPSV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 384 EEFTERFGVRqIGEFYGATECNcsianmdGKVGSCGFNSRI--LPhvyPIRLVKVNEDTMELLRDAQGL-CIPCQAGEP- 459
Cdd:PLN02479 327 LFAMSEKGFR-VTHTYGLSETY-------GPSTVCAWKPEWdsLP---PEEQARLNARQGVRYIGLEGLdVVDTKTMKPv 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 460 ---GLLVGQInqqdpLRRFDGYVSESATSKKIAHSVFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEV 536
Cdd:PLN02479 396 padGKTMGEI-----VMRGNMVMKGYLKNPKANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEV 468
|
....
gi 768002382 537 EGVL 540
Cdd:PLN02479 469 ENVV 472
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
235-548 |
4.93e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 43.27 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 235 IPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAG-NIIGV-----GQCLIYG 308
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfNSCTLfpllsGVPVVFA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 309 LTVVLRKKFSasRFWDDcikynctingvRHCRLLCLVVQYIGeicrYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEF 386
Cdd:PRK06334 257 YNPLYPKKIV--EMIDE-----------AKVTFLGSTPVFFD----YILKTAKKQESCLPSLRFVVigGDAFKDSLYQEA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 387 TERFGVRQIGEFYGATECN--CSIANMDG-KVGSCgfnsrilphvypirlVKVNEDTMELLRDAQGLCIPCQAGEPGLLV 463
Cdd:PRK06334 320 LKTFPHIQLRQGYGTTECSpvITINTVNSpKHESC---------------VGMPIRGMDVLIVSEETKVPVSSGETGLVL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 464 GQINQQdplrrFDGYVSESATSKKIAHSvfskGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRL 543
Cdd:PRK06334 385 TRGTSL-----FSGYLGEDFGQGFVELG----GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
....*
gi 768002382 544 LGQTD 548
Cdd:PRK06334 456 FGQNA 460
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
247-311 |
5.84e-04 |
|
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: 43.11 E-value: 5.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768002382 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDC----LPLYHSAGNIIGVGQCLIYGLTV 311
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESvvsyLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
104-621 |
7.06e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 42.77 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAkaGMEAALLNVNLRREP--LAFCLGTSGAKALIF 181
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVS--GSGAVCHTINPRLFPeqIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 182 GGEMVAAVAEVSGHLG--KSLIKFCSGDLGPEGILP-----------DTHLLDPLLKEASTAPLAqipskgmddrlfyiY 248
Cdd:PRK07008 118 DLTFLPLVDALAPQCPnvKGWVAMTDAAHLPAGSTPllcyetlvgaqDGDYDWPRFDENQASSLC--------------Y 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 249 TSGTTGLPKAAIVVHsRYYRMAAFGH---HAYRMQAADVLYDCLPLYHS-------AGNIIGV-----GQCL----IYGL 309
Cdd:PRK07008 184 TSGTTGNPKGALYSH-RSTVLHAYGAalpDAMGLSARDAVLPVVPMFHVnawglpySAPLTGAklvlpGPDLdgksLYEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 310 TVVLRKKFSAS--RFWDDCIKYnCTINGVRHCRLLCLVvqyIGeicryllkqpvreaerrhrvrlavGNGLRPAIWEEFT 387
Cdd:PRK07008 263 IEAERVTFSAGvpTVWLGLLNH-MREAGLRFSTLRRTV---IG------------------------GSACPPAMIRTFE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 388 ERFGVRQIgEFYGATEcncsianMDGKVGSCGFNSRILphvypirlvKVNEDTMELLRDAQGLCIpcqAGEPGLLVGQIN 467
Cdd:PRK07008 315 DEYGVEVI-HAWGMTE-------MSPLGTLCKLKWKHS---------QLPLDEQRKLLEKQGRVI---YGVDMKIVGDDG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 468 QQDPlrrFDGYVSESATSKK--IAHSVFsKGDSAYL------SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGV 539
Cdd:PRK07008 375 RELP---WDGKAFGDLQVRGpwVIDRYF-RGDASPLvdgwfpTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 540 LSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRL 616
Cdd:PRK07008 451 AVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPddvVFVDAIPH---TATGKLQKLKL 527
|
....*
gi 768002382 617 qREGF 621
Cdd:PRK07008 528 -REQF 531
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
105-298 |
7.26e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 42.68 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIfLEGRPEFV-----GLWLglakAGMEAALLNVNLRREPLAF-------CLG 172
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAV-LAGAPVEIaptaqGLWM----RGASLTMLHQPTPRTDLAVwaedtlrVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 173 TSGAKALIFGGEMVAAVAEVSGHlgkslikfcsgdlgpeGILPDThlldplLKEASTAPLAQIPSKGMDDRLFYIYTSGT 252
Cdd:PRK07768 106 MIGAKAVVVGEPFLAAAPVLEEK----------------GIRVLT------VADLLAADPIDPVETGEDDLALMQLTSGS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768002382 253 TGLPKAAIVVHSRYYRMAAFGHHAYRMQAA-DVLYDCLPLYHSAGNI 298
Cdd:PRK07768 164 TGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMV 210
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
105-197 |
5.83e-03 |
|
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: 39.75 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI--FG 182
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIgiPK 83
|
90
....*....|....*
gi 768002382 183 GEMVAAVAEVSGHLG 197
Cdd:cd05910 84 ADEPAAILFTSGSTG 98
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
399-594 |
7.83e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.21 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 399 YGATECNCSIANM------DGKVgSCGfnsRILPHvypirlvkvnedtmellrdAQgLCIPCQAgepgllVGQINQQDPl 472
Cdd:PRK07445 261 YGMTETASQIATLkpddflAGNN-SSG---QVLPH-------------------AQ-ITIPANQ------TGNITIQAQ- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002382 473 RRFDGYVSEsatsKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGV-LSRLLGQtDVAV 551
Cdd:PRK07445 310 SLALGYYPQ----ILDSQGIFETDDLGYLDAQ-------GYLHILGRNSQKIITGGENVYPAEVEAAiLATGLVQ-DVCV 377
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768002382 552 YGVAVPgVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARP 594
Cdd:PRK07445 378 LGLPDP-HWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQP 419
|
|
| |
