|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1-498 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 860.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 1 MTDPTVSRLLMPLAEIDDRGVYFEDSFTSWREHLRHGAAIAAALRARLDPARPPHVGVLLQNTPFFSAMLVAAGMSGIVP 80
Cdd:PRK07867 2 SSAPTVAELLLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 81 VGLNPVRRGAALLRDINHADCQLVLADSASAGPLAD----IEHVNVESTEWSDEVAAHSGTELTFQSASPADLFMLIFTS 156
Cdd:PRK07867 82 VGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGldpgVRVINVDSPAWADELAAHRDAEPPFRVADPDDLFMLIFTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 157 GTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYG 236
Cdd:PRK07867 162 GTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 237 ATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNEGVAGDLERFARRFGCVVQDGFGSTEGGVAIARTPDTPAGSLGPLP 316
Cdd:PRK07867 242 ATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGVAITRTPDTPPGALGPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 317 AGIEIVDPDTGRPCPAGV------------VGELVNTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAG 384
Cdd:PRK07867 322 PGVAIVDPDTGTECPPAEdadgrllnadeaIGELVNTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 385 RLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQPDLGPKQWPSY 464
Cdd:PRK07867 402 RLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQPDLGPKQWPSY 481
|
490 500 510
....*....|....*....|....*....|....
gi 2321332536 465 VRISAGLPGTVTFKVLKRQLAAEGVDCGDPVFAI 498
Cdd:PRK07867 482 VRVCAELPRTATFKVLKRQLSAEGVDCADPVWWI 515
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
4-496 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 650.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 4 PTVSRLLMPLAEIDDRGVYFEDSFTSWREHLRHGAAIAAALRARLDPARPPHVGVLLQNTPFFSAMLVAAGMSGIVPVGL 83
Cdd:PRK13388 3 DTIAQLLRDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 84 NPVRRGAALLRDINHADCQLVLADSASAG-----PLADIEHVNVESTEWSDEVAAHsGTELTFQSASPADLFMLIFTSGT 158
Cdd:PRK13388 83 NTTRRGAALAADIRRADCQLLVTDAEHRPlldglDLPGVRVLDVDTPAYAELVAAA-GALTPHREVDAMDPFMLIFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 159 SGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGAT 238
Cdd:PRK13388 162 TGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 239 YANYVGKPLSYVLATPEQPDDSENPLRAVYGNEGVAGDLERFARRFGCVVQDGFGSTEGGVAIARTPDTPAGSLGPLPAG 318
Cdd:PRK13388 242 YFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTPPGSIGRGAPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 319 IEIVDPDTGRPCPAGV-------------VGELVNTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGR 385
Cdd:PRK13388 322 VAIYNPETLTECAVARfdahgallnadeaIGELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 386 LGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQPDLGPKQWPSYV 465
Cdd:PRK13388 402 TADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYV 481
|
490 500 510
....*....|....*....|....*....|.
gi 2321332536 466 RISAGLPGTVTFKVLKRQLAAEGVDCGDPVF 496
Cdd:PRK13388 482 RIAADLPSTATNKVLKRELIAQGWATGDPVT 512
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-484 |
1.70e-168 |
|
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: 482.18 E-value: 1.70e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 25 DSFTSWREHLRHGAAIAAALRARLDPaRPPHVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLV 104
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIR-PGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 105 LADsasagpladiehvnvestewsdevaahsgteltfqsaspadLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFG 184
Cdd:cd05934 80 VVD-----------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 185 LGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPL 264
Cdd:cd05934 119 LGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 265 RAVYGNEGVAGDLERFARRFGCVVQDGFGSTEGGVAIARTPD--TPAGSLGPLPAGIE--IVDPDtGRPCPAGVVGELVN 340
Cdd:cd05934 199 RAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDepRRPGSIGRPAPGYEvrIVDDD-GQELPAGEPGELVI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 341 TA--GPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVY 418
Cdd:cd05934 278 RGlrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVV 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 419 AVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQPDlgPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05934 358 AVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLA--YFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
55-487 |
4.99e-97 |
|
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: 300.57 E-value: 4.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLAdsasagpladiehvnvestewsdevaah 134
Cdd:COG0318 51 RVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT---------------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 sgteltfqsaspadlFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQ 214
Cdd:COG0318 103 ---------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 215 GSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLR-AVYGNEGVAGDL-ERFARRFGCVVQDGF 292
Cdd:COG0318 168 ATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRlVVSGGAPLPPELlERFEERFGVRIVEGY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 293 GSTEGGVAIARTPD----TPAGSLGPLPAGIE--IVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIY 366
Cdd:COG0318 248 GLTETSPVVTVNPEdpgeRRPGSVGRPLPGVEvrIVDED-GRELPPGEVGEIV-VRGPNVMKGYWNDPEATAEAFRDGWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 367 HSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKF 446
Cdd:COG0318 326 RTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEEL 405
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2321332536 447 RVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:COG0318 406 RAFLRER--LARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
56-497 |
8.63e-78 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 254.80 E-value: 8.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTP-FFSAMLvaagmsGIVPVG-----LNPVRRGAALLRDINHADCQLVLADSASAGPLADI-EHVNVESTEWS 128
Cdd:PRK08279 90 VALLMENRPeYLAAWL------GLAKLGavvalLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEArADLARPPRLWV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 129 ------------DEVAAHSGTELTFQSASPADLFM-----LIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVC 191
Cdd:PRK08279 164 aggdtlddpegyEDLAAAAAGAPTTNPASRSGVTAkdtafYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 192 YVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNe 271
Cdd:PRK08279 244 YCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGN- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 272 GVAGDL-ERFARRFGcvVQD---GFGSTEGGV----------AIARTPDTPAGslgplPAGIEIVDPDTGRP-------- 329
Cdd:PRK08279 323 GLRPDIwDEFQQRFG--IPRileFYAASEGNVgfinvfnfdgTVGRVPLWLAH-----PYAIVKYDVDTGEPvrdadgrc 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 330 --CPAGVVGELVNTAGP-GRFEGYYNDEAAEAERMAGGI------YHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTA 400
Cdd:PRK08279 396 ikVKPGEVGLLIGRITDrGPFDGYTDPEASEKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATT 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 401 PIERVLLRYPDTAEVAVYAVPDPVVGDRV-MAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKV 479
Cdd:PRK08279 476 EVENALSGFPGVEEAVVYGVEVPGTDGRAgMAAIVLADGAEFDLAALAAHLYER--LPAYAVPLFVRLVPELETTGTFKY 553
|
490 500
....*....|....*....|.
gi 2321332536 480 LKRQLAAEGVD---CGDPVFA 497
Cdd:PRK08279 554 RKVDLRKEGFDpskVDDPLYV 574
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
148-480 |
4.22e-75 |
|
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: 239.88 E-value: 4.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNavLVGWAVAAACQG-SIALRRKFSAS 226
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIG--GLFGLLGALLAGgTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 227 GFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAV-YGNEGVAGDL-ERFARRFGCVVQDGFGSTEGGVAIART 304
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALvSGGAPLPPELlERFEEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 305 P----DTPAGSLGPLPAGIE--IVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAG 378
Cdd:cd04433 159 PpdddARKPGSVGRPVPGVEvrIVDPD-GGELPPGEIGELV-VRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 379 YAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGP 458
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRER--LAP 314
|
330 340
....*....|....*....|..
gi 2321332536 459 KQWPSYVRISAGLPGTVTFKVL 480
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
56-490 |
2.75e-74 |
|
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: 241.49 E-value: 2.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSAsagpladiehvnvestewsdevaahs 135
Cdd:cd05940 31 VALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVDAA-------------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 136 gteltfqsaspadlfMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQG 215
Cdd:cd05940 85 ---------------LYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 216 SIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNeGVAGDL-ERFARRFGCV-VQDGFG 293
Cdd:cd05940 150 TLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGN-GLRPDIwEEFKERFGVPrIAEFYA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 294 STEGGVAIARTPDTP-----AGSLGPLPAGIEIV--DPDTGRP----------CPAGVVGELVNTAGP-GRFEGYYNDEA 355
Cdd:cd05940 229 ATEGNSGFINFFGKPgaigrNPSLLRKVAPLALVkyDLESGEPirdaegrcikVPRGEPGLLISRINPlEPFDGYTDPAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 356 AEAE------RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRV 429
Cdd:cd05940 309 TEKKilrdvfKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 430 -MAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAEGVD 490
Cdd:cd05940 389 gMAAIVLQPNEEFDLSALAAHLEKN--LPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
51-489 |
1.27e-71 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 236.96 E-value: 1.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 51 ARPPHVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSA--------SAGPLA------- 115
Cdd:PRK06155 69 KRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAllaaleaaDPGDLPlpavwll 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 116 DIEHVNVESTEWSDEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSM 195
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 196 PLFHSNAvLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNEGVAG 275
Cdd:PRK06155 229 PLFHTNA-LNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 276 DLERFARRFGCVVQDGFGSTEGGVAIARTPDTP-AGSLGPLPAGIE--IVDPDtGRPCPAGVVGELVNTAG-PGRF-EGY 350
Cdd:PRK06155 308 LHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQrPGSMGRLAPGFEarVVDEH-DQELPDGEPGELLLRADePFAFaTGY 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 351 YNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVM 430
Cdd:PRK06155 387 FGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVM 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 431 AALVLAPGTRFDTDKFRVFLaeQPDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAEGV 489
Cdd:PRK06155 467 AAVVLRDGTALEPVALVRHC--EPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
56-481 |
3.93e-61 |
|
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: 206.31 E-value: 3.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPvRRGAALLRDInhadcqlvladsasagpladiehvnvestewsdevAAHS 135
Cdd:cd17631 48 VAVLSKNSPEFLELLFAAARLGAVFVPLNF-RLTPPEVAYI-----------------------------------LADS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 136 GTELTFqsaspADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQG 215
Cdd:cd17631 92 GAKVLF-----DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 216 SIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPE--QPDDSEnpLRAV-YGNEGVAGDLERFARRFGCVVQDGF 292
Cdd:cd17631 167 TVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRfaTTDLSS--LRAViYGGAPMPERLLRALQARGVKFVQGY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 293 GSTE-GGVAIARTPD---TPAGSLG-PLP-AGIEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIY 366
Cdd:cd17631 245 GMTEtSPGVTFLSPEdhrRKLGSAGrPVFfVEVRIVDPD-GREVPPGEVGEIV-VRGPHVMAGYWNRPEATAAAFRDGWF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 367 HSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKF 446
Cdd:cd17631 323 HTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDEL 402
|
410 420 430
....*....|....*....|....*....|....*
gi 2321332536 447 RVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLK 481
Cdd:cd17631 403 IAHCRER--LARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
55-490 |
9.60e-61 |
|
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: 206.51 E-value: 9.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADsasagpladiehvnvestewsdevaah 134
Cdd:cd05937 33 FVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD--------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 sgteltfqsasPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQ 214
Cdd:cd05937 86 -----------PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 215 GSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNeGVAGDL-ERFARRFGC-VVQDGF 292
Cdd:cd05937 155 GTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGN-GLRPDIwERFRERFNVpEIGEFY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 293 GSTEGGVAIAR--TPDTPAGSLG--------PLPAGIEIV--DPDTGRP-----------CPAGVVGEL---VNTAGPGR 346
Cdd:cd05937 234 AATEGVFALTNhnVGDFGAGAIGhhglirrwKFENQVVLVkmDPETDDPirdpktgfcvrAPVGEPGEMlgrVPFKNREA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 347 FEGYYNDEAAEAERMA------GGIYH-SGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYA 419
Cdd:cd05937 314 FQGYLHNEDATESKLVrdvfrkGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 420 VPDPVVGDRV-MAALVLAPGTRFDTDKFRVFLAEqpdLGPKQWPSY-----VRISAGLPGTVTFKVLKRQLAAEGVD 490
Cdd:cd05937 394 VKVPGHDGRAgCAAITLEESSAVPTEFTKSLLAS---LARKNLPSYavplfLRLTEEVATTDNHKQQKGVLRDEGVD 467
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
56-490 |
2.33e-60 |
|
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: 205.35 E-value: 2.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVaaGMS--GIVPVGLNPVRRGAALLRDINHADCQLVLadsasagpladIEHVNVESTEWSDEVAA 133
Cdd:cd05939 31 VALFMENRLEFVALWL--GLAkiGVETALINSNLRLESLLHCITVSKAKALI-----------FNLLDPLLTQSSTEPPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 134 HSGTELTfqsaspaDLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAAC 213
Cdd:cd05939 98 QDDVNFR-------DKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 214 QGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNeGVAGDL-ERFARRFGcVVQDG- 291
Cdd:cd05939 171 GSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGN-GLRPQIwEQFVRRFG-IPQIGe 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 292 -FGSTEGGVAIARTpDTPAGSLGPL--------PAGIEIVDPDTGR----------PCPAGVVGELVNTAGPG----RFE 348
Cdd:cd05939 249 fYGATEGNSSLVNI-DNHVGACGFNsrilpsvyPIRLIKVDEDTGElirdsdglciPCQPGEPGLLVGKIIQNdplrRFD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 349 GYYNdEAAEAERMAGGIYHSGDLAY-------RDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVP 421
Cdd:cd05939 328 GYVN-EGATNKKIARDVFKKGDSAFlsgdvlvMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVE 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 422 DPVVGDRV-MAALVlAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAEGVD 490
Cdd:cd05939 407 VPGVEGRAgMAAIV-DPERKVDLDRFSAVLAKS--LPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYD 473
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
56-485 |
2.28e-58 |
|
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: 200.62 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLA------DIEHVNVEStEWSD 129
Cdd:cd05926 42 VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGELGPASraasklGLAILELAL-DVGV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 130 EVAAHSGTELTFQSASPA-----------DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLF 198
Cdd:cd05926 121 LIRAPSAESLSNLLADKKnaksegvplpdDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 199 HSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSE-NPLRAV-YGNEGVAGD 276
Cdd:cd05926 201 HVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPpPKLRFIrSCSASLPPA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 277 -LERFARRFGCVVQDGFGSTEGGVAIARTPDTPA----GSLGPlPAGIEIVD-PDTGRPCPAGVVGELVnTAGPGRFEGY 350
Cdd:cd05926 281 vLEALEATFGAPVLEAYGMTEAAHQMTSNPLPPGprkpGSVGK-PVGVEVRIlDEDGEILPPGVVGEIC-LRGPNVTRGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 351 YNDEAAEAER-MAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRV 429
Cdd:cd05926 359 LNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEV 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 430 MAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLA 485
Cdd:cd05926 439 AAAVVLREGASVTEEELRAFCRKH--LAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
56-484 |
1.58e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 199.26 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNpVRRGAALLRDI-NHADCQLVLADSASAGPLADI-------EHV------- 120
Cdd:PRK06187 59 VAVFDWNSHEYLEAYFAVPKIGAVLHPIN-IRLKPEEIAYIlNDAEDRVVLVDSEFVPLLAAIlpqlptvRTVivegdgp 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 121 ----NVESTEWSDEVAAHSGTELtFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMP 196
Cdd:PRK06187 138 aaplAPEVGEYEELLAAASDTFD-FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 197 LFHSNAVlvGWAVAAACQG-SIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLR-AVYGNEGVA 274
Cdd:PRK06187 217 MFHVHAW--GLPYLALMAGaKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRlVIYGGAALP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 275 GDL-ERFARRFGCVVQDGFGSTEGG--VAIARTPD------TPAGSLGPLPAGIE--IVDPDtGRPCPA--GVVGELVnT 341
Cdd:PRK06187 295 PALlREFKEKFGIDLVQGYGMTETSpvVSVLPPEDqlpgqwTKRRSAGRPLPGVEarIVDDD-GDELPPdgGEVGEII-V 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 342 AGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVP 421
Cdd:PRK06187 373 RGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 422 DPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK06187 453 DEKWGERPVAVVVLKPGATLDAKELRAFLRGR--LAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
145-496 |
5.66e-56 |
|
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: 195.20 E-value: 5.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 145 SPADLFMLIFTSGTSGEPKAVKCSHSKVaIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFS 224
Cdd:cd05938 142 TIKSPALYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 225 ASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNeGVAGDL-ERFARRFGCV-VQDGFGSTEGGVAIA 302
Cdd:cd05938 221 ASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGN-GLRADVwREFLRRFGPIrIREFYGSTEGNIGFF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 303 RTPDTPaGSLGP--------LPAGIEIVDPDTGRP-------C---PAGVVGELV---NTAGPgrFEGYYNDEA-AEAER 360
Cdd:cd05938 300 NYTGKI-GAVGRvsylykllFPFELIKFDVEKEEPvrdaqgfCipvAKGEPGLLVakiTQQSP--FLGYAGDKEqTEKKL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 361 MA-----GGIY-HSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRV-MAAL 433
Cdd:cd05938 377 LRdvfkkGDVYfNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIgMAAV 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 434 VLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAEGVDCG---DPVF 496
Cdd:cd05938 457 KLKPGHEFDGKKLYQHVREY--LPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSiisDPLY 520
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
55-388 |
2.50e-53 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 185.21 E-value: 2.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLAD--------------IEHV 120
Cdd:pfam00501 48 RVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKLEELLealgklevvklvlvLDRD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 121 NVESTEWSDEVAAHSG-TELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTM----TQRFGLGPDDVCYVSM 195
Cdd:pfam00501 128 PVLKEEPLPEEAKPADvPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 196 PLFHSNAVLVGWAVAAACQGSIALRRKFSA---SGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVY-GNE 271
Cdd:pfam00501 208 PLFHDFGLSLGLLGPLLAGATVVLPPGFPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsGGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 272 GVAGDL-ERFARRFGCVVQDGFGSTEGGVAIA-----RTPDTPAGSLGPLPAGIE--IVDPDTGRPCPAGVVGELVnTAG 343
Cdd:pfam00501 288 PLPPELaRRFRELFGGALVNGYGLTETTGVVTtplplDEDLRSLGSVGRPLPGTEvkIVDDETGEPVPPGEPGELC-VRG 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2321332536 344 PGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGD 388
Cdd:pfam00501 367 PGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKD 412
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
55-484 |
7.86e-50 |
|
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: 176.98 E-value: 7.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADsasagpladiehvnvesTEWSDEVAAH 134
Cdd:cd05936 51 RVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVA-----------------VSFTDLLAAG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 SGTELTFQsASPADLFMLIFTSGTSGEPKAVKCSHSKVaIAGVTMTQR---FGLGPDDVCYVSMPLFHSNAVLVGWAVAA 211
Cdd:cd05936 114 APLGERVA-LTPEDVAVLQYTSGTTGVPKGAMLTHRNL-VANALQIKAwleDLLEGDDVVLAALPLFHVFGLTVALLLPL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 212 ACQGSIALRRKFSASGFIADVRRYGATYanYVGKPLSYVlATPEQPDDSENPLRAV-YGNEGvaGD------LERFARRF 284
Cdd:cd05936 192 ALGATIVLIPRFRPIGVLKEIRKHRVTI--FPGVPTMYI-ALLNAPEFKKRDFSSLrLCISG--GAplpvevAERFEELT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 285 GCVVQDGFGSTEGG-VAIARTPDTP--AGSLG-PLPaGIE--IVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEA 358
Cdd:cd05936 267 GVPIVEGYGLTETSpVVAVNPLDGPrkPGSIGiPLP-GTEvkIVDDD-GEELPPGEVGELW-VRGPQVMKGYWNRPEETA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 359 ERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG 438
Cdd:cd05936 344 EAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2321332536 439 TRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05936 424 ASLTEEEIIAFCREQ--LAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
56-494 |
2.33e-49 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 178.00 E-value: 2.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTP-FFSAMLVAAGMsGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGP----------------LADIE 118
Cdd:COG0365 67 VAIYLPNIPeAVIAMLACARI-GAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGgkvidlkekvdealeeLPSLE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 119 HV----------NVESTEWSDEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSkVAIAGVTMTQR--FGLG 186
Cdd:COG0365 146 HVivvgrtgadvPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHG-GYLVHAATTAKyvLDLK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 187 PDDVCYVSMPLF----HSNAVLVGWAVAAAcqgSIALRRKF---SASGFIADVRRYGATY----ANYVGKPLSYVLATPE 255
Cdd:COG0365 225 PGDVFWCTADIGwatgHSYIVYGPLLNGAT---VVLYEGRPdfpDPGRLWELIEKYGVTVfftaPTAIRALMKAGDEPLK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 256 QPDDSenPLRAVygneGVAGD------LERFARRFGCVVQDGFGSTE-GGVAIARTPDTP--AGSLG-PLPaGIE--IVD 323
Cdd:COG0365 302 KYDLS--SLRLL----GSAGEplnpevWEWWYEAVGVPIVDGWGQTEtGGIFISNLPGLPvkPGSMGkPVP-GYDvaVVD 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 324 PDtGRPCPAGVVGELV-NTAGPGRFEGYYNDEAAEAERMAG---GIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGT 399
Cdd:COG0365 375 ED-GNPVPPGEEGELViKGPWPGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGT 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 400 APIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFD---TDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVT 476
Cdd:COG0365 454 AEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREE--LGPYAYPREIEFVDELPKTRS 531
|
490 500
....*....|....*....|
gi 2321332536 477 FKVLKRQL--AAEGVDCGDP 494
Cdd:COG0365 532 GKIMRRLLrkIAEGRPLGDT 551
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
55-484 |
4.43e-48 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 173.72 E-value: 4.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFsaMLVAAGMSGI----VPVGLNPVRRGAALLrdINHADCQLVLAdSASAGPLAD---------IEHVN 121
Cdd:PRK08008 64 KVALHLDNCPEF--IFCWFGLAKIgaimVPINARLLREESAWI--LQNSQASLLVT-SAQFYPMYRqiqqedatpLRHIC 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 122 VESTEWSDEVAAHSGTELTFQSA---------SPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCY 192
Cdd:PRK08008 139 LTRVALPADDGVSSFTQLKAQQPatlcyapplSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 193 VSMPLFHSNAVLVGwAVAAACQGS-IALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAV--YG 269
Cdd:PRK08008 219 TVMPAFHIDCQCTA-AMAAFSAGAtFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVmfYL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 270 NEGVAgDLERFARRFGCVVQDGFGSTEGGVAIarTPDTPAG-----SLGPlpAGI----EIVDpDTGRPCPAGVVGELVN 340
Cdd:PRK08008 298 NLSDQ-EKDAFEERFGVRLLTSYGMTETIVGI--IGDRPGDkrrwpSIGR--PGFcyeaEIRD-DHNRPLPAGEIGEICI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 341 TAGPGR--FEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAV 417
Cdd:PRK08008 372 KGVPGKtiFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 418 YAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK08008 452 VGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQ--NMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
56-438 |
8.54e-48 |
|
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: 172.01 E-value: 8.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLAD----------SASAGPLADIEHVNVE-- 123
Cdd:cd05911 38 VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDpdglekvkeaAKELGPKDKIIVLDDKpd 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 124 -STEWSDEVAAHSGTELTFQSA----SPADLFMLIFTSGTSGEPKAVKCSHsKVAIAGVTMTQRF---GLGPDDVCYVSM 195
Cdd:cd05911 118 gVLSIEDLLSPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPKGVCLSH-RNLIANLSQVQTFlygNDGSNDVILGFL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 196 PLFHSNAVLvgWAVAAACQG-SIALRRKFSASGFIADVRRYGATYAnYVGKPLSYVLAT-PEQPDDSENPLRAV-YGNEG 272
Cdd:cd05911 197 PLYHIYGLF--TTLASLLNGaTVIIMPKFDSELFLDLIEKYKITFL-YLVPPIAAALAKsPLLDKYDLSSLRVIlSGGAP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 273 VAGDL-ERFARRFG-CVVQDGFGSTEGGVAIARTPDTPA--GSLGPLPAGIE--IVDPDTGRPCPAGVVGEL-VNtaGPG 345
Cdd:cd05911 274 LSKELqELLAKRFPnATIKQGYGMTETGGILTVNPDGDDkpGSVGRLLPNVEakIVDDDGKDSLGPNEPGEIcVR--GPQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 346 RFEGYYNDEAAEAE-RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPV 424
Cdd:cd05911 352 VMKGYYNNPEATKEtFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEV 431
|
410
....*....|....
gi 2321332536 425 VGDRVMAALVLAPG 438
Cdd:cd05911 432 SGELPRAYVVRKPG 445
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
55-487 |
3.23e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 171.24 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRG---AALLRDinhADCQLVLA-------DSASAGPLADIEHVNVES 124
Cdd:PRK07656 57 RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAdeaAYILAR---GDAKALFVlglflgvDYSATTRLPALEHVVICE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 125 TE-----------WSDEVAAHSGTElTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYV 193
Cdd:PRK07656 134 TEeddphtekmktFTDFLAAGDPAE-RAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 194 SMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYanYVGKPLSY--VLATPEQPDDSENPLR-AVYGN 270
Cdd:PRK07656 213 ANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERITV--LPGPPTMYnsLLQHPDRSAEDLSSLRlAVTGA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 271 EGVAGDL-ERFARRFGC-VVQDGFGSTE-GGVA----IARTPDTPAGSLGPLPAGIE--IVDPDtGRPCPAGVVGELVnT 341
Cdd:PRK07656 291 ASMPVALlERFESELGVdIVLTGYGLSEaSGVTtfnrLDDDRKTVAGTIGTAIAGVEnkIVNEL-GEEVPVGEVGELL-V 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 342 AGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAV 420
Cdd:PRK07656 369 RGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2321332536 421 PDPVVGDRVMAALVLAPGTRFDTD-----------KFRVflaeqpdlgpkqwPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK07656 449 PDERLGEVGKAYVVLKPGAELTEEeliaycrehlaKYKV-------------PRSIEFLDELPKNATGKVLKRALREK 513
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
148-484 |
4.64e-46 |
|
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: 165.97 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCY-VSMP---LFHSNAVLVGWAVAAAcqGSIALRRKF 223
Cdd:cd05972 82 DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWnIADPgwaKGAWSSFFGPWLLGAT--VFVYEGPRF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 224 SASGFIADVRRYGATyaNYVGKPLSYVLATPEQPDDSENP-LRAVYG-----NEGVagdLERFARRFGCVVQDGFGSTEG 297
Cdd:cd05972 160 DAERILELLERYGVT--SFCGPPTAYRMLIKQDLSSYKFShLRLVVSageplNPEV---IEWWRAATGLPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 298 GVAIARTPDTPA--GSLG-PLPA-GIEIVDpDTGRPCPAGVVGEL-VNTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLA 372
Cdd:cd05972 235 GLTVGNFPDMPVkpGSMGrPTPGyDVAIID-DDGRELPPGEEGDIaIKLPPPGLFLGYVGDPEKTEASIRGDYYLTGDRA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 373 YRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG---TRFDTDKFRVF 449
Cdd:cd05972 314 YRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepSEELAEELQGH 393
|
330 340 350
....*....|....*....|....*....|....*
gi 2321332536 450 LAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05972 394 VKKV--LAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
144-484 |
8.99e-44 |
|
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: 160.24 E-value: 8.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKF 223
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 224 SASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRA-VYGNEGVAGDL-ERFARRFGCVVQDGFGSTEGGVAI 301
Cdd:cd05903 170 DPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTfVCGGATVPRSLaRRAAELLGAKVCSAYGSTECPGAV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 302 ARTPDTPAGSLG-----PLPaGIEI-VDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRD 375
Cdd:cd05903 250 TSITPAPEDRRLytdgrPLP-GVEIkVVDDTGATLAPGVEGELL-SRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 376 DAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpD 455
Cdd:cd05903 328 EDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQ-G 406
|
330 340
....*....|....*....|....*....
gi 2321332536 456 LGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05903 407 VAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-479 |
1.09e-41 |
|
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: 155.99 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNP-------------------------VRRGAALLRDINHADCQLVLADSAS 110
Cdd:cd05959 57 VLLIMLDTVDFPTAFLGAIRAGIVPVPVNTlltpddyayyledsrarvvvvsgelAPVLAAALTKSEHTLVVLIVSGGAG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 111 AGPLADiehvnvestEWSDEVAAHSGtELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQR-FGLGPDD 189
Cdd:cd05959 137 PEAGAL---------LLAELVAAEAE-QLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 190 VCYVSMPLFHS----NAVLVGWAVAAACqgsIALRRKFSASGFIADVRRYGATYanYVGKPLSY--VLATPEQPDDSENP 263
Cdd:cd05959 207 VCFSAAKLFFAyglgNSLTFPLSVGATT---VLMPERPTPAAVFKRIRRYRPTV--FFGVPTLYaaMLAAPNLPSRDLSS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 264 LR-AVYGNEGVAGDL-ERFARRFGCVVQDGFGSTEGG-VAIARTP-DTPAGSLG-PLPA-GIEIVDPDtGRPCPAGVVGE 337
Cdd:cd05959 282 LRlCVSAGEALPAEVgERWKARFGLDILDGIGSTEMLhIFLSNRPgRVRYGTTGkPVPGyEVELRDED-GGDVADGEPGE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 338 LVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAV 417
Cdd:cd05959 361 LY-VRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAV 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2321332536 418 YAVPDPVVGDRVMAALVLAPGTRF---DTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKV 479
Cdd:cd05959 440 VGVEDEDGLTKPKAFVVLRPGYEDseaLEEELKEFVKDR--LAPYKYPRWIVFVDELPKTATGKI 502
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
66-487 |
2.56e-41 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 155.60 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 66 FSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLA-------DSASAG-----PLADIEHVNVESTEWSD---- 129
Cdd:PRK13295 93 FTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfDHAAMArrlrpELPALRHVVVVGGDGADsfea 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 130 -------EVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNA 202
Cdd:PRK13295 173 llitpawEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 203 VLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRA-VYGNEGVAGDL-ERF 280
Cdd:PRK13295 253 FMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTfLCAGAPIPGALvERA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 281 ARRFGCVVQDGFGSTEGGVAIARTPDTP----AGSLG-PLPaGIE--IVDPDtGRPCPAGVVGELVNTaGPGRFEGY--- 350
Cdd:PRK13295 333 RAALGAKIVSAWGMTENGAVTLTKLDDPderaSTTDGcPLP-GVEvrVVDAD-GAPLPAGQIGRLQVR-GCSNFGGYlkr 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 351 --YNDEAAEaermagGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDR 428
Cdd:PRK13295 410 pqLNGTDAD------GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGER 483
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 429 VMAALVLAPGTRFDTDKFRVFLAEQpDLGPKQWPSYVRISAGLPGTVTFKV----LKRQLAAE 487
Cdd:PRK13295 484 ACAFVVPRPGQSLDFEEMVEFLKAQ-KVAKQYIPERLVVRDALPRTPSGKIqkfrLREMLRGE 545
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
56-486 |
6.35e-41 |
|
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: 152.44 E-value: 6.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPvrrgaallrdinhadcqlvladsasAGPLADIEHV--NVESTEWSDevaa 133
Cdd:cd05941 40 VAFLAPPSAEYVVAQLAIWRAGGVAVPLNP-------------------------SYPLAELEYVitDSEPSLVLD---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 134 hsgteltfqsasPAdlfMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAAC 213
Cdd:cd05941 91 ------------PA---LILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 214 QGSIALRRKFSASGFIADVRRYGATYanYVGKPLSY--VLATPEQpDDSENPLRAVYGNEG----VAG-------DLERF 280
Cdd:cd05941 156 GASVEFLPKFDPKEVAISRLMPSITV--FMGVPTIYtrLLQYYEA-HFTDPQFARAAAAERlrlmVSGsaalpvpTLEEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 281 ARRFGCVVQDGFGSTEGGVAIARTPDTP--AGSLG-PLPaGIE--IVDPDTGRPCPAGVVGELvNTAGPGRFEGYYND-E 354
Cdd:cd05941 233 EAITGHTLLERYGMTEIGMALSNPLDGErrPGTVGmPLP-GVQarIVDEETGEPLPRGEVGEI-QVRGPSVFKEYWNKpE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 355 AAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLG-DWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAAL 433
Cdd:cd05941 311 ATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVV 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 434 VLAPGTR-FDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAA 486
Cdd:cd05941 391 VLRAGAAaLSLEELKEWAKQR--LAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
55-484 |
3.85e-40 |
|
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: 149.94 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTP-----FFSAMLVAAgmsgiVPVGLNPVRRGaallRDINHadcqlVLADSASagpladiehvnvestewsd 129
Cdd:cd05935 28 RVGICLQNSPqyviaYFAIWRANA-----VVVPINPMLKE----RELEY-----ILNDSGA------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 130 eVAAHSGTELTfqsaspaDLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAV 209
Cdd:cd05935 75 -KVAVVGSELD-------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGN-----EGVAgdlERFARRF 284
Cdd:cd05935 147 AVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGgapmpPAVA---EKLLKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 285 GCVVQDGFGSTEggvAIARTPDTPAGS-----LGPLPAGIE--IVDPDTGRPCPAGVVGELVnTAGPGRFEGYYN--DEA 355
Cdd:cd05935 224 GLRFVEGYGLTE---TMSQTHTNPPLRpklqcLGIP*FGVDarVIDIETGRELPPNEVGEIV-VRGPQIFKGYWNrpEET 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 356 AEAERMAGG--IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAAL 433
Cdd:cd05935 300 EESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 434 VLAPGTRFDTDKFRVFLAEQPDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05935 380 VLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
137-486 |
4.42e-40 |
|
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: 149.96 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 137 TELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSM-PLFHSNAVLVGWAVAAACQG 215
Cdd:cd05969 79 TEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTAdPGWVTGTVYGIWAPWLNGVT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 216 SIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDS--ENPLRAVY-GNEGVAGDLERFA-RRFGCVVQDG 291
Cdd:cd05969 159 NVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKydLSSLRFIHsVGEPLNPEAIRWGmEVFGVPIHDT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 292 FGSTE-GGVAIARTPDTPA--GSLG-PLPaGIE--IVDPDtGRPCPAGVVGELVNTAG-PGRFEGYYNDEAAEAERMAGG 364
Cdd:cd05969 239 WWQTEtGSIMIANYPCMPIkpGSMGkPLP-GVKaaVVDEN-GNELPPGTKGILALKPGwPSMFRGIWNDEERYKNSFIDG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 365 IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRfDTD 444
Cdd:cd05969 317 WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PSD 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2321332536 445 KFRVFLAE--QPDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAA 486
Cdd:cd05969 396 ELKEEIINfvRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
56-487 |
3.07e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 148.88 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSG--IVPVGLNPVRRGAALLrdINHADCQLVLADSASAGPLADIEHVNV--ESTEWSDEV 131
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGavFLPINYRLAADEVAYI--LGDAGAKLLLVDEEFDAIVALETPKIVidAAAQADSRR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 132 AAHSGTELTFQSAS-PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAV-LVGWAV 209
Cdd:PRK06145 133 LAQGGLEIPPQAAVaPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGIAV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAAcQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLR-AVYGNEGVAgdlERFARRFGCVV 288
Cdd:PRK06145 213 LWV-GGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAwCIGGGEKTP---ESRIRDFTRVF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 Q-----DGFGSTE--GG---VAIARTPDTpAGSLGPLPAGIEI-VDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAE 357
Cdd:PRK06145 289 TraryiDAYGLTEtcSGdtlMEAGREIEK-IGSTGRALAHVEIrIADGAGRWLPPNMKGEIC-MRGPKVTKGYWKDPEKT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 358 AERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAP 437
Cdd:PRK06145 367 AEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2321332536 438 GTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK06145 447 GATLTLEALDRHCRQR--LASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
133-486 |
7.55e-39 |
|
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: 146.42 E-value: 7.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 133 AHSGTE--LTFQSASPAdlfMLIFTSGTSGEPKAVKCSHSKVA--IAGVTMTQRFGLGPDDVCY-------------VSM 195
Cdd:cd05971 75 SNSGASalVTDGSDDPA---LIIYTSGTTGPPKGALHAHRVLLghLPGVQFPFNLFPRDGDLYWtpadwawigglldVLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 196 PLFHSNAVLVGWAvaaacqgsialRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVY-GNEGVA 274
Cdd:cd05971 152 PSLYFGVPVLAHR-----------MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIAtGGESLG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 275 GDLERFARR-FGCVVQDGFGSTEGGVAIARTPDT-PA--GSLG-PLPAG-IEIVDpDTGRPCPAGVVGEL-VNTAGPGRF 347
Cdd:cd05971 221 EELLGWAREqFGVEVNEFYGQTECNLVIGNCSALfPIkpGSMGkPIPGHrVAIVD-DNGTPLPPGEVGEIaVELPDPVAF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 348 EGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGD 427
Cdd:cd05971 300 LGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGE 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 428 RVMAALVLAPG-TRFDTDK--FRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAA 486
Cdd:cd05971 380 IVKAFVVLNPGeTPSDALAreIQELVKTR--LAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
148-438 |
2.36e-35 |
|
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: 138.40 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKcsHSKVAIAGVTMTQRF--GLGPDDVcyvsmplfHSNAVLVGWAVA----------AACQG 215
Cdd:cd05970 186 DILLVYFSSGTTGMPKMVE--HDFTYPLGHIVTAKYwqNVREGGL--------HLTVADTGWGKAvwgkiygqwiAGAAV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 216 SIALRRKFSASGFIADVRRYGAT--------YANYVGKPLS-YVLATPEQPDDSENPLravygNEGVagdLERFARRFGC 286
Cdd:cd05970 256 FVYDYDKFDPKALLEKLSKYGVTtfcapptiYRFLIREDLSrYDLSSLRYCTTAGEAL-----NPEV---FNTFKEKTGI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 287 VVQDGFGSTEGGVAIARTP--DTPAGSLG-PLPA-GIEIVDPDtGRPCPAGVVGELV-NTAG--P-GRFEGYYNDEAAEA 358
Cdd:cd05970 328 KLMEGFGQTETTLTIATFPwmEPKPGSMGkPAPGyEIDLIDRE-GRSCEAGEEGEIViRTSKgkPvGLFGGYYKDAEKTA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 359 ERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG 438
Cdd:cd05970 407 EVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKG 486
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-485 |
2.78e-35 |
|
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: 137.19 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 52 RPPHVGVLLQNTPFFSAMLVAAGMSG----IVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIEHVNVESTEW 127
Cdd:cd05922 17 RGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDPGTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 128 SD-EVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPlFHSNAVLVG 206
Cdd:cd05922 97 LDaDGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLP-LSYDYGLSV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 207 WAVAAACQGSIALRRKFS-ASGFIADVRRYGATyaNYVGKPLSYVLATPEQPDDSENP-LRAVygnEGVAGDL-ERFARR 283
Cdd:cd05922 176 LNTHLLRGATLVLTNDGVlDDAFWEDLREHGAT--GLAGVPSTYAMLTRLGFDPAKLPsLRYL---TQAGGRLpQETIAR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 284 FGCVVQDG-----FGSTEGGVAIARTP----DTPAGSLG-PLPAG-IEIVDPDtGRPCPAGVVGELVNTaGPGRFEGYYN 352
Cdd:cd05922 251 LRELLPGAqvyvmYGQTEATRRMTYLPperiLEKPGSIGlAIPGGeFEILDDD-GTPTPPGEPGEIVHR-GPNVMKGYWN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 353 DEAAE-AERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPvVGDRVMA 431
Cdd:cd05922 329 DPPYRrKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLAL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 432 ALVLAPGTrfDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLA 485
Cdd:cd05922 408 FVTAPDKI--DPKDVLRSLAER--LPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
148-452 |
3.95e-35 |
|
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: 133.93 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRrKFSASG 227
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVME-KFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 228 FIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNEGVAgDLERFARRFGCVVQDGFGSTE--GGVAIARTP 305
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPE-TIQRFEETTGATFWSLYGQTEtsGLVTLSPYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 306 DTP--AGSLGPLpAGIEIVDpDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFA 383
Cdd:cd17637 159 ERPgsAGRPGPL-VRVRIVD-DNDRPVPAGETGEIV-VRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 384 GRLG--DWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAE 452
Cdd:cd17637 236 GRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGS 306
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
56-417 |
7.40e-35 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 134.70 E-value: 7.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLN---PVRRGAALLRDinhADCQLVLADSASAGPLAD--IEHVNVESTeWSDE 130
Cdd:TIGR01733 28 VAVLLERSAELVVAILAVLKAGAAYVPLDpayPAERLAFILED---AGARLLLTDSALASRLAGlvLPVILLDPL-ELAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 131 VAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAV--LVGWA 208
Cdd:TIGR01733 104 LDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVeeIFGAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 209 VAAACQGSI--ALRRKFSASGFIAdVRRYGATYANYVGKPLSYVLATPEQPDDSenpLRAVY--GNEGVAGDLERFARRF 284
Cdd:TIGR01733 184 LAGATLVVPpeDEERDDAALLAAL-IAEHPVTVLNLTPSLLALLAAALPPALAS---LRLVIlgGEALTPALVDRWRARG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 285 G-CVVQDGFGSTEG--GVAIARTPDTPAGSLGPLPAG-------IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDE 354
Cdd:TIGR01733 260 PgARLINLYGPTETtvWSTATLVDPDDAPRESPVPIGrplantrLYVLDDD-LRPVPVGVVGELY-IGGPGVARGYLNRP 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 355 AAEAERMA---------GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAV 417
Cdd:TIGR01733 338 ELTAERFVpdpfaggdgARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
96-484 |
1.61e-34 |
|
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: 135.84 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 96 INHADCQLVLADS-------ASAGPLADIEHV-------------NVESTEWSDEVAAHSGTEL--TFQSASPADLFmli 153
Cdd:cd12119 93 INHAEDRVVFVDRdflplleAIAPRLPTVEHVvvmtddaampepaGVGVLAYEELLAAESPEYDwpDFDENTAAAIC--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 154 FTSGTSGEPKAVKCSHSKVAI--AGVTMTQRFGLGPDDVCYVSMPLFHSNAvlvgWAV--AAACQGS-IALRRKFSASGF 228
Cdd:cd12119 170 YTSGTTGNPKGVVYSHRSLVLhaMAALLTDGLGLSESDVVLPVVPMFHVNA----WGLpyAAAMVGAkLVLPGPYLDPAS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 229 IAD-VRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVY--GNEGVAGDLERFARRfGCVVQDGFGSTEG---GVAIA 302
Cdd:cd12119 246 LAElIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEER-GVRVIHAWGMTETsplGTVAR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 303 RTPDTPAGSL----------GPLPAGIE--IVDPDTGR-PCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSG 369
Cdd:cd12119 325 PPSEHSNLSEdeqlalrakqGRPVPGVElrIVDDDGRElPWDGKAVGELQ-VRGPWVTKSYYKNDEESEALTEDGWLRTG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 370 DLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVF 449
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEF 483
|
410 420 430
....*....|....*....|....*....|....*.
gi 2321332536 450 LAeqpDLGPKQW-PSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd12119 484 LA---DKVAKWWlPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
56-453 |
2.36e-34 |
|
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: 135.05 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFsAMLVAAGMS-GIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADI--------EHVNVESTE 126
Cdd:cd05904 60 VLLLSPNSIEF-PVAFLAVLSlGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLalpvvlldSAEFDSLSF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 127 WSDEVAAHSgTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHsKVAIAGVTMTQRF---GLGPDDVCYVSMPLFHS--- 200
Cdd:cd05904 139 SDLLFEADE-AEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTH-RNLIAMVAQFVAGegsNSDSEDVFLCVLPMFHIygl 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 201 NAVLVGwavAAACQGSIALRRKFSASGFIADVRRYGATYAnYVGKPLsyVLATPEQPDDSENPLRAVygnEGV------- 273
Cdd:cd05904 217 SSFALG---LLRLGATVVVMPRFDLEELLAAIERYKVTHL-PVVPPI--VLALVKSPIVDKYDLSSL---RQImsgaapl 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 274 -AGDLERFARRFGCV-VQDGFGSTEGGVAIARTPDT-----PAGSLGPLPAGIE--IVDPDTGRPCPAGVVGELVnTAGP 344
Cdd:cd05904 288 gKELIEAFRAKFPNVdLGQGYGMTESTGVVAMCFAPekdraKYGSVGRLVPNVEakIVDPETGESLPPNQTGELW-IRGP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 345 GRFEGYYNDEAAEAERMAG-GIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDP 423
Cdd:cd05904 367 SIMKGYLNNPEATAATIDKeGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDE 446
|
410 420 430
....*....|....*....|....*....|
gi 2321332536 424 VVGDRVMAALVLAPGTRFDTDKFRVFLAEQ 453
Cdd:cd05904 447 EAGEVPMAFVVRKPGSSLTEDEIMDFVAKQ 476
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
56-484 |
1.29e-33 |
|
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: 131.82 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSAsagpladiehvnvestewsdevaahs 135
Cdd:cd05919 38 VLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD-------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 136 gteltfqsaspaDLFMLIFTSGTSGEPKAVKCSHSK-VAIAGVTMTQRFGLGPDDVCYVSMPLFHS----NAVLVGWAVA 210
Cdd:cd05919 92 ------------DIAYLLYSSGTTGPPKGVMHAHRDpLLFADAMAREALGLTPGDRVFSSAKMFFGyglgNSLWFPLAVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 211 AACqgsIALRRKFSASGFIADVRRYGATYanYVGKPLSY--VLATPEQPDDSENPLR-AVYGNEGV-AGDLERFARRFGC 286
Cdd:cd05919 160 ASA---VLNPGWPTAERVLATLARFRPTV--LYGVPTFYanLLDSCAGSPDALRSLRlCVSAGEALpRGLGERWMEHFGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 287 VVQDGFGSTEGG-VAIARTPDT-PAGSLG-PLP-AGIEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMA 362
Cdd:cd05919 235 PILDGIGATEVGhIFLSNRPGAwRLGSTGrPVPgYEIRLVDEE-GHTIPPGEEGDLL-VRGPSAAVGYWNNPEKSRATFN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 363 GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFD 442
Cdd:cd05919 313 GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2321332536 443 ---TDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05919 393 eslARDIHRHLLER--LSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
56-487 |
1.45e-33 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 133.47 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIEH------VNVES----T 125
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTrwwpltVNVGGdsgpS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 126 EWSDEVAAHSGTELTFQSASP----ADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSN 201
Cdd:PRK05852 151 GGTLSVHLDAATEPTPATSTPeglrPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGH 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 202 AVLVGWAVAAACQGSIAL--RRKFSASGFIADVRRYGATYANYVGKPLSYVL--ATPEQPDDSENPLRAVYGNEG--VAG 275
Cdd:PRK05852 231 GLIAALLATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLerAATEPSGRKPAALRFIRSCSAplTAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 276 DLERFARRFGCVVQDGFGSTEGGVAIART-------PDTPAGSLGPLP----AGIEIVDPDtGRPCPAGVVGElVNTAGP 344
Cdd:PRK05852 311 TAQALQTEFAAPVVCAFGMTEATHQVTTTqiegigqTENPVVSTGLVGrstgAQIRIVGSD-GLPLPAGAVGE-VWLRGT 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 345 GRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPV 424
Cdd:PRK05852 389 TVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 425 VGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTfKVLKRQLAAE 487
Cdd:PRK05852 469 YGEAVAAVIVPRESAPPTAEELVQFCRER--LAAFEIPASFQEASGLPHTAK-GSLDRRAVAE 528
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-485 |
2.25e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 129.32 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 154 FTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGwAVAAACQGS--IALRRKFSASGFIAD 231
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLG-VLACLTHGAtmVFPSPSFDPLAVLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 232 VRRYGATyANYvGKPLSYVlATPEQPDDSENPLRAVYGneGVAGD-------LERFARRFGCV-VQDGFGSTEG--GVAI 301
Cdd:cd05917 88 IEKEKCT-ALH-GVPTMFI-AELEHPDFDKFDLSSLRT--GIMAGapcppelMKRVIEVMNMKdVTIAYGMTETspVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 302 ARTPDTP---AGSLG-PLP-AGIEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAG-GIYHSGDLAYRD 375
Cdd:cd05917 163 TRTDDSIekrVNTVGrIMPhTEAKIVDPEGGIVPPVGVPGELC-IRGYSVMKGYWNDPEKTAEAIDGdGWLHTGDLAVMD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 376 DAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpd 455
Cdd:cd05917 242 EDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGK-- 319
|
330 340 350
....*....|....*....|....*....|
gi 2321332536 456 LGPKQWPSYVRISAGLPGTVTFKVLKRQLA 485
Cdd:cd05917 320 IAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
56-484 |
3.26e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.98 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLAD-IEHVNVESTEWSDEV--A 132
Cdd:PRK08316 64 VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAaLALLPVDTLILSLVLggR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 133 AHSGTELTFQSASPA-------------DLFMLIFTSGTSGEPKAVKCSHSKVA-------IAGvtmtqrfGLGPDDVCY 192
Cdd:PRK08316 144 EAPGGWLDFADWAEAgsvaepdveladdDLAQILYTSGTESLPKGAMLTHRALIaeyvsciVAG-------DMSADDIPL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 193 VSMPLFHSNA--VLVGWAVAAACQGSIAlrRKFSASGFIADVRRYGATyaNYVGKPLSYVlATPEQPDDSENPL----RA 266
Cdd:PRK08316 217 HALPLYHCAQldVFLGPYLYVGATNVIL--DAPDPELILRTIEAERIT--SFFAPPTVWI-SLLRHPDFDTRDLsslrKG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 267 VYGNEGVAGD-LERFARRF-GCVVQDGFGSTE-GGVAIARTPD---TPAGSLGPLPAGIE--IVDPDtGRPCPAGVVGEL 338
Cdd:PRK08316 292 YYGASIMPVEvLKELRERLpGLRFYNCYGQTEiAPLATVLGPEehlRRPGSAGRPVLNVEtrVVDDD-GNDVAPGEVGEI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 339 VNTaGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVY 418
Cdd:PRK08316 371 VHR-SPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 419 AVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK08316 450 GLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRAR--LAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
55-438 |
6.52e-33 |
|
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: 130.88 E-value: 6.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNpVRRGAALLRDI-NHADCQLVLADsasagpladiehvnvESTEWSDEVAA 133
Cdd:cd12118 56 TVAVLAPNTPAMYELHFGVPMAGAVLNALN-TRLDAEEIAFIlRHSEAKVLFVD---------------REFEYEDLLAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 134 HSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAAC 213
Cdd:cd12118 120 GDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 214 QGSIALRrKFSASGFIADVRRYGATyaNYVGKPLSYVLATPEQPDDSENPLRAVYGNegVAGDLERFA-----RRFGCVV 288
Cdd:cd12118 200 GTNVCLR-KVDAKAIYDLIEKHKVT--HFCGAPTVLNMLANAPPSDARPLPHRVHVM--TAGAPPPAAvlakmEELGFDV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 QDGFGSTEG-GVAIART---------PDTPAGSLG------PLPAGIEIVDPDTGRPCPA-GV-VGELV---NTAgpgrF 347
Cdd:cd12118 275 THVYGLTETyGPATVCAwkpewdelpTEERARLKArqgvryVGLEEVDVLDPETMKPVPRdGKtIGEIVfrgNIV----M 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 348 EGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGD 427
Cdd:cd12118 351 KGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGE 430
|
410
....*....|.
gi 2321332536 428 RVMAALVLAPG 438
Cdd:cd12118 431 VPCAFVELKEG 441
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
54-484 |
1.08e-32 |
|
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: 130.09 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 54 PHVGVLLQNTPFFSAMLVAAGMSGIVPVGL---NPVRRGAALLRDinhADCQLVLADSASAGPLAdiehVNVESTEWSDE 130
Cdd:cd17646 49 DRVAVLLPRSADLVVALLAVLKAGAAYLPLdpgYPADRLAYMLAD---AGPAVVLTTADLAARLP----AGGDVALLGDE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 131 VAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPL-FHSNAVLVGWAV 209
Cdd:cd17646 122 ALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLsFDVSVWELFWPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAACQGSIALRRKFSASGFIAD-VRRYGATYANYVGKPLSYVLATPEqpDDSENPLRAVY-GNEGVAGDL-ERFARRFGC 286
Cdd:cd17646 202 VAGARLVVARPGGHRDPAYLAAlIREHGVTTCHFVPSMLRVFLAEPA--AGSCASLRRVFcSGEALPPELaARFLALPGA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 287 VVQDGFGSTEGGVAIARTPDTPAGSLGPLPAG-------IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAE 359
Cdd:cd17646 280 ELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGrpvpntrLYVLDDA-LRPVPVGVPGELY-LGGVQLARGYLGRPALTAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 360 RM------AGG-IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAA 432
Cdd:cd17646 358 RFvpdpfgPGSrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGY 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 433 LVLAPG-TRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17646 438 VVPAAGaAGPDTAALRAHLAER--LPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
56-486 |
8.55e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 128.51 E-value: 8.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIE---------HVNVESTE 126
Cdd:PRK07788 102 VAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPpdlgrlrawGGNPDDDE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 127 WS-------DEVAAHSGTELTFQSASPAdlFMLIFTSGTSGEPKAVKCSHSK--VAIAGvtMTQRFGLGPDDVCYVSMPL 197
Cdd:PRK07788 182 PSgstdetlDDLIAGSSTAPLPKPPKPG--GIVILTSGTTGTPKGAPRPEPSplAPLAG--LLSRVPFRAGETTLLPAPM 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 198 FHSNAVLVgWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQ----PDDSEnpLRAVYgnegV 273
Cdd:PRK07788 258 FHATGWAH-LTLAMALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEvlakYDTSS--LKIIF----V 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 274 AG-----DL-ERFARRFGCVVQDGFGSTEggVAIArTPDTPA------GSLGPLPAG--IEIVDPDtGRPCPAGVVGEL- 338
Cdd:PRK07788 331 SGsalspELaTRALEAFGPVLYNLYGSTE--VAFA-TIATPEdlaeapGTVGRPPKGvtVKILDEN-GNEVPRGVVGRIf 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 339 VNTAGPgrFEGYYNDEAAEaerMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVY 418
Cdd:PRK07788 407 VGNGFP--FEGYTDGRDKQ---IIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVI 481
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2321332536 419 AVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAA 486
Cdd:PRK07788 482 GVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRD--NLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
152-484 |
1.54e-31 |
|
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: 126.72 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 152 LIFTSGTSGEPKAVKCSHSKVAI---AGVTMTQRFGLGPDDVCYVSMPLFHsNAVLVGWAVAAACQGSIALRRKFSASGF 228
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPdndTLMAAALGFGPGADSVYLSPAPLYH-AAPFRWSMTALFMGGTLVLMEKFDPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 229 IADVRRYGATYANYVGKPLSYVLATPEQPDDSEN--PLRAVYGNEGVAGDL--ERFARRFGCVVQDGFGSTEG-GVAIAR 303
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPWvkEQWIDWGGPIIWEYYGGTEGqGLTIIN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 304 TPD--TPAGSLG-PLPAGIEIVDPDtGRPCPAGVVGELVNTAGPGrFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYA 380
Cdd:cd05929 289 GEEwlTHPGSVGrAVLGKVHILDED-GNEVPPGEIGEVYFANGPG-FEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 381 YFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDT---DKFRVFLAEQpdLG 457
Cdd:cd05929 367 YLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTalaEELIAFLRDR--LS 444
|
330 340
....*....|....*....|....*..
gi 2321332536 458 PKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05929 445 RYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
55-484 |
2.10e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 126.56 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNpvRRGAA-----LLRD------INHADCQLVLADSASAGPlADIEHVNVE 123
Cdd:PRK08276 38 VVAILLENNPEFFEVYWAARRSGLYYTPIN--WHLTAaeiayIVDDsgakvlIVSAALADTAAELAAELP-AGVPLLLVV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 124 S------TEWSDEVAAHSGTELTFQSASpadlFMLIFTSGTSGEPKAVKCSHSKVAI---AGVTMTQ---RFGLGPDDVC 191
Cdd:PRK08276 115 AgpvpgfRSYEEALAAQPDTPIADETAG----ADMLYSSGTTGRPKGIKRPLPGLDPdeaPGMMLALlgfGMYGGPDSVY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 192 YVSMPLFHSnAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVgkPLSYV--LATPEQpddsenpLRAVYg 269
Cdd:PRK08276 191 LSPAPLYHT-APLRFGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLV--PTMFVrmLKLPEE-------VRARY- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 270 negvagDLE--RFA------------RR----FGCVVQDGFGSTEG-GVAIARTPD--TPAGSLG-PLPAGIEIVDPDtG 327
Cdd:PRK08276 260 ------DVSslRVAihaaapcpvevkRAmidwWGPIIHEYYASSEGgGVTVITSEDwlAHPGSVGkAVLGEVRILDED-G 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 328 RPCPAGVVGELVNTAGPGRFEgYYNDEAAEAE-RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVL 406
Cdd:PRK08276 333 NELPPGEIGTVYFEMDGYPFE-YHNDPEKTAAaRNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 407 LRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFD---TDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQ 483
Cdd:PRK08276 412 VTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGdalAAELIAWLRGR--LAHYKCPRSIDFEDELPRTPTGKLYKRR 489
|
.
gi 2321332536 484 L 484
Cdd:PRK08276 490 L 490
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
152-486 |
2.14e-31 |
|
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: 123.21 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 152 LIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSN--AVLVGWAVAAAcqgSIALRRKFSASGfi 229
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGglAILVRSLLAGA---ELVLLERNQALA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 230 ADVRRYGATYANYVGKPLSYVLATPEQPDDSENpLRAVY--GNEGVAGDLERFARRfGCVVQDGFGSTE--GGVAIARTP 305
Cdd:cd17630 80 EDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKS-LRAVLlgGAPIPPELLERAADR-GIPLYTTYGMTEtaSQVATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 306 DTPAGSLGPLPAGIEIVDPDTGRPCPagvvgelvntAGPGRFEGYYNDEAAEaERMAGGIYHSGDLAYRDDAGYAYFAGR 385
Cdd:cd17630 158 GFGRGGVGVLLPGRELRIVEDGEIWV----------GGASLAMGYLRGQLVP-EFNEDGWFTTKDLGELHADGRLTVLGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 386 LGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTrfDTDKFRVFLAEQpdLGPKQWPSYV 465
Cdd:cd17630 227 ADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA--DPAELRAWLKDK--LARFKLPKRI 302
|
330 340
....*....|....*....|.
gi 2321332536 466 RISAGLPGTVTFKVLKRQLAA 486
Cdd:cd17630 303 YPVPELPRTGGGKVDRRALRA 323
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
52-484 |
2.55e-31 |
|
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: 126.49 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 52 RPPHVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSA-------SAGPLADIEHVNVES 124
Cdd:TIGR02262 54 REERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGAllpvikaALGKSPHLEHRVVVG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 125 ------TEWSDEVAAHSGTELTfQSASPADLFMLIFTSGTSGEPKAVKCSHSK-VAIAGVTMTQRFGLGPDDVCYVSMPL 197
Cdd:TIGR02262 134 rpeageVQLAELLATESEQFKP-AATQADDPAFWLYSSGSTGMPKGVVHTHSNpYWTAELYARNTLGIREDDVCFSAAKL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 198 FHS----NAVLVGWAVAAAcqgSIALRRKFSASGFIADVRRYGATYanYVGKPLSY--VLATPEQPDDSENPLR-AVYGN 270
Cdd:TIGR02262 213 FFAyglgNALTFPMSVGAT---TVLMGERPTPDAVFDRLRRHQPTI--FYGVPTLYaaMLADPNLPSEDQVRLRlCTSAG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 271 EGVAGDL-ERFARRFGCVVQDGFGSTE-GGVAIARTP-DTPAGSLG-PLPA-GIEIVDpDTGRPCPAGVVGELVnTAGPG 345
Cdd:TIGR02262 288 EALPAEVgQRWQARFGVDIVDGIGSTEmLHIFLSNLPgDVRYGTSGkPVPGyRLRLVG-DGGQDVADGEPGELL-ISGPS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 346 RFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVV 425
Cdd:TIGR02262 366 SATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDG 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 426 GDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:TIGR02262 446 LIKPKAFVVLRPGQTALETELKEHVKDR--LAPYKYPRWIVFVDDLPKTATGKIQRFKL 502
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
152-481 |
4.80e-30 |
|
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: 119.91 E-value: 4.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 152 LIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIAD 231
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 232 VRRYGATYANyvGKPLSY--VLATPEQPDDSENPLR-AVYGNEGVAGDL-ERFARRFGC-VVQDGFGSTEGGVAIARTPD 306
Cdd:cd17638 85 IERERITVLP--GPPTLFqsLLDHPGRKKFDLSSLRaAVTGAATVPVELvRRMRSELGFeTVLTAYGLTEAGVATMCRPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 307 TPAgslgplpagiEIVDPDTGRPCPAGVV-----GELVnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYA 380
Cdd:cd17638 163 DDA----------ETVATTCGRACPGFEVriaddGEVL-VRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 381 YFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQ 460
Cdd:cd17638 232 RITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRER--LANYK 309
|
330 340
....*....|....*....|.
gi 2321332536 461 WPSYVRISAGLPGTVTFKVLK 481
Cdd:cd17638 310 VPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
89-488 |
7.70e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 122.46 E-value: 7.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 89 GAALLrdINHADCQLVLADSASAGPlaDIEHVNVE-----STEWSDEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPK 163
Cdd:PRK07470 104 GARAM--ICHADFPEHAAAVRAASP--DLTHVVAIggaraGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 164 AVKCSHSKVAIagvTMTQRF-----GLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGAT 238
Cdd:PRK07470 180 AAVLTHGQMAF---VITNHLadlmpGTTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSERFDPAEVWALVERHRVT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 239 YANYVGKPLSYVLATP--EQPDDSEnpLRAV-YgnegvAG------DLERFARRFGCVVQDGFGSTEGGVAIARTP---- 305
Cdd:PRK07470 257 NLFTVPTILKMLVEHPavDRYDHSS--LRYViY-----AGapmyraDQKRALAKLGKVLVQYFGLGEVTGNITVLPpalh 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 306 ---DTPA---GSLGPLPAGIEI-VDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAG 378
Cdd:PRK07470 330 daeDGPDariGTCGFERTGMEVqIQDDEGRELPPGETGEIC-VIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 379 YAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAeqPDLGP 458
Cdd:PRK07470 409 FLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLD--GKVAR 486
|
410 420 430
....*....|....*....|....*....|....
gi 2321332536 459 KQWPSYVRISAGLP----GTVTFKVLKRQLAAEG 488
Cdd:PRK07470 487 YKLPKRFFFWDALPksgyGKITKKMVREELEERG 520
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-487 |
9.11e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 122.55 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 114 LADIEHVNVESTEWSDEVAAhsgteltfqsaspadlfmLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYV 193
Cdd:PRK06087 172 IADYEPLTTAITTHGDELAA------------------VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMM 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 194 SMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRR------YGATyanyvgkPLSYVLATPEQPDDSENPLRAV 267
Cdd:PRK06087 234 PAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQqrctcmLGAT-------PFIYDLLNLLEKQPADLSALRF 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 268 Y--GNEGVAGDLERFARRFGCVVQDGFGSTEGGVAIARTPDTP----AGSLGPLPAGIEI--VDPDTgRPCPAGVVGELV 339
Cdd:PRK06087 307 FlcGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPlsrfMHTDGYAAAGVEIkvVDEAR-KTLPPGCEGEEA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 340 nTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVY 418
Cdd:PRK06087 386 -SRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 419 AVPDPVVGDRVMAALVLAPGTRFDT-DKFRVFLAEQpDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPHHSLTlEEVVAFFSRK-RVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
148-485 |
1.24e-29 |
|
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: 120.66 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSH-SKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNA----VLVGWAVAAACqgsIALRRK 222
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHrDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGlggvLLFPFGVGASG---VLLEEA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 223 fSASGFIADVRRYGATYanYVGKPLSY--VLATPEQPDDSENPLR-AVYGNEGVAGDL-ERFARRFGCVVQDGFGSTEG- 297
Cdd:cd05958 175 -TPDLLLSAIARYKPTV--LFTAPTAYraMLAHPDAAGPDLSSLRkCVSAGEALPAALhRAWKEATGIPIIDGIGSTEMf 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 298 GVAIARTP-DTPAGSLG-PLPA-GIEIVDpDTGRPCPAGVVGELVNTaGPgrfEGY-YNDEAAEAERMAGGIYHSGDLAY 373
Cdd:cd05958 252 HIFISARPgDARPGATGkPVPGyEAKVVD-DEGNPVPDGTIGRLAVR-GP---TGCrYLADKRQRTYVQGGWNITGDTYS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 374 RDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDkfrvfLAEQ 453
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPV-----LARE 401
|
330 340 350
....*....|....*....|....*....|....*...
gi 2321332536 454 ------PDLGPKQWPSYVRISAGLPGTVTFKVLKRQLA 485
Cdd:cd05958 402 lqdhakAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
55-440 |
2.00e-29 |
|
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: 120.90 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVrrgaALLRDINHA--DCQL-------VLADSASAGPLADIEH----VN 121
Cdd:cd05909 33 NVGVMLPPSAGGALANFALALSGKVPVMLNYT----AGLRELRACikLAGIktvltskQFIEKLKLHHLFDVEYdariVY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 122 VE----STEWSDEVAAhsGTELTFQSAS-----------PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLG 186
Cdd:cd05909 109 LEdlraKISKADKCKA--FLAGKFPPKWllrifgvapvqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 187 PDDVCYVSMPLFHSNAVLVGwaVAAACQGSIALRRKFS---ASGFIADVRRYGATYanyvgkplsyVLATP--------- 254
Cdd:cd05909 187 PEDVVFGALPFFHSFGLTGC--LWLPLLSGIKVVFHPNpldYKKIPELIYDKKATI----------LLGTPtflrgyara 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 255 EQPDDSENpLRAVY-GNEGVAGDL-ERFARRFGCVVQDGFGSTEGGVAIA-RTPDTP--AGSLG-PLPaGIE--IVDPDT 326
Cdd:cd05909 255 AHPEDFSS-LRLVVaGAEKLKDTLrQEFQEKFGIRILEGYGTTECSPVISvNTPQSPnkEGTVGrPLP-GMEvkIVSVET 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 327 GRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVL 406
Cdd:cd05909 333 HEEVPIGEGGLLL-VRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDIL 411
|
410 420 430
....*....|....*....|....*....|....*
gi 2321332536 407 L-RYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTR 440
Cdd:cd05909 412 SeILPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDP 446
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
56-487 |
3.31e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 120.30 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIEHVnvestewSDEVAAHS 135
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAAGRTDVEDL-------AAFIASAD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 136 GTELTFQSASPADLFMLI-FTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQ 214
Cdd:PRK09088 123 ALEPADTPSIPPERVSLIlFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 215 GSIALRRKFSAS---GFIADVRrYGATYanYVGKPlSYVLATPEQPDDSENPLR---AVY--GNEGVAGDLERFARRfGC 286
Cdd:PRK09088 203 GSILVSNGFEPKrtlGRLGDPA-LGITH--YFCVP-QMAQAFRAQPGFDAAALRhltALFtgGAPHAAEDILGWLDD-GI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 287 VVQDGFGSTEGGVAIARTPD-----TPAGSLG-PLPA-GIEIVDpDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAE 359
Cdd:PRK09088 278 PMVDGFGMSEAGTVFGMSVDcdvirAKAGAAGiPTPTvQTRVVD-DQGNDCPAGVPGELL-LRGPNLSPGYWRRPQATAR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 360 -RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG 438
Cdd:PRK09088 356 aFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 439 TRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKV----LKRQLAAE 487
Cdd:PRK09088 436 APLDLERIRSHLSTR--LAKYKVPKHLRLVDALPRTASGKLqkarLRDALAAG 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
146-484 |
8.32e-29 |
|
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: 116.81 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIAL------ 219
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 220 RRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYGNEGVAGDLERFARRFGCVVQDGFGSTEGGV 299
Cdd:cd05944 81 RNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 300 AIART-PDTPA--GSLG-PLPAG---IEIVDPDTG--RPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGD 370
Cdd:cd05944 161 LVAVNpPDGPKrpGSVGlRLPYArvrIKVLDGVGRllRDCAPDEVGEIC-VAGPGVFGGYLYTEGNKNAFVADGWLNTGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 371 LAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFL 450
Cdd:cd05944 240 LGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWA 319
|
330 340 350
....*....|....*....|....*....|....*
gi 2321332536 451 AEQ-PDLGPKqwPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05944 320 RDHvPERAAV--PKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
56-486 |
1.36e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 118.56 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADI-EHVNV--ESTEWSDEVA 132
Cdd:PRK13383 88 VGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGAdDAVAVidPATAGAEESG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 133 AHSGTeltfqsASPADLFMLifTSGTSGEPKAVKCSHSKVAIAGVTMT--QRFGLGPDDVCYVSMPLFHSNAvLVGWAVA 210
Cdd:PRK13383 168 GRPAV------AAPGRIVLL--TSGTTGKPKGVPRAPQLRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLG-LGMLMLT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 211 AACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDdSENPL---RAVYGnegvAGDL------ERFA 281
Cdd:PRK13383 239 IALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVR-ARNPLpqlRVVMS----SGDRldptlgQRFM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 282 RRFGCVVQDGFGSTEGGVAIARTP----DTPAgSLGPLPAG--IEIVDPDtGRPCPAGVVGELV---NTAGPGrfegyYN 352
Cdd:PRK13383 314 DTYGDILYNGYGSTEVGIGALATPadlrDAPE-TVGKPVAGcpVRILDRN-NRPVGPRVTGRIFvggELAGTR-----YT 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 353 DEAAEAerMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAA 432
Cdd:PRK13383 387 DGGGKA--VVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAF 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 433 LVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAA 486
Cdd:PRK13383 465 VVLHPGSGVDAAQLRDYLKDR--VSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
55-487 |
1.40e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 118.14 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSasagPLADiEHVNVESTEWSdEVAAH 134
Cdd:PRK03640 54 RVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD----DFEA-KLIPGISVKFA-ELMNG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 SGTELTFQSASPADLFM-LIFTSGTSGEPKAVKCS---HSKVAIAGVTmtqRFGLGPDDVCYVSMPLFH-SNAVLVGWAV 209
Cdd:PRK03640 128 PKEEAEIQEEFDLDEVAtIMYTSGTTGKPKGVIQTygnHWWSAVGSAL---NLGLTEDDCWLAAVPIFHiSGLSILMRSV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAACqgSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLAtpEQPDDSENP-LRAVYGNEGVAGD--LERFARRFGC 286
Cdd:PRK03640 205 IYGM--RVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLE--RLGEGTYPSsFRCMLLGGGPAPKplLEQCKEKGIP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 287 VVQDgFGSTEGGVAI-ARTPD---TPAGSLG-PL-PAGIEIVDpdTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAER 360
Cdd:PRK03640 281 VYQS-YGMTETASQIvTLSPEdalTKLGSAGkPLfPCELKIEK--DGVVVPPFEEGEIV-VKGPNVTKGYLNREDATRET 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 361 MAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGdRVMAALVLApGTR 440
Cdd:PRK03640 357 FQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG-QVPVAFVVK-SGE 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2321332536 441 FDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK03640 435 VTEEELRHFCEEK--LAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
127-484 |
1.70e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 119.29 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 127 WSDEVAAHSGTELTFQSA-SPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLV 205
Cdd:PRK07529 192 FDAELARQPGDRLFSGRPiGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLV 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 206 GWAVAAACQGSIAL------RRKFSASGFIADVRRYGATYANYVGKPLSYVLATP-EQPDDSEnpLRavYGNEGVA---- 274
Cdd:PRK07529 272 TGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPvDGHDISS--LR--YALCGAAplpv 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 275 GDLERFARRFGCVVQDGFGSTEGGVAIARTP-DTP--AGSLG-PLP---AGIEIVDPDTG--RPCPAGVVGELVnTAGPG 345
Cdd:PRK07529 348 EVFRRFEAATGVRIVEGYGLTEATCVSSVNPpDGErrIGSVGlRLPyqrVRVVILDDAGRylRDCAVDEVGVLC-IAGPN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 346 RFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVV 425
Cdd:PRK07529 427 VFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHA 506
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 426 GDRVMAALVLAPGTRFDTDKFRVFLAEQ---PDLGPKQwpsyVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK07529 507 GELPVAYVQLKPGASATEAELLAFARDHiaeRAAVPKH----VRILDALPKTAVGKIFKPAL 564
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
148-484 |
1.71e-28 |
|
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: 117.28 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVcyvsmplfHSNAVLVGWAVAA--------ACQGSIAL 219
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDV--------HWNISSPGWAKHAwscffapwNAGATVFL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 220 --RRKFSASGFIADVRRYGATyaNYVGKPLSYVLATPEQPDDSENPLRAVYGnegvAGD------LERFARRFGCVVQDG 291
Cdd:cd05974 158 fnYARFDAKRVLAALVRYGVT--TLCAPPTVWRMLIQQDLASFDVKLREVVG----AGEplnpevIEQVRRAWGLTIRDG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 292 FGSTEGGVAIARTPDTP--AGSLG-PLPA-GIEIVDPDtGRPCPAGVVGELVNTAGP-GRFEGYYNDEAAEAERMAGGIY 366
Cdd:cd05974 232 YGQTETTALVGNSPGQPvkAGSMGrPLPGyRVALLDPD-GAPATEGEVALDLGDTRPvGLMKGYAGDPDKTAHAMRGGYY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 367 HSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTD-K 445
Cdd:cd05974 311 RTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtA 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2321332536 446 FRVFLAEQPDLGPkqwpsYVRIS----AGLPGTVTFKVLKRQL 484
Cdd:cd05974 391 LEIFRFSRERLAP-----YKRIRrlefAELPKTISGKIRRVEL 428
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
56-485 |
2.09e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 118.04 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIEHV-NVESTEWSDEVAAH 134
Cdd:PRK06839 56 IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVsYVQRVISITSLKEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 SGTELT-FQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAAC 213
Cdd:PRK06839 136 EDRKIDnFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 214 QGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYgnEGVAGDLERFARRF---GCVVQD 290
Cdd:PRK06839 216 GGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFY--NGGAPCPEELMREFidrGFLFGQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 291 GFGSTEGGVAI--------ARTPdtpaGSLG-PLP-AGIEIVDPDTGRpCPAGVVGELVnTAGPGRFEGYYNDEAAEAER 360
Cdd:PRK06839 294 GFGMTETSPTVfmlseedaRRKV----GSIGkPVLfCDYELIDENKNK-VEVGEVGELL-IRGPNVMKEYWNRPDATEET 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 361 MAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTR 440
Cdd:PRK06839 368 IQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSV 447
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2321332536 441 FDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLA 485
Cdd:PRK06839 448 LIEKDVIEHCRLF--LAKYKIPKEIVFLKELPKNATGKIQKAQLV 490
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
56-484 |
2.68e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 117.88 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNT-PFFSAMLvAAGMSGIVPVGLN---PVRRGAALLRD------INHADcqlVLADSASAGPladiEHVNVEST 125
Cdd:PRK12406 39 VALLMRNDfAFFEAAY-AAMRLGAYAVPVNwhfKPEEIAYILEDsgarvlIAHAD---LLHGLASALP----AGVTVLSV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 126 EWSDEVAAHSGTELTFQSASPADLFM--------------------LIFTSGTSGEPKAVKCSHSKVAIAGVTMTQR--- 182
Cdd:PRK12406 111 PTPPEIAAAYRISPALLTPPAGAIDWegwlaqqepydgppvpqpqsMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRali 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 183 FGLGPDDVCYVSMPLFHSNAVLVGwAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQP----D 258
Cdd:PRK12406 191 YGLKPGIRALLTGPLYHSAPNAYG-LRAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVrakyD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 259 DSEnpLRAV-YGNEGVAGDLER-FARRFGCVVQDGFGSTEGGVAIARTPD---TPAGSLGPLPAGIEI--VDPDtGRPCP 331
Cdd:PRK12406 270 VSS--LRHViHAAAPCPADVKRaMIEWWGPVIYEYYGSTESGAVTFATSEdalSHPGTVGKAAPGAELrfVDED-GRPLP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 332 AGVVGEL-VNTAGPGRFEgYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYP 410
Cdd:PRK12406 347 QGEIGEIySRIAGNPDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVP 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 411 DTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK12406 426 GVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKAR--LAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
146-453 |
5.08e-28 |
|
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: 116.09 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAV--LVGWAVAAACQGSIALRRKF 223
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVweIFGALLAGATLVVLPEEVRK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 224 SASGFIADVRRYGATYANYVgkP--LSYVLATPEQPDDSenPLRAVY-GNEGVAGDL-ERFARRF-GCVVQDGFGSTEGG 298
Cdd:cd05930 172 DPEALADLLAEEGITVLHLT--PslLRLLLQELELAALP--SLRLVLvGGEALPPDLvRRWRELLpGARLVNLYGPTEAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 299 VAIA----RTPDTPAGS--LG-PLP-AGIEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAER-----MAGG- 364
Cdd:cd05930 248 VDATyyrvPPDDEEDGRvpIGrPIPnTRVYVLDEN-LRPVPPGVPGELY-IGGAGLARGYLNRPELTAERfvpnpFGPGe 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 365 -IYHSGDLAYRDDAGYAYFAGRLGDWM-----RVD-GEnlgtapIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAP 437
Cdd:cd05930 326 rMYRTGDLVRWLPDGNLEFLGRIDDQVkirgyRIElGE------IEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE 399
|
330
....*....|....*.
gi 2321332536 438 GTRFDTDKFRVFLAEQ 453
Cdd:cd05930 400 GGELDEEELRAHLAER 415
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
144-487 |
1.01e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 116.24 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLgPDDVCY-VSMPLFHSNAVLVGWAVAAAcqGSIALRRK 222
Cdd:PRK06188 165 ALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEW-PADPRFlMCTPLSHAGGAFFLPTLLRG--GTVIVLAK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 223 FSASGFIADVRRYGATYANYVGKPLsYVLAtpEQPDDSENPLRA----VYGNEGVAGDLERFA-RRFGCVVQDGFGSTEG 297
Cdd:PRK06188 242 FDPAEVLRAIEEQRITATFLVPTMI-YALL--DHPDLRTRDLSSletvYYGASPMSPVRLAEAiERFGPIFAQYYGQTEA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 298 GVAIA------RTPDTPA--GSLG-PLPA-GIEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYH 367
Cdd:PRK06188 319 PMVITylrkrdHDPDDPKrlTSCGrPTPGlRVALLDED-GREVAQGEVGEIC-VRGPLVMDGYWNRPEETAEAFRDGWLH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 368 SGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFR 447
Cdd:PRK06188 397 TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQ 476
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2321332536 448 VFLAEQPdlGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK06188 477 AHVKERK--GSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
55-487 |
1.63e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 116.03 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQ-LVLADS-----------------ASAGPLAD 116
Cdd:PRK12583 72 RVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRwVICADAfktsdyhamlqellpglAEGQPGAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 117 I-----EHVNVES---------TEWSDEVAAH---SGTELTFQSAS--PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGV 177
Cdd:PRK12583 152 AcerlpELRGVVSlapapppgfLAWHELQARGetvSREALAERQASldRDDPINIQYTSGTTGFPKGATLSHHNILNNGY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 178 TMTQRFGLGPDDVCYVSMPLFHS----NAVLVGWAVAAACqgsIALRRKFSASGFIADVRRYGATyANYvGKPLSYvLAT 253
Cdd:PRK12583 232 FVAESLGLTEHDRLCVPVPLYHCfgmvLANLGCMTVGACL---VYPNEAFDPLATLQAVEEERCT-ALY-GVPTMF-IAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 254 PEQPDDSENPLRAVygNEGV-AGD------LERFARRFGCV-VQDGFGSTEGG-VAIARTPDTP----AGSLGPLPAGIE 320
Cdd:PRK12583 306 LDHPQRGNFDLSSL--RTGImAGApcpievMRRVMDEMHMAeVQIAYGMTETSpVSLQTTAADDlerrVETVGRTQPHLE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 321 --IVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENL 397
Cdd:PRK12583 384 vkVVDPD-GATVPRGEIGELC-TRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENI 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 398 GTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTF 477
Cdd:PRK12583 462 YPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKAR--IAHFKVPRYFRFVDEFPMTVTG 539
|
490
....*....|...
gi 2321332536 478 KVLK---RQLAAE 487
Cdd:PRK12583 540 KVQKfrmREISIE 552
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
56-484 |
3.02e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 115.04 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPffsAMLVA---AGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAG----PLADIEH-----VNVE 123
Cdd:PRK08162 71 VAVLLPNIP---AMVEAhfgVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEvareALALLPGpkplvIDVD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 124 STEWSD---------EVAAHSGTElTFQSASPADLFMLI---FTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVC 191
Cdd:PRK08162 148 DPEYPGgrfigaldyEAFLASGDP-DFAWTLPADEWDAIalnYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 192 YVSMPLFHSNAVLVGWAVAAAcQGSIALRRKFSASGFIADVRRYGATYanYVGKP--LSYVLATPEQPddSENPLRAVYG 269
Cdd:PRK08162 227 LWTLPMFHCNGWCFPWTVAAR-AGTNVCLRKVDPKLIFDLIREHGVTH--YCGAPivLSALINAPAEW--RAGIDHPVHA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 270 NegVAGD------LERfARRFGCVVQDGFGSTE--GGVAI-ARTPDTPAGSLG-------------PLPAGIEIVDPDTG 327
Cdd:PRK08162 302 M--VAGAappaavIAK-MEEIGFDLTHVYGLTEtyGPATVcAWQPEWDALPLDeraqlkarqgvryPLQEGVTVLDPDTM 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 328 RPCPAG--VVGELV---NTAgpgrFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPI 402
Cdd:PRK08162 379 QPVPADgeTIGEIMfrgNIV----MKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEV 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 403 ERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAgLPGTVTFKVLKR 482
Cdd:PRK08162 455 EDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREH--LAGFKVPKAVVFGE-LPKTSTGKIQKF 531
|
..
gi 2321332536 483 QL 484
Cdd:PRK08162 532 VL 533
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
148-479 |
4.59e-27 |
|
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: 113.38 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVkcSHSKVAIAGVTMTQRFGLG--PDDVCYvsmplfhsNAVLVGWA--VAAACQGSIAL--RR 221
Cdd:cd05973 89 DPFVMMFTSGTTGLPKGV--PVPLRALAAFGAYLRDAVDlrPEDSFW--------NAADPGWAygLYYAITGPLALghPT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 222 KFSASGFIAD-----VRRYGATyaNYVGKPLSYVL---ATPEQPDDSENPLRAVY-GNEGVAGDLER-FARRFGCVVQDG 291
Cdd:cd05973 159 ILLEGGFSVEstwrvIERLGVT--NLAGSPTAYRLlmaAGAEVPARPKGRLRRVSsAGEPLTPEVIRwFDAALGVPIHDH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 292 FGSTEGGVAIAR--TPDTP--AGSLG-PLPAGIEIVDPDTGRPCPAGVVGEL---VNTAGPGRFEGYYNDEAAEAermAG 363
Cdd:cd05973 237 YGQTELGMVLANhhALEHPvhAGSAGrAMPGWRVAVLDDDGDELGPGEPGRLaidIANSPLMWFRGYQLPDTPAI---DG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 364 GIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDT 443
Cdd:cd05973 314 GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTP 393
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2321332536 444 DkfrvfLAEQPDLGPKQ------WPSYVRISAGLPGTVTFKV 479
Cdd:cd05973 394 A-----LADELQLHVKKrlsahaYPRTIHFVDELPKTPSGKI 430
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
144-453 |
6.87e-27 |
|
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: 112.73 E-value: 6.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVcYVSMPLFHSNAVLVGWAVAAACQGS-IALRRK 222
Cdd:cd05945 94 ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDV-FLNQAPFSFDLSVMDLYPALASGATlVPVPRD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 223 fsasgFIADVRRYGATYANYvgkPLSYVLATP--------EQPDDSEN--PLRAVY--GNEGVAGDLERFARRF-GCVVQ 289
Cdd:cd05945 173 -----ATADPKQLFRFLAEH---GITVWVSTPsfaamcllSPTFTPESlpSLRHFLfcGEVLPHKTARALQQRFpDARIY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 290 DGFGSTEGGVAIA--RTPDTPAGSLGPLPAG-------IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDE--AAEA 358
Cdd:cd05945 245 NTYGPTEATVAVTyiEVTPEVLDGYDRLPIGyakpgakLVILDED-GRPVPPGEKGELV-ISGPSVSKGYLNNPekTAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 359 ERMAGG--IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLA 436
Cdd:cd05945 323 FFPDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK 402
|
330
....*....|....*...
gi 2321332536 437 PGT-RFDTDKFRVFLAEQ 453
Cdd:cd05945 403 PGAeAGLTKAIKAELAER 420
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
319-487 |
8.30e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 113.75 E-value: 8.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 319 IEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENL 397
Cdd:PRK08315 382 VKIVDPETGETVPRGEQGELC-TRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENI 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 398 GTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTF 477
Cdd:PRK08315 461 YPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGK--IAHYKIPRYIRFVDEFPMTVTG 538
|
170
....*....|...
gi 2321332536 478 KVLK---RQLAAE 487
Cdd:PRK08315 539 KIQKfkmREMMIE 551
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
50-486 |
1.87e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 112.54 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 50 PARPPH-VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAG----PLADIEHVnVES 124
Cdd:PRK13382 89 PIGEPRvVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSAtvdrALADCPQA-TRI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 125 TEWSDE---------VAAHSGTELTfqsASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSM 195
Cdd:PRK13382 168 VAWTDEdhdltvevlIAAHAGQRPE---PTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 196 PLFHSnavlvgW-----AVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDD--SENPLR--A 266
Cdd:PRK13382 245 PMFHA------WgfsqlVLAASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNrySGRSLRfaA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 267 VYGNEGVAGDLERFARRFGCVVQDGFGSTEGG-VAIA------RTPDTpAGSlgplPAG---IEIVDPDtGRPCPAGVVG 336
Cdd:PRK13382 319 ASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGmIATAtpadlrAAPDT-AGR----PAEgteIRILDQD-FREVPTGEVG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 337 ELVnTAGPGRFEGYYNDEAAEaerMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVA 416
Cdd:PRK13382 393 TIF-VRNDTQFDGYTSGSTKD---FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAA 468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 417 VYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAA 486
Cdd:PRK13382 469 VIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDN--LANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
55-484 |
2.28e-26 |
|
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: 111.65 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRgaalLRDINHadcqLVLADSASAGPLADiEHVNVESTEWSDEVAAh 134
Cdd:cd05920 67 RVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHR----RSELSA----FCAHAEAVAYIVPD-RHAGFDHRALARELAE- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 sgteltfqsaSPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHsNAVLVGWAV--AAA 212
Cdd:cd05920 137 ----------SIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH-NFPLACPGVlgTLL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 213 CQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVygNEGVAGDLERFARR----FGCVV 288
Cdd:cd05920 206 AGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLL--QVGGARLSPALARRvppvLGCTL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 QDGFGSTEGGVAIAR---TPDTPAGSLG-PLPAG--IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM- 361
Cdd:cd05920 284 QQVFGMAEGLLNYTRlddPDEVIIHTQGrPMSPDdeIRVVDEE-GNPVPPGEEGELL-TRGPYTIRGYYRAPEHNARAFt 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 362 AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPgTRF 441
Cdd:cd05920 362 PDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPP 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2321332536 442 DTDKFRVFLAEQpdlGPKQW--PSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05920 441 SAAQLRRFLRER---GLAAYklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
51-488 |
4.84e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 110.46 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 51 ARPPHVGVLLQNTPFFSAMLVAAGMSGIVPVGLNP---VRRGAALLRDinhADCQLVLADSASAgpLADIEHVNVESTEW 127
Cdd:PRK07787 43 AGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPdsgVAERRHILAD---SGAQAWLGPAPDD--PAGLPHVPVRLHAR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 128 SDEVAAHSGTEltfqsaSPAdlfMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGW 207
Cdd:PRK07787 118 SWHRYPEPDPD------APA---LIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 208 AVAAACQGSIALRRKFSASGFiADVRRYGATYanYVGKPLSY--VLATPEQPDDSENPLRAVYGNEGV-AGDLERFARRF 284
Cdd:PRK07787 189 LGPLRIGNRFVHTGRPTPEAY-AQALSEGGTL--YFGVPTVWsrIAADPEAARALRGARLLVSGSAALpVPVFDRLAALT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 285 GCVVQDGFGSTEGGVAIARTPDTP--AGSLGPLPAGIE--IVDpDTGRPCPAGV--VGELvNTAGPGRFEGYYNDEAAEA 358
Cdd:PRK07787 266 GHRPVERYGMTETLITLSTRADGErrPGWVGLPLAGVEtrLVD-EDGGPVPHDGetVGEL-QVRGPTLFDGYLNRPDATA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 359 E-RMAGGIYHSGDLAYRDDAGYAYFAGRLG-DWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVla 436
Cdd:PRK07787 344 AaFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-- 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 437 PGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAEG 488
Cdd:PRK07787 422 GADDVAADELIDFVAQQ--LSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
55-484 |
4.91e-26 |
|
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: 110.82 E-value: 4.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGI--VPVGLN-PVRRGAALLRDinhADCQLVLADSASAGPLADIEHVNVEstewsDEV 131
Cdd:cd12114 39 LVAVTLPKGPEQVVAVLGILAAGAayVPVDIDqPAARREAILAD---AGARLVLTDGPDAQLDVAVFDVLIL-----DLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 132 AAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAA 211
Cdd:cd12114 111 ALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 212 AcQGSIAL----RRKfSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYgnegVAGDL------ERFA 281
Cdd:cd12114 191 A-GATLVLpdeaRRR-DPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVL----LSGDWipldlpARLR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 282 RRF-GCVVQDGFGSTEGGV-AIARTPDTPAGSLGPLPAG-------IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYN 352
Cdd:cd12114 265 ALApDARLISLGGATEASIwSIYHPIDEVPPDWRSIPYGrplanqrYRVLDPR-GRDCPDWVPGELW-IGGRGVALGYLG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 353 DEAAEAERM-----AGGIYHSGDLA-YRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPvvG 426
Cdd:cd12114 343 DPELTAARFvthpdGERLYRTGDLGrYRPD-GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP--G 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 427 DRVMAALVLA--PGTRFDTDKFRVFLAEQ-PDLGPkqwPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd12114 420 GKRLAAFVVPdnDGTPIAPDALRAFLAQTlPAYMI---PSRVIALEALPLTANGKVDRAAL 477
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
55-484 |
5.01e-26 |
|
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: 110.68 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHAD-CQLVLADSAsaGPLADIEHVNVESTEWSDEV-- 131
Cdd:cd05923 55 RVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEmTAAVIAVDA--QVMDAIFQSGVRVLALSDLVgl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 132 --AAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGL--GPDDVCYVSMPLFHSNAVLVGW 207
Cdd:cd05923 133 gePESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 208 AVAAACQGSIALRRKFSASGFIADVRRYGATyaNYVGKPLSY--VLATPEQPDDSENPLRAVygneGVAGD------LER 279
Cdd:cd05923 213 VAALALDGTYVVVEEFDPADALKLIEQERVT--SLFATPTHLdaLAAAAEFAGLKLSSLRHV----TFAGAtmpdavLER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 280 FARRFGCVVQDGFGSTEG-GVAIARTPDTPAGSLGPLPAGIEIVdPDTGRP---CPAGVVGELVNTA-GPGRFEGYYNDE 354
Cdd:cd05923 287 VNQHLPGEKVNIYGTTEAmNSLYMRDARTGTEMRPGFFSEVRIV-RIGGSPdeaLANGEEGELIVAAaADAAFTGYLNQP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 355 AAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALV 434
Cdd:cd05923 366 EATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVV 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2321332536 435 LAPGtRFDTDKFRVFLAEQPDLGPKQWPSYVRISAgLPGTVTFKVLKRQL 484
Cdd:cd05923 446 PREG-TLSADELDQFCRASELADFKRPRRYFFLDE-LPKNAMNKVLRRQL 493
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
141-484 |
7.99e-26 |
|
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: 110.63 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 141 FQSASPA---------DLFMLIFTSGTSGEPKAVKCSHSKVAIaGVTMTQRF--GLGPDDVCYvsmplfhsNAVLVGWAV 209
Cdd:cd05928 159 LNEASTEhhcvetgsqEPMAIYFTSGTTGSPKMAEHSHSSLGL-GLKVNGRYwlDLTASDIMW--------NTSDTGWIK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAAC-------QGS---IALRRKFSASGFIADVRRYGATyaNYVGKPLSYVLATpeQPDDSENPLRA----VYGNEGVAG 275
Cdd:cd05928 230 SAWSslfepwiQGAcvfVHHLPRFDPLVILKTLSSYPIT--TFCGAPTVYRMLV--QQDLSSYKFPSlqhcVTGGEPLNP 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 276 D-LERFARRFGCVVQDGFGSTEGGV--AIARTPDTPAGSLGP--LPAGIEIVDpDTGRPCPAGVVGELVNTAGPGR---- 346
Cdd:cd05928 306 EvLEKWKAQTGLDIYEGYGQTETGLicANFKGMKIKPGSMGKasPPYDVQIID-DNGNVLPPGTEGDIGIRVKPIRpfgl 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 347 FEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVG 426
Cdd:cd05928 385 FSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRG 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 427 DRVMAALVLAPGTR-FDTDKFRVFLAE--QPDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05928 465 EVVKAFVVLAPQFLsHDPEQLTKELQQhvKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
56-453 |
1.05e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 110.07 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAG---PLADIEHVNVESTEWSDEVA 132
Cdd:PLN02246 78 VMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDklkGLAEDDGVTVVTIDDPPEGC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 133 AH-------SGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHsKVAIAGVtmTQR-------FGLGPDDVCYVSMPLF 198
Cdd:PLN02246 158 LHfseltqaDENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH-KGLVTSV--AQQvdgenpnLYFHSDDVILCVLPMF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 199 HS---NAVLV-GWAVAAAcqgsIALRRKFSASGFIADVRRYGATYANYVgKPLsyVLATPEQPDDSENPLRAV----YGN 270
Cdd:PLN02246 235 HIyslNSVLLcGLRVGAA----ILIMPKFEIGALLELIQRHKVTIAPFV-PPI--VLAIAKSPVVEKYDLSSIrmvlSGA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 271 EGVAGDLER-FARRF-GCVVQDGFGSTEGG------VAIARTP-DTPAGSLGPL--PAGIEIVDPDTGRPCPAGVVGELV 339
Cdd:PLN02246 308 APLGKELEDaFRAKLpNAVLGQGYGMTEAGpvlamcLAFAKEPfPVKSGSCGTVvrNAELKIVDPETGASLPRNQPGEIC 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 340 nTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVY 418
Cdd:PLN02246 388 -IRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVV 466
|
410 420 430
....*....|....*....|....*....|....*
gi 2321332536 419 AVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQ 453
Cdd:PLN02246 467 PMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQ 501
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
148-479 |
1.67e-25 |
|
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: 106.96 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSH-SKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSAS 226
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANkTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 227 GFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAV-YGNEGVAGDLERFARRFGCV-VQDGFGSTEGGVAIART 304
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIgYGGSRAIAADVRFIEATGLTnTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 305 PD---TPAGSLG-PLP-AGIEIVDPDtGRPCPAGVVGELVNTAgPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGY 379
Cdd:cd17635 162 TDddsIEINAVGrPYPgVDVYLAATD-GIAGPSASFGTIWIKS-PANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 380 AYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPgtrfDTDKFRV---FLAEQPDL 456
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA----ELDENAIralKHTIRREL 315
|
330 340
....*....|....*....|...
gi 2321332536 457 GPKQWPSYVRISAGLPGTVTFKV 479
Cdd:cd17635 316 EPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
113-484 |
2.14e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 109.28 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 113 PLADIEHVNVesTEWSDEVAAhsGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKV---AIAGVTMtqrFGLGPDD 189
Cdd:PRK08314 160 PLQALAPGGV--VAWKEALAA--GLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmanAVGSVLW---SNSTPES 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 190 VCYVSMPLFHSNAVLVGWAVAAACQGSIAL--RRKFSASGFIadVRRYGATYANYVGKPLSYVLATP--EQPDDSEnpLR 265
Cdd:PRK08314 233 VVLAVLPLFHVTGMVHSMNAPIYAGATVVLmpRWDREAAARL--IERYRVTHWTNIPTMVVDFLASPglAERDLSS--LR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 266 AVYGN-----EGVAgdlERFARRFGCVVQDGFGSTEggvAIARTPDTPAGSLGPLPAGI-------EIVDPDTGRPCPAG 333
Cdd:PRK08314 309 YIGGGgaampEAVA---ERLKELTGLDYVEGYGLTE---TMAQTHSNPPDRPKLQCLGIptfgvdaRVIDPETLEELPPG 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 334 VVGELVnTAGPGRFEGYYNDEAAEAE---RMAGGIY-HSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRY 409
Cdd:PRK08314 383 EVGEIV-VHGPQVFKGYWNRPEATAEafiEIDGKRFfRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKH 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2321332536 410 PDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQPDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK08314 462 PAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
143-484 |
2.52e-25 |
|
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: 108.22 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 143 SASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDvCYVSMPLFHSNAVLVGWAVAAACQGSIALR-- 220
Cdd:cd17649 90 THHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGD-RELQFASFNFDGAHEQLLPPLICGACVVLRpd 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 221 RKFSASGFIAD-VRRYGATYANYvgkPLSY----VLATPEQPDDSENPLRA-VYGNEGVAGDLERFARRFGCVVQDGFGS 294
Cdd:cd17649 169 ELWASADELAEmVRELGVTVLDL---PPAYlqqlAEEADRTGDGRPPSLRLyIFGGEALSPELLRRWLKAPVRLFNAYGP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 295 TEGGV-AIARTPDTPAGSLGP-LPAG-------IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAER----- 360
Cdd:cd17649 246 TEATVtPLVWKCEAGAARAGAsMPIGrplggrsAYILDAD-LNPVPVGVTGELY-IGGEGLARGYLGRPELTAERfvpdp 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 361 -MAGG--IYHSGDLA-YRDDAGYAYfAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPvVGDRVMAALVLA 436
Cdd:cd17649 324 fGAPGsrLYRTGDLArWRDDGVIEY-LGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLR 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2321332536 437 PGTRFDTDK--FRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17649 402 AAAAQPELRaqLRTALRAS--LPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
51-484 |
2.76e-25 |
|
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: 108.53 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 51 ARPPH--VGVLLQNTPFFSAMLVAAGMSGIVPVGLN---PVRRGAALLRDinhADCQLVLADSASAGPLADIEHVnVEST 125
Cdd:cd12116 33 GVGPGdrVAVYLPRSARLVAAMLAVLKAGAAYVPLDpdyPADRLRYILED---AEPALVLTDDALPDRLPAGLPV-LLLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 126 EWSDEVAAHSGTEltfqSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDD-------VCY------ 192
Cdd:cd12116 109 LAAAAAAPAAPRT----PVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDrllavttYAFdislle 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 193 VSMPLFHSNAVLVgwAVAAACQGSIALRRKFSASGfIADVRrygATYANYVGkplsyVLATPEQPddsENPLRAVYGNEG 272
Cdd:cd12116 185 LLLPLLAGARVVI--APRETQRDPEALARLIEAHS-ITVMQ---ATPATWRM-----LLDAGWQG---RAGLTALCGGEA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 273 VAGDL-ERFARRFGCVVQdGFGSTEGGVAIARTPDTPAgsLGPLPAG-------IEIVDPDtGRPCPAGVVGELVnTAGP 344
Cdd:cd12116 251 LPPDLaARLLSRVGSLWN-LYGPTETTIWSTAARVTAA--AGPIPIGrplantqVYVLDAA-LRPVPPGVPGELY-IGGD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 345 GRFEGYYNDEAAEAERM--------AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVA 416
Cdd:cd12116 326 GVAQGYLGRPALTAERFvpdpfagpGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 417 VYAVPDPvvGDRVMAALVLAP-GTRFDTDKFRVFLAEQPdlgPKQW-PSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd12116 406 VVVREDG--GDRRLVAYVVLKaGAAPDAAALRAHLRATL---PAYMvPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
118-438 |
3.04e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 109.21 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 118 EHVNVESTEWS-DEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDV--CyVS 194
Cdd:PRK04319 175 EDVEEGPGTLDfNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVywC-TA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 195 MPlfhsnavlvGWA-------VAAACQG--SIALRRKFSASGFIADVRRYGAT--Y-----------------ANYVGKP 246
Cdd:PRK04319 254 DP---------GWVtgtsygiFAPWLNGatNVIDGGRFSPERWYRILEDYKVTvwYtaptairmlmgagddlvKKYDLSS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 247 LSYVLATPEqpddsenPLRAvygnEGVAGDLERFARRfgcvVQDGFGSTE-GGVAIARTP--DTPAGSLG-PLPaGIE-- 320
Cdd:PRK04319 325 LRHILSVGE-------PLNP----EVVRWGMKVFGLP----IHDNWWMTEtGGIMIANYPamDIKPGSMGkPLP-GIEaa 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 321 IVDpDTGRPCPAGVVGELVNTAG-PGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGT 399
Cdd:PRK04319 389 IVD-DQGNELPPNRMGNLAIKKGwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGP 467
|
330 340 350
....*....|....*....|....*....|....*....
gi 2321332536 400 APIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG 438
Cdd:PRK04319 468 FEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPG 506
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
56-484 |
3.32e-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: 108.20 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLN---PVRRGAALLRDinhADCQLVLADSASAGPLADIEHVnveSTEWSDEVA 132
Cdd:cd17651 48 VALCARRSAELVVALLAILKAGAAYVPLDpayPAERLAFMLAD---AGPVLVLTHPALAGELAVELVA---VTLLDQPGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 133 AHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAvAAA 212
Cdd:cd17651 122 AAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFS-TLC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 213 CQGSIALRR---KFSASGFIADVRRYGAT--YANYVgkplsYVLATPEQPDDSENP---LRAVY-GNE--GVAGDLERF- 280
Cdd:cd17651 201 AGATLVLPPeevRTDPPALAAWLDEQRISrvFLPTV-----ALRALAEHGRPLGVRlaaLRYLLtGGEqlVLTEDLREFc 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 281 ARRFGCVVQDGFGSTEGGVAIART-PDTPAGSLGPLPAG-------IEIVDPDtGRPCPAGVVGELvNTAGPGRFEGYYN 352
Cdd:cd17651 276 AGLPGLRLHNHYGPTETHVVTALSlPGDPAAWPAPPPIGrpidntrVYVLDAA-LRPVPPGVPGEL-YIGGAGLARGYLN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 353 DEAAEAERMA-------GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVV 425
Cdd:cd17651 354 RPELTAERFVpdpfvpgARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 426 GDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17651 434 EKRLVAYVVGDPEAPVDAAELRAALATH--LPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
56-487 |
4.09e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 108.59 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLAD------IEHVNVES----- 124
Cdd:PRK06178 86 VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQvraetsLRHVIVTSladvl 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 125 -------------------TEWSDEVAAHSGTELTFQSASPA--DLFMLIFTSGTSGEPKAvkCSHSK---VAIAGVTMT 180
Cdd:PRK06178 166 paeptlplpdslraprlaaAGAIDLLPALRACTAPVPLPPPAldALAALNYTGGTTGMPKG--CEHTQrdmVYTAAAAYA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 181 QRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDS 260
Cdd:PRK06178 244 VAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 261 ENPLRAVYGNEGVAGDLERFARRF----GCVVQDG-FGSTEggvaiARTPDT---------------PAGSLGPLP-AGI 319
Cdd:PRK06178 324 LSSLRQVRVVSFVKKLNPDYRQRWraltGSVLAEAaWGMTE-----THTCDTftagfqdddfdllsqPVFVGLPVPgTEF 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 320 EIVDPDTGRPCPAGVVGELVNTAgPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGT 399
Cdd:PRK06178 399 KICDFETGELLPLGAEGEIVVRT-PSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFP 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 400 APIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSyVRISAGLPGTVTFKV 479
Cdd:PRK06178 478 SEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCREN--MAVYKVPE-IRIVDALPMTATGKV 554
|
....*...
gi 2321332536 480 LKRQLAAE 487
Cdd:PRK06178 555 RKQDLQAL 562
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
281-487 |
4.33e-25 |
|
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: 108.31 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 281 ARR----FGCVVQDGFGSTEGGVAIARtPDTP----AGSLG-PLPAG--IEIVDPDtGRPCPAGVVGELVnTAGPGRFEG 349
Cdd:COG1021 317 ARRvrpaLGCTLQQVFGMAEGLVNYTR-LDDPeeviLTTQGrPISPDdeVRIVDED-GNPVPPGEVGELL-TRGPYTIRG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 350 YYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDR 428
Cdd:COG1021 394 YYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGER 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 429 VMAALVLApGTRFDTDKFRVFLAEQpDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:COG1021 474 SCAFVVPR-GEPLTLAELRRFLRER-GLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
138-484 |
4.34e-25 |
|
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: 107.05 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 138 ELTFQSASPA----DLFMLIFTSGTSGEPKAVKCS---HSKVAIAGVtmtQRFGLGPDDVCYVSMPLFH-SNAVLVGWAV 209
Cdd:cd05912 64 ELAFQLKDSDvkldDIATIMYTSGTTGKPKGVQQTfgnHWWSAIGSA---LNLGLTEDDNWLCALPLFHiSGLSILMRSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAACqgSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLAtpEQPDDSENPLRAVY-GNEGVAGDLERFARRFGCVV 288
Cdd:cd05912 141 IYGM--TVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE--ILGEGYPNNLRCILlGGGPAPKPLLEQCKEKGIPV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 QDGFGSTEGGVAIAR-TPD---TPAGSLG-PL-PAGIEIVDPDTgrpcPAGVVGELVnTAGPGRFEGYYNDEAAEAERMA 362
Cdd:cd05912 217 YQSYGMTETCSQIVTlSPEdalNKIGSAGkPLfPVELKIEDDGQ----PPYEVGEIL-LKGPNVTKGYLNRPDATEESFE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 363 GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLApgTRFD 442
Cdd:cd05912 292 NGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPIS 369
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2321332536 443 TDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05912 370 EEELIAYCSEK--LAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
148-484 |
1.57e-24 |
|
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: 106.84 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQ-RFG--LGPDDVCYVSMPLFHSNAVL--VGWAVaaaCQGSIALRRK 222
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGnqIIPDTAILTVIPFHHGFGMFttLGYLI---CGFRVVLMYK 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 223 FSASGFIADVRRYGATYANYVgKPLSYVLATPEQPD--DSENPLRAVYGNEGVAGDL-ERFARRFGC-VVQDGFGSTEGG 298
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLV-PTLFAFFAKSTLVDkyDLSNLHEIASGGAPLSKEVgEAVAKRFKLpGIRQGYGLTETT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 299 VAIARTPDT--PAGSLGPLPAGIE--IVDPDTGRPCPAGVVGELVnTAGPGRFEGYYND-EAAEAERMAGGIYHSGDLAY 373
Cdd:cd17642 341 SAILITPEGddKPGAVGKVVPFFYakVVDLDTGKTLGPNERGELC-VKGPMIMKGYVNNpEATKALIDKDGWLHSGDIAY 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 374 RDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQ 453
Cdd:cd17642 420 YDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQ 499
|
330 340 350
....*....|....*....|....*....|.
gi 2321332536 454 PDLGpKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17642 500 VSTA-KRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
145-493 |
2.08e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.40 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 145 SPAdlfMLIFTSGTSGEPKAVKCSHSKvaIAGVTMTQRFGLG---PDDVCYVSMPLFHSNA---VLVGWAVAAACqgSIA 218
Cdd:PRK07786 175 SPA---LIMYTSGTTGRPKGAVLTHAN--LTGQAMTCLRTNGadiNSDVGFVGVPLFHIAGigsMLPGLLLGAPT--VIY 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 219 LRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPE-QPDDSEnpLRAVYGNEGVAGD--LERFARRF-GCVVQDGFGS 294
Cdd:PRK07786 248 PLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQaRPRDLA--LRVLSWGAAPASDtlLRQMAATFpEAQILAAFGQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 295 TE---------GGVAIARTpdtpaGSLG-PLPA-GIEIVDpDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAG 363
Cdd:PRK07786 326 TEmspvtcmllGEDAIRKL-----GSVGkVIPTvAARVVD-ENMNDVPVGEVGEIV-YRAPTLMSGYWNNPEATAEAFAG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 364 GIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGT-RFD 442
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDaALT 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 443 TDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL-----AAEGVDCGD 493
Cdd:PRK07786 479 LEDLAEFLTDR--LARYKHPKALEIVDALPRNPAGKVLKTELrerygACVNVERRS 532
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
56-487 |
2.78e-24 |
|
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: 107.25 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPffsAMLVAagMSGI-------VPVGLN-PVRRGAALLRDinhADCQLVLADSASAGPLAD--IEHVNVEST 125
Cdd:COG1020 529 VGVCLERSL---EMVVA--LLAVlkagaayVPLDPAyPAERLAYMLED---AGARLVLTQSALAARLPElgVPVLALDAL 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 126 EWSDEvaahsGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVA--IAGvtMTQRFGLGPDDVcyvsMPLFHS--- 200
Cdd:COG1020 601 ALAAE-----PATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVnlLAW--MQRRYGLGPGDR----VLQFASlsf 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 201 --------NAVLVGWAVAAACQGSIAlrrkfSASGFIADVRRYGATYANYVgkPlSYVLATPEQPDDSENPLRAVY-GNE 271
Cdd:COG1020 670 dasvweifGALLSGATLVLAPPEARR-----DPAALAELLARHRVTVLNLT--P-SLLRALLDAAPEALPSLRLVLvGGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 272 GVAGDL-ERFARRF-GCVVQDGFGSTEGGV-AIARTPDTPAGSLGPLPAG-------IEIVDPDtGRPCPAGVVGELVnT 341
Cdd:COG1020 742 ALPPELvRRWRARLpGARLVNLYGPTETTVdSTYYEVTPPDADGGSVPIGrpiantrVYVLDAH-LQPVPVGVPGELY-I 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 342 AGPGRFEGYYNDEAAEAER-------MAGG-IYHSGDLAYRDDAGYAYFAGRL-------GdwMRVD-GEnlgtapIERV 405
Cdd:COG1020 820 GGAGLARGYLNRPELTAERfvadpfgFPGArLYRTGDLARWLPDGNLEFLGRAddqvkirG--FRIElGE------IEAA 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 406 LLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQPDLGPkqWPSYVRISAGLPGTVTFKVLKRQLA 485
Cdd:COG1020 892 LLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYM--VPAAVVLLLPLPLTGNGKLDRLALP 969
|
..
gi 2321332536 486 AE 487
Cdd:COG1020 970 AP 971
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
146-484 |
3.70e-24 |
|
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: 104.70 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKVaIAGVTMTQR-FGLGPDDVCYvsmpLFHSNA----VLVGWAvAAACQGSIAL- 219
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANV-LALFAATQRwFGFNEDDVWT----LFHSYAfdfsVWEIWG-ALLHGGRLVVv 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 220 ----RRkfSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAV-YGNEGV-AGDLERFARRFGCV---VQD 290
Cdd:cd17643 166 pyevAR--SPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYViFGGEALeAAMLRPWAGRFGLDrpqLVN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 291 GFGSTEGGVAIARTPDTPA------GSL--GPLPA-GIEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM 361
Cdd:cd17643 244 MYGITETTVHVTFRPLDAAdlpaaaASPigRPLPGlRVYVLDAD-GRPVPPGVVGELY-VSGAGVARGYLGRPELTAERF 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 362 ----AGGI----YHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAAL 433
Cdd:cd17643 322 vanpFGGPgsrmYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYV 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 434 VLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17643 402 VADDGAAADIAELRALLKEL--LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
58-484 |
3.70e-24 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 105.83 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 58 VLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADI--------EHVNVESTEWSD 129
Cdd:PLN02330 85 VVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLglpvivlgEEKIEGAVNWKE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 130 --EVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVaIAGVTMTQrFGLGPDDVCYVS----MPLFHSNAV 203
Cdd:PLN02330 165 llEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNL-VANLCSSL-FSVGPEMIGQVVtlglIPFFHIYGI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 204 lVGWAVAA-ACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATP--EQPDDSENPLRAVYGNEG-VAGDL-E 278
Cdd:PLN02330 243 -TGICCATlRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPivEEFDLSKLKLQAIMTAAApLAPELlT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 279 RFARRF-GCVVQDGFGSTEGGVAIARTPDTPAG-------SLGPLPAGIEI--VDPDTGRPCPAGVVGELVnTAGPGRFE 348
Cdd:PLN02330 322 AFEAKFpGVQVQEAYGLTEHSCITLTHGDPEKGhgiakknSVGFILPNLEVkfIDPDTGRSLPKNTPGELC-VRSQCVMQ 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 349 GYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGD 427
Cdd:PLN02330 401 GYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGE 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 428 RVMAALVLAPGTRFDTDKFRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PLN02330 481 IPAACVVINPKAKESEEDILNFVAA--NVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
145-487 |
3.94e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 105.85 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 145 SPADLFMLIFTSGTSGEPKAVKCSHSKVaIAGVTMTQRF--GLGPDD-VCYVSMPLFHSNAVLVGWAVAAACQGSIALRR 221
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNL-FANAAQGKAWvpGLGDGPeRVLAALPMFHAYGLTLCLTLAVSIGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 222 KFSASGFIADVRRYGATYANYVgkPLSY--VLATPEQPDDSENPLR-AVYGnegvAGDL-----ERFARRFGCVVQDGFG 293
Cdd:PRK05605 296 APDIDLILDAMKKHPPTWLPGV--PPLYekIAEAAEERGVDLSGVRnAFSG----AMALpvstvELWEKLTGGLLVEGYG 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 294 STEGGVAIARTPDTP---AGSLG-PLPAG-IEIVDPDT-GRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYH 367
Cdd:PRK05605 370 LTETSPIIVGNPMSDdrrPGYVGvPFPDTeVRIVDPEDpDETMPDGEEGELL-VRGPQVFKGYWNRPEETAKSFLDGWFR 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 368 SGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFR 447
Cdd:PRK05605 449 TGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLR 528
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2321332536 448 VFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK05605 529 AYCREH--LTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
56-484 |
4.58e-24 |
|
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: 104.98 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPffsAMLVaaGMSGI-------VPVGLN-PVRRGAALLRDinhADCQLVLADSASAGPLADIEHVNVESTEW 127
Cdd:cd12117 50 VGVLAERSP---ELVV--ALLAVlkagaayVPLDPElPAERLAFMLAD---AGAKVLLTDRSLAGRAGGLEVAVVIDEAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 128 SDEVAAHSGTeltfqSASPADLFMLIFTSGTSGEPKAVKCSHSkvAIAGVTMTQRFG-LGPDDVCyvsmpLFHSN----- 201
Cdd:cd12117 122 DAGPAGNPAV-----PVSPDDLAYVMYTSGSTGRPKGVAVTHR--GVVRLVKNTNYVtLGPDDRV-----LQTSPlafda 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 202 -------AVLVGWAVAAACQGSIALRRKFSASgfiadVRRYGATYAnYVGKPLSYVLAtpeqpddSENP-----LRAVY- 268
Cdd:cd12117 190 stfeiwgALLNGARLVLAPKGTLLDPDALGAL-----IAEEGVTVL-WLTAALFNQLA-------DEDPecfagLRELLt 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 269 GNEGVAGDLERFARRFGC--VVQDGFGSTEGGV-AIARTPDTPAGSLGPLPAG-------IEIVDPDtGRPCPAGVVGEL 338
Cdd:cd12117 257 GGEVVSPPHVRRVLAACPglRLVNGYGPTENTTfTTSHVVTELDEVAGSIPIGrpiantrVYVLDED-GRPVPPGVPGEL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 339 VnTAGPGRFEGYYNDEAAEAERMA-------GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPD 411
Cdd:cd12117 336 Y-VGGDGLALGYLNRPALTAERFVadpfgpgERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPG 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 412 TAEVAVYAVPDPVVGDRVMAALVLAPGTrfDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd12117 415 VREAVVVVREDAGGDKRLVAYVVAEGAL--DAAELRAFLRER--LPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
148-487 |
5.09e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 105.50 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKV---AIAGVTMTQRFGLGPDDVCYVsMPLFHSNAVLVGWAVAAACQGSIALRRKFS 224
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLvsnTLMGVQWLYNCKEGEEVVLGV-LPFFHVYGMTAVMNLSIMQGYKMVLIPKFD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 225 ASGFIADVRRYGATYanYVGKPLSYV--LATPEQPDDSENPLRA-VYGNEGVAGDL-ERFARRFGCVVQDGFGSTEGGVA 300
Cdd:PRK06710 286 MKMVFEAIKKHKVTL--FPGAPTIYIalLNSPLLKEYDISSIRAcISGSAPLPVEVqEKFETVTGGKLVEGYGLTESSPV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 301 I-------ARTPdtpaGSLG-PLP-AGIEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDL 371
Cdd:PRK06710 364 ThsnflweKRVP----GSIGvPWPdTEAMIMSLETGEALPPGEIGEIV-VKGPQIMKGYWNKPEETAAVLQDGWLHTGDV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 372 AYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLA 451
Cdd:PRK06710 439 GYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFAR 518
|
330 340 350
....*....|....*....|....*....|....*.
gi 2321332536 452 EQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK06710 519 KY--LAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
151-444 |
2.57e-23 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 100.45 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 151 MLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSnAVLVGWAVAAACQGSIALRRKFSASGFIA 230
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 231 DVRRYGATYANYVGKPLSYVLA--TPEQPDDSEnpLRAVYG----NEGVAGDLERFARRFGcvvqdGFGSTEGG-----V 299
Cdd:cd17636 83 LIEAERCTHAFLLPPTIDQIVElnADGLYDLSS--LRSSPAapewNDMATVDTSPWGRKPG-----GYGQTEVMglatfA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 300 AIARTPDTPAGSLGPLpAGIEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGY 379
Cdd:cd17636 156 ALGGGAIGGAGRPSPL-VQVRILDED-GREVPDGEVGEIV-ARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2321332536 380 AYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTD 444
Cdd:cd17636 233 LSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEA 297
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
127-480 |
3.30e-23 |
|
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: 103.04 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 127 WSDEVAAHSGTELTfQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAI-AGVTMTQRFGLGPDDVCYVsmplfhsnAVLV 205
Cdd:cd17634 213 WRDLIAKASPEHQP-EAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVyAATTMKYVFDYGPGDIYWC--------TADV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 206 GWAVAAA--CQGSIALrrkfSASGFIAD--------------VRRYGATYANYvgKPLSYVLATPEQPDDSENPLRAVYG 269
Cdd:cd17634 284 GWVTGHSylLYGPLAC----GATTLLYEgvpnwptparmwqvVDKHGVNILYT--APTAIRALMAAGDDAIEGTDRSSLR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 270 NEGVAGD------LERFARRFG---CVVQDGFGSTEGGVAIArtpdTPAGSLGPLPAG----------IEIVDpDTGRPC 330
Cdd:cd17634 358 ILGSVGEpinpeaYEWYWKKIGkekCPVVDTWWQTETGGFMI----TPLPGAIELKAGsatrpvfgvqPAVVD-NEGHPQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 331 PAGVVGELVNTAG-PGRFEGYYNDEAAEAE---RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVL 406
Cdd:cd17634 433 PGGTEGNLVITDPwPGQTRTLFGDHERFEQtyfSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVL 512
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 407 LRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG-TRFDT--DKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVL 480
Cdd:cd17634 513 VAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGvEPSPElyAELRNWVRKE--IGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
152-484 |
5.32e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 102.08 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 152 LIFTSGTSGEPKAVKCSHSKVAIA---GVTM--TQRFGLGPDDVCYVSMPLFHSnAVLVGWAVAAACQGSIALRRKFSAS 226
Cdd:PRK13391 159 MLYSSGTTGRPKGIKRPLPEQPPDtplPLTAflQRLWGFRSDMVYLSPAPLYHS-APQRAVMLVIRLGGTVIVMEHFDAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 227 GFIADVRRYGATYANYVGKPLSYVLATPEQPDDSEN--PLR-AVYGNEGVAGDL-ERFARRFGCVVQDGFGSTEG-GVAI 301
Cdd:PRK13391 238 QYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDlsSLEvAIHAAAPCPPQVkEQMIDWWGPIIHEYYAATEGlGFTA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 302 ARTPDTPA--GSLG-PLPAGIEIVDPDtGRPCPAGVVGElVNTAGPGRFEgYYNDEA--AEAERMAGGIYHSGDLAYRDD 376
Cdd:PRK13391 318 CDSEEWLAhpGTVGrAMFGDLHILDDD-GAELPPGEPGT-IWFEGGRPFE-YLNDPAktAEARHPDGTWSTVGDIGYVDE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 377 AGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTD---KFRVFLAEQ 453
Cdd:PRK13391 395 DGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPAlaaELIAFCRQR 474
|
330 340 350
....*....|....*....|....*....|.
gi 2321332536 454 pdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK13391 475 --LSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
56-444 |
6.77e-23 |
|
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: 101.93 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAAL--LRDInHADCQ--LVLADSASAGPLADIEH----VNVESTEW 127
Cdd:cd05931 51 VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAerLAAI-LADAGprVVLTTAAALAAVRAFAAsrpaAGTPRLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 128 SDEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCyVS-MPLFHSNAVLVG 206
Cdd:cd05931 130 VDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV-VSwLPLYHDMGLIGG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 207 WAVAAACQGSIALrrkFSASGFIAD-------VRRYGATYAnyVGKPLSYVLA----TPEQP---DDSEnpLRAVY-GNE 271
Cdd:cd05931 209 LLTPLYSGGPSVL---MSPAAFLRRplrwlrlISRYRATIS--AAPNFAYDLCvrrvRDEDLeglDLSS--WRVALnGAE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 272 GV-AGDLERFARRFG-------------------------------CVVQDGFGSTEGGVAIARTPDTPAG---SLGPLP 316
Cdd:cd05931 282 PVrPATLRRFAEAFApfgfrpeafrpsyglaeatlfvsggppgtgpVVLRVDRDALAGRAVAVAADDPAARelvSCGRPL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 317 AG--IEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM-------AGGIYHSGDLAYRDDaGYAYFAGRLG 387
Cdd:cd05931 362 PDqeVRIVDPETGRELPDGEVGEIW-VRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFLHD-GELYITGRLK 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 388 DWMRVDGENLGTAPIERVLLRYPD---TAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTD 444
Cdd:cd05931 440 DLIIVRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPDDGEERLVVVAEVERGADPADLA 499
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
141-495 |
9.69e-23 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 101.46 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 141 FQSASPADLFMLI---FTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSI 217
Cdd:PLN02479 186 FAWKPPADEWQSIalgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 218 ALRrKFSASGFIADVRRYGATYanYVGKP--LSYVLATPeqPDDSENPL-RAVYGNegVAGDLERFARRFGcVVQDGFGS 294
Cdd:PLN02479 266 CLR-QVTAKAIYSAIANYGVTH--FCAAPvvLNTIVNAP--KSETILPLpRVVHVM--TAGAAPPPSVLFA-MSEKGFRV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 295 TEG-GVAIARTPDT-----------PAGSLGPLPA----------GIEIVDPDTGRPCPA--GVVGELVnTAGPGRFEGY 350
Cdd:PLN02479 338 THTyGLSETYGPSTvcawkpewdslPPEEQARLNArqgvryigleGLDVVDTKTMKPVPAdgKTMGEIV-MRGNMVMKGY 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 351 YNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVM 430
Cdd:PLN02479 417 LKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPC 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 431 AALVLAPGTRfDTDKFRV------FLAEQPdlgPKQWPSYVRISAGLPGTVTFKVLKRQLAAEGVDCGdPV 495
Cdd:PLN02479 497 AFVTLKPGVD-KSDEAALaedimkFCRERL---PAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMG-PV 562
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
55-434 |
1.16e-22 |
|
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: 100.36 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPvrrgaallrdinhadcqlvladSASAgpladiehvnvESTEWsdeVAAH 134
Cdd:cd05907 32 RVAILSRNRPEWTIADLAILAIGAVPVPIYP----------------------TSSA-----------EQIAY---ILND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 SGTELTFQSAsPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVcYVSM-PLFHSNAVLVGWAVAAAC 213
Cdd:cd05907 76 SEAKALFVED-PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDR-HLSFlPLAHVFERRAGLYVPLLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 214 QGSIALrrKFSASGFIADVRRYGATYanYVGKPLSY------VLATPEQPDDSENPLRAVYGN--EGVAG------DLER 279
Cdd:cd05907 154 GARIYF--ASSAETLLDDLSEVRPTV--FLAVPRVWekvyaaIKVKAVPGLKRKLFDLAVGGRlrFAASGgaplpaELLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 280 FARRFGCVVQDGFGSTE-GGVAIARTPDTP-AGSLG-PLPaGIEI-VDPDtgrpcpagvvGELVnTAGPGRFEGYYNDEA 355
Cdd:cd05907 230 FFRALGIPVYEGYGLTEtSAVVTLNPPGDNrIGTVGkPLP-GVEVrIADD----------GEIL-VRGPNVMLGYYKNPE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 356 AEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVD-GENLGTAPIERVLLRYPDTAEVAVYAVPDPVVgdrvmAAL 433
Cdd:cd05907 298 ATAEALdADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIGDGRPFL-----VAL 372
|
.
gi 2321332536 434 V 434
Cdd:cd05907 373 I 373
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
55-489 |
1.62e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 101.54 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLqnTPFFSAMLV--AAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLAD-------SASAGPLADIEHVNVEST 125
Cdd:PRK08633 667 NVGILL--PPSVAGALAnlALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSrkfleklKNKGFDLELPENVKVIYL 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 126 EwsDEVAAHSGTE------------------LTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGP 187
Cdd:PRK08633 745 E--DLKAKISKVDkltallaarllparllkrLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 188 DDVCYVSMPLFHSNAVLVG-WAVAAACQGSIALRRKFSASGFIADVRRYGATYanyvgkplsyVLATPE----------- 255
Cdd:PRK08633 823 DDVILSSLPFFHSFGLTVTlWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATI----------LLGTPTflrlylrnkkl 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 256 QPDDSENpLR-AVYGNEGVAGDL-ERFARRFGCVVQDGFGSTE-GGVAIARTPD-----------TPAGSLG-PLPA-GI 319
Cdd:PRK08633 893 HPLMFAS-LRlVVAGAEKLKPEVaDAFEEKFGIRILEGYGATEtSPVASVNLPDvlaadfkrqtgSKEGSVGmPLPGvAV 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 320 EIVDPDTGRPCPAGVVGeLVNTAGPGRFEGYYNDEA--AEAERMAGGI--YHSGDLAYRDDAGYAYFAGRLGDWMRVDGE 395
Cdd:PRK08633 972 RIVDPETFEELPPGEDG-LILIGGPQVMKGYLGDPEktAEVIKDIDGIgwYVTGDKGHLDEDGFLTITDRYSRFAKIGGE 1050
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 396 NLGTAPIERVLLR--YPDTAEVAVYAVPDPVVGDRVmaALVLAPGTRfDTDKFRVFLAEQPDlgPKQW-PSYVRISAGLP 472
Cdd:PRK08633 1051 MVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGEKL--VVLHTCGAE-DVEELKRAIKESGL--PNLWkPSRYFKVEALP 1125
|
490 500
....*....|....*....|.
gi 2321332536 473 ----GTVTFKVLKRqLAAEGV 489
Cdd:PRK08633 1126 llgsGKLDLKGLKE-LALALL 1145
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
56-421 |
2.19e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.78 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPffsAMLVaaGMSGIVPVG-----LN---PVRRGAALLRDinhADCQLVLADSASAGPL---ADIEHVNVES 124
Cdd:PRK12467 565 VGIAVERSI---EMVV--GLLAVLKAGgayvpLDpeyPQDRLAYMLDD---SGVRLLLTQSHLLAQLpvpAGLRSLCLDE 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 125 TEwsDEVAAHSG--TELTFqsaSPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDvcyvSMPLFHS-N 201
Cdd:PRK12467 637 PA--DLLCGYSGhnPEVAL---DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD----SMLMVSTfA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 202 AVLVGWA--VAAACQGSIALRRK---FSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSenPLRA-VYGNEGVAG 275
Cdd:PRK12467 708 FDLGVTElfGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR--PQRAlVCGGEALQV 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 276 DLERFARRF--GCVVQDGFGSTEG--GVAIARTPDTPAGSLG-----PLP-AGIEIVDPDTgRPCPAGVVGELVnTAGPG 345
Cdd:PRK12467 786 DLLARVRALgpGARLINHYGPTETtvGVSTYELSDEERDFGNvpigqPLAnLGLYILDHYL-NPVPVGVVGELY-IGGAG 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 346 RFEGYYNDEAAEAERM-------AGG-IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAV 417
Cdd:PRK12467 864 LARGYHRRPALTAERFvpdpfgaDGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV 943
|
....
gi 2321332536 418 YAVP 421
Cdd:PRK12467 944 LAQP 947
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
127-493 |
4.16e-22 |
|
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: 99.87 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 127 WSDEVAAHSGTEltFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAI-AGVTMTQRFGLGPDDVCYVSMPLfhsnavlv 205
Cdd:cd05968 218 SYDEEKETAGDG--AERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLTWFTDL-------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 206 GWAVAA-ACQGSIALRRK---------FSASGFIAD-VRRYGATyanYVGKPLSYVLATPEQPDDSENP-----LRaVYG 269
Cdd:cd05968 288 GWMMGPwLIFGGLILGATmvlydgapdHPKADRLWRmVEDHEIT---HLGLSPTLIRALKPRGDAPVNAhdlssLR-VLG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 270 NEGVAGDLERFARRFGCVVQDGF------GSTE------GGVAIarTPDTPAGSLGPLPAGIEIVDPDTGRPCPaGVVGE 337
Cdd:cd05968 364 STGEPWNPEPWNWLFETVGKGRNpiinysGGTEisggilGNVLI--KPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 338 LVNTAG-PGRFEGYYNDEAAEAE---RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTA 413
Cdd:cd05968 441 LVLLAPwPGMTRGFWRDEDRYLEtywSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 414 EVAVYAVPDPVVGDRVMAALVLAPGTRFdTDKFRVFLAE--QPDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE--GV 489
Cdd:cd05968 521 ESAAIGVPHPVKGEAIVCFVVLKPGVTP-TEALAEELMErvADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAylGK 599
|
....
gi 2321332536 490 DCGD 493
Cdd:cd05968 600 ELGD 603
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
96-494 |
1.12e-21 |
|
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: 98.54 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 96 INHADCQLVLadSASAG----------PLAD---------IEHVNVESTEWSDEVAAHSGTELTFQS----ASPAD---- 148
Cdd:cd05967 150 IDDAKPKLIV--TASCGiepgkvvpykPLLDkalelsghkPHHVLVLNRPQVPADLTKPGRDLDWSEllakAEPVDcvpv 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 149 -----LFMLiFTSGTSGEPKAVKCSHSKVAIAGV-TMTQRFGLGPDDV----------------CYVsmPLFHSNAVL-- 204
Cdd:cd05967 228 aatdpLYIL-YTSGTTGKPKGVVRDNGGHAVALNwSMRNIYGIKPGDVwwaasdvgwvvghsyiVYG--PLLHGATTVly 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 205 ----VGWAVAAACQGSIA---LRRKFSASGFIADVRRYGaTYANYVGKplsYVLATpeqpddsenpLRAVYgnegVAGD- 276
Cdd:cd05967 305 egkpVGTPDPGAFWRVIEkyqVNALFTAPTAIRAIRKED-PDGKYIKK---YDLSS----------LRTLF----LAGEr 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 277 -----LERFARRFGCVVQDGFGSTEGGVAIARTP------DTPAGSLG-PLPA-GIEIVDpDTGRPCPAGVVGELVNTA- 342
Cdd:cd05967 367 ldpptLEWAENTLGVPVIDHWWQTETGWPITANPvgleplPIKAGSPGkPVPGyQVQVLD-EDGEPVGPNELGNIVIKLp 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 343 -GPGRFEGYYNDEAAEAERMAG---GIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVY 418
Cdd:cd05967 446 lPPGCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVV 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 419 AVPDPVVGDRVMAALVLAPGTRFDTDKFR---VFLAEQpDLGPKQWPSYVRISAGLPGTVTFKVLKRQLA--AEGVDCGD 493
Cdd:cd05967 526 GVRDELKGQVPLGLVVLKEGVKITAEELEkelVALVRE-QIGPVAAFRLVIFVKRLPKTRSGKILRRTLRkiADGEDYTI 604
|
.
gi 2321332536 494 P 494
Cdd:cd05967 605 P 605
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
120-485 |
1.58e-21 |
|
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: 96.99 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 120 VNVESTEWSDEVAA---HSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDD-VCYVSM 195
Cdd:cd17653 75 VPLDAKLPSARIQAilrTSGATLLLTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrVAQVLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 196 PLFHSNAvlvgWAVAAA-CQGSIALRRKFSASgfIADVrrygatyanyvGKPLSYVLATPE-----QPDDSENpLRAVY- 268
Cdd:cd17653 155 IAFDACI----GEIFSTlCNGGTLVLADPSDP--FAHV-----------ARTVDALMSTPSilstlSPQDFPN-LKTIFl 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 269 GNEGVAGDLERfARRFGCVVQDGFGSTEGGVAIART---PDTPAgSLG-PLP-AGIEIVDPDTgRPCPAGVVGELVnTAG 343
Cdd:cd17653 217 GGEAVPPSLLD-RWSPGRRLYNAYGPTECTISSTMTellPGQPV-TIGkPIPnSTCYILDADL-QPVPEGVVGEIC-ISG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 344 PGRFEGYYNDEAAEAERMAGG-------IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVA 416
Cdd:cd17653 293 VQVARGYLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQA 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 417 vYAVpdpVVGDRVMAalVLAPGTrFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLA 485
Cdd:cd17653 373 -AAI---VVNGRLVA--FVTPET-VDVDGLRSELAKH--LPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
133-410 |
2.75e-21 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 96.27 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 133 AHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWaVAAA 212
Cdd:cd17640 74 NHSESVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEY-FIFA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 213 CQGSIALRrkfSASGFIADVRRYGATYanYVGKPLSY-VLATPEQPDDSENP-------LRAVYGNE---GVAGD----- 276
Cdd:cd17640 153 CGCSQAYT---SIRTLKDDLKRVKPHY--IVSVPRLWeSLYSGIQKQVSKSSpikqflfLFFLSGGIfkfGISGGgalpp 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 277 -LERFARRFGCVVQDGFGSTE--GGVAIARTPDTPAGSLG-PLP-AGIEIVDPDTGRPCPAGVVGeLVNTAGPGRFEGYY 351
Cdd:cd17640 228 hVDTFFEAIGIEVLNGYGLTEtsPVVSARRLKCNVRGSVGrPLPgTEIKIVDPEGNVVLPPGEKG-IVWVRGPQVMKGYY 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 352 NDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRV-DGENLGTAPIERVLLRYP 410
Cdd:cd17640 307 KNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLsNGENVEPQPIEEALMRSP 367
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
50-461 |
3.26e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 96.39 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 50 PARPPHVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIEHVNVESTEWSD 129
Cdd:PRK07638 47 ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEWKR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 130 EVAAHSGTELTFQSASPADLFMLiFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNaVLVGWAV 209
Cdd:PRK07638 127 MIEKYLPTYAPIENVQNAPFYMG-FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-FLYGAIS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVL---ATPEQPDdsenpLRAVYGNEGVAGDLERFARRFGC 286
Cdd:PRK07638 205 TLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYkenRVIENKM-----KIISSGAKWEAEAKEKIKNIFPY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 287 V-VQDGFGSTEGGVAIARTPDT---PAGSLG-PL-PAGIEIVDPDtGRPCPAGVVGEL-VNTagPGRFEGYYNDEAAEAE 359
Cdd:PRK07638 280 AkLYEFYGASELSFVTALVDEEserRPNSVGrPFhNVQVRICNEA-GEEVQKGEIGTVyVKS--PQFFMGYIIGGVLARE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 360 RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDrVMAALVLAPGT 439
Cdd:PRK07638 357 LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE-KPVAIIKGSAT 435
|
410 420
....*....|....*....|....
gi 2321332536 440 RfdtDKFRVFLAEQ--PDLGPKQW 461
Cdd:PRK07638 436 K---QQLKSFCLQRlsSFKIPKEW 456
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
286-493 |
1.32e-20 |
|
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: 94.94 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 286 CVVQDGFGSTE-GGVAIARTP---DTPAGSLG-PLPaGIE--IVDPDtGRPCPAGVVGELVNTAG-PGRFEGYYNDEaae 357
Cdd:cd05966 382 CPIVDTWWQTEtGGIMITPLPgatPLKPGSATrPFF-GIEpaILDEE-GNEVEGEVEGYLVIKRPwPGMARTIYGDH--- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 358 aERMA-------GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVM 430
Cdd:cd05966 457 -ERYEdtyfskfPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIY 535
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 431 AALVLAPGTRFDTD---KFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKR---QLAAEGVDCGD 493
Cdd:cd05966 536 AFVTLKDGEEPSDElrkELRKHVRKE--IGPIATPDKIQFVPGLPKTRSGKIMRRilrKIAAGEEELGD 602
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
52-423 |
1.73e-20 |
|
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: 94.27 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 52 RPPHVgVLLQ---NTPFFSAmLVAAGMSGIVPVGLNPV---RRGAALLRDINHADCQL----VLADSASAGPLADIE--- 118
Cdd:cd05906 62 RPGDS-VILQfddNEDFIPA-FWACVLAGFVPAPLTVPptyDEPNARLRKLRHIWQLLgspvVLTDAELVAEFAGLEtls 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 119 HVNVESTEWSDEVAAHSGTELTFQSaSPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLF 198
Cdd:cd05906 140 GLPGIRVLSIEELLDTAADHDLPQS-RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 199 HSnAVLVGWAVAAACQGSIALRrkFSASGFIADVR-------RYGATYA---NYVGKPLSYVLATPEQPDDSENPLRAVY 268
Cdd:cd05906 219 HV-GGLVELHLRAVYLGCQQVH--VPTEEILADPLrwldlidRYRVTITwapNFAFALLNDLLEEIEDGTWDLSSLRYLV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 269 --GNEGVAGDLERFAR---RFGC---VVQDGFGSTE--GGVAIAR---TPDTPAG----SLG-PLP-AGIEIVDpDTGRP 329
Cdd:cd05906 296 naGEAVVAKTIRRLLRllePYGLppdAIRPAFGMTEtcSGVIYSRsfpTYDHSQAlefvSLGrPIPgVSMRIVD-DEGQL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 330 CPAGVVGELvNTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLR 408
Cdd:cd05906 375 LPEGEVGRL-QVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEE 452
|
410
....*....|....*..
gi 2321332536 409 YPD--TAEVAVYAVPDP 423
Cdd:cd05906 453 VPGvePSFTAAFAVRDP 469
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
56-456 |
3.70e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 93.55 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVpvgLNPV------RRGAALLRdinHADCQLVLADSASAgPLADiEHVNVESTEWS- 128
Cdd:PLN03102 67 VSVLAPNTPAMYEMHFAVPMAGAV---LNPIntrldaTSIAAILR---HAKPKILFVDRSFE-PLAR-EVLHLLSSEDSn 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 129 -----------DEVAAHSGTELTF----QSASP-----ADLFM---------LIFTSGTSGEPKAVKCSHSKVAIAGVTM 179
Cdd:PLN03102 139 lnlpvifiheiDFPKRPSSEELDYecliQRGEPtpslvARMFRiqdehdpisLNYTSGTTADPKGVVISHRGAYLSTLSA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 180 TQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRkFSASGFIADVRRYGATYANYVGKPLSYVL---ATPEQ 256
Cdd:PLN03102 219 IIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnSLDLS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 257 PDDSenPLRAVYGNEGVAGDLERFARRFGCVVQDGFGSTEGGVAIA---------RTPDTPAGSLGPLP-------AGIE 320
Cdd:PLN03102 298 PRSG--PVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLfcewqdewnRLPENQQMELKARQgvsilglADVD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 321 IVDPDTGRPCP--AGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLG 398
Cdd:PLN03102 376 VKNKETQESVPrdGKTMGEIV-IKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENIS 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2321332536 399 TAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQPDL 456
Cdd:PLN03102 455 SVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERDL 512
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
52-484 |
3.85e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 93.15 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 52 RPPHVGVLLQ-NTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIEHVNVESTEWSDE 130
Cdd:PRK13390 47 RTGDVVALLSdNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 131 VAAHSGTELTFQSASPADL-----FMLIFTSGTSGEPKAVKCSHSK----------VAIAGVTmtqrFGLGPDDVCYVSM 195
Cdd:PRK13390 127 IDGFGSFEAALAGAGPRLTeqpcgAVMLYSSGTTGFPKGIQPDLPGrdvdapgdpiVAIARAF----YDISESDIYYSSA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 196 PLFHSnAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVgkPLSYV----LATPEQPDDSENPLRAV-YGN 270
Cdd:PRK13390 203 PIYHA-APLRWCSMVHALGGTVVLAKRFDAQATLGHVERYRITVTQMV--PTMFVrllkLDADVRTRYDVSSLRAViHAA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 271 EGVAGDLER-FARRFGCVVQDGFGSTEG-GVAIARTPDTPA--GSLGPLPAGIEIVDPDTGRPCPAGVVGELV--NTAGP 344
Cdd:PRK13390 280 APCPVDVKHaMIDWLGPIVYEYYSSTEAhGMTFIDSPDWLAhpGSVGRSVLGDLHICDDDGNELPAGRIGTVYfeRDRLP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 345 GRfegYYND--EAAEAERMAGGIYHS-GDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVP 421
Cdd:PRK13390 360 FR---YLNDpeKTAAAQHPAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 422 DPVVGDRVMAALVLAPGTRFDTDKFRVFL-AEQPDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK13390 437 DPEMGEQVKAVIQLVEGIRGSDELARELIdYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
96-444 |
4.19e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.02 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 96 INHADCQLVLADSASAGPLADI-EHVNVESTEWSD--------EVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVK 166
Cdd:PRK07514 96 IGDAEPALVVCDPANFAWLSKIaAAAGAPHVETLDadgtgsllEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAM 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 167 CSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRygATYanYVGKP 246
Cdd:PRK07514 176 LSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPR--ATV--MMGVP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 247 LSYV--LATPEQPDDSENPLRA-VYGNEGVAGDLER-FARRFGCVVQDGFGSTEGGVaIARTP---DTPAGSLG-PLPaG 318
Cdd:PRK07514 252 TFYTrlLQEPRLTREAAAHMRLfISGSAPLLAETHReFQERTGHAILERYGMTETNM-NTSNPydgERRAGTVGfPLP-G 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 319 IE--IVDPDTGRPCPAGVVGeLVNTAGPGRFEGYYN-DEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGE 395
Cdd:PRK07514 330 VSlrVTDPETGAELPPGEIG-MIEVKGPNVFKGYWRmPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGY 408
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2321332536 396 NLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTD 444
Cdd:PRK07514 409 NVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEA 457
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
148-484 |
5.24e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 92.98 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVaIAGVTMTQRFGL------GPDDVCYVSMPLFHSNAvLVGWAVAAACQGS-IALR 220
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNL-IAMVELFVRFEAsqyeypGSDNVYLAALPMFHIYG-LSLFVVGLLSLGStIVVM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 221 RKFSASGFIADVRRYGATYANYVgKPLSYVLATPEQPDDSENPLRAVYGNEGVAGDLERFARRFGCVVQ-----DGFGST 295
Cdd:PLN02574 277 RRFDASDMVKVIDRFKVTHFPVV-PPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPhvdfiQGYGMT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 296 EGGVAIARTPDTPA----GSLGPLPAGIE--IVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM-AGGIYHS 368
Cdd:PLN02574 356 ESTAVGTRGFNTEKlskySSVGLLAPNMQakVVDWSTGCLLPPGNCGELW-IQGPGVMKGYLNNPKATQSTIdKDGWLRT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 369 GDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRV 448
Cdd:PLN02574 435 GDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVIN 514
|
330 340 350
....*....|....*....|....*....|....*.
gi 2321332536 449 FLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PLN02574 515 YVAKQ--VAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
278-484 |
1.56e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 91.59 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 278 ERFARR----FGCVVQDGFGSTEGGVAIARTPDTPA---GSLG-PLPAGIE--IVDPDtGRPCPAGVVGELVnTAGPGRF 347
Cdd:PRK10946 314 ETLARRipaeLGCQLQQVFGMAEGLVNYTRLDDSDErifTTQGrPMSPDDEvwVADAD-GNPLPQGEVGRLM-TRGPYTF 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 348 EGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVG 426
Cdd:PRK10946 392 RGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 427 DRVMAALVLAPGTRfdTDKFRVFLAEQpdlGPKQW--PSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK10946 472 EKSCAFLVVKEPLK--AVQLRRFLREQ---GIAEFklPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
55-434 |
3.54e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 90.54 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSAS--------AGPLADIEHV-NVEST 125
Cdd:COG1022 67 RVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEqldkllevRDELPSLRHIvVLDPR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 126 EWSDEVAAHS-------GTELTFQ--------SASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDV 190
Cdd:COG1022 147 GLRDDPRLLSldellalGREVADPaelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 191 CYVSMPLFHS--NAVLVGWAVAAACQG---SI---------------------------ALRRKFSASGFI--------A 230
Cdd:COG1022 227 TLSFLPLAHVfeRTVSYYALAAGATVAfaeSPdtlaedlrevkptfmlavprvwekvyaGIQAKAEEAGGLkrklfrwaL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 231 DV-RRYGAtyANYVGKPLSYVLATPEQPDD----SenPLRAVYGNE---GVAG------DLERFARRFGCVVQDGFGSTE 296
Cdd:COG1022 307 AVgRRYAR--ARLAGKSPSLLLRLKHALADklvfS--KLREALGGRlrfAVSGgaalgpELARFFRALGIPVLEGYGLTE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 297 -GGVAIARTPDTP-AGSLGPLPAGIEI-VDPDtgrpcpagvvGELVnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLA 372
Cdd:COG1022 383 tSPVITVNRPGDNrIGTVGPPLPGVEVkIAED----------GEIL-VRGPNVMKGYYKNPEATAEAFdADGWLHTGDIG 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 373 YRDDAGYAYFAGRLGDwMRV--DGENLGTAPIERVLLRYPDTAEVAvyavpdpVVGDR--VMAALV 434
Cdd:COG1022 452 ELDEDGFLRITGRKKD-LIVtsGGKNVAPQPIENALKASPLIEQAV-------VVGDGrpFLAALI 509
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
85-472 |
5.89e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 90.49 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 85 PVRRGAALLRDinhADCQLVLADSASAGPLADIEhvNVESTEWSDEVAAHSGTELtfQSASPADLFMLIFTSGTSGEPKA 164
Cdd:PRK10252 543 PDDRLKMMLED---ARPSLLITTADQLPRFADVP--DLTSLCYNAPLAPQGAAPL--QLSQPHHTAYIIFTSGSTGRPKG 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 165 VKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPL------------FHSNAVLVgWAVAAACQGSIALRRKFsasgfiadv 232
Cdd:PRK10252 616 VMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCsfdvsvweffwpFIAGAKLV-MAEPEAHRDPLAMQQFF--------- 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 233 RRYGATYANYVGKPLSYVLA--TPEQPDDSENPLRAVY--GNEGVAGDLERFARRFGCVVQDGFGSTEGGVAIARTP--- 305
Cdd:PRK10252 686 AEYGVTTTHFVPSMLAAFVAslTPEGARQSCASLRQVFcsGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPafg 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 306 -DTPAGSLGPLPAG-------IEIVDpDTGRPCPAGVVGELVNTaGPGRFEGYYNDEAAEAER------MAGG-IYHSGD 370
Cdd:PRK10252 766 eELAAVRGSSVPIGypvwntgLRILD-ARMRPVPPGVAGDLYLT-GIQLAQGYLGRPDLTASRfiadpfAPGErMYRTGD 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 371 LA-YRDDAGYAYFaGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAV----PDPVVGD--RVMAALVLAPGTRFDT 443
Cdd:PRK10252 844 VArWLDDGAVEYL-GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqAAATGGDarQLVGYLVSQSGLPLDT 922
|
410 420
....*....|....*....|....*....
gi 2321332536 444 DKFRVFLAEQpdLGPKQWPSYVRISAGLP 472
Cdd:PRK10252 923 SALQAQLRER--LPPHMVPVVLLQLDQLP 949
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
56-461 |
1.02e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.02 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLN---PVRRGAALLRDinhADCQLVLADSASAGPLADIEHVNVESTEWSD-EV 131
Cdd:PRK12316 564 VGVAMERSIEMVVALLAILKAGGAYVPLDpeyPAERLAYMLED---SGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAaWL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 132 AAHSgTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPL-FHSNAVLVGWAVA 210
Cdd:PRK12316 641 EGYS-EENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFWPLM 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 211 AACQGSIALRRK-FSASGFIADVRRYGATYANYVGKPLSYVLatPEQPDDSENPLRA-VYGNEGVAGDLER--FARRFGC 286
Cdd:PRK12316 720 SGARLVVAAPGDhRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTSLRRiVCSGEALPADAQEqvFAKLPQA 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 287 VVQDGFGSTEGGVAIARTPDTPAGSlGPLPAG-------IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAE 359
Cdd:PRK12316 798 GLYNLYGPTEAAIDVTHWTCVEEGG-DSVPIGrpianlaCYILDAN-LEPVPVGVLGELY-LAGRGLARGYHGRPGLTAE 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 360 RMAGG-------IYHSGDLA-YRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPdpvvGDRVMA 431
Cdd:PRK12316 875 RFVPSpfvagerMYRTGDLArYRAD-GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVG 949
|
410 420 430
....*....|....*....|....*....|..
gi 2321332536 432 ALVL-APGTRFDTDKFRVFLAEQPD-LGPKQW 461
Cdd:PRK12316 950 YVVLeSEGGDWREALKAHLAASLPEyMVPAQW 981
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
55-489 |
1.10e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 89.78 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPffSAMLVAAGMS--GIVPVGLNP-------VRRGAA--LLRDINHADCQ-------LVL----------A 106
Cdd:PRK07868 499 RVGVLMETRP--SALVAIAALSrlGAVAVLMPPdtdlaaaVRLGGVteIITDPTNLEAArqlpgrvLVLgggesrdldlP 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 107 DSASAGPLADIEHVNVESTEWSDEVAAHSGteltfqsaspaDLFMLIFtSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLG 186
Cdd:PRK07868 577 DDADVIDMEKIDPDAVELPGWYRPNPGLAR-----------DLAFIAF-STAGGELVAKQITNYRWALSAFGTASAAALD 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 187 PDDVCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRA 266
Cdd:PRK07868 645 RRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 267 VYGNEGVAGDLERFARRFGCV-VQDGFGSTEGGVAIARTPDTPAGSLG-PLPAGIEI----VDPDTG----------RPC 330
Cdd:PRK07868 725 FIGSGMPTGLWERVVEAFAPAhVVEFFATTDGQAVLANVSGAKIGSKGrPLPGAGRVelaaYDPEHDlileddrgfvRRA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 331 PAGVVGELVNTAGPGrfegyyNDEAAEAERmagGIYHSGD-------LAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIE 403
Cdd:PRK07868 805 EVNEVGVLLARARGP------IDPTASVKR---GVFAPADtwisteyLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVT 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 404 RVLLRYPDTAEVAVYAVPdpvVGDR--VMAALVLAPGTRFDTDKFRVFLAEQPdlgPKQWPSYVRISAGLPGTVTFKVLK 481
Cdd:PRK07868 876 DALGRIGGVDLAVTYGVE---VGGRqlAVAAVTLRPGAAITAADLTEALASLP---VGLGPDIVHVVPEIPLSATYRPTV 949
|
....*...
gi 2321332536 482 RQLAAEGV 489
Cdd:PRK07868 950 SALRAAGI 957
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
146-484 |
2.38e-18 |
|
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: 87.52 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFhSNAVLVGWAVAAACQGSIAL----RR 221
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASF-SFDVFAGDFARSLLNGGTLVicpdEV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 222 KFSASGFIADVRRYGATYANYVG---KPL-SYVLATPEQPDDsenpLRA-VYGNEGV-AGDLERFARRFG--CVVQDGFG 293
Cdd:cd17650 171 KLDPAALYDLILKSRITLMESTPaliRPVmAYVYRNGLDLSA----MRLlIVGSDGCkAQDFKTLAARFGqgMRIINSYG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 294 STE----------GGVAIARTPDTPAGSlgPLP-AGIEIVDPdTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM- 361
Cdd:cd17650 247 VTEatidstyyeeGRDPLGDSANVPIGR--PLPnTAMYVLDE-RLQPQPVGVAGELY-IGGAGVARGYLNRPELTAERFv 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 362 -----AGG-IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEvAVYAVPDPVVGDRVMAALVL 435
Cdd:cd17650 323 enpfaPGErMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEARLCAYVV 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2321332536 436 APGTrFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17650 402 AAAT-LNTAELRAFLAKE--LPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
144-484 |
4.18e-18 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 86.54 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDD-VCYVSMPLFhsNAVLVGWAVAAACQGSIAL--- 219
Cdd:cd17652 90 TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVLQFASPSF--DASVWELLMALLAGATLVLapa 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 220 RRKFSASGFIADVRRYGATYANYVGKPLSYVlatpeqPDDSENPLRA-VYGNEGVAGDL-ERFARrfGCVVQDGFGSTEG 297
Cdd:cd17652 168 EELLPGEPLADLLREHRITHVTLPPAALAAL------PPDDLPDLRTlVVAGEACPAELvDRWAP--GRRMINAYGPTET 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 298 GVAIARTPDTPAGslGPLPAGIEI------VDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM--------AG 363
Cdd:cd17652 240 TVCATMAGPLPGG--GVPPIGRPVpgtrvyVLDARLRPVPPGVPGELY-IAGAGLARGYLNRPGLTAERFvadpfgapGS 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 364 GIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDT 443
Cdd:cd17652 317 RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTA 396
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2321332536 444 DKFRVFLAEQpdLGPKQWPS-YVRISAgLPGTVTFKVLKRQL 484
Cdd:cd17652 397 AELRAHLAER--LPGYMVPAaFVVLDA-LPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
66-489 |
4.80e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 66 FSAMLVAAGmsGIVPVGLN-PVRRGAALLRDINHAdcqLVLADSASAGPLADIEHVNVESTEWSDEVAAHSGTELTFQSA 144
Cdd:PRK12316 2070 LLAVLKAGG--AYVPLDPNyPAERLAYMLEDSGAA---LLLTQRHLLERLPLPAGVARLPLDRDAEWADYPDTAPAVQLA 2144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 145 sPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDvCYVSMPLFHSNAVLVGWAVaAACQGSIALRRK-- 222
Cdd:PRK12316 2145 -GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPAD-CELQFMSFSFDGAHEQWFH-PLLNGARVLIRDde 2221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 223 -FSASGFIADVRRYGATYANYVGKPLsYVLATPEQPDDSENPLRA-VYGNEGV-AGDLERFARRFGCV-VQDGFGSTEGG 298
Cdd:PRK12316 2222 lWDPEQLYDEMERHGVTILDFPPVYL-QQLAEHAERDGRPPAVRVyCFGGEAVpAASLRLAWEALRPVyLFNGYGPTEAV 2300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 299 VAIAR---TPDTPAGSLGPlPAG-------IEIVDPDTgRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM------- 361
Cdd:PRK12316 2301 VTPLLwkcRPQDPCGAAYV-PIGralgnrrAYILDADL-NLLAPGMAGELY-LGGEGLARGYLNRPGLTAERFvpdpfsa 2377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 362 -AGGIYHSGDLA-YRDDAGYAYFaGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVpDPVVGDRVMAALVLAPGT 439
Cdd:PRK12316 2378 sGERLYRTGDLArYRADGVVEYL-GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAA 2455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2321332536 440 RFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAEGV 489
Cdd:PRK12316 2456 EDLLAELRAWLAAR--LPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDV 2503
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
89-434 |
8.57e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 89 GAALLRDINHADCQLVLADSASAGPLADIEhvnvestEWSDEVAAHSGTELtfqsaSPADLFMLIFTSGTSGEPKAVKCS 168
Cdd:PRK12316 4648 GAALLLTQSHLLQRLPIPDGLASLALDRDE-------DWEGFPAHDPAVRL-----HPDNLAYVIYTSGSTGRPKGVAVS 4715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 169 HSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLvGWAVAAACQGSIALRRK--FSASGFIADVRRYGATYANYVGKP 246
Cdd:PRK12316 4716 HGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHE-GLYHPLINGASVVIRDDslWDPERLYAEIHEHRVTVLVFPPVY 4794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 247 LSYVLATPEQPDDSENPLRAVYGNEGVAGDLERFARRFGCVVQ--DGFGSTEGGVAIA--RTPDTPAGSLGPLPAG---- 318
Cdd:PRK12316 4795 LQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYlfNGYGPTETTVTVLlwKARDGDACGAAYMPIGtplg 4874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 319 ---IEIVDpDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM--------AGGIYHSGDLA-YRDDaGYAYFAGRL 386
Cdd:PRK12316 4875 nrsGYVLD-GQLNPLPVGVAGELY-LGGEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLArYRAD-GVIDYLGRV 4951
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2321332536 387 GDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPvVGDRVMAALV 434
Cdd:PRK12316 4952 DHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVV 4998
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
145-484 |
2.78e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 84.54 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 145 SPADLFMLIFTSGTSGEPKAVKCSHSKV------AIAGVTMTQRFGLGpDDVCYVSMPLFHSNAVLVGWAV---AAACQG 215
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLvanmqqAHQWLAGTGKLEEG-CEVVITALPLYHIFALTANGLVfmkIGGCNH 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 216 SIALRRKFSasGFIADVRRYGATYANYVGKPLSYVLATP--EQPDDSEnpLRAVYG-----NEGVAgdlERFARRFGCVV 288
Cdd:PRK08751 285 LISNPRDMP--GFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQIDFSS--LKMTLGggmavQRSVA---ERWKQVTGLTL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 QDGFGSTEGGVAIARTP---DTPAGSLG-PLPAGIEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM-AG 363
Cdd:PRK08751 358 VEAYGLTETSPAACINPltlKEYNGSIGlPIPSTDACIKDDAGTVLAIGEIGELC-IKGPQVMKGYWKRPEETAKVMdAD 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 364 GIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVlapgtrfdt 443
Cdd:PRK08751 437 GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV--------- 507
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2321332536 444 DKFRVFLAE------QPDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK08751 508 KKDPALTAEdvkahaRANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
124-487 |
3.51e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 84.30 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 124 STEWSDEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSH----SKVAIAGVTMTQRFGLGPDD-----VCyvS 194
Cdd:PRK07059 181 HVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPRPdqlnfVC--A 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 195 MPLFHSNAVLVGWAVAAACQG-SIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVYG---- 269
Cdd:PRK07059 259 LPLYHIFALTVCGLLGMRTGGrNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGggma 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 270 -NEGVAgdlERFARRFGCVVQDGFGSTEGG-VAIARTPDTPA--GSLG-PLPAG-IEIVDpDTGRPCPAGVVGELVnTAG 343
Cdd:PRK07059 339 vQRPVA---ERWLEMTGCPITEGYGLSETSpVATCNPVDATEfsGTIGlPLPSTeVSIRD-DDGNDLPLGEPGEIC-IRG 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 344 PGRFEGYYN--DEAAEAeRMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVP 421
Cdd:PRK07059 414 PQVMAGYWNrpDETAKV-MTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVP 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 422 DPVVGDRVMAALVLAPGTRFDTDKFRvFLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK07059 493 DEHSGEAVKLFVVKKDPALTEEDVKA-FCKER--LTNYKRPKFVEFRTELPKTNVGKILRRELRDG 555
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
146-484 |
4.66e-17 |
|
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: 83.37 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDD--VCYVSMPLFHSNAVLVGWAVAAACQGSIALRRKF 223
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSFDASAWEIFPHLTAGAALHVVPSERRL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 224 sasgfiaDVRRYGaTYANYVGKPLSYvLATP--EQPDDSEN-PLRAVYgnegVAGDLERFARRFGCVVQDGFGSTEGGVA 300
Cdd:cd17645 183 -------DLDALN-DYFNQEGITISF-LPTGaaEQFMQLDNqSLRVLL----TGGDKLKKIERKGYKLVNNYGPTENTVV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 301 IARTP-DTPAGSLgplPAG-------IEIVDPDTgRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGG-------I 365
Cdd:cd17645 250 ATSFEiDKPYANI---PIGkpidntrVYILDEAL-QLQPIGVAGELC-IAGEGLARGYLNRPELTAEKFIVHpfvpgerM 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 366 YHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPvVGDRVMAALVLAPgTRFDTDK 445
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDA-DGRKYLVAYVTAP-EEIPHEE 402
|
330 340 350
....*....|....*....|....*....|....*....
gi 2321332536 446 FRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17645 403 LREWLKN--DLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
148-422 |
5.95e-16 |
|
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: 78.60 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAvLVGWAVAAACQGSIALRRKFSASG 227
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLF-LYGAISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 228 FIADVRRYGATyANYVGKPLSYVLATPEQPddsENPLRAVY--GNEGVAGDLERFARRF-GCVVQDGFGSTEGGVAIART 304
Cdd:cd17633 80 WIRKINQYNAT-VIYLVPTMLQALARTLEP---ESKIKSIFssGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 305 PDT--PAGSLGPLPAGIEIVDPDTGrpcpAGVVGEL-VNTagPGRFEGYyndeAAEAERMAGGIYHSGDLAYRDDAGYAY 381
Cdd:cd17633 156 NQEsrPPNSVGRPFPNVEIEIRNAD----GGEIGKIfVKS--EMVFSGY----VRGGFSNPDGWMSVGDIGYVDEEGYLY 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2321332536 382 FAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPD 422
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPD 266
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
319-493 |
7.43e-16 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 80.38 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 319 IEIVDPDTGRPCPAGVVGELVNTAG--PGRFEGYYNDEA-------AEAERMaggIYHSGDLAYRDDAGYAYFAGRLGDW 389
Cdd:PRK10524 422 VKLLNEVTGEPCGPNEKGVLVIEGPlpPGCMQTVWGDDDrfvktywSLFGRQ---VYSTFDWGIRDADGYYFILGRTDDV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 390 MRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQ------PDLGPKQWPS 463
Cdd:PRK10524 499 INVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEKEimalvdSQLGAVARPA 578
|
170 180 190
....*....|....*....|....*....|..
gi 2321332536 464 YVRISAGLPGTVTFKVLKRQLAA--EGVDCGD 493
Cdd:PRK10524 579 RVWFVSALPKTRSGKLLRRAIQAiaEGRDPGD 610
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
136-487 |
9.45e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.81 E-value: 9.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 136 GTELTFQSASPA--DLFMLIFTSGTSGEPKAVKCSHSKVaIAGVT-----MTQRFGLGPDdVCYVSMPLFHSNAVLVG-W 207
Cdd:PRK05677 194 GAGQPVTEANPQadDVAVLQYTGGTTGVAKGAMLTHRNL-VANMLqcralMGSNLNEGCE-ILIAPLPLYHIYAFTFHcM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 208 AVAAACQGSIALRRKFSASGFIADVRRYgaTYANYVG-KPLSYVLATPEQPDDSENPLRAVYGNEGVAGDL---ERFARR 283
Cdd:PRK05677 272 AMMLIGNHNILISNPRDLPAMVKELGKW--KFSGFVGlNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLataERWKEV 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 284 FGCVVQDGFGSTEGGVAIARTP--DTPAGSLG-PLPAG-IEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAE 359
Cdd:PRK05677 350 TGCAICEGYGMTETSPVVSVNPsqAIQVGTIGiPVPSTlCKVIDDD-GNELPLGEVGELC-VKGPQVMKGYWQRPEATDE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 360 RM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG 438
Cdd:PRK05677 428 ILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG 507
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2321332536 439 TRFDTDKFRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK05677 508 ETLTKEQVMEHMRA--NLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
70-453 |
1.09e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.59 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 70 LVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADIEHVNVESTEWSDEVAAHSGTELTFQSASPADL 149
Cdd:PRK12467 1641 LLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNL 1720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 150 FMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDvcyvSMPLFHSNAVLVG-WAV-AAACQGSIALRRKFSAS- 226
Cdd:PRK12467 1721 AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD----VVLQFTSFAFDVSvWELfWPLINGARLVIAPPGAHr 1796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 227 ---GFIADVRRYGATYANYVGKPLSYVLATPEQpddSENPL---RAVYGNEGVAGDLERFA-RRFGCV-VQDGFGSTEGG 298
Cdd:PRK12467 1797 dpeQLIQLIERQQVTTLHFVPSMLQQLLQMDEQ---VEHPLslrRVVCGGEALEVEALRPWlERLPDTgLFNLYGPTETA 1873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 299 VAIARTPDTPAGSLG--PLPAGIEIVDPDTG------RPCPAGVVGELVNTaGPGRFEGYYNDEAAEAERM--------A 362
Cdd:PRK12467 1874 VDVTHWTCRRKDLEGrdSVPIGQPIANLSTYildaslNPVPIGVAGELYLG-GVGLARGYLNRPALTAERFvadpfgtvG 1952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 363 GGIYHSGDLA-YRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVpDPVVGDRVMAALVLAPGTRF 441
Cdd:PRK12467 1953 SRLYRTGDLArYRAD-GVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLV 2030
|
410
....*....|..
gi 2321332536 442 DTDKFRVFLAEQ 453
Cdd:PRK12467 2031 DDDEAQVALRAI 2042
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
85-486 |
2.05e-15 |
|
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: 78.52 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 85 PVRRGAALLRDinhADCQLVLADSASAGPLADIEHVNVEstewsDEVAAHSGTELTFQSAS-PADLFMLIFTSGTSGEPK 163
Cdd:cd17655 82 PEERIQYILED---SGADILLTQSHLQPPIAFIGLIDLL-----DEDTIYHEESENLEPVSkSDDLAYVIYTSGSTGKPK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 164 AVKCSHSKVAIAGVTMTQRFGLGPDDvcyvSMPLFHSNAV-LVGWAVAAA--CQGSIALRRKFSASGFIADVRRYGATYA 240
Cdd:cd17655 154 GVMIEHRGVVNLVEWANKVIYQGEHL----RVALFASISFdASVTEIFASllSGNTLYIVRKETVLDGQALTQYIRQNRI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 241 NYVGKPLSYVLATPEQPDDSENPLRA-VYGNEGVAGDL-ERFARRFG--CVVQDGFGSTEGGV---------AIARTPDT 307
Cdd:cd17655 230 TIIDLTPAHLKLLDAADDSEGLSLKHlIVGGEALSTELaKKIIELFGtnPTITNAYGPTETTVdasiyqyepETDQQVSV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 308 PAGSlgplPAG---IEIVDpDTGRPCPAGVVGELVnTAGPGRFEGYYN-----------DEAAEAERMaggiYHSGDLA- 372
Cdd:cd17655 310 PIGK----PLGntrIYILD-QYGRPQPVGVAGELY-IGGEGVARGYLNrpeltaekfvdDPFVPGERM----YRTGDLAr 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 373 YRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPgtRFDTDKFRVFLAE 452
Cdd:cd17655 380 WLPD-GNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREFLAR 456
|
410 420 430
....*....|....*....|....*....|....*.
gi 2321332536 453 Q-PDLgpkQWPSY-VRIsAGLPGTVTFKVLKRQLAA 486
Cdd:cd17655 457 ElPDY---MIPSYfIKL-DEIPLTPNGKVDRKALPE 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
143-482 |
2.17e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.43 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 143 SASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPL-FHSNAVLVGWAVAAACQGSIALRR 221
Cdd:PRK12467 3233 RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFsFDGAQERFLWTLICGGCLVVRDND 3312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 222 KFSASGFIADVRRYGATYANYvgkPLSYVLATPEQPDDSE-NPL-RAVYGNEGVA-GDLERFARRFGCV-VQDGFGSTE- 296
Cdd:PRK12467 3313 LWDPEELWQAIHAHRISIACF---PPAYLQQFAEDAGGADcASLdIYVFGGEAVPpAAFEQVKRKLKPRgLTNGYGPTEa 3389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 297 ---------GGVAIARTPDTPAGSlgPLPA-GIEIVDpDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM----- 361
Cdd:PRK12467 3390 vvtvtlwkcGGDAVCEAPYAPIGR--PVAGrSIYVLD-GQLNPVPVGVAGELY-IGGVGLARGYHQRPSLTAERFvadpf 3465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 362 --AGG-IYHSGDLA-YRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVpDPVVGDRVMAALVLAP 437
Cdd:PRK12467 3466 sgSGGrLYRTGDLArYRAD-GVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD 3543
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2321332536 438 GTRFDTDKFRVFLAEQ-PD-LGPKQWPSYVRISAGLPGTVTFKVLKR 482
Cdd:PRK12467 3544 PQGDWRETLRDHLAASlPDyMVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
148-484 |
2.20e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 78.71 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAiagVTMTQRFG----LGPD---------DVCYVSMPLFHSnavlvgWAVAAAC- 213
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNLV---ANMLQVRAclsqLGPDgqplmkegqEVMIAPLPLYHI------YAFTANCm 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 214 ------QGSIALRRKFSASGFIADVRRYgaTYANYVGKPLSYV--LATPE--QPDDSENPLRAVYGNEGVAGDLERFARR 283
Cdd:PRK12492 279 cmmvsgNHNVLITNPRDIPGFIKELGKW--RFSALLGLNTLFValMDHPGfkDLDFSALKLTNSGGTALVKATAERWEQL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 284 FGCVVQDGFGSTEGGVAIARTPDTPAGSLG----PLPAGIEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAE 359
Cdd:PRK12492 357 TGCTIVEGYGLTETSPVASTNPYGELARLGtvgiPVPGTALKVIDDDGNELPLGERGELC-IKGPQVMKGYWQQPEATAE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 360 RM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVmAALVLAPG 438
Cdd:PRK12492 436 ALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAV-KLFVVARD 514
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2321332536 439 TRFDTDKFRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK12492 515 PGLSVEELKAYCKE--NFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
144-490 |
2.82e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 78.25 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLIFT-SGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPL---FHSNAVLVGWAVAAAcqgsIAL 219
Cdd:PRK06164 177 AADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFcgvFGFSTLLGALAGGAP----LVC 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 220 RRKFSASGFIADVRRYGATYANYVGKPLSYVLAT-PEQPDDSENPLRAVYGNEGVAGDLERFARRFGCVVQDGFGSTEGG 298
Cdd:PRK06164 253 EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTaGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGSSEVQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 299 VAIARTPDTPAGSLGPLPAG--------IEIVDPDTGRPCPAGVVGELvNTAGPGRFEGYYND-EAAEAERMAGGIYHSG 369
Cdd:PRK06164 333 ALVALQPATDPVSVRIEGGGrpaspearVRARDPQDGALLPDGESGEI-EIRAPSLMRGYLDNpDATARALTDDGYFRTG 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 370 DLAY-RDDAGYAYfAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVpDPVVGDRVMAALVLAPGTRFDTDKFRV 448
Cdd:PRK06164 412 DLGYtRGDGQFVY-QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMA 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2321332536 449 FLAEQpdLGPKQWPSYVRISAGLPGTVT---FKVLK---RQLAAEGVD 490
Cdd:PRK06164 490 ACREA--LAGFKVPARVQVVEAFPVTESangAKIQKhrlREMAQARLA 535
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
144-453 |
5.83e-15 |
|
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: 76.27 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLiFTSGTSGEPKAVKCSHS---KVAIAGVTMT-----------QRFGLGPDDVCYVSMPLFHSNAVLVGWAV 209
Cdd:cd05924 1 RSADDLYIL-YTGGTTGMPKGVMWRQEdifRMLMGGADFGtgeftpsedahKAAAAAAGTVMFPAPPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAACQGSIALRRKFSASGFIADVRRYGATYANYVG----KPLSYVLATPEQPDDSEnpLRAVyGNEGVAGDLE---RFAR 282
Cdd:cd05924 80 LLGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGdamaRPLIDALRDAGPYDLSS--LFAI-SSGGALLSPEvkqGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 283 RF-GCVVQDGFGSTEGG---VAIARTPDTPAGSLGPLPAGIEIVDPDTGR-PCPAGVVGELvntAGPGRF-EGYYNDEAA 356
Cdd:cd05924 157 LVpNITLVDAFGSSETGftgSGHSAGSGPETGPFTRANPDTVVLDDDGRVvPPGSGGVGWI---ARRGHIpLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 357 EAE--RMAGGIYHS--GDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAA 432
Cdd:cd05924 234 TAEtfPEVDGVRYAvpGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAV 313
|
330 340
....*....|....*....|.
gi 2321332536 433 LVLAPGTRFDTDKFRVFLAEQ 453
Cdd:cd05924 314 VQLREGAGVDLEELREHCRTR 334
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
286-484 |
8.21e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 77.10 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 286 CVVQDGFGSTE-GGVAIARTP---DTPAGSLG-PLPaGI--EIVDpDTGRPCPAGVVGELVNTAG-PGRFEGYYNDEaae 357
Cdd:PRK00174 396 CPIVDTWWQTEtGGIMITPLPgatPLKPGSATrPLP-GIqpAVVD-EEGNPLEGGEGGNLVIKDPwPGMMRTIYGDH--- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 358 aERMA-------GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVM 430
Cdd:PRK00174 471 -ERFVktyfstfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIY 549
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 431 AALVLAPGtRFDTDKFRVFLAEQ--PDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK00174 550 AFVTLKGG-EEPSDELRKELRNWvrKEIGPIAKPDVIQFAPGLPKTRSGKIMRRIL 604
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
131-423 |
1.06e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.52 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 131 VAAHSGTELTFQSAsPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDvCYVSMPLFHSNAVLVGWAVA 210
Cdd:PRK05691 2318 LAAYSDAPLPFLSL-PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD-CELHFYSINFDAASERLLVP 2395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 211 AACQGSIALRR--KFSASGFIADVRRYGATYANYV---GKPLSYVLATPEQpddsENPLRAVY-GNEGVAGD-LERFARR 283
Cdd:PRK05691 2396 LLCGARVVLRAqgQWGAEEICQLIREQQVSILGFTpsyGSQLAQWLAGQGE----QLPVRMCItGGEALTGEhLQRIRQA 2471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 284 FG-CVVQDGFGSTEGGVA--IARTPDTPAGSLGPLPAG-------IEIVDPDTGrPCPAGVVGELVnTAGPGRFEGYYND 353
Cdd:PRK05691 2472 FApQLFFNAYGPTETVVMplACLAPEQLEEGAASVPIGrvvgarvAYILDADLA-LVPQGATGELY-VGGAGLAQGYHDR 2549
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2321332536 354 EAAEAERM--------AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDP 423
Cdd:PRK05691 2550 PGLTAERFvadpfaadGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP 2627
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
129-431 |
1.31e-14 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 76.38 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 129 DEVAAHSGTELTFQSAS-PADLFMLIFTSGTSGEPKAVKCSHS--------KVAIAGvtmtqrfgLGPDDVCYVSMPLFH 199
Cdd:PLN02860 153 EMLKQRALGTTELDYAWaPDDAVLICFTSGTTGRPKGVTISHSalivqslaKIAIVG--------YGEDDVYLHTAPLCH 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 200 ----SNA---VLVGwavaaACQgsiALRRKFSASGFIADVRRYGATYANYVGKPLSYVLA-TPEQPDDSENP--LRAVYG 269
Cdd:PLN02860 225 igglSSAlamLMVG-----ACH---VLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISlTRKSMTWKVFPsvRKILNG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 270 NEGVAGDLERFARR-FGCV-VQDGFGSTE----------------GGVAIARTPDTPAGSLGPLPAGIEIvdpdtGRPCP 331
Cdd:PLN02860 297 GGSLSSRLLPDAKKlFPNAkLFSAYGMTEacssltfmtlhdptleSPKQTLQTVNQTKSSSVHQPQGVCV-----GKPAP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 332 ----------AGVVGELVnTAGPGRFEGYYNDEAAEAE-RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTA 400
Cdd:PLN02860 372 hvelkigldeSSRVGRIL-TRGPHVMLGYWGQNSETASvLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPE 450
|
330 340 350
....*....|....*....|....*....|.
gi 2321332536 401 PIERVLLRYPDTAEVAVYAVPDPVVGDRVMA 431
Cdd:PLN02860 451 EVEAVLSQHPGVASVVVVGVPDSRLTEMVVA 481
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
143-456 |
1.66e-14 |
|
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: 75.66 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 143 SASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYvsmpLFHSNA-------VLVGWAVAA-ACQ 214
Cdd:cd05918 102 TSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVL----QFASYTfdvsileIFTTLAAGGcLCI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 215 GSiALRRKFSASGFIadvRRYGATYAnyvgkplsyvLATPE-----QPDDSENPLRAVYGNEGV-AGDLERFARRfgCVV 288
Cdd:cd05918 178 PS-EEDRLNDLAGFI---NRLRVTWA----------FLTPSvarllDPEDVPSLRTLVLGGEALtQSDVDTWADR--VRL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 QDGFGSTE---GGVAIARTPDTPAGSLG-PLPAGIEIVDPDT-GRPCPAGVVGELVNtAGP--GRfeGYYNDEAAEAE-- 359
Cdd:cd05918 242 INAYGPAEctiAATVSPVVPSTDPRNIGrPLGATCWVVDPDNhDRLVPIGAVGELLI-EGPilAR--GYLNDPEKTAAaf 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 360 ------RMAGG------IYHSGDLAYRDDAGYAYFAGRLGDW-----MRVD-GEnlgtapIERVLLRYPDTAE---VAVY 418
Cdd:cd05918 319 iedpawLKQEGsgrgrrLYRTGDLVRYNPDGSLEYVGRKDTQvkirgQRVElGE------IEHHLRQSLPGAKevvVEVV 392
|
330 340 350
....*....|....*....|....*....|....*...
gi 2321332536 419 AVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQPDL 456
Cdd:cd05918 393 KPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEF 430
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
144-484 |
1.67e-14 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 75.51 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGL-GPDDvcyvSMPLFHSNAVL---VGWAVAAACQGSIAL 219
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGrDNGD----EAVLFFSNYVFdffVEQMTLALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 220 rrKFSASGFIADVRRYgaTYANyvGKPLSYVLATP---EQPD-DSENPLRAV--YGNEGVAGDLERFARRFGCVVQDGFG 293
Cdd:cd17648 167 --VPPDEMRFDPDRFY--AYIN--REKVTYLSGTPsvlQQYDlARLPHLKRVdaAGEEFTAPVFEKLRSRFAGLIINAYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 294 STEGGV-AIARTPDTPA---GSLG-PLPAGIEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM------- 361
Cdd:cd17648 241 PTETTVtNHKRFFPGDQrfdKSLGrPVRNTKCYVLNDAMKRVPVGAVGELY-LGGDGVARGYLNRPELTAERFlpnpfqt 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 362 ----AGG----IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGD-----R 428
Cdd:cd17648 320 eqerARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkY 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321332536 429 VMAALVLAPGTRFDTDKFRVFLAEQPdlgPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17648 400 LVGYYLPEPGHVPESDLLSFLRAKLP---RYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
56-461 |
1.73e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.92 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSASAGPLADieHVNVESTEWSDEVAAHS 135
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQ--GVQVLDLDRGDENYAEA 3187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 136 GTELtfqSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDD-VCYVSMPLFHSNAVLVGWAVAAACQ 214
Cdd:PRK12316 3188 NPAI---RTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDrVLQFTTFSFDVFVEELFWPLMSGAR 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 215 GSIALRRKFSASGFIAD-VRRYGATYANYVGKPLSYVLATPEqPDDSENPLRAVYGNEGVAGDLERfARRFGCVVQDGFG 293
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVElINSEGVDVLHAYPSMLQAFLEEED-AHRCTSLKRIVCGGEALPADLQQ-QVFAGLPLYNLYG 3342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 294 STEGGVAIA------RTPDT-PAGSlgPLPAGIEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM----- 361
Cdd:PRK12316 3343 PTEATITVThwqcveEGKDAvPIGR--PIANRACYILDGSLEPVPVGALGELY-LGGEGLARGYHNRPGLTAERFvpdpf 3419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 362 --AGGIYHSGDLA-YRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPdpvvGDRVMAALVLAPG 438
Cdd:PRK12316 3420 vpGERLYRTGDLArYRAD-GVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDE 3494
|
410 420
....*....|....*....|....*
gi 2321332536 439 TRFDTDKFRVFLAEQ-PD-LGPKQW 461
Cdd:PRK12316 3495 AGDLREALKAHLKASlPEyMVPAHL 3519
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
84-484 |
2.06e-14 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 75.70 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 84 NPVRRGAAL--LRDINHAdcqlVLADSASAGPLADI-------EHVNVESTEWSD-------EVAAHSGTELTFQSASPA 147
Cdd:PLN02654 200 NAVKRGPKTinLKDIVDA----ALDESAKNGVSVGIcltyenqLAMKREDTKWQEgrdvwwqDVVPNYPTKCEVEWVDAE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAV-KCSHSKVAIAGVTMTQRFGLGPDDV------C-------YVSM-PLFHSNAVLV------- 205
Cdd:PLN02654 276 DPLFLLYTSGSTGKPKGVlHTTGGYMVYTATTFKYAFDYKPTDVywctadCgwitghsYVTYgPMLNGATVLVfegapny 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 206 -----GWAVAAACQGSIAlrrkFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDdseNP--LRAVYGnegVAGDLE 278
Cdd:PLN02654 356 pdsgrCWDIVDKYKVTIF----YTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPI---NPsaWRWFFN---VVGDSR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 279 rfarrfgCVVQDGFGSTE-GGVAIarTPDTPAGSLGPLPA-----GIE--IVDpDTGRPCPAGVVGEL-VNTAGPGRFEG 349
Cdd:PLN02654 426 -------CPISDTWWQTEtGGFMI--TPLPGAWPQKPGSAtfpffGVQpvIVD-EKGKEIEGECSGYLcVKKSWPGAFRT 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 350 YYND-EAAEAERMA--GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVG 426
Cdd:PLN02654 496 LYGDhERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKG 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 427 DRVMAALVLAPGTRFDTD-KFRVFLAEQPDLGPKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PLN02654 576 QGIYAFVTLVEGVPYSEElRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
68-484 |
2.56e-14 |
|
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: 75.20 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 68 AMLVAAGmsGIVPVGLN-PVRRGAALLRDinhADCQLVLADSASAGPLAD-IEHVNVEStewsDEVAAHSGTELTFQSAS 145
Cdd:cd17656 57 GILKAGG--AFVPIDPEyPEERRIYIMLD---SGVRVVLTQRHLKSKLSFnKSTILLED----PSISQEDTSNIDYINNS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 pADLFMLIFTSGTSGEPKAVKCSHSKVA-IAGVTMTQRFGLGPDDVCYVSMPLFHsnaVLVGWAVAAACQG------SIA 218
Cdd:cd17656 128 -DDLLYIIYTSGTTGKPKGVQLEHKNMVnLLHFEREKTNINFSDKVLQFATCSFD---VCYQEIFSTLLSGgtlyiiREE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 219 LRRkfsasgfiaDVRRYGATYANY----VGKPLSYV--LATPEQ--PDDSENPLRAVYGNEG--VAGDLERFARRFGCVV 288
Cdd:cd17656 204 TKR---------DVEQLFDLVKRHnievVFLPVAFLkfIFSEREfiNRFPTCVKHIITAGEQlvITNEFKEMLHEHNVHL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 QDGFGSTEGGVAIART--PDTPAGSLGPL--PAG---IEIVDpDTGRPCPAGVVGEL-VNTAGPGRfeGYYNDEAAEAER 360
Cdd:cd17656 275 HNHYGPSETHVVTTYTinPEAEIPELPPIgkPISntwIYILD-QEQQLQPQGIVGELyISGASVAR--GYLNRQELTAEK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 361 MAGG-------IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAAL 433
Cdd:cd17656 352 FFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 434 VlaPGTRFDTDKFRVFLAEQ-PDLgpkQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd17656 432 V--MEQELNISQLREYLAKQlPEY---MIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
55-453 |
4.83e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.54 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 55 HVGVLLQNTPFFSAMLVAAGMSGIVPVGLNpVRRGAALLRDI-NHADCQLVLADSASAGPLADI---------------- 117
Cdd:PRK07798 55 HVGIYARNRIEYVEAMLGAFKARAVPVNVN-YRYVEDELRYLlDDSDAVALVYEREFAPRVAEVlprlpklrtlvvvedg 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 118 --EHVNVESTEWSDEVAAHSGtELTFQSASPADLFMLiFTSGTSGEPKAVKCSHS---KVAIAGVT------------MT 180
Cdd:PRK07798 134 sgNDLLPGAVDYEDALAAGSP-ERDFGERSPDDLYLL-YTGGTTGMPKGVMWRQEdifRVLLGGRDfatgepiedeeeLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 181 QRFGLGPDDVCYVSMPLFHSNAVlvgWAVAAA--CQGSIAL--RRKFSASGFIADVRRYGATYANYVG----KPLSYVLA 252
Cdd:PRK07798 212 KRAAAGPGMRRFPAPPLMHGAGQ---WAAFAAlfSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVGdamaRPLLDALE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 253 TPEQPDDSEnpLRAVyGNEGVA-------GDLERFARRfgcVVQDGFGSTEGGV-AIARTPDTPAGSLGP---LPAGIEI 321
Cdd:PRK07798 289 ARGPYDLSS--LFAI-ASGGALfspsvkeALLELLPNV---VLTDSIGSSETGFgGSGTVAKGAVHTGGPrftIGPRTVV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 322 VDPDTGRPCP-AGVVGELvntAGPGRFE-GYYNDEAAEAE--RMAGGIYHS--GDLAYRDDAGYAYFAGRlgDWMRVD-- 393
Cdd:PRK07798 363 LDEDGNPVEPgSGEIGWI---ARRGHIPlGYYKDPEKTAEtfPTIDGVRYAipGDRARVEADGTITLLGR--GSVCINtg 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 394 GENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQ 453
Cdd:PRK07798 438 GEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSS 497
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
278-429 |
1.24e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 73.16 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 278 ERFARRFGCVVQDGFGSTEGGVAIARTP---DTPAGSLG-PLPAG-IEIVDpDTGRPCPAGVVGELVnTAGPGRFEGYYN 352
Cdd:PRK08974 343 ERWVKLTGQYLLEGYGLTECSPLVSVNPydlDYYSGSIGlPVPSTeIKLVD-DDGNEVPPGEPGELW-VKGPQVMLGYWQ 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 353 DEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRV 429
Cdd:PRK08974 421 RPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
56-484 |
1.29e-13 |
|
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: 72.85 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLNPVRRGAALLRDINHADCQLVLADSA-------SAGPLADIEHVNVESTEWS 128
Cdd:cd05915 52 VATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNllplveaIRGELKTVQHFVVMDEKAP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 129 DEVAAHSGTELTFQSASPADL---FMLIFTSGTSGEPKAVKCSHSKVAI--AGVTMTQRFGLGPDDVCYVSMPLFHSNAV 203
Cdd:cd05915 132 EGYLAYEEALGEEADPVRVPEraaCGMAYTTGTTGLPKGVVYSHRALVLhsLAASLVDGTALSEKDVVLPVVPMFHVNAW 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 204 LVGWAVAAACQGSIALRRKFSASGFIADVRRYGATyaNYVGK-PLSYVLATPEQPDDSENP--LRAVYGNEGVAGDLERF 280
Cdd:cd05915 212 CLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVT--FTAGVpTVWLALADYLESTGHRLKtlRRLVVGGSAAPRSLIAR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 281 ARRFGCVVQDGFGSTEG---GVAIARTPD------------TPAGSLGPLPAGIEIVDPDTGRPCPAGVVGELVNTAGPG 345
Cdd:cd05915 290 FERMGVEVRQGYGLTETspvVVQNFVKSHleslseeekltlKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPW 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 346 RFEGYYND-EAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPV 424
Cdd:cd05915 370 ITGGYYGNeEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPK 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 425 VGDRVMAALVLAPGTRFDTDKFRVFLAEQPDLgpKQWPSYVRISAGLPGTVTFKVLKRQL 484
Cdd:cd05915 450 WQERPLAVVVPRGEKPTPEELNEHLLKAGFAK--WQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
126-417 |
2.19e-13 |
|
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: 72.12 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 126 EWSDEVAAHS---GTELTFqsasPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFH--- 199
Cdd:cd05932 117 QWDDLIAQHPpleERPTRF----PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHvte 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 200 SNAVLVGWAVaaacqGSIALRRKFSASGFIADVRRYGATYanYVGKPLSYVL-------ATPEQPDD------------- 259
Cdd:cd05932 193 RVFVEGGSLY-----GGVLVAFAESLDTFVEDVQRARPTL--FFSVPRLWTKfqqgvqdKIPQQKLNlllkipvvnslvk 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 260 -------SENPLR-AVYGNEGVAGDLERFARRFGCVVQDGFGSTEG-GVAIARTP-DTPAGSLGPLPAGIEIVDPDTGRp 329
Cdd:cd05932 266 rkvlkglGLDQCRlAGCGSAPVPPALLEWYRSLGLNILEAYGMTENfAYSHLNYPgRDKIGTVGNAGPGVEVRISEDGE- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 330 cpagvvgelVNTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRV-DGENLGTAPIERVLL 407
Cdd:cd05932 345 ---------ILVRSPALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLA 415
|
330
....*....|
gi 2321332536 408 RYPDTAEVAV 417
Cdd:cd05932 416 EHDRVEMVCV 425
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
92-422 |
2.51e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.89 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 92 LLRDINHADCQLVLADSASAGPLADIEHVNVEST-EWS-----DEVAAHSGTELTFQsasPADLFMLIFTSGTSGEPKAV 165
Cdd:PRK05691 108 LLSIIADAEPRLLLTVADLRDSLLQMEELAAANApELLcvdtlDPALAEAWQEPALQ---PDDIAFLQYTSGSTALPKGV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 166 KCSHSKVAIAGVTMTQRFG--LGPDDVCYVSMPLFHSNAvLVGWAVAAACQGSIALRrkFSASGFIAD-------VRRYG 236
Cdd:PRK05691 185 QVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMG-LIGGLLQPIFSGVPCVL--MSPAYFLERplrwleaISEYG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 237 ATYANyvGKPLSYVLATPEQPDDSENPL-----RAVY-GNEGVAGD-LERFARRF-GC-VVQDGF--------------G 293
Cdd:PRK05691 262 GTISG--GPDFAYRLCSERVSESALERLdlsrwRVAYsGSEPIRQDsLERFAEKFaACgFDPDSFfasyglaeatlfvsG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 294 STEG---------GVAIARTPDTP-AGSL-----GPLPA-GIEIVDPDTGRPCPAGVVGElVNTAGPGRFEGYYNDEAAE 357
Cdd:PRK05691 340 GRRGqgipaleldAEALARNRAEPgTGSVlmscgRSQPGhAVLIVDPQSLEVLGDNRVGE-IWASGPSIAHGYWRNPEAS 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 358 AE---RMAGGIY-HSGDLAYRDDaGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTA---EVAVYAVPD 422
Cdd:PRK05691 419 AKtfvEHDGRTWlRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkgRVAAFAVNH 489
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
56-484 |
4.15e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 68.11 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGL---NPVRRGAALLRDinhADCQLVLADsasagpladiehvnvestewsdeva 132
Cdd:cd12115 52 VGVCLERTPDLVVALLAVLKAGAAYVPLdpaYPPERLRFILED---AQARLVLTD------------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 133 ahsgteltfqsasPADLFMLIFTSGTSGEPKAVKCSHSKVA--------------IAGVtmtqrfgLGPDDVCY------ 192
Cdd:cd12115 104 -------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAaflqwaaaafsaeeLAGV-------LASTSICFdlsvfe 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 193 VSMPLFH------SNAVLVGWAVAAACQGSI------ALRRKFSASGFIADVRrygatYANYVGKPLSYVLatpeqpdds 260
Cdd:cd12115 164 LFGPLATggkvvlADNVLALPDLPAAAEVTLintvpsAAAELLRHDALPASVR-----VVNLAGEPLPRDL--------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 261 enpLRAVYGNEGVAgdlerfarrfgcVVQDGFGSTEggvaiARTPDT----PAGSLGPLPAG-------IEIVDpDTGRP 329
Cdd:cd12115 230 ---VQRLYARLQVE------------RVVNLYGPSE-----DTTYSTvapvPPGASGEVSIGrplantqAYVLD-RALQP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 330 CPAGVVGELVnTAGPGRFEGYYNDEAAEAER-----MAGG--IYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPI 402
Cdd:cd12115 289 VPLGVPGELY-IGGAGVARGYLGRPGLTAERflpdpFGPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 403 ERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQ------PDLgpkqwpsYVRISAgLPGTVT 476
Cdd:cd12115 368 EAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRlpaymvPSR-------FVRLDA-LPLTPN 439
|
....*...
gi 2321332536 477 FKVLKRQL 484
Cdd:cd12115 440 GKIDRSAL 447
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
141-422 |
7.57e-12 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 67.24 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 141 FQSASPADLFMLIFTSGTSGEPKAVKCSHSKVaIAGVT-MTQRFG--LGPDDVCYVSMPLFH------SNAVL-----VG 206
Cdd:cd17639 82 FTDGKPDDLACIMYTSGSTGNPKGVMLTHGNL-VAGIAgLGDRVPelLGPDDRYLAYLPLAHifelaaENVCLyrggtIG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 207 W--------AVAAACQGSI--------------------ALRRKFSASGFIADVRRYGATYANyvgkpLSYVLATPEQPD 258
Cdd:cd17639 161 YgsprtltdKSKRGCKGDLtefkptlmvgvpaiwdtirkGVLAKLNPMGGLKRTLFWTAYQSK-----LKALKEGPGTPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 259 DSE---NPLRAVYGNE---------GVAGDLERFARRFGCVVQDGFGSTE--GGVAIARTPDTPAGSLGPLPAGIEI--V 322
Cdd:cd17639 236 LDElvfKKVRAALGGRlrymlsggaPLSADTQEFLNIVLCPVIQGYGLTEtcAGGTVQDPGDLETGRVGPPLPCCEIklV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 323 D-PDTG----RPCPAgvvGELVnTAGPGRFEGYY-NDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRV-DGE 395
Cdd:cd17639 316 DwEEGGystdKPPPR---GEIL-IRGPNVFKGYYkNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGE 391
|
330 340
....*....|....*....|....*..
gi 2321332536 396 NLGTAPIERVLLRYPDTAEVAVYAVPD 422
Cdd:cd17639 392 YIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
152-484 |
1.19e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.70 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 152 LIFTSGTSGEPKAVKCSH-SKVAIAGVTMT-QRFGLGPDDVCYVSMPLFHSNAvlvgWAVAAACQGSIAlrrKFSASGFI 229
Cdd:PRK06018 182 MCYTSGTTGDPKGVLYSHrSNVLHALMANNgDALGTSAADTMLPVVPLFHANS----WGIAFSAPSMGT---KLVMPGAK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 230 ADvrryGAT-YANYVGKPLSYVLATPE---------QPDDSENPL--RAVYGNEGVAGDLERFARRFGCVVQDGFGSTEg 297
Cdd:PRK06018 255 LD----GASvYELLDTEKVTFTAGVPTvwlmllqymEKEGLKLPHlkMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTE- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 298 gvaiartpDTPAGSLGPLPAGIEIVDPDT--------GRPcPAGVVGELVNTAG---------PGRFE--------GYYN 352
Cdd:PRK06018 330 --------MSPLGTLAALKPPFSKLPGDArldvlqkqGYP-PFGVEMKITDDAGkelpwdgktFGRLKvrgpavaaAYYR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 353 DEAAEAErmAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAA 432
Cdd:PRK06018 401 VDGEILD--DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLI 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 433 LVLAPGTRFDTDKFRVFLAEQPdlgPKQW-PSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK06018 479 VQLKPGETATREEILKYMDGKI---AKWWmPDDVAFVDAIPHTATGKILKTAL 528
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
134-414 |
1.35e-11 |
|
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: 66.31 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 134 HSGTELTFQSaSPADLFMLIFTSGTSGEPKAVKCSHSKVA--IAGVTMTQRfgLGPDDVCYVSMPLFHSNAVLVGWAVAA 211
Cdd:cd05914 77 HSEAKAIFVS-DEDDVALINYTSGTTGNSKGVMLTYRNIVsnVDGVKEVVL--LGKGDKILSILPLHHIYPLTFTLLLPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 212 ACQGSIALRRKFSASGFIA------------------DVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRA------- 266
Cdd:cd05914 154 LNGAHVVFLDKIPSAKIIAlafaqvtptlgvpvplviEKIFKMDIIPKLTLKKFKFKLAKKINNRKIRKLAFKkvheafg 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 267 ------VYGNEGVAGDLERFARRFGCVVQDGFGSTEGGVAIARTP--DTPAGSLGPLpagIEIVDPDTGRPCPAGVVGEL 338
Cdd:cd05914 234 gnikefVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPpnRIRLGSAGKV---IDGVEVRIDSPDPATGEGEI 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 339 VnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDwMRV--DGENLGTAPIERVLLRYPDTAE 414
Cdd:cd05914 311 I-VRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKE-MIVlsSGKNIYPEEIEAKINNMPFVLE 387
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
151-489 |
1.46e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 66.21 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 151 MLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGwAVAAACQGSI-----ALRRKFSa 225
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICG-VLAALTRGSKpviitNKNPKFA- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 226 sgfIADVRRYgATYANYVGKPLSYVLA--TPEQ-------------PDDSENPLRAVygnegvagdLERFARRFGCvvqd 290
Cdd:PRK08308 183 ---LNILRNT-PQHILYAVPLMLHILGrlLPGTfqfhavmtsgtplPEAWFYKLRER---------TTYMMQQYGC---- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 291 gfgSTEGGVAIARTPDTPaGSLG-PLP-AGIEIvDPDTGRPcpagvvGELVNTAGPGRFegyyndeaaeaermaggiyHS 368
Cdd:PRK08308 246 ---SEAGCVSICPDMKSH-LDLGnPLPhVSVSA-GSDENAP------EEIVVKMGDKEI-------------------FT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 369 GDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVmAALVLAPGTrFDTDKFRV 448
Cdd:PRK08308 296 KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERV-KAKVISHEE-IDPVQLRE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2321332536 449 FLAEQpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAEGV 489
Cdd:PRK08308 374 WCIQH--LAPYQVPHEIESVTEIPKNANGKVSRKLLELGEV 412
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
139-339 |
1.57e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 65.94 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 139 LTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGvTMTQRF----GLGPDDVCYVSMPL--------FHSNAVLVG 206
Cdd:COG1541 75 FGLFAVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWA-ELFARSlraaGVRPGDRVQNAFGYglftgglgLHYGAERLG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 207 WAVAAACQGSIALRRKFsasgfiadVRRYGATYanYVGKPlSYVL-----ATPEQPDDSENPLR-AVYGNEGVAGDL-ER 279
Cdd:COG1541 154 ATVIPAGGGNTERQLRL--------MQDFGPTV--LVGTP-SYLLylaevAEEEGIDPRDLSLKkGIFGGEPWSEEMrKE 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2321332536 280 FARRFGCVVQDGFGSTEGGVAIARtpDTPAGSLGPLPAG---IEIVDPDTGRPCPAGVVGELV 339
Cdd:COG1541 223 IEERWGIKAYDIYGLTEVGPGVAY--ECEAQDGLHIWEDhflVEIIDPETGEPVPEGEEGELV 283
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
114-486 |
3.69e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.41 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 114 LADIEHVNVESTEWSDEvAAHSGtELTFQSASPA----DLFMLIFTSGTSGEPKAVKCShSKVAIAGVTMTQRFGLG--- 186
Cdd:PRK05857 134 LHSIPVIAVDIAAVTRE-SEHSL-DAASLAGNADqgseDPLAMIFTSGTTGEPKAVLLA-NRTFFAVPDILQKEGLNwvt 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 187 --PDDVCYVSMPLFHSNAVLvgWAVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPL 264
Cdd:PRK05857 211 wvVGETTYSPLPATHIGGLW--WILTCLMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 265 RAVY--GNEGVAGDLeRFARRFGCVVQDGFGSTEGGVAIARTPdTPAGSLGPLPAG----------IEIVDPDTGRP--- 329
Cdd:PRK05857 289 RLVGygGSRAIAADV-RFIEATGVRTAQVYGLSETGCTALCLP-TDDGSIVKIEAGavgrpypgvdVYLAATDGIGPtap 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 330 --CPAGVVGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLL 407
Cdd:PRK05857 367 gaGPSASFGTLW-IKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 408 RYPDTAEVAVYAVPDPVVGDRVMAALVlaPGTRFDTD-----KFRVFLAEQPDLGPKQWPSYVRISAGLPGTVTFKVLKR 482
Cdd:PRK05857 446 GVSGVREAACYEIPDEEFGALVGLAVV--ASAELDESaaralKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRA 523
|
....
gi 2321332536 483 QLAA 486
Cdd:PRK05857 524 SLAA 527
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
60-487 |
4.84e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 65.05 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 60 LQNTPFFSAMLVAAGMSGIVPVGLNPvrrgaALLRD---INHADCQLVLAdsASAGPLAD--IEHVNVESTEWSDEVAah 134
Cdd:PRK06060 62 LPDSPDLVQLLLACLARGVMAFLANP-----ELHRDdhaLAARNTEPALV--VTSDALRDrfQPSRVAEAAELMSEAA-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 135 sgteltfqSASPADLFML--------IFTSGTSGEPKAVKCSHSKV-AIAGVTMTQRFGLGPDDVCYVSMPLFHS----N 201
Cdd:PRK06060 133 --------RVAPGGYEPMggdalayaTYTSGTTGPPKAAIHRHADPlTFVDAMCRKALRLTPEDTGLCSARMYFAyglgN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 202 AVlvgWAVAAAcqGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQPDDSENPLRAVY--GNEGVAGDLER 279
Cdd:PRK06060 205 SV---WFPLAT--GGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVsaGEALELGLAER 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 280 FARRFGCV-VQDGFGSTE-GGVAIARTPDT-PAGSLGPL--PAGIEIVDPDtGRPCPAGVVGELVnTAGPGRFEGYYNde 354
Cdd:PRK06060 280 LMEFFGGIpILDGIGSTEvGQTFVSNRVDEwRLGTLGRVlpPYEIRVVAPD-GTTAGPGVEGDLW-VRGPAIAKGYWN-- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 355 AAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALV 434
Cdd:PRK06060 356 RPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 435 LAPGTRFD----TDKFRVFLAEqpdLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PRK06060 436 ATSGATIDgsvmRDLHRGLLNR---LSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
96-372 |
1.59e-10 |
|
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: 63.39 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 96 INHADCQLVLADSasagpladiehvNVESTEWSDEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVA-- 173
Cdd:cd05927 75 LNHAEISIVFCDA------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVsn 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 174 IAGV--TMTQRFGLGPDDVcYVS-MPLFHSNAVLVGWAVAA--AC----QGSI--------ALR--------RKFSasgf 228
Cdd:cd05927 143 VAGVfkILEILNKINPTDV-YISyLPLAHIFERVVEALFLYhgAKigfySGDIrlllddikALKptvfpgvpRVLN---- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 229 iadvRRYGATYANYVGKP----------LSYVLATPEQPDDSENPL--RAVY----------------GNEGVAGDLERF 280
Cdd:cd05927 218 ----RIYDKIFNKVQAKGplkrklfnfaLNYKLAELRSGVVRASPFwdKLVFnkikqalggnvrlmltGSAPLSPEVLEF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 281 ARR-FGCVVQDGFGSTE--GGVAIARTPDTPAGSLG-PLPAgIEI--VD-PDTG----RPCPAGVVgeLVNtaGPGRFEG 349
Cdd:cd05927 294 LRVaLGCPVLEGYGQTEctAGATLTLPGDTSVGHVGgPLPC-AEVklVDvPEMNydakDPNPRGEV--CIR--GPNVFSG 368
|
330 340
....*....|....*....|....
gi 2321332536 350 YYNDEAAEAERMA-GGIYHSGDLA 372
Cdd:cd05927 369 YYKDPEKTAEALDeDGWLHTGDIG 392
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
96-484 |
2.69e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.42 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 96 INHADCQLVLADS---------ASAGP-------LADIEHVNVESTE---WSDEVAAHSGT----ELTFQSASPadlfmL 152
Cdd:PRK07008 107 VNHAEDRYVLFDLtflplvdalAPQCPnvkgwvaMTDAAHLPAGSTPllcYETLVGAQDGDydwpRFDENQASS-----L 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 153 IFTSGTSGEPKAVKCSH-SKVAIA-GVTMTQRFGLGPDDVCYVSMPLFHSNAvlvgWAV--AAACQGSialrrKFSASGF 228
Cdd:PRK07008 182 CYTSGTTGNPKGALYSHrSTVLHAyGAALPDAMGLSARDAVLPVVPMFHVNA----WGLpySAPLTGA-----KLVLPGP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 229 IAD-------VRRYGATYAnyVGKP------LSYVlatpeqpddSENPLRAVYGNEGVAGD-------LERFARRFGCVV 288
Cdd:PRK07008 253 DLDgkslyelIEAERVTFS--AGVPtvwlglLNHM---------REAGLRFSTLRRTVIGGsacppamIRTFEDEYGVEV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 289 QDGFGSTE----GGVA------IARTPDTPAGSL---GPLPAGIE--IVDPDtGRPCP-AGVV-GELVnTAGPGRFEGYY 351
Cdd:PRK07008 322 IHAWGMTEmsplGTLCklkwkhSQLPLDEQRKLLekqGRVIYGVDmkIVGDD-GRELPwDGKAfGDLQ-VRGPWVIDRYF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 352 NDEAAEaerMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMA 431
Cdd:PRK07008 400 RGDASP---LVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLL 476
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 432 ALVLAPGTRFDTDKFRVFLAEQPdlgPKQW-PSYVRISAGLPGTVTFKVLKRQL 484
Cdd:PRK07008 477 VVVKRPGAEVTREELLAFYEGKV---AKWWiPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
140-429 |
4.13e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 62.29 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 140 TFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAvLVGWAVAAACQG---- 215
Cdd:PRK06814 786 YFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFG-LTGGLVLPLLSGvkvf 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 216 -------------------SIALrrkFSASGFIADVRRYGATYANYvgkPLSYVLATPEQPDDSEnplRAVYgnegvagd 276
Cdd:PRK06814 865 lypsplhyriipeliydtnATIL---FGTDTFLNGYARYAHPYDFR---SLRYVFAGAEKVKEET---RQTW-------- 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 277 lerfARRFGCVVQDGFGSTEGGVAIARtpDTP----AGSLGPLPAGIEI-VDPDTGrpCPAGvvGELVnTAGPGRFEGYY 351
Cdd:PRK06814 928 ----MEKFGIRILEGYGVTETAPVIAL--NTPmhnkAGTVGRLLPGIEYrLEPVPG--IDEG--GRLF-VRGPNVMLGYL 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 352 NDEAAEA-ERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRY-PDTAEVAVyAVPDPVVGDRV 429
Cdd:PRK06814 997 RAENPGVlEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAV-SIPDARKGERI 1075
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
146-444 |
5.63e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 61.76 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNA--------VLVGWAVAaacqgsi 217
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfnsctlfpLLSGVPVV------- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 218 alrrkFSASGFIAD--VRRYGATYANYVGKP---LSYVLATPEQPDDSENPLR-AVYGNEGVAGDLERFARRFGCVVQ-- 289
Cdd:PRK06334 255 -----FAYNPLYPKkiVEMIDEAKVTFLGSTpvfFDYILKTAKKQESCLPSLRfVVIGGDAFKDSLYQEALKTFPHIQlr 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 290 DGFGSTEGGVAIA-RTPDTPAGS--LGPLPAGIE--IVDPDTGRPCPAGVVGeLVNTAGPGRFEGYY-NDEAAEAERMAG 363
Cdd:PRK06334 330 QGYGTTECSPVITiNTVNSPKHEscVGMPIRGMDvlIVSEETKVPVSSGETG-LVLTRGTSLFSGYLgEDFGQGFVELGG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 364 GI-YHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRY------PDTAEVAVYAVPdpvvGDRVMAALVla 436
Cdd:PRK06334 409 ETwYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLP----GEKVRLCLF-- 482
|
....*...
gi 2321332536 437 pgTRFDTD 444
Cdd:PRK06334 483 --TTFPTS 488
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
311-461 |
6.27e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.16 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 311 SLG-PLP-AGIEIVDPDTGrpcpagvvgeLVNTAGPGRFEGYYNDEAAEAermagGIYHSGDLAYRDDAGYAYFAGRLGD 388
Cdd:PRK07445 284 SSGqVLPhAQITIPANQTG----------NITIQAQSLALGYYPQILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQ 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2321332536 389 WMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTrFDTDKFRVFLAEQ--PDLGPKQW 461
Cdd:PRK07445 349 KIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLEELKTAIKDQlsPFKQPKHW 422
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
148-404 |
8.15e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.17 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVS-MPLFHSNAvLVGWAVAAACQGSIALrrKFSAS 226
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSwLPLFHDMG-MVGFLTVPMYFGAELV--KVTPM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 227 GFIAD-------VRRYGATyaNYVGKPLSYVLAT---PEQPDDSE---NPLR-AVYGNEGV-AGDLERFAR---RFG--- 285
Cdd:PRK07768 230 DFLRDpllwaelISKYRGT--MTAAPNFAYALLArrlRRQAKPGAfdlSSLRfALNGAEPIdPADVEDLLDagaRFGlrp 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 286 -CVVQdGFGSTEGGVAIArTPDTPAG-----------------------------SLGPLPAGIE--IVDPDtGRPCPAG 333
Cdd:PRK07768 308 eAILP-AYGMAEATLAVS-FSPCGAGlvvdevdadllaalrravpatkgntrrlaTLGPPLPGLEvrVVDED-GQVLPPR 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 334 VVGELvNTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIER 404
Cdd:PRK07768 385 GVGVI-ELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIER 454
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
153-423 |
8.80e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.07 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 153 IFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFhsnaVLVGWAVAAAcqgSIALRRKFSASGF---- 228
Cdd:PRK09274 180 LFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF----ALFGPALGMT---SVIPDMDPTRPATvdpa 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 229 --IADVRRYGATyaNYVGKP--LSYVLATPEQPDDSENPLRAVYgnegVAGD------LERFARRF--GCVVQDGFGSTE 296
Cdd:PRK09274 253 klFAAIERYGVT--NLFGSPalLERLGRYGEANGIKLPSLRRVI----SAGApvpiavIERFRAMLppDAEILTPYGATE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 297 -------GGVAI--ARTPDTPAGS---LG-PLP-AGIEIVDPDTG--------RPCPAGVVGELVnTAGPGRFEGYYNDE 354
Cdd:PRK09274 327 alpissiESREIlfATRAATDNGAgicVGrPVDgVEVRIIAISDApipewddaLRLATGEIGEIV-VAGPMVTRSYYNRP 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 355 AAEAE----RMAGGIYH-SGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDP 423
Cdd:PRK09274 406 EATRLakipDGQGDVWHrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP 479
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
148-486 |
9.23e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 148 DLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPL-FHSNAVLVGWAVAAACQGSIALRRKFSAS 226
Cdd:PRK05691 1274 NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIsFDVSVWECFWPLITGCRLVLAGPGEHRDP 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 227 GFIAD-VRRYGATYANYVgKPLSYVLAtpEQPDDSE-NPLRAVY-GNEGVAGDLER--FARRFGCVVQDGFGSTEGGVAI 301
Cdd:PRK05691 1354 QRIAElVQQYGVTTLHFV-PPLLQLFI--DEPLAAAcTSLRRLFsGGEALPAELRNrvLQRLPQVQLHNRYGPTETAINV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 302 A----RTPDTPAGSLG-PLPAGIEIVDPDTGRPCPAGVVGELVnTAGPGRFEGYYNDEAAEAERM-------AGG-IYHS 368
Cdd:PRK05691 1431 ThwqcQAEDGERSPIGrPLGNVLCRVLDAELNLLPPGVAGELC-IGGAGLARGYLGRPALTAERFvpdplgeDGArLYRT 1509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 369 GDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYaVPDPVVGDRVMAALVLAPGTRFDTDKFRV 448
Cdd:PRK05691 1510 GDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKA 1588
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2321332536 449 FLAEQ-PD-LGPKQwpsYVRISAgLPGTVTFKVLKRQLAA 486
Cdd:PRK05691 1589 ALAAElPEyMVPAQ---LIRLDQ-MPLGPSGKLDRRALPE 1624
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
56-423 |
1.10e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.79 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVPVGLN-PVRRGAallRD--INHADCQLVLAD-SASAGPLADIEHVNvESTEWSDEV 131
Cdd:PRK09192 77 VALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGG---REsyIAQLRGMLASAQpAAIITPDELLPWVN-EATHGNPLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 132 AAHSGTEL--------TFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVaIAGVTMTQRFGL--GPDDVCYVSMPLFHSN 201
Cdd:PRK09192 153 HVLSHAWFkalpeadvALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL-MANLRAISHDGLkvRPGDRCVSWLPFYHDM 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 202 AvLVGWAVAA-ACQGSIAL-------RRKFSASGFIAdvrRYGATYAnyVGKPLSYVLATPEQPDDSENPL-----RAVy 268
Cdd:PRK09192 232 G-LVGFLLTPvATQLSVDYlptrdfaRRPLQWLDLIS---RNRGTIS--YSPPFGYELCARRVNSKDLAELdlscwRVA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 269 gneGVAGD------LERFARRFGcvvQDGF---------GSTEGGVAI------------------------ARTPDTPA 309
Cdd:PRK09192 305 ---GIGADmirpdvLHQFAEAFA---PAGFddkafmpsyGLAEATLAVsfsplgsgivveevdrdrleyqgkAVAPGAET 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 310 GSLG-------PLPA-GIEIVDPDtGRPCPAGVVGElVNTAGPGRFEGYYNDEAAEAERMAGGIYHSGDLAYRDDaGYAY 381
Cdd:PRK09192 379 RRVRtfvncgkALPGhEIEIRNEA-GMPLPERVVGH-ICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLLD-GYLY 455
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2321332536 382 FAGRLGDWMRVDGENLGTAPIERVLLRYPD--TAEVAVYAVPDP 423
Cdd:PRK09192 456 ITGRAKDLIIINGRNIWPQDIEWIAEQEPElrSGDAAAFSIAQE 499
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
402-478 |
2.23e-09 |
|
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: 53.70 E-value: 2.23e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 402 IERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEQpdLGPKQWPSYVRISAGLPGTVTFK 478
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREE--LGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
146-445 |
4.00e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 58.95 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKV--------AIAGVTMTQRFglgpddvcYVSMPLFHSNAVLVGWAVAAACQGSI 217
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLlanveqikTIADFTPNDRF--------MSALPLFHSFGLTVGLFTPLLTGAEV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 218 ALRRK-------------------FSASGFIADVRRYGATYANYvgkPLSYVLATPEQPDDSenpLRAVYGNegvagdle 278
Cdd:PRK08043 436 FLYPSplhyrivpelvydrnctvlFGTSTFLGNYARFANPYDFA---RLRYVVAGAEKLQES---TKQLWQD-------- 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 279 rfarRFGCVVQDGFGSTEGG--VAIARTPDTPAGSLGPLPAGIEivdpdtGR--PCPAGVVGELVNTAGPGRFEGYYNDE 354
Cdd:PRK08043 502 ----KFGLRILEGYGVTECApvVSINVPMAAKPGTVGRILPGMD------ARllSVPGIEQGGRLQLKGPNIMNGYLRVE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 355 --------AAEAER--MAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPV 424
Cdd:PRK08043 572 kpgvlevpTAENARgeMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDAS 651
|
330 340
....*....|....*....|.
gi 2321332536 425 VGDrvmaALVLapgtrFDTDK 445
Cdd:PRK08043 652 KGE----ALVL-----FTTDS 663
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-424 |
5.74e-09 |
|
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: 58.24 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 152 LIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVCYVSMPLFHSNAVLVGWAVAAAcqgSIALRRKFSAS--GFI 229
Cdd:cd05910 90 ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSVIP---DMDPTRPARADpqKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 230 ADVRRYGATyaNYVGKP--LSYVLATPEQPDDSENPLRAV--YGNEGVAGDLERFARrfgcVVQDG------FGSTE--- 296
Cdd:cd05910 167 GAIRQYGVS--IVFGSPalLERVARYCAQHGITLPSLRRVlsAGAPVPIALAARLRK----MLSDEaeiltpYGATEalp 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 297 -----GGVAIARTPDTPAGSLG-----PLP----AGIEIVDP-----DTGRPCPAGVVGELVNTaGPGRFEGYYNDEAAE 357
Cdd:cd05910 241 vssigSRELLATTTAATSGGAGtcvgrPIPgvrvRIIEIDDEpiaewDDTLELPRGEIGEITVT-GPTVTPTYVNRPVAT 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321332536 358 A----ERMAGGIYH-SGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPV 424
Cdd:cd05910 320 AlakiDDNSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG 391
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
56-439 |
8.57e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 57.87 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 56 VGVLLQNTPFFSAMLVAAGMSGIVpvgLNPVRRgaALLRD-----INHADCQLVLADSASAGPLADI-------EHVNVE 123
Cdd:PRK05620 67 VGSMMYNCAEHLEVLFAVACMGAV---FNPLNK--QLMNDqivhiINHAEDEVIVADPRLAEQLGEIlkecpcvRAVVFI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 124 STEWSDEVAAHSGTELTFQS-------------------ASPAdlfMLIFTSGTSGEPKAVKCSHSKVAIAGVTM--TQR 182
Cdd:PRK05620 142 GPSDADSAAAHMPEGIKVYSyealldgrstvydwpeldeTTAA---AICYSTGTTGAPKGVVYSHRSLYLQSLSLrtTDS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 183 FGLGPDDVCYVSMPLFHsnavLVGWAV--AAACQGSIALRRKFSASG-----FIADV--RRYGATYANYVGKPLSYVLAT 253
Cdd:PRK05620 219 LAVTHGESFLCCVPIYH----VLSWGVplAAFMSGTPLVFPGPDLSAptlakIIATAmpRVAHGVPTLWIQLMVHYLKNP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 254 PEQPDdsenpLRAVY-GNEGVAGDL-ERFARRFGCVVQDGFGSTEGGV--AIARTPDTPAG--------SLGPLPAGIEI 321
Cdd:PRK05620 295 PERMS-----LQEIYvGGSAVPPILiKAWEERYGVDVVHVWGMTETSPvgTVARPPSGVSGearwayrvSQGRFPASLEY 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 322 VDPDTGRPCPAG--------VVGELVNTA----------GPG-RFEGYYNDEAAEaERMAGGIYHSGDLAYRDDAGYAYF 382
Cdd:PRK05620 370 RIVNDGQVMESTdrnegeiqVRGNWVTASyyhspteeggGAAsTFRGEDVEDAND-RFTADGWLRTGDVGSVTRDGFLTI 448
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2321332536 383 AGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGT 439
Cdd:PRK05620 449 HDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGI 505
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
140-434 |
9.77e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 54.72 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 140 TFQSASPADLFMLIFTSGTSGEPKAVKCSHSKV--AIAGVTMTQRFGlgPDDVcYVS-MPLFH----SNAVLVGWAVAAA 212
Cdd:PLN02736 214 PFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLiaNVAGSSLSTKFY--PSDV-HISyLPLAHiyerVNQIVMLHYGVAV 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 213 --CQGSI--------ALRRKFSAS----------GFIADVRRYGAT-----YANYVGKPLSYVLATPEQPDDSE---NPL 264
Cdd:PLN02736 291 gfYQGDNlklmddlaALRPTIFCSvprlynriydGITNAVKESGGLkerlfNAAYNAKKQALENGKNPSPMWDRlvfNKI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 265 RA---------VYGNEGVAGDLERFARR-FGCVVQDGFGSTEGGVAIARTP--DTPAGSLG-PLPA-GIEIVD-PDTG-- 327
Cdd:PLN02736 371 KAklggrvrfmSSGASPLSPDVMEFLRIcFGGRVLEGYGMTETSCVISGMDegDNLSGHVGsPNPAcEVKLVDvPEMNyt 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 328 ---RPCPAGVVGelvnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLayrddaGYAYFAGRLGDWMR-------VDGEN 396
Cdd:PLN02736 451 sedQPYPRGEIC----VRGPIIFKGYYKDEVQTREVIdEDGWLHTGDI------GLWLPGGRLKIIDRkknifklAQGEY 520
|
330 340 350
....*....|....*....|....*....|....*...
gi 2321332536 397 LGTAPIERVLLRYPDTAEVAVYavpdpvvGDRVMAALV 434
Cdd:PLN02736 521 IAPEKIENVYAKCKFVAQCFVY-------GDSLNSSLV 551
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
144-418 |
2.33e-07 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 53.20 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 144 ASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDVcYVSM-PLfhsnavlvGW------AVAAACQGS 216
Cdd:cd17641 155 GKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDE-YVSVlPL--------PWigeqmySVGQALVCG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 217 IALRRKFSASGFIADVRRYGATYanYVGKP------LSYVL-----ATP-----------------------EQPDDSEN 262
Cdd:cd17641 226 FIVNFPEEPETMMEDLREIGPTF--VLLPPrvwegiAADVRarmmdATPfkrfmfelgmklglraldrgkrgRPVSLWLR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 263 ------------PLR----------AVYGNEGVAGDLERFARRFGCVVQDGFGSTE--GGVAIARTPDTPAGSLGPLPAG 318
Cdd:cd17641 304 laswladallfrPLRdrlgfsrlrsAATGGAALGPDTFRFFHAIGVPLKQLYGQTElaGAYTVHRDGDVDPDTVGVPFPG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 319 IEI-VDPdtgrpcpagvVGELVnTAGPGRFEGYYNDEAAEAE-RMAGGIYHSGDLAYRDDAGYAYFAGRLGDWMRV-DGE 395
Cdd:cd17641 384 TEVrIDE----------VGEIL-VRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGT 452
|
330 340
....*....|....*....|...
gi 2321332536 396 NLGTAPIERVLLRYPDTAEVAVY 418
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVL 475
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
327-486 |
1.06e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 50.81 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 327 GRPCPAG---VVGELVNTAGPGRFEGYYN--DEAAEAERmagGIYHSGDLAYRDDaGYAYFAGRLGDWMRVDGENLGTAP 401
Cdd:PRK07824 195 GVPLDGVrvrVEDGRIALGGPTLAKGYRNpvDPDPFAEP---GWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 402 IERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTRFDTDKFRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKVLK 481
Cdd:PRK07824 271 VEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVAR--TLDRTAAPRELHVVDELPRRGIGKVDR 348
|
....*
gi 2321332536 482 RQLAA 486
Cdd:PRK07824 349 RALVR 353
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
107-359 |
2.06e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.50 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 107 DSASAGPLADIEHVNVESTEWSDEVAAHSGTELTFqsASPADLFMLIFTSGTSGEPKAVKCSHSKV--AIAGVtMTQRFG 184
Cdd:PLN02387 212 GVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDL--PSPNDIAVIMYTSGSTGLPKGVMMTHGNIvaTVAGV-MTVVPK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 185 LGPDDVCYVSMPLFH------SNAVL-VGWAV----------------------AAACQGSI-------------ALRRK 222
Cdd:PLN02387 289 LGKNDVYLAYLPLAHilelaaESVMAaVGAAIgygspltltdtsnkikkgtkgdASALKPTLmtavpaildrvrdGVRKK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 223 FSASG------F-IADVRRYGATYANYVG-----KPLSYVLATpeqpddseNPLRAVYGNE------GVA---GDLERFA 281
Cdd:PLN02387 369 VDAKGglakklFdIAYKRRLAAIEGSWFGawgleKLLWDALVF--------KKIRAVLGGRirfmlsGGAplsGDTQRFI 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 282 RR-FGCVVQDGFGSTE--GGVAIARTPDTPAGSLG-PLPAG-IEIVDPDTG------RPCPAG--VVGelvntaGPGRFE 348
Cdd:PLN02387 441 NIcLGAPIGQGYGLTEtcAGATFSEWDDTSVGRVGpPLPCCyVKLVSWEEGgylisdKPMPRGeiVIG------GPSVTL 514
|
330
....*....|.
gi 2321332536 349 GYYNDEAAEAE 359
Cdd:PLN02387 515 GYFKNQEKTDE 525
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
82-462 |
1.23e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 47.56 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 82 GLNP---VRRGAALLRDINhADCQLVLADSASAGPLAdieHVNVESTEWSDEVAahsgteltFQSASPADLfmlIFTSGT 158
Cdd:PRK09029 82 PLNPqlpQPLLEELLPSLT-LDFALVLEGENTFSALT---SLHLQLVEGAHAVA--------WQPQRLATM---TLTSGS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 159 SGEPKAVkcSHSKVA----IAGVTMTQRFglGPDDVCYVSMPLFH--SNAVLVGWAVAAACqgsIALRRKfsaSGFIADV 232
Cdd:PRK09029 147 TGLPKAA--VHTAQAhlasAEGVLSLMPF--TAQDSWLLSLPLFHvsGQGIVWRWLYAGAT---LVVRDK---QPLEQAL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 233 RryGATYANYVGKPLSYVLATPEQPddseNPLRAV-YGNEGVAGDLERFARRFGCVVQDGFGSTEGGVAI-ARTPDTPAG 310
Cdd:PRK09029 217 A--GCTHASLVPTQLWRLLDNRSEP----LSLKAVlLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVcAKRADGLAG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 311 SLGPLPaGIEIVdpdtgrpcpagVVGELVNTAGPGRFEGYYNDeaaeaermaGGIYhsgDLAyrDDAGyaYFAGR-LGDW 389
Cdd:PRK09029 291 VGSPLP-GREVK-----------LVDGEIWLRGASLALGYWRQ---------GQLV---PLV--NDEG--WFATRdRGEW 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 390 M--------RVD------GENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPGTrfDTDKFRVFLAEQpd 455
Cdd:PRK09029 343 QngeltilgRLDnlffsgGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEA--AVVNLAEWLQDK-- 418
|
....*..
gi 2321332536 456 LGPKQWP 462
Cdd:PRK09029 419 LARFQQP 425
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
151-403 |
1.28e-05 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 47.74 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 151 MLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPDDV---CYVS-MPLFHSNA----VLVGWAVAA--------ACQ 214
Cdd:cd05933 154 TLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqeSVVSyLPLSHIAAqildIWLPIKVGGqvyfaqpdALK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 215 GSIA------------------------LRRKFSASGFIadvRRYGATYANYVG-------------KPLSY------VL 251
Cdd:cd05933 234 GTLVktlrevrptafmgvprvwekiqekMKAVGAKSGTL---KRKIASWAKGVGletnlklmggespSPLFYrlakklVF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 252 ATPEQPDDSENPLRAVYGNEGVAGDLERFARRFGCVVQDGFGSTE--GGVAIARTPDTPAGSLGPLPAGIE--IVDPDtg 327
Cdd:cd05933 311 KKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSEtsGPHTISNPQAYRLLSCGKALPGCKtkIHNPD-- 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2321332536 328 rpcpAGVVGELVnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGRLGDWMRV-DGENLGTAPIE 403
Cdd:cd05933 389 ----ADGIGEIC-FWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPVPIE 461
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
102-495 |
2.05e-05 |
|
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: 47.27 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 102 QLVLADSASAGPLADIEHvNVESTEWSDEVAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVkcSHSkvaiAGVTMTQ 181
Cdd:cd05943 205 AVVVVPYTVAAGQPDLSK-IAKALTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCI--VHG----AGGTLLQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 182 -------RFGLGPDD--------------------------VCYVSMPLFHSNAVLvgWAVAAACQGSIalrrkFSAS-G 227
Cdd:cd05943 278 hlkehilHCDLRPGDrlfyyttcgwmmwnwlvsglavgatiVLYDGSPFYPDTNAL--WDLADEEGITV-----FGTSaK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 228 FIADVRRYGATYANYV-----------GKPLSyvlatPEQPDdsenplravYGNEGVAGDLErfarrfgcvvqdgFGSTE 296
Cdd:cd05943 351 YLDALEKAGLKPAETHdlsslrtilstGSPLK-----PESFD---------YVYDHIKPDVL-------------LASIS 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 297 GGVAIAR-----TPDTP-------AGSLGplpAGIEIVDPDtGRPCPaGVVGELVNTAG-PGRFEGYYNDEAAEAERMA- 362
Cdd:cd05943 404 GGTDIIScfvggNPLLPvyrgeiqCRGLG---MAVEAFDEE-GKPVW-GEKGELVCTKPfPSMPVGFWNDPDGSRYRAAy 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 363 ----GGIYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVVGDRVMAALVLAPG 438
Cdd:cd05943 479 fakyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG 558
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 439 TRFD---TDKFRVFLAEqpDLGPKQWPSYVRISAGLPGTVTFKvlKRQLAAEGVDCGDPV 495
Cdd:cd05943 559 VELDdelRKRIRSTIRS--ALSPRHVPAKIIAVPDIPRTLSGK--KVEVAVKKIIAGRPV 614
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
73-385 |
2.51e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 46.89 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 73 AGMSGIVPVGLNpVRRGAALLRDINHADCQLVLADSASAGplADIEHVNVESteWSDEVAAHSGTELTFQSASPA---DL 149
Cdd:PTZ00216 192 TECKAIVCNGKN-VPNLLRLMKSGGMPNTTIIYLDSLPAS--VDTEGCRLVA--WTDVVAKGHSAGSHHPLNIPEnndDL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 150 FMLIFTSGTSGEPKAVKCSHSKVAiAGV-TMTQRFG--LGP--DDVCYVS-MPLFH-----------SNAVLVGW----- 207
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHGSLT-AGIlALEDRLNdlIGPpeEDETYCSyLPLAHimefgvtniflARGALIGFgsprt 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 208 ---AVAAACqGSIALRRKFsasgFIADVRRYGATYANYVGKPLSYVLATPEQPDDS--ENPLRAV-------YGNEGVAG 275
Cdd:PTZ00216 346 ltdTFARPH-GDLTEFRPV----FLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHayQSRLRALkegkdtpYWNEKVFS 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 276 DLER-FARR----------------------FGCVVQdGFGSTE----GGvaIARTPDTPAGSLGPLPAGIEI--VDPD- 325
Cdd:PTZ00216 421 APRAvLGGRvramlsgggplsaatqefvnvvFGMVIQ-GWGLTEtvccGG--IQRTGDLEPNAVGQLLKGVEMklLDTEe 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2321332536 326 ---TGRPCPAGvvgELVnTAGPGRFEGYYNDEAAEAERM-AGGIYHSGDLAYRDDAGYAYFAGR 385
Cdd:PTZ00216 498 ykhTDTPEPRG---EIL-LRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGR 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
331-461 |
4.19e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 331 PAGVVGELVnTAGPGRFEGYYNDE------------AAEAERMaggiYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLG 398
Cdd:PRK05691 4062 PLGAVGELC-VAGTGVGRGYVGDPlrtalafvphpfGAPGERL----YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIE 4136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2321332536 399 TAPIERVLLRYPDTAEVAVyAVPDPVVGDRVMAALV-----LAPGTRFDTDKFRVfLAEQPD-LGPKQW 461
Cdd:PRK05691 4137 LGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVphqtvLAQGALLERIKQRL-RAELPDyMVPLHW 4203
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
277-386 |
2.31e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 43.73 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 277 LERF--ARRFgcvvqDGFGSTEGGVA---IARTPDTPAgSLGPLPAG-------IEIVDpDTGRPCPAGVVGELVnTAGP 344
Cdd:PRK04813 281 LERFpsATIY-----NTYGPTEATVAvtsIEITDEMLD-QYKRLPIGyakpdspLLIID-EEGTKLPDGEQGEIV-ISGP 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2321332536 345 GRFEGYYNDEA--AEAERMAGGI--YHSGDLAYRDDaGYAYFAGRL 386
Cdd:PRK04813 353 SVSKGYLNNPEktAEAFFTFDGQpaYHTGDAGYLED-GLLFYQGRI 397
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
277-422 |
2.89e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.39 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 277 LERFARRFG------CVVQDGFGSTEGGVAIA-RTPDTP------------AGSLGPLPAG---------------IEIV 322
Cdd:PRK05850 305 LKRFADRFApfnlreTAIRPSYGLAEATVYVAtREPGQPpesvrfdyeklsAGHAKRCETGggtplvsygsprsptVRIV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 323 DPDTGRPCPAGVVGEL----VNTAgpgrfEGYYNDEAAEAERMAGGIYH------------SGDLAYRDDaGYAYFAGRL 386
Cdd:PRK05850 385 DPDTCIECPAGTVGEIwvhgDNVA-----AGYWQKPEETERTFGATLVDpspgtpegpwlrTGDLGFISE-GELFIVGRI 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2321332536 387 GDWMRVDGENlgtapiervllRYPDTAE----------VAVYAVPD 422
Cdd:PRK05850 459 KDLLIVDGRN-----------HYPDDIEatiqeitggrVAAISVPD 493
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
131-420 |
4.53e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.83 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 131 VAAHSGTELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGLGPD-DVCYVSMPLFHSNAvlVGWAV 209
Cdd:PRK05851 136 TAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMG--LAFLL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 210 AAACQGS---IALRRKFSASGF--IADVRRYGATYA-------NYVGKPLSYVlatpeqPDDSENPLR-AVYGNEGVAGD 276
Cdd:PRK05851 214 TAALAGAplwLAPTTAFSASPFrwLSWLSDSRATLTaapnfayNLIGKYARRV------SDVDLGALRvALNGGEPVDCD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 277 -LERFAR---RFG---CVVQDGFGSTEGGVAIA--------RTPD--TPAGS-------LGPLPAGIE--IVDPDTGRPC 330
Cdd:PRK05851 288 gFERFATamaPFGfdaGAAAPSYGLAESTCAVTvpvpgiglRVDEvtTDDGSgarrhavLGNPIPGMEvrISPGDGAAGV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 331 PAGVVGElVNTAGPGRFEGYYNDEAAEaermAGGIYHSGDLAYRDDAGYAyFAGRLGDWMRVDGENLGTAPIERVLLRYP 410
Cdd:PRK05851 368 AGREIGE-IEIRGASMMSGYLGQAPID----PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
330
....*....|
gi 2321332536 411 DTAEVAVYAV 420
Cdd:PRK05851 442 GVREGAVVAV 451
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
319-413 |
9.48e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 41.46 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 319 IEIVDPDTGRPCPAGVVGELVNT-----AGPGRFegyyndeaaeaermaggiYHSGDLA--YRDDAGYAYFAGRLG---- 387
Cdd:cd05913 259 PEIIDPETGEPVPPGEVGELVFTtltkeAMPLIR------------------YRTRDITrlLPGPCPCGRTHRRIDritg 320
|
90 100
....*....|....*....|....*....
gi 2321332536 388 --DWM-RVDGENLGTAPIERVLLRYPDTA 413
Cdd:cd05913 321 rsDDMlIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
369-487 |
1.07e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 41.60 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 369 GDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTA-EVAVYAVPDPVVG-DRVMAALVL--APGTRFDTD 444
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAADESVlETAAIGVPPPGGGpEQLVIAAVLkdPPGSNPDLN 673
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2321332536 445 KFR-VFLAE-QPDLGPKQWPSYVRISAGLPGTVTFKVLKRQLAAE 487
Cdd:PLN03052 674 ELKkIFNSAiQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
129-423 |
1.78e-03 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 40.88 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 129 DEVAAHSGT---ELTFQSASPADLFMLIFTSGTSGEPKAVKCSHSKVAIAGVTMTQRFGL--GPDDVCYVSMPLFHS--- 200
Cdd:cd05921 144 AELAATPPTaavDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFfgEEPPVLVDWLPWNHTfgg 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 201 ----NAVLVGwavaaacQGSIALRR-KFSASGF---IADVRRYGATYANYVgkPLSYVLATPEQPDDS-------ENPLR 265
Cdd:cd05921 224 nhnfNLVLYN-------GGTLYIDDgKPMPGGFeetLRNLREISPTVYFNV--PAGWEMLVAALEKDEalrrrffKRLKL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 266 AVYGNEGVAGD----LERFARR---FGCVVQDGFGSTEGGVAIART--PDTPAGSLG-PLPaGIEIvdpdtgRPCPAGVV 335
Cdd:cd05921 295 MFYAGAGLSQDvwdrLQALAVAtvgERIPMMAGLGATETAPTATFThwPTERSGLIGlPAP-GTEL------KLVPSGGK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 336 GElVNTAGPGRFEGYYndEAAEAERMA---GGIYHSGD---LAYRDD--AGYaYFAGRL--------GDW-----MRVDG 394
Cdd:cd05921 368 YE-VRVKGPNVTPGYW--RQPELTAQAfdeEGFYCLGDaakLADPDDpaKGL-VFDGRVaedfklasGTWvsvgpLRARA 443
|
330 340
....*....|....*....|....*....
gi 2321332536 395 ENLGTAPIERVLLRYPDTAEVAVYAVPDP 423
Cdd:cd05921 444 VAACAPLVHDAVVAGEDRAEVGALVFPDL 472
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
146-371 |
1.84e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 40.95 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 146 PADLFMLIFTSGTSGEPKAVKCSHSKVA--IAGVTM-TQRF--GLGPDDVCYVSMPL------------FHSNAVlVGW- 207
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAVAtfVRGVDLfMEQFedKMTHDDVYLSFLPLahildrmieeyfFRKGAS-VGYy 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 208 -------------------------------AVAAACQGSIALRRKFSASGFIADVRRYGATYANYVGKPLSYVLATPEQ 256
Cdd:PLN02430 298 hgdlnalrddlmelkptllagvprvferiheGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLAFRKV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 257 PDDSENPLR-AVYGNEGVAGDLERFARRFGC--VVQdGFGSTE--GGVAIArTPDTPA--GSLGPLPAGIEI-------- 321
Cdd:PLN02430 378 KAKLGGRLRlLISGGAPLSTEIEEFLRVTSCafVVQ-GYGLTEtlGPTTLG-FPDEMCmlGTVGAPAVYNELrleevpem 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2321332536 322 -VDPDTGRPCpagvvGELVnTAGPGRFEGYYNDEAAEAERMAGGIYHSGDL 371
Cdd:PLN02430 456 gYDPLGEPPR-----GEIC-VRGKCLFSGYYKNPELTEEVMKDGWFHTGDI 500
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
346-435 |
3.07e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 40.11 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321332536 346 RFEGYYNdeaaeaermaggiyhSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLLRYPDTAEVAVYAVPDPVV 425
Cdd:PTZ00237 489 KFPGYYN---------------SGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDC 553
|
90
....*....|
gi 2321332536 426 GDRVMAALVL 435
Cdd:PTZ00237 554 YNVPIGLLVL 563
|
|
| |
