|
Name |
Accession |
Description |
Interval |
E-value |
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
26-489 |
0e+00 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 678.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 26 TYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCTLP 102
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQgirSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 103 LELRGFQIVSLDDIEFAGRdittnglldntmgiqYDTSnetvvpkespsniLNTSFNLDDIASIMFTSGTTGPQKAVPQT 182
Cdd:TIGR01923 81 LEEKDFQADSLDRIEAAGR---------------YETS-------------LSASFNMDQIATLMFTSGTTGKPKAVPHT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 183 FRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNaeQILTMIKNERITHISLVPQTLNW 262
Cdd:TIGR01923 133 FRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 263 LMQQGLHePYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPEMLHARPDtVGMPSANVDVKIKNPN 342
Cdd:TIGR01923 211 LLDEGGH-NENLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEMLHARPD-VGRPLAGREIKIKVDN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 343 KEGHGELMIKGANVMNGYLYPTDLTGTFE-NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI 421
Cdd:TIGR01923 289 KEGHGEIMVKGANLMKGYLYQGELTPAFEqQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446270502 422 SDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:TIGR01923 369 QEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
24-491 |
0e+00 |
|
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: 645.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 24 SYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLifct 100
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALgvrKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 101 lplelrgfqivslddiefagrdittnglldntmgiqydtsnetvvpkespsnilntsfnlDDIASIMFTSGTTGPQKAVP 180
Cdd:cd05912 77 ------------------------------------------------------------DDIATIMYTSGTTGKPKGVQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 181 QTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTL 260
Cdd:cd05912 97 QTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTML 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 261 NWLMQQGLH-EPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPEMLHARPDTVGMPSANVDVKIK 339
Cdd:cd05912 177 QRLLEILGEgYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 340 NPN--KEGHGELMIKGANVMNGYLYPTDLTGT-FENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAK 416
Cdd:cd05912 257 DDGqpPYEVGEILLKGPNVTKGYLNRPDATEEsFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446270502 417 QFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05912 337 SHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-489 |
3.11e-151 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 440.17 E-value: 3.11e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 1 MDFWLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMIN 77
Cdd:PRK03640 4 MPNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALgvkKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 78 TRLTPNEMTNQMKSIDVQLIFCtlplelrgfqivsldDIEFAGRDITtnglldntmGIQYDTSNETVVPKESPsnILNTS 157
Cdd:PRK03640 84 TRLSREELLWQLDDAEVKCLIT---------------DDDFEAKLIP---------GISVKFAELMNGPKEEA--EIQEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 158 FNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK03640 138 FDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQgLHE---PYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLT 314
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQRLLER-LGEgtyPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 ATPEMLHARPDTVGMPSANVDVKIKNPNKEG----HGELMIKGANVMNGYLY-PTDLTGTFENGYFNTGDIAEIDHEGYV 389
Cdd:PRK03640 297 LSPEDALTKLGSAGKPLFPCELKIEKDGVVVppfeEGEIVVKGPNVTKGYLNrEDATRETFQDGWFKTGDIGYLDEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 390 MIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKH 469
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|
gi 446270502 470 FEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHEL 476
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-489 |
1.30e-129 |
|
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: 383.78 E-value: 1.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 4 WLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRL 80
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALgvgPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 81 TPNEMTNQMKSIDVQLIFCtlplelrgfqivslddiefagrdittnglldntmgiqydtsnetvvpkespsnilntsfnl 160
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 ddiASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNAE 239
Cdd:COG0318 103 ---ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPY---NLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTA 315
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYdlsSLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 316 TPEMLHARPDTVGMPSANVDVKIKNPN----KEGH-GELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDHEGYV 389
Cdd:COG0318 260 PEDPGERRPGSVGRPLPGVEVRIVDEDgrelPPGEvGEIVVRGPNVMKGYWNDPEATAeAFRDGWLRTGDLGRLDEDGYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 390 MIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVP 467
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVP 419
|
490 500
....*....|....*....|..
gi 446270502 468 KHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRAL 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
162-485 |
4.38e-122 |
|
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: 360.45 E-value: 4.38e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 LTMIKNERITHISLVPQTLNWLMQQGLHEPYN---LQKILLGGAKLSATMIETALQY-NLPIYNSFGMTETCSQFLTATP 317
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDlssLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 318 EMLHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLT-GTFENGYFNTGDIAEIDHEGYVMI 391
Cdd:cd04433 161 DDDARKPGSVGRPVPGVEVRIVDPDGGelppgEIGELVVRGPSVMKGYWNNPEATaAVDEDGWYRTGDLGRLDEDGYLYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 392 YDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKH 469
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVlrPGADLDAEELRAHVRERLAPYKVPRR 320
|
330
....*....|....*.
gi 446270502 470 FEKVDTLPYTSTGKLQ 485
Cdd:cd04433 321 VVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
5-486 |
2.27e-95 |
|
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: 295.29 E-value: 2.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALgvaKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 82 PNEMTNQmksidvqlifctlplelrgfqivsLDDiefagrdittnglldntmgiqydtSNETVVpkespsnilntsfnLD 161
Cdd:cd17631 81 PPEVAYI------------------------LAD------------------------SGAKVL--------------FD 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFNAEQ 240
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLlRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 241 ILTMIKNERITHISLVPQTLNWLMQQGLHEPYN---LQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATP 317
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHPRFATTDlssLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 318 EMLHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYL-YPTDLTGTFENGYFNTGDIAEIDHEGYVMI 391
Cdd:cd17631 259 EDHRRKLGSAGRPVFFVEVRIVDPDGRevppgEVGEIVVRGPHVMAGYWnRPEATAAAFRDGWFHTGDLGRLDEDGYLYI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 392 YDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKH 469
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVprPGAELDEDELIAHCRERLARYKIPKS 418
|
490
....*....|....*..
gi 446270502 470 FEKVDTLPYTSTGKLQR 486
Cdd:cd17631 419 VEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
5-402 |
1.21e-91 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 285.36 E-value: 1.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIAI-TDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRL 80
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALgvgKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 81 TPNEMTNQMKSIDVQLIFCTlplelRGFQIVSLDDIEFAGRDITTNGLLDNTMGIQYDTSNETVVPKESPsNILNTSFNL 160
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITD-----DALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP-PPPPPPPDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK----ESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDK 235
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 FNA---EQILTMIKNERITHISLVPQTLNWLMQQGLHEPYN---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTET 308
Cdd:pfam00501 235 FPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALlssLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 CSQFLTATPEMLH-ARPDTVGMPSANVDVKIKNPNKEG------HGELMIKGANVMNGYLYPTDLT-GTF-ENGYFNTGD 379
Cdd:pfam00501 315 TGVVTTPLPLDEDlRSLGSVGRPLPGTEVKIVDDETGEpvppgePGELCVRGPGVMKGYLNDPELTaEAFdEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 446270502 380 IAEIDHEGYVMIYDRRKDLIISG 402
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
5-489 |
8.96e-89 |
|
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: 279.45 E-value: 8.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKA--YQQS-RVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNlgVQPGdRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 82 PNEMTNQMKSIDVQLIFCTLPLElrgfqivslDDIEFAgrdittnglldntmgiqydtsnETVVPKESPSnilntsfnLD 161
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFT---------DLLAAG----------------------APLGERVALT--------PE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDR--DTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNA 238
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLegDDVVLAALPLFHVFGLTVaLLLPLALGATIVLIPRFRP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKLSATMIETALQ-YNLPIYNSFGMTEtCSQFLT 314
Cdd:cd05936 206 IGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLcisGGAPLPVEVAERFEElTGVPIVEGYGLTE-TSPVVA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 ATPEMLHARPDTVGMPSANVDVKIKNPNKE----G-HGELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDHEGY 388
Cdd:cd05936 285 VNPLDGPRKPGSIGIPLPGTEVKIVDDDGEelppGeVGELWVRGPQVMKGYWNRPEETAeAFVDGWLRTGDIGYMDEDGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 389 VMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKV 466
Cdd:cd05936 365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVlkEGASLTEEEIIAFCREQLAGYKV 444
|
490 500
....*....|....*....|...
gi 446270502 467 PKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05936 445 PRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
5-489 |
4.61e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 266.28 E-value: 4.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIIlihaCWLAnieIAMI----- 76
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALgvkKGDRVAVFDWNSHEYLE----AYFA---VPKIgavlh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 77 --NTRLTPNEMTNQMKSIDVQLIFC---TLPL------ELRGFQIVSLDDIEFAGRDITTNGLLDNTMGIQYDTsNETVV 145
Cdd:PRK06187 85 piNIRLKPEEIAYILNDAEDRVVLVdseFVPLlaailpQLPTVRTVIVEGDGPAAPLAPEVGEYEELLAAASDT-FDFPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 146 PKEspsnilntsfnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVI 225
Cdd:PRK06187 164 IDE------------NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 226 EGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPY---NLQKILLGGAKLSATMIETALQ-YNLPIYN 301
Cdd:PRK06187 232 AGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVdfsSLRLVIYGGAALPPALLREFKEkFGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 302 SFGMTETCS--QFLTATPEMLH--ARPDTVGMPSANVDVKIKN------PNKEGH-GELMIKGANVMNGYL-YPTDLTGT 369
Cdd:PRK06187 312 GYGMTETSPvvSVLPPEDQLPGqwTKRRSAGRPLPGVEARIVDddgdelPPDGGEvGEIIVRGPWLMQGYWnRPEATAET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 370 FENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE--SD 447
Cdd:PRK06187 392 IDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKpgAT 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446270502 448 ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06187 472 LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
162-486 |
3.53e-81 |
|
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: 254.95 E-value: 3.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 ltMIKNERITHISLVPQTLNWLMQ--QGLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQfLTATPEM 319
Cdd:cd17630 81 --DLAPPGVTHVSLVPTQLQRLLDsgQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQ-VATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 320 LHARPDtVGMPSANVDVKIKNPnkeghGELMIKGANVMNGYLYPTDLTGTFENGYFNTGDIAEIDHEGYVMIYDRRKDLI 399
Cdd:cd17630 158 GFGRGG-VGVLLPGRELRIVED-----GEIWVGGASLAMGYLRGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 400 ISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYT 479
Cdd:cd17630 232 ISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRT 311
|
....*..
gi 446270502 480 STGKLQR 486
Cdd:cd17630 312 GGGKVDR 318
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
17-485 |
1.79e-78 |
|
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: 253.29 E-value: 1.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 17 AITDGQE--SYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKS 91
Cdd:cd05911 1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLglkKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 92 IDVQLIFCTLPL----------ELRGFQIVSLDDIEFAGRDITTngLLDNTMGIQYdtSNETVVPKESPsnilntsfnlD 161
Cdd:cd05911 81 SKPKVIFTDPDGlekvkeaakeLGPKDKIIVLDDKPDGVLSIED--LLSPTLGEED--EDLPPPLKDGK----------D 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLG--FDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAE 239
Cdd:cd05911 147 DTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPY---NLQKILLGGAKLSATMIET--ALQYNLPIYNSFGMTETCSQfLT 314
Cdd:cd05911 227 LFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYdlsSLRVILSGGAPLSKELQELlaKRFPNATIKQGYGMTETGGI-LT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 ATPEMLHaRPDTVGMPSANVDVKIKNPNKEGH------GELMIKGANVMNGYLY-PTDLTGTF-ENGYFNTGDIAEIDHE 386
Cdd:cd05911 306 VNPDGDD-KPGSVGRLLPNVEAKIVDDDGKDSlgpnepGEICVRGPQVMKGYYNnPEATKETFdEDGWLHTGDIGYFDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 387 GYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKY 464
Cdd:cd05911 385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKpgEKLTEKEVKDYVAKKVASY 464
|
490 500
....*....|....*....|....*
gi 446270502 465 kvpKHFEK----VDTLPYTSTGKLQ 485
Cdd:cd05911 465 ---KQLRGgvvfVDEIPKSASGKIL 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
5-489 |
2.80e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 248.28 E-value: 2.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALgigKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 82 PNEMTNQMKSIDVQLIFCtlplelrgfqivsLDDieFAGRDITTNG---LLDNTMGIQYDTSNETVVPKESPSNILNT-- 156
Cdd:PRK07656 91 ADEAAYILARGDAKALFV-------------LGL--FLGVDYSATTrlpALEHVVICETEEDDPHTEKMKTFTDFLAAgd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 157 ------SFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFT 229
Cdd:PRK07656 156 paerapEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAgVNAPLMRGAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 230 VRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKLSATMIEtALQYNLPIY---NSF 303
Cdd:PRK07656 236 ILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLavtGAASMPVALLE-RFESELGVDivlTGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 304 GMTEtCSQFLTATPemLH----ARPDTVGMPSANVDVKIKNPNKEGH-----GELMIKGANVMNGYL-YPTDLTGTF-EN 372
Cdd:PRK07656 315 GLSE-ASGVTTFNR--LDddrkTVAGTIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYdDPEATAAAIdAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 373 GYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISK 450
Cdd:PRK07656 392 GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVlkPGAELTE 471
|
490 500 510
....*....|....*....|....*....|....*....
gi 446270502 451 AQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07656 472 EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
16-489 |
6.73e-76 |
|
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: 246.84 E-value: 6.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 16 IAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSII-LIHACWLANIeIAMINTRLTPNEMTNQMKS 91
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAALgikKGDRVAIALPNGLEFVVaFLAAARAGAV-VAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 92 IDVQLIFctLPLELRGFQIVSLDDIEFAGRDITtnglLDNTMGIQYDTSNETVVPKESPSNILNTSFNL-DDIASIMFTS 170
Cdd:cd05926 85 LGSKLVL--TPKGELGPASRAASKLGLAILELA----LDVGVLIRAPSAESLSNLLADKKNAKSEGVPLpDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 171 GTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFNAEQILTMIKNER 249
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLvASLLSTLAAGGSVVLPPRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 250 ITHISLVPQTLNWLMQQGLHEPYN----LQKILLGGAKLSATmIETALQ--YNLPIYNSFGMTETCSQfLTATP-EMLHA 322
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPESpppkLRFIRSCSASLPPA-VLEALEatFGAPVLEAYGMTEAAHQ-MTSNPlPPGPR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 323 RPDTVGMPSaNVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLT--GTFENGYFNTGDIAEIDHEGYVMIYDRR 395
Cdd:cd05926 317 KPGSVGKPV-GVEVRILDEDGEilppgVVGEICLRGPNVTRGYLNNPEANaeAAFKDGWFRTGDLGYLDADGYLFLTGRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 396 KDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKV 473
Cdd:cd05926 396 KELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGasVTEEELRAFCRKHLAAFKVPKKVYFV 475
|
490
....*....|....*.
gi 446270502 474 DTLPYTSTGKLQRNKL 489
Cdd:cd05926 476 DELPKTATGKIQRRKV 491
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
3-491 |
4.96e-75 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 244.77 E-value: 4.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 3 FWLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAK----RLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINT 78
Cdd:PRK06839 6 YWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAyliyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 79 RLTPNEMTNQMKSIDVQLIFCtlplelrgfqivsldDIEFAGrdittnglldNTMGIQYDTSNETVVPKESPSNILNTSF 158
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFV---------------EKTFQN----------MALSMQKVSYVQRVISITSLKEIEDRKI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 ------NLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVL-LRAVIEGFTVR 231
Cdd:PRK06839 141 dnfvekNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 232 IVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKLSATMIETALQYNLPIYNSFGMTET 308
Cdd:PRK06839 221 VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWfynGGAPCPEELMREFIDRGFLFGQGFGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 CSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAE 382
Cdd:PRK06839 301 SPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNkvevgEVGELLIRGPNVMKEYWNRPDATEeTIQDGWLCTGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQH 460
Cdd:PRK06839 381 VDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHCRLF 460
|
490 500 510
....*....|....*....|....*....|.
gi 446270502 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK06839 461 LAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
9-489 |
3.65e-62 |
|
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: 210.94 E-value: 3.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 9 AQQNGHHIAITDGQ--ESYTYQNLYceasLLAKRLKAYQQSRVGLYID-------NSIQSIILIHACWLANIEIAMINTR 79
Cdd:cd05904 15 ASAHPSRPALIDAAtgRALTYAELE----RRVRRLAAGLAKRGGRKGDvvlllspNSIEFPVAFLAVLSLGAVVTTANPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 80 LTPNEMTNQMKSIDVQLIFCTLPL--ELRGF--QIVSLDDIEFagrdittnGLLDNTMGIQYDTSNETVVPKESPsniln 155
Cdd:cd05904 91 STPAEIAKQVKDSGAKLAFTTAELaeKLASLalPVVLLDSAEF--------DSLSFSDLLFEADEAEPPVVVIKQ----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 156 tsfnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK--ESLGFDRDTNWLSVLPIYHISGLSVLLRAVIE-GFTVRI 232
Cdd:cd05904 158 -----DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVagEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRlGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 233 VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQK---ILLGGAKLSATMIETALQyNLP---IYNSFGMT 306
Cdd:cd05904 233 MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSlrqIMSGAAPLGKELIEAFRA-KFPnvdLGQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 307 E-TCSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKEGH------GELMIKGANVMNGYL---YPTDLTGTFEnGYFN 376
Cdd:cd05904 312 EsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlppnqtGELWIRGPSIMKGYLnnpEATAATIDKE-GWLH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLI 454
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkPGSSLTEDEIM 470
|
490 500 510
....*....|....*....|....*....|....*
gi 446270502 455 AYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05904 471 DFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
21-489 |
4.01e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 210.43 E-value: 4.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 21 GQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLI 97
Cdd:PRK09088 19 LGRRWTYAELDALVGRLAAVLRRRgcvDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 98 FCTLPLELRGFQIVSLDdiefagrdittnGLLDNTMGIQYDTSNEtvVPKESPSNILntsfnlddiasimFTSGTTGPQK 177
Cdd:PRK09088 99 LGDDAVAAGRTDVEDLA------------AFIASADALEPADTPS--IPPERVSLIL-------------FTSGTSGQPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 178 AVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFNAEQILTMIKNER--ITHIS 254
Cdd:PRK09088 152 GVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLaVGGSILVSNGFEPKRTLGRLGDPAlgITHYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 255 LVPQTLNWLMQQGLHEPYNLQK---ILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQF-LTATPEMLHARPDTVGMP 330
Cdd:PRK09088 232 CVPQMAQAFRAQPGFDAAALRHltaLFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFgMSVDCDVIRAKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 331 SANVDVKIKNPNKEG-----HGELMIKGANVMNGYLY-PTDLTGTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGG 403
Cdd:PRK09088 312 TPTVQTRVVDDQGNDcpagvPGELLLRGPNLSPGYWRrPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISGG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 404 ENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTST 481
Cdd:PRK09088 392 ENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVpaDGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTAS 471
|
....*...
gi 446270502 482 GKLQRNKL 489
Cdd:PRK09088 472 GKLQKARL 479
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
9-489 |
6.80e-59 |
|
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: 201.76 E-value: 6.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 9 AQQNGHHIAITDGQESYT----YQNLYCEASLLAKRLKaYQQSRVGLYIDNsiqsiilIHACWLANIEIAM-------IN 77
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTwrqtYDRCRRLASALAALGI-SRGDTVAVLAPN-------TPAMYELHFGVPMagavlnaLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 78 TRLTPNEMTNQMKSIDVQLIFCtlplelrgfqivsldDIEFAGRDITTNGlldntmgiqyDTSNETVVPKESpsnilnts 157
Cdd:cd12118 86 TRLDAEEIAFILRHSEAKVLFV---------------DREFEYEDLLAEG----------DPDFEWIPPADE-------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 158 fnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:cd12118 133 ---WDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLM------QQGLHEPYNlqkILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQ 311
Cdd:cd12118 210 AKAIYDLIEKHKVTHFCGAPTVLNMLAnappsdARPLPHRVH---VMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTAT--PE----------MLHARPDtVGMPSAN-VDVKIKNPNK------EGHGELMIKGANVMNGYLYPTDLTG-TFE 371
Cdd:cd12118 287 ATVCAwkPEwdelpteeraRLKARQG-VRYVGLEeVDVLDPETMKpvprdgKTIGEIVFRGNIVMKGYLKNPEATAeAFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 372 NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLyFVSESDISKA 451
Cdd:cd12118 366 GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FVELKEGAKV 444
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446270502 452 ---QLIAYLSQHLAKYKVPKHFEKVDtLPYTSTGKLQRNKL 489
Cdd:cd12118 445 teeEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
18-489 |
1.94e-56 |
|
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: 195.93 E-value: 1.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 18 ITDGQESYTYQNLYCEASLLA---KRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDV 94
Cdd:cd12119 19 HEGEVHRYTYAEVAERARRLAnalRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 95 QLIFCTLPLELRGFQIV-SLDDIE--FAGRDITTNGLLDNTMGIQYdtsnETVVPKESPsNILNTSFNLDDIASIMFTSG 171
Cdd:cd12119 99 RVVFVDRDFLPLLEAIApRLPTVEhvVVMTDDAAMPEPAGVGVLAY----EELLAAESP-EYDWPDFDENTAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 172 TTGPQKAVPQTFRN--HYASAIGCKESLGF-DRDTnWLSVLPIYHISGLSVLLRAVIEGftVRIV---DKFNAEQILTMI 245
Cdd:cd12119 174 TTGNPKGVVYSHRSlvLHAMAALLTDGLGLsESDV-VLPVVPMFHVNAWGLPYAAAMVG--AKLVlpgPYLDPASLAELI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 246 KNERITHISLVPQTLNWLMQQGLHEPYNLQ---KILLGGAKLSATMIETALQYNLPIYNSFGMTETC--SQFLTATPEML 320
Cdd:cd12119 251 EREGVTFAAGVPTVWQGLLDHLEANGRDLSslrRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSplGTVARPPSEHS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 321 HARPD-------TVGMPSANVDVKIKNPNK-------EGHGELMIKGANVMNGYLYPTD-LTGTFENGYFNTGDIAEIDH 385
Cdd:cd12119 331 NLSEDeqlalraKQGRPVPGVELRIVDDDGrelpwdgKAVGELQVRGPWVTKSYYKNDEeSEALTEDGWLRTGDVATIDE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAK 463
Cdd:cd12119 411 DGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVlkEGATVTAEELLEFLADKVAK 490
|
490 500
....*....|....*....|....*.
gi 446270502 464 YKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12119 491 WWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
161-489 |
1.76e-54 |
|
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: 188.74 E-value: 1.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFD-RDTNWLSVlPIYHISG-LSVLLRAVIEGFTVRIVDKFNA 238
Cdd:cd05903 93 DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGpGDVFLVAS-PMAHQTGfVYGFTLPLLLGAPVVLQDIWDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHI----SLVPQTLNWLMQQGLHEPyNLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFL 313
Cdd:cd05903 172 DKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLS-RLRTFVCGGATVPRSLARRAAElLGAKVCSAYGSTECPGAVT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 314 TATPEMLHARPDTVGMPSANVDVKI-----KNPNKEGHGELMIKGANVMNGYLYPTDLTGT-FENGYFNTGDIAEIDHEG 387
Cdd:cd05903 251 SITPAPEDRRLYTDGRPLPGVEIKVvddtgATLAPGVEGELLSRGPSVFLGYLDRPDLTADaAPEGWFRTGDLARLDEDG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSES--DISKAQLIAYLSQH-LAKY 464
Cdd:cd05903 331 YLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgaLLTFDELVAYLDRQgVAKQ 410
|
330 340
....*....|....*....|....*
gi 446270502 465 KVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05903 411 YWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
161-489 |
5.57e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 189.43 E-value: 5.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLlRAVIEGFTVRIVDKFNAEQ 240
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL-PTLLRGGTVIVLAKFDPAE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 241 ILTMIKNERITHISLVPQTLNWLMQQG-LHEP--YNLQKILLGGAKLSATMIETALQYNLPIY-NSFGMTEtCSQFLTAT 316
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTMIYALLDHPdLRTRdlSSLETVYYGASPMSPVRLAEAIERFGPIFaQYYGQTE-APMVITYL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 317 PEMLHARPD-----TVGMPSANVDVKIKNPN----KEGH-GELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDH 385
Cdd:PRK06188 326 RKRDHDPDDpkrltSCGRPTPGLRVALLDEDgrevAQGEvGEICVRGPLVMDGYWNRPEETAeAFRDGWLHTGDVAREDE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAK 463
Cdd:PRK06188 406 DGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlrPGAAVDAAELQAHVKERKGS 485
|
330 340
....*....|....*....|....*.
gi 446270502 464 YKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06188 486 VHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
14-489 |
2.90e-52 |
|
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: 182.87 E-value: 2.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 14 HHIAITDGQESYTYQNLYCEASLLAKRL----KAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMtnqm 89
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLlalgKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 90 ksidvqlifctlplelrgfqivslddiefagrdittnglldntmgiqydtsnETVVPKESPSNILntsfnldDIASIMFT 169
Cdd:cd05941 77 ----------------------------------------------------EYVITDSEPSLVL-------DPALILYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 170 SGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFNAEQILTMIKNE 248
Cdd:cd05941 98 SGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLvNALLCPLFAGASVEFLPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 249 RITHISLVPQTLNWLMQQGLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSF------------GMTETcsqfLTAT 316
Cdd:cd05941 178 SITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWeaitghtlleryGMTEI----GMAL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 317 PEMLHA--RPDTVGMPSANVDVKIKNPN------KEGHGELMIKGANVMNGYL-YPTDLTGTF-ENGYFNTGDIAEIDHE 386
Cdd:cd05941 254 SNPLDGerRPGTVGMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWnKPEATKEEFtDDGWFKTGDLGVVDED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 387 GYVMIYDRRKDLII-SGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD---ISKAQLIAYLSQHLA 462
Cdd:cd05941 334 GYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaaLSLEELKEWAKQRLA 413
|
490 500
....*....|....*....|....*..
gi 446270502 463 KYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
164-489 |
5.64e-52 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 182.50 E-value: 5.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 164 ASIMF-TSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRdTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDkfnaeqiL 242
Cdd:PRK07445 122 GWIMIpTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQ-VNSFCVLPLYHVSGLMQFMRSFLTGGKLVILP-------Y 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 243 TMIKNERITH-------ISLVPQTLNWLMQQGLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTA 315
Cdd:PRK07445 194 KRLKSGQELPpnpsdffLSLVPTQLQRLLQLRPQWLAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 316 TPEMLHARPDTVGMPSANVDVKIKNPNKeghGELMIKGANVMNGYlYPTdltgTFEN-GYFNTGDIAEIDHEGYVMIYDR 394
Cdd:PRK07445 274 KPDDFLAGNNSSGQVLPHAQITIPANQT---GNITIQAQSLALGY-YPQ----ILDSqGIFETDDLGYLDAQGYLHILGR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 395 RKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ-VPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKV 473
Cdd:PRK07445 346 NSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEvVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPV 425
|
330
....*....|....*.
gi 446270502 474 DTLPYTSTGKLQRNKL 489
Cdd:PRK07445 426 PQLPRNPQGKINRQQL 441
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
166-486 |
2.55e-51 |
|
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: 177.21 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTMI 245
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 246 KNERITHISLVPQTLNWLMQQGLHEpYNLQKILLGGAKLSATMIETALQY--NLPIYNSFGMTETcsQFLTATPEMLHAR 323
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE-SKIKSIFSSGQKLFESTKKKLKNIfpKANLIEFYGTSEL--SFITYNFNQESRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 324 PDTVGMPSANVDVKIKNPNKEGHGELMIKGANVMNGYLYPTDLTgtfENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGG 403
Cdd:cd17633 162 PNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSN---PDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 404 ENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESdISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:cd17633 239 INIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
...
gi 446270502 484 LQR 486
Cdd:cd17633 318 IAR 320
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
162-486 |
5.25e-51 |
|
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: 176.54 E-value: 5.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNAEQ 240
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 241 ILTMIKNERITHISLVPQtlnwLMQQGLHEPY-------NLQKILLGGAKLSATMIETaLQYNLPIYN---SFGMTETCS 310
Cdd:cd17638 81 ILEAIERERITVLPGPPT----LFQSLLDHPGrkkfdlsSLRAAVTGAATVPVELVRR-MRSELGFETvltAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 QFLTATPEMLHARPDTVGMPSANVDVKIKNPnkeghGELMIKGANVMNGYLYPTDLTGTF--ENGYFNTGDIAEIDHEGY 388
Cdd:cd17638 156 ATMCRPGDDAETVATTCGRACPGFEVRIADD-----GEVLVRGYNVMQGYLDDPEATAEAidADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 389 VMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQ--LIAYLSQHLAKYKV 466
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEedVIAWCRERLANYKV 310
|
330 340
....*....|....*....|
gi 446270502 467 PKHFEKVDTLPYTSTGKLQR 486
Cdd:cd17638 311 PRFVRFLDELPRNASGKVMK 330
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
9-484 |
9.87e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 180.51 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 9 AQQNGHHIAITDGQESYTYQNL--YCE---ASLLAKRLKAYQqsRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPN 83
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELdaAVNrvaAALLDLGLKKGD--RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 84 EMTNQMKSIDVQLIFC------TLPLELRGFQIVSLDDIEFAGRDITTNGLLDNTMGIQydtSNETVVPKESPSNilnts 157
Cdd:PRK08316 99 ELAYILDHSGARAFLVdpalapTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAE---AGSVAEPDVELAD----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 158 fnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKF 236
Cdd:PRK08316 171 ---DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVfLGPYLYVGATNVILDAP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 237 NAEQILTMIKNERIThiSL-VPQTLnW--LMQQGLHEPYN---LQKILLGGAKLSATMIETaLQYNLP---IYNSFGMTE 307
Cdd:PRK08316 248 DPELILRTIEAERIT--SFfAPPTV-WisLLRHPDFDTRDlssLRKGYYGASIMPVEVLKE-LRERLPglrFYNCYGQTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 308 TCSqflTAT---PEMLHARPDTVGMPSANVDVKI----KNPNKEGH-GELMIKGANVMNGYLYPTDLTG-TFENGYFNTG 378
Cdd:PRK08316 324 IAP---LATvlgPEEHLRRPGSAGRPVLNVETRVvdddGNDVAPGEvGEIVHRSPQLMLGYWDDPEKTAeAFRGGWFHSG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 379 DIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ------VPKlyfvSESDISKAQ 452
Cdd:PRK08316 401 DLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEavtavvVPK----AGATVTEDE 476
|
490 500 510
....*....|....*....|....*....|..
gi 446270502 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:PRK08316 477 LIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
48-489 |
4.49e-50 |
|
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: 176.90 E-value: 4.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 48 RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMtnqmksidvqlifctlplelrgfqivslddiEFagrdittng 127
Cdd:cd05935 28 RVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKEREL-------------------------------EY--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 128 lldntmgiqydtsnetvVPKESPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLS 207
Cdd:cd05935 68 -----------------ILNDSGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 208 VLPIYHISGL-SVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAK 283
Cdd:cd05935 131 CLPLFHVTGFvGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVltgGGAP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 284 LSATMIE-----TALQYNlpiyNSFGMTETCSQflTATPEMLHARPDTVGMPSANVDVKIKN--------PNKEGhgELM 350
Cdd:cd05935 211 MPPAVAEkllklTGLRFV----EGYGLTETMSQ--THTNPPLRPKLQCLGIP*FGVDARVIDietgrelpPNEVG--EIV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 351 IKGANVMNGYL---YPTDLTGTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAV 425
Cdd:cd05935 283 VRGPQIFKGYWnrpEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVC 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446270502 426 CVGHPDDTWGQVPKLYFV----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05935 363 VISVPDERVGEEVKAFIVlrpeYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-489 |
6.19e-50 |
|
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: 174.00 E-value: 6.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDK-FNA 238
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLgVLACLTHGATMVFPSPsFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVP----QTLNwLMQQGLHEPYNLQKILLGGAKLSATMIETALQ-YNLP-IYNSFGMTETcsqf 312
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPtmfiAELE-HPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEvMNMKdVTIAYGMTET---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 313 ltaTPEMLHARPD--------TVGMPSANVDVKIKNPnkEG--------HGELMIKGANVMNGYLYPTDLTGTFEN--GY 374
Cdd:cd05917 157 ---SPVSTQTRTDdsiekrvnTVGRIMPHTEAKIVDP--EGgivppvgvPGELCIRGYSVMKGYWNDPEKTAEAIDgdGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 375 FNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQ 452
Cdd:cd05917 232 LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkEGAELTEED 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 446270502 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05917 312 IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
7-489 |
8.22e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 177.28 E-value: 8.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 7 KQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRL--KAYQQSRVGLYIDNSIQSIILI----HACWLAnieiAMINTRL 80
Cdd:PRK07638 9 KHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLneKESKNKTIAILLENRIEFLQLFagaaMAGWTC----VPLDIKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 81 TPNEMTNQMKSIDVQLIFCTlplelrGFQIVSLDDIEfaGRDIttngLLDNTMGiqyDTSNETvvPKESP-SNILNTSFN 159
Cdd:PRK07638 85 KQDELKERLAISNADMIVTE------RYKLNDLPDEE--GRVI----EIDEWKR---MIEKYL--PTYAPiENVQNAPFY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 160 LDdiasimFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHisglSVLLRAVIE----GFTVRIVDK 235
Cdd:PRK07638 148 MG------FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVH----SLFLYGAIStlyvGQTVHLMRK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 FNAEQILTMIKNERITHISLVPQTLNWLMQQGlHEPYNLQKILLGGAKLSATMIEtALQYNLP---IYNSFGMTETcsQF 312
Cdd:PRK07638 218 FIPNQVLDKLETENISVMYTVPTMLESLYKEN-RVIENKMKIISSGAKWEAEAKE-KIKNIFPyakLYEFYGASEL--SF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 313 LTA-TPEMLHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLTGTF-ENGYFNTGDIAEIDH 385
Cdd:PRK07638 294 VTAlVDEESERRPNSVGRPFHNVQVRICNEAGEevqkgEIGTVYVKSPQFFMGYIIGGVLARELnADGWMTVRDVGYEDE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDisKAQLIAYLSQHLAKYK 465
Cdd:PRK07638 374 EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSAT--KQQLKSFCLQRLSSFK 451
|
490 500
....*....|....*....|....
gi 446270502 466 VPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07638 452 IPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
20-428 |
2.42e-49 |
|
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: 175.48 E-value: 2.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 20 DGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLAnieiamintrltpnemtnqmksidvql 96
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALgvePGDRVAILSRNRPEWTIADLAILAI--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 97 ifctlplelrGFQIVSLddiefagrdittnglldntmgiqYDTSNEtvvpkESPSNILNTS-----F--NLDDIASIMFT 169
Cdd:cd05907 54 ----------GAVPVPI-----------------------YPTSSA-----EQIAYILNDSeakalFveDPDDLATIIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 170 SGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHI----SGLSVLLRAvieGFTVRIVdkFNAEQILTMI 245
Cdd:cd05907 96 SGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVferrAGLYVPLLA---GARIYFA--SSAETLLDDL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 246 KNERITHISLVPQTL----NWLMQQGLHEpynLQKILL-------------GGAKLSATMIETALQYNLPIYNSFGMTET 308
Cdd:cd05907 171 SEVRPTVFLAVPRVWekvyAAIKVKAVPG---LKRKLFdlavggrlrfaasGGAPLPAELLHFFRALGIPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 CSQFLTATPEMLhaRPDTVGMPSANVDVKIKNpnkegHGELMIKGANVMNGYLYPTDLTG--TFENGYFNTGDIAEIDHE 386
Cdd:cd05907 248 SAVVTLNPPGDN--RIGTVGKPLPGVEVRIAD-----DGEILVRGPNVMLGYYKNPEATAeaLDADGWLHTGDLGEIDED 320
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446270502 387 GYVMIYDRRKDLII-SGGENIYPYQIETVAKQFPGISDAVCVG 428
Cdd:cd05907 321 GFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
128-486 |
2.72e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 177.88 E-value: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 128 LLDNTMGIQYDTSNEtvvPKESPsnilntsfnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK---ESLGfDRDTN 204
Cdd:PRK05605 199 LVDAAIGGDGSDVSH---PRPTP----------DDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKawvPGLG-DGPER 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 205 WLSVLPIYHISGLS-VLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPqTLnwlmqqglhepYnlQKILLGGAK 283
Cdd:PRK05605 265 VLAALPMFHAYGLTlCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVP-PL-----------Y--EKIAEAAEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 284 --LSATMIETALQ--YNLP--------------IYNSFGMTETcSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKEG 345
Cdd:PRK05605 331 rgVDLSGVRNAFSgaMALPvstvelwekltgglLVEGYGLTET-SPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 346 H-------GELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQ 417
Cdd:PRK05605 410 EtmpdgeeGELLVRGPQVFKGYWNRPEETAkSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE 489
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446270502 418 FPGISDAVCVGHPDDTWGQ--VPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK05605 490 HPGVEDAAVVGLPREDGSEevVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
162-489 |
5.75e-49 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 173.63 E-value: 5.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNAEQ 240
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVsVLAALSVGATLVLLPRFSASR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 241 ILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILLGGAKLSATMIETAL--QYNLPIYNSFGMTETCSQFLTATPE 318
Cdd:cd05934 162 FWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFeeRFGVRLLEGYGMTETIVGVIGPRDE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 319 mlHARPDTVGMPSANVDVKIKNPNkeGH-------GELMIKGAN---VMNGYLYPTDLTGT-FENGYFNTGDIAEIDHEG 387
Cdd:cd05934 242 --PRRPGSIGRPAPGYEVRIVDDD--GQelpagepGELVIRGLRgwgFFKGYYNMPEATAEaMRNGWFHTGDLGYRDADG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYK 465
Cdd:cd05934 318 FFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGetLDPEELFAFCEGQLAYFK 397
|
330 340
....*....|....*....|....
gi 446270502 466 VPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05934 398 VPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-489 |
8.74e-49 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 176.09 E-value: 8.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 2 DFWlYKQAQQNGHHIAITDGQ-ESYTYQNLYCEASLLAKRLKAyQQSRVGLYIdnSIQSIILIHAC--WLANIEIAMINT 78
Cdd:PRK06087 27 DYW-QQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLA-KGIEPGDRV--AFQLPGWCEFTiiYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 79 RLTPN----EMTNQMKSIDVQLIFC------------TLPL--ELRGFQ-IVSLDDIEFAGRDITTNGLLDNtmgiqydt 139
Cdd:PRK06087 103 PLLPSwreaELVWVLNKCQAKMFFAptlfkqtrpvdlILPLqnQLPQLQqIVGVDKLAPATSSLSLSQIIAD-------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 140 sNEtvvPKESPSNIlntsfNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISG-LS 218
Cdd:PRK06087 175 -YE---PLTTAITT-----HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 219 VLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHIS----LVPQTLNWLMQQGLHEPyNLQKILLGGAKLSATMIETALQ 294
Cdd:PRK06087 246 GVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPADLS-ALRFFLCGGTTIPKKVARECQQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 295 YNLPIYNSFGMTETCSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKE----GH-GELMIKGANVMNGYLYPTDLTGT 369
Cdd:PRK06087 325 RGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKtlppGCeGEEASRGPNVFMGYLDEPELTAR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 370 F--ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV---S 444
Cdd:PRK06087 405 AldEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlkaP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446270502 445 ESDISKAQLIAYLS-QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06087 485 HHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
4-489 |
3.91e-48 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 174.53 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 4 WLYKQAQQNGHHIAI-----TDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAM 75
Cdd:COG0365 14 CLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALgvkKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 76 INTRLTPNEMTNQMKSIDVQLIFCTLPLELRGFQIVSLDDIEFAGRDITTnglLDNTMGIQY---------DTSNETVVP 146
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS---LEHVIVVGRtgadvpmegDLDWDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 147 KESPS-NILNTSFnlDDIASIMFTSGTTGPQKAVPQTFRNHYASA-------IGCKESlgfDR-----DTNWlsvlpIYH 213
Cdd:COG0365 171 AASAEfEPEPTDA--DDPLFILYTSGTTGKPKGVVHTHGGYLVHAattakyvLDLKPG---DVfwctaDIGW-----ATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 214 IS---------GLSVLLravIEGftvrIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEP--YN---LQKILL 279
Cdd:COG0365 241 HSyivygpllnGATVVL---YEG----RPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLkkYDlssLRLLGS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 280 GGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTATPEMlHARPDTVGMPSANVDVKIKNPnkEGH-------GELMI 351
Cdd:COG0365 314 AGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIFISNLPGL-PVKPGSMGKPVPGYDVAVVDE--DGNpvppgeeGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 352 KGAN--VMNGYLYPTDLT-----GTFEnGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDA 424
Cdd:COG0365 391 KGPWpgMFRGYWNDPERYretyfGRFP-GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 425 VCVGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG0365 470 AVVGVPDEIRGQVVKAFVVlkpgvEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
4-467 |
7.10e-48 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 171.59 E-value: 7.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 4 WLYKQ-AQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKA---YQQSRVGLYIDNSIQSIIlihaCWLANIE----IAM 75
Cdd:PRK09029 7 WPWRHwAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQqgvVEGSGVALRGKNSPETLL----AYLALLQcgarVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 76 INTRLtPNEMTNQMK-SIDVQLIFCtlpleLRGFQIVSLDdiefagrdittnglldntmgiqydtsneTVVPKESPSNIL 154
Cdd:PRK09029 83 LNPQL-PQPLLEELLpSLTLDFALV-----LEGENTFSAL----------------------------TSLHLQLVEGAH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 155 NTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD 234
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVRD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 235 KFNAEQILTMiknerITHISLVPQTLNWLMQQgLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSqflT 314
Cdd:PRK09029 209 KQPLEQALAG-----CTHASLVPTQLWRLLDN-RSEPLSLKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMAS---T 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 ATPEMLHARPDtVGMPSANVDVKIKNpnkeghGELMIKGANVMNGYLY---PTDLTGtfENGYFNTGDIAEIDhEGYVMI 391
Cdd:PRK09029 280 VCAKRADGLAG-VGSPLPGREVKLVD------GEIWLRGASLALGYWRqgqLVPLVN--DEGWFATRDRGEWQ-NGELTI 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446270502 392 YDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVP 467
Cdd:PRK09029 350 LGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAEWLQDKLARFQQP 425
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
154-492 |
5.48e-47 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 171.14 E-value: 5.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 154 LNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIV 233
Cdd:PLN02860 165 LDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 234 DKFNAEQILTMIKNERITHISLVPQTLNWL-----MQQGLHEPYNLQKILLGGAKLSATMIETALQY--NLPIYNSFGMT 306
Cdd:PLN02860 245 PKFDAKAALQAIKQHNVTSMITVPAMMADLisltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfpNAKLFSAYGMT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 307 ETCSQ--FLT------ATPEMLHARPDT-------------VGMPSANVDVKIKNPNKEGHGELMIKGANVMNGY--LYP 363
Cdd:PLN02860 325 EACSSltFMTlhdptlESPKQTLQTVNQtksssvhqpqgvcVGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYwgQNS 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 364 TDLTGTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDD----------- 432
Cdd:PLN02860 405 ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSrltemvvacvr 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446270502 433 -----TWGQVPKLYFVSESDISKAQLIAYLS-QHLAKYKVPKHF-EKVDTLPYTSTGKLQRNKLYRG 492
Cdd:PLN02860 485 lrdgwIWSDNEKENAKKNLTLSSETLRHHCReKNLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
76-489 |
6.28e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 170.73 E-value: 6.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 76 INTRLTPNEMTNQMKSIDVQLIFCTLPL-----ELRgfQIVSLDDIEFAGRDITTNGLLDntmgiqYDTSNETVVPKESP 150
Cdd:PRK07786 97 VNFRLTPPEIAFLVSDCGAHVVVTEAALapvatAVR--DIVPLLSTVVVAGGSSDDSVLG------YEDLLAEAGPAHAP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 151 SNILNtsfnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDR--DTNWLSVlPIYHISGLSVLLRAVIEGF 228
Cdd:PRK07786 169 VDIPN-----DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADInsDVGFVGV-PLFHIAGIGSMLPGLLLGA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 229 TVRI--VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQ-KILLGGAKLSATMIETALQYNLP---IYNS 302
Cdd:PRK07786 243 PTVIypLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLAlRVLSWGAAPASDTLLRQMAATFPeaqILAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 303 FGMTE----TCsqfltatpeMLH-----ARPDTVGMPSANVDVKIKNPNKE----GH-GELMIKGANVMNGYLY-PTDLT 367
Cdd:PRK07786 323 FGQTEmspvTC---------MLLgedaiRKLGSVGKVIPTVAARVVDENMNdvpvGEvGEIVYRAPTLMSGYWNnPEATA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 GTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV---S 444
Cdd:PRK07786 394 EAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnD 473
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446270502 445 ESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07786 474 DAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
16-489 |
8.45e-47 |
|
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: 170.40 E-value: 8.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 16 IAITDG--QESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMK 90
Cdd:cd17642 34 IAFTDAhtGVNYSYAEYLEMSVRLAEALKKYglkQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 91 SIDVQLIFCTLplelRGFQIVSldDIEFAGRDITTNGLLDNTMGIQYDTSNETVVPKESPSNILNTSFNL------DDIA 164
Cdd:cd17642 114 ISKPTIVFCSK----KGLQKVL--NVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPpsfdrdEQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 165 SIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDR---DTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQiipDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 LTMIKNERITHISLVPQTLNWLMQQGLHEPY---NLQKILLGGAKLSATMIE-TALQYNLP-IYNSFGMTETCSQFLTaT 316
Cdd:cd17642 268 LRSLQDYKVQSALLVPTLFAFFAKSTLVDKYdlsNLHEIASGGAPLSKEVGEaVAKRFKLPgIRQGYGLTETTSAILI-T 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 317 PEMlHARPDTVG--MPSANVDV------KIKNPNKEghGELMIKGANVMNGYLYPTDLTGTF--ENGYFNTGDIAEIDHE 386
Cdd:cd17642 347 PEG-DDKPGAVGkvVPFFYAKVvdldtgKTLGPNER--GELCVKGPMIMKGYVNNPEATKALidKDGWLHSGDIAYYDED 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 387 GYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKY 464
Cdd:cd17642 424 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGktMTEKEVMDYVASQVSTA 503
|
490 500
....*....|....*....|....*.
gi 446270502 465 KVPKHFEK-VDTLPYTSTGKLQRNKL 489
Cdd:cd17642 504 KRLRGGVKfVDEVPKGLTGKIDRRKI 529
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
26-484 |
1.17e-46 |
|
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: 169.05 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 26 TYQNLYCEASLLAKRLKAY--QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCT--- 100
Cdd:cd05909 9 TYRKLLTGAIALARKLAKMtkEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSkqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 101 --------LPLELRGFQIVSLDDIEfagRDITT----NGLLDNTMGIQYDTSNETVVPKESpsnilntsfnlDDIASIMF 168
Cdd:cd05909 89 ieklklhhLFDVEYDARIVYLEDLR---AKISKadkcKAFLAGKFPPKWLLRIFGVAPVQP-----------DDPAVILF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 169 TSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIV-DKFNAEQILTMIK 246
Cdd:cd05909 155 TSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGcLWLPLLSGIKVVFHpNPLDYKKIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 247 NERITHISLVPQTLNWLMQQGlhEPYN---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTATPEMlHA 322
Cdd:cd05909 235 DKKATILLGTPTFLRGYARAA--HPEDfssLRLVVAGAEKLKDTLRQEFQEkFGIRILEGYGTTECSPVISVNTPQS-PN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 323 RPDTVGMPSANVDVKIKNPnkEGH--------GELMIKGANVMNGYLYPTDLTGT-FENGYFNTGDIAEIDHEGYVMIYD 393
Cdd:cd05909 312 KEGTVGRPLPGMEVKIVSV--ETHeevpigegGLLLVRGPNVMLGYLNEPELTSFaFGDGWYDTGDIGKIDGEGFLTITG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 394 RRKDLIISGGENIYPYQIETVAKQFPGISDAVCV-GHPDDTWGQVPKLyFVSESDISKAQLIAYLSQH-LAKYKVPKHFE 471
Cdd:cd05909 390 RLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVvSVPDGRKGEKIVL-LTTTTDTDPSSLNDILKNAgISNLAKPSYIH 468
|
490
....*....|...
gi 446270502 472 KVDTLPYTSTGKL 484
Cdd:cd05909 469 QVEEIPLLGTGKP 481
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
14-489 |
2.15e-46 |
|
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: 168.46 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 14 HHIAITD--GQESYTYQNLYCEASLLAKRLKA---YQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQ 88
Cdd:cd05923 16 DACAIADpaRGLRLTYSELRARIEAVAARLHArglRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 89 MKSIDVQLIFCT---LPLE---LRGFQIVSLDDiefagrdittngllDNTMGIQYDTSNETVVPKESPsnilntsfnlDD 162
Cdd:cd05923 96 IERGEMTAAVIAvdaQVMDaifQSGVRVLALSD--------------LVGLGEPESAGPLIEDPPREP----------EQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 163 IASIMFTSGTTGPQKA--VPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFNAE 239
Cdd:cd05923 152 PAFVFYTSGTTGLPKGavIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFfAVLVAALALDGTYVVVEEFDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPYNL---QKILLGGAKLSATMIETaLQYNLP--IYNSFGMTETCSQFLt 314
Cdd:cd05923 232 DALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLsslRHVTFAGATMPDAVLER-VNQHLPgeKVNIYGTTEAMNSLY- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 atpeMLHARPDTVGMPSANVDVKIKN---------PNKEgHGELMIK--GANVMNGYLYPTDLTGT-FENGYFNTGDIAE 382
Cdd:cd05923 310 ----MRDARTGTEMRPGFFSEVRIVRiggspdealANGE-EGELIVAaaADAAFTGYLNQPEATAKkLQDGWYRTGDVGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ-VPKLYFVSESDISKAQLIAY-LSQH 460
Cdd:cd05923 385 VDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQsVTACVVPREGTLSADELDQFcRASE 464
|
490 500
....*....|....*....|....*....
gi 446270502 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05923 465 LADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
156-491 |
3.28e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 167.44 E-value: 3.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 156 TSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTV---- 230
Cdd:PRK07529 208 RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVtGLAPLARGAHVvlat 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 231 --------------RIVDKFnaeqiltmikneRITHISLVPQTLNWLMQQ--GLHEPYNLQKILLGGAKLSATMIETALQ 294
Cdd:PRK07529 288 pqgyrgpgvianfwKIVERY------------RINFLSGVPTVYAALLQVpvDGHDISSLRYALCGAAPLPVEVFRRFEA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 295 YN-LPIYNSFGMTE-TCSQflTATPEMLHARPDTVGMPSANVDVKIKNPNKEGH----------GELMIKGANVMNGYLY 362
Cdd:PRK07529 356 ATgVRIVEGYGLTEaTCVS--SVNPPDGERRIGSVGLRLPYQRVRVVILDDAGRylrdcavdevGVLCIAGPNVFSGYLE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 363 PTDLTGTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLY 441
Cdd:PRK07529 434 AAHNKGLWlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446270502 442 --FVSESDISKAQLIAYLSQHLA-KYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK07529 514 vqLKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
159-489 |
5.14e-45 |
|
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: 163.28 E-value: 5.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 NLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DRDTNWLSVLP--IYHI--SGLSVLL----RAVIEGft 229
Cdd:cd05972 79 DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLrPDDIHWNIADPgwAKGAwsSFFGPWLlgatVFVYEG-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 230 vrivDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE--PYNLQKILLGGAKLSATMIETAL-QYNLPIYNSFGMT 306
Cdd:cd05972 157 ----PRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSykFSHLRLVVSAGEPLNPEVIEWWRaATGLPIRDGYGQT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 307 ET---CSQFLTATPemlhaRPDTVGMPSANVDVKIKN-------PNKEGHGELMIKGANVMNGYL-YPTDLTGTFENGYF 375
Cdd:cd05972 233 ETgltVGNFPDMPV-----KPGSMGRPTPGYDVAIIDddgrelpPGEEGDIAIKLPPPGLFLGYVgDPEKTEASIRGDYY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-----SESDISK 450
Cdd:cd05972 308 LTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVltsgyEPSEELA 387
|
330 340 350
....*....|....*....|....*....|....*....
gi 446270502 451 AQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05972 388 EELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-483 |
5.45e-45 |
|
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: 161.11 E-value: 5.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIV------ 233
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVtLLTPLASGAHVVLAgpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 234 DKFNAEQILTMIKNERITHISLVPQTLNWLMQQglhePYN-----LQKILLGGAKLSATM---IETALqyNLPIYNSFGM 305
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVYAALLQV----PVNadissLRFAMSGAAPLPVELrarFEDAT--GLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 306 TEtCSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKEGH----------GELMIKGANVMNGYLYPTDLTGTF-ENGY 374
Cdd:cd05944 156 TE-ATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRllrdcapdevGEICVAGPGVFGGYLYTEGNKNAFvADGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 375 FNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLY--FVSESDISKAQ 452
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqLKPGAVVEEEE 314
|
330 340 350
....*....|....*....|....*....|..
gi 446270502 453 LIAYLSQHLA-KYKVPKHFEKVDTLPYTSTGK 483
Cdd:cd05944 315 LLAWARDHVPeRAAVPKHIEVLEELPVTAVGK 346
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
5-429 |
1.36e-44 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 165.27 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIAI---TDGQ-ESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLA-------- 69
Cdd:COG1022 17 LRRRAARFPDRVALrekEDGIwQSLTWAEFAERVRALAAGLLALgvkPGDRVAILSDNRPEWVIADLAILAAgavtvpiy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 70 ---------------NIEIAMINTRltpnEMTNQMKSI-----DVQLIFCTLPLELRGF-QIVSLDDIEFAGRDITTNGL 128
Cdd:COG1022 97 ptssaeevayilndsGAKVLFVEDQ----EQLDKLLEVrdelpSLRHIVVLDPRGLRDDpRLLSLDELLALGREVADPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 129 LDNTMgiqydtsnETVVPkespsnilntsfnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSV 208
Cdd:COG1022 173 LEARR--------AAVKP--------------DDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 209 LPIYHISGLSVLLRAVIEGFTVRIVDkfNAEQILTMIKNERITHISLVP---------------------QTL-NWLMQQ 266
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAFAE--SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkRKLfRWALAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 267 GL-HEPYNLQ----------------KILL----------------GGAKLSATMIE--TALqyNLPIYNSFGMTETCSq 311
Cdd:COG1022 309 GRrYARARLAgkspslllrlkhaladKLVFsklrealggrlrfavsGGAALGPELARffRAL--GIPVLEGYGLTETSP- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTATPEmLHARPDTVGMPSANVDVKIknpnkEGHGELMIKGANVMNGYLYPTDLTG-TF-ENGYFNTGDIAEIDHEGYV 389
Cdd:COG1022 386 VITVNRP-GDNRIGTVGPPLPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATAeAFdADGWLHTGDIGELDEDGFL 459
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446270502 390 MIYDRRKDLII-SGGENIYPYQIETVAKQFPGISDAVCVGH 429
Cdd:COG1022 460 RITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGD 500
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
161-489 |
4.71e-44 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 161.97 E-value: 4.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLR-AVIEGFTVRIVDKFNAE 239
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNvALLAGASMIFLPKFDPD 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKneRITHISLVPQTLNWLMQqglhEPyNLQKILLGGAKL----SATM-IETALQYN----LPIYNSFGMTETCs 310
Cdd:PRK07514 236 AVLALMP--RATVMMGVPTFYTRLLQ----EP-RLTREAAAHMRLfisgSAPLlAETHREFQertgHAILERYGMTETN- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 qFLTATPEMLHARPDTVGMPSANVDVKIKNPnKEGH-------GELMIKGANVMNGYLYPTDLTGT-F-ENGYFNTGDIA 381
Cdd:PRK07514 308 -MNTSNPYDGERRAGTVGFPLPGVSLRVTDP-ETGAelppgeiGMIEVKGPNVFKGYWRMPEKTAEeFrADGFFITGDLG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 382 EIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVG--HPDdtWGQ------VPKlyfvSESDISKAQL 453
Cdd:PRK07514 386 KIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGvpHPD--FGEgvtavvVPK----PGAALDEAAI 459
|
330 340 350
....*....|....*....|....*....|....*.
gi 446270502 454 IAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07514 460 LAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
161-489 |
8.89e-44 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 162.14 E-value: 8.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLR-AVIEGFTVRIVDKFNAE 239
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMmPVMLGATAVLQDIWDPA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPYN---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTA 315
Cdd:PRK13295 277 RAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPvssLRTFLCAGAPIPGALVERARAaLGAKIVSAWGMTENGAVTLTK 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 316 TPEMLHARPDTVGMPSANVDVKIKNPNKEG-----HGELMIKGANVMNGYLYPTDLTGTFENGYFNTGDIAEIDHEGYVM 390
Cdd:PRK13295 357 LDDPDERASTTDGCPLPGVEVRVVDADGAPlpagqIGRLQVRGCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 391 IYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ------VPKlyfvSESDISKAQLIAYL-SQHLAK 463
Cdd:PRK13295 437 ISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGEracafvVPR----PGQSLDFEEMVEFLkAQKVAK 512
|
330 340
....*....|....*....|....*.
gi 446270502 464 YKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13295 513 QYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
9-489 |
9.21e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 162.02 E-value: 9.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 9 AQQNGHHIAITDGQESYTYQNLYcEAS------LLAKRLKAyqQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTP 82
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELD-EQSnalargLLALGVRA--GDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 83 NEMTNQMKSIDVQLIF---------CTLPLELRGFQ--IVSLDDIEFAGRDITTnglLDNTMgiqyDTSNETVVPK-ESP 150
Cdd:PRK07788 136 PQLAEVAAREGVKALVyddeftdllSALPPDLGRLRawGGNPDDDEPSGSTDET---LDDLI----AGSSTAPLPKpPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 151 SNIlntsfnlddiasIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTV 230
Cdd:PRK07788 209 GGI------------VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 231 RIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLH--EPY---NLQKILLGGAKLSATMIETAL-QYNLPIYNSFG 304
Cdd:PRK07788 277 VLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEvlAKYdtsSLKIIFVSGSALSPELATRALeAFGPVLYNLYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 305 MTEtCSQFLTATPEMLHARPDTVGMPSANVDVKI----KNPNKEGH-GELMIKGANVMNGYlypTDlTGTFE--NGYFNT 377
Cdd:PRK07788 357 STE-VAFATIATPEDLAEAPGTVGRPPKGVTVKIldenGNEVPRGVvGRIFVGNGFPFEGY---TD-GRDKQiiDGLLSS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 378 GDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE--SDISKAQLIA 455
Cdd:PRK07788 432 GDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKApgAALDEDAIKD 511
|
490 500 510
....*....|....*....|....*....|....
gi 446270502 456 YLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07788 512 YVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
166-486 |
2.25e-43 |
|
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: 156.28 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTG-PQKAVpQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTM 244
Cdd:cd17637 5 IIHTAAVAGrPRGAV-LSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 245 IKNERITHISLVPQTLNWLMQQGLHEPYNLQKI-LLGGAKLSATMIETALQYNLPIYNSFGMTETcSQFLTATPemLHAR 323
Cdd:cd17637 84 IEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrHVLGLDAPETIQRFEETTGATFWSLYGQTET-SGLVTLSP--YRER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 324 PDTVGMPSANVDVKI----KNPNKEGH-GELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDHEGYvMIYDRR-- 395
Cdd:cd17637 161 PGSAGRPGPLVRVRIvddnDRPVPAGEtGEIVVRGPLVFQGYWNLPELTAyTFRNGWHHTGDLGRFDEDGY-LWYAGRkp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 396 -KDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEK 472
Cdd:cd17637 240 eKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVlkPGATLTADELIEFVGSRIARYKKPRYVVF 319
|
330
....*....|....
gi 446270502 473 VDTLPYTSTGKLQR 486
Cdd:cd17637 320 VEALPKTADGSIDR 333
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
162-489 |
3.77e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 160.50 E-value: 3.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYH------------ISGLSVLLRaviegft 229
Cdd:PRK08162 183 DAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHcngwcfpwtvaaRAGTNVCLR------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 230 vrivdKFNAEQILTMIKNERITHISLVPQTLNWL------MQQGLHEPYnlqKILLGGAKLSATMIETALQYNLPIYNSF 303
Cdd:PRK08162 256 -----KVDPKLIFDLIREHGVTHYCGAPIVLSALinapaeWRAGIDHPV---HAMVAGAAPPAAVIAKMEEIGFDLTHVY 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 304 GMTET------CSQfltaTPE----------MLHARPD---------TVGMPSANVDVkiknPNK-EGHGELMIKGANVM 357
Cdd:PRK08162 328 GLTETygpatvCAW----QPEwdalplderaQLKARQGvryplqegvTVLDPDTMQPV----PADgETIGEIMFRGNIVM 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 358 NGYLYPTDLTG-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ 436
Cdd:PRK08162 400 KGYLKNPKATEeAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGE 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446270502 437 VPKLyFVSESD---ISKAQLIAYLSQHLAKYKVPKHFEkVDTLPYTSTGKLQRNKL 489
Cdd:PRK08162 480 VPCA-FVELKDgasATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-489 |
5.00e-43 |
|
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: 158.37 E-value: 5.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 48 RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSI----DVQLIFCTLPL--ELRGFQIVSLDDIEFAGR 121
Cdd:cd05922 20 RVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLvadaGGRIVLADAGAadRLRDALPASPDPGTVLDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 122 DittnglldntmGIQYDTSNETVVPKESPsnilntsfnldDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDR 201
Cdd:cd05922 100 D-----------GIRAARASAPAHEVSHE-----------DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 202 DTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQ-ILTMIKNERITHISLVPQTLNWLMQQGLH-EPY-NLQKIL 278
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATGLAGVPSTYAMLTRLGFDpAKLpSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 279 LGGAKLSATMIEtALQYNLP---IYNSFGMTETCSQFLTATPEMLHARPDTVGMPSANVDVKIKN------PNKEgHGEL 349
Cdd:cd05922 238 QAGGRLPQETIA-RLRELLPgaqVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDddgtptPPGE-PGEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 350 MIKGANVMNGYL----YPTDLTGTfeNGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAV 425
Cdd:cd05922 316 VHRGPNVMKGYWndppYRRKEGRG--GGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446270502 426 CVGHPDDTWGQVpKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05922 394 AVGLPDPLGEKL-ALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
4-489 |
6.93e-43 |
|
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: 159.54 E-value: 6.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 4 WLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIeI---AMIN 77
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALglrPGDRVVVQLPNVAEFVIVFFALFRAGA-IpvfALPA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 78 TRLTpnEMTNQMKSID-VQLIFCTlplELRGFqivslDDIEFAGRdittngLLDNTMGIQY---------DTSNETVVpk 147
Cdd:COG1021 109 HRRA--EISHFAEQSEaVAYIIPD---RHRGF-----DYRALARE------LQAEVPSLRHvlvvgdageFTSLDALL-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 148 ESPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLS--VLLRAVI 225
Cdd:COG1021 171 AAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSspGVLGVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 226 EGFTVRIVDKFNAEQILTMIKNERITHISLVP-QTLNWLmQQGLHEPYN---LQKILLGGAKLS---ATMIETA----LQ 294
Cdd:COG1021 251 AGGTVVLAPDPSPDTAFPLIERERVTVTALVPpLALLWL-DAAERSRYDlssLRVLQVGGAKLSpelARRVRPAlgctLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 295 ynlpiyNSFGMTE--TCSQFLTATPEMLHarpDTVGMP-SANVDVKI----KNPNKEGH-GELMIKGANVMNGYlY--P- 363
Cdd:COG1021 330 ------QVFGMAEglVNYTRLDDPEEVIL---TTQGRPiSPDDEVRIvdedGNPVPPGEvGELLTRGPYTIRGY-YraPe 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 364 ---TDLTgtfENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKL 440
Cdd:COG1021 400 hnaRAFT---PDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446270502 441 YFV-SESDISKAQLIAYL-SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG1021 477 FVVpRGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
17-489 |
1.38e-42 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 159.41 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 17 AITDGQESYTYQNLYCEASLLAKRLKAYQQSRvglyidNSIQSIIL--IHACWLANIEIAM-------INTRLTPNEMTN 87
Cdd:PLN03102 32 SIIYGKTRFTWPQTYDRCCRLAASLISLNITK------NDVVSVLApnTPAMYEMHFAVPMagavlnpINTRLDATSIAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 88 QMKSIDVQLIFCTL---PLELRGFQIVSLDDIEFAGRDITTNGLLDNTMGIQYDTSNETVVPKESPSNILNTSF----NL 160
Cdd:PLN03102 106 ILRHAKPKILFVDRsfePLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEELDYECLIQRGEPTPSLVARMfriqDE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCkeSLGFDRDTN--WLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNA 238
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYLSTLSA--IIGWEMGTCpvYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLMQQG---LHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFL-- 313
Cdd:PLN03102 264 PEIYKNIEMHNVTHMCCVPTVFNILLKGNsldLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLfc 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 314 ------TATPE----MLHARPDTVGMPSANVDVK----IKNPNKEGH--GELMIKGANVMNGYLY-PTDLTGTFENGYFN 376
Cdd:PLN03102 344 ewqdewNRLPEnqqmELKARQGVSILGLADVDVKnketQESVPRDGKtmGEIVIKGSSIMKGYLKnPKATSEAFKHGWLN 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV---SESDI----- 448
Cdd:PLN03102 424 TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVlekGETTKedrvd 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446270502 449 ----SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN03102 504 klvtRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
161-489 |
9.50e-42 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 156.75 E-value: 9.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLG-FDRDTNWLSV--LPIYHISGLSV--LLRAVIEGFTVRIVDK 235
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpLLHPGKELVVtaLPLYHIFALTVncLLFIELGGQNLLITNP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 FNAEQILTMIKNERITHISLVPQTLN-WLMQQGLHE-PYNLQKILLGGA----KLSATMIETALQYNLpiYNSFGMTEtC 309
Cdd:PRK08974 286 RDIPGFVKELKKYPFTAITGVNTLFNaLLNNEEFQElDFSSLKLSVGGGmavqQAVAERWVKLTGQYL--LEGYGLTE-C 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 310 SQFLTATPEMLHARPDTVGMPSANVDVKIKN------PNKEGhGELMIKGANVMNGYLY-PTDLTGTFENGYFNTGDIAE 382
Cdd:PRK08974 363 SPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDddgnevPPGEP-GELWVKGPQVMLGYWQrPEATDEVIKDGWLATGDIAV 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-SESDISKAQLIAYLSQHL 461
Cdd:PRK08974 442 MDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVkKDPSLTEEELITHCRRHL 521
|
330 340
....*....|....*....|....*...
gi 446270502 462 AKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08974 522 TGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
161-489 |
2.84e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 154.27 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFNAE 239
Cdd:PRK06145 149 TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLwVGGTLRIHREFDPE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQqgLHEPY-----NLQKILLGGAKLSATMIE--TALQYNLPIYNSFGMTETCS-- 310
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLSRVLT--VPDRDrfdldSLAWCIGGGEKTPESRIRdfTRVFTRARYIDAYGLTETCSgd 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 QFLTATPEMlhARPDTVGMPSANVDVKIKN-------PNKEGhgELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAE 382
Cdd:PRK06145 307 TLMEAGREI--EKIGSTGRALAHVEIRIADgagrwlpPNMKG--EICMRGPKVTKGYWKDPEKTAeAFYGDWFRSGDVGY 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQH 460
Cdd:PRK06145 383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQR 462
|
330 340
....*....|....*....|....*....
gi 446270502 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
14-489 |
5.89e-41 |
|
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: 152.30 E-value: 5.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 14 HHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIeiamintrltpnemtnqmk 90
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERgvgPGDLVAVLLERSLEMVVAILAVLKAGA------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 91 sidvqlifCTLPLelrgfqivsldDIEF-AGRdittnglldntmgIQY--DTSNETVVpkespsniLNTSfnlDDIASIM 167
Cdd:cd05930 63 --------AYVPL-----------DPSYpAER-------------LAYilEDSGAKLV--------LTDP---DDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 168 FTSGTTGPQKAVP---QTFRNHYASAigcKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDK---FNAEQI 241
Cdd:cd05930 100 YTSGSTGKPKGVMvehRGLVNLLLWM---QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEevrKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 LTMIKNERITHISLVPQTLNWLMQQGLHE-PYNLQKILLGGAKLSATMIETALQYNLP--IYNSFGMTET--CSQFLTAT 316
Cdd:cd05930 177 ADLLAEEGITVLHLTPSLLRLLLQELELAaLPSLRLVLVGGEALPPDLVRRWRELLPGarLVNLYGPTEAtvDATYYRVP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 317 PEMLHARPDTVGMPSANVDVKIKNPN----KEGH-GELMIKGANVMNGYLYPTDLTG------TFENG--YFNTGDIAEI 383
Cdd:cd05930 257 PDDEEDGRVPIGRPIPNTRVYVLDENlrpvPPGVpGELYIGGAGLARGYLNRPELTAerfvpnPFGPGerMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 384 DHEGyVMIYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSES--DISKAQLIAYLSQH 460
Cdd:cd05930 337 LPDG-NLEFLGRIDDQVKiRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAER 415
|
490 500
....*....|....*....|....*....
gi 446270502 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05930 416 LPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
166-489 |
7.16e-41 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 153.76 E-value: 7.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVPQTFRNHY--ASAIgckeslgFDRdTNWLS------VLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIgtLKAI-------LDR-TPWRAeeptviVAPMFHAWGFSQLVLAASLACTIVTRRRFD 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQglhEPYNLQKILLGGAKLSAT---------MIETALQYNLPIYNSFGMTET 308
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDL---PAEVRNRYSGRSLRFAAAsgsrmrpdvVIAFMDQFGDVIYNNYNATEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 cSQFLTATPEMLHARPDTVGMPSANVDVKIKNPN----KEGH-GELMIKGANVMNGYLYPTdlTGTFENGYFNTGDIAEI 383
Cdd:PRK13382 350 -GMIATATPADLRAAPDTAGRPAEGTEIRILDQDfrevPTGEvGTIFVRNDTQFDGYTSGS--TKDFHDGFMASGDVGYL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 384 DHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQ--LIAYLSQHL 461
Cdd:PRK13382 427 DENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPetLKQHVRDNL 506
|
330 340
....*....|....*....|....*...
gi 446270502 462 AKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13382 507 ANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
156-489 |
8.81e-41 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 154.21 E-value: 8.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 156 TSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYAS---AIGCKESLGFDRDTNW-------LSVLPIYHISGLSV--LLRA 223
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqVRACLSQLGPDGQPLMkegqevmIAPLPLYHIYAFTAncMCMM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 224 VIEGFTVRIVDKFNAEQILTMIKNERITHIslvpQTLNWLMQQGLHEP-------YNLQKILLGGAKL-SATMIETALQY 295
Cdd:PRK12492 282 VSGNHNVLITNPRDIPGFIKELGKWRFSAL----LGLNTLFVALMDHPgfkdldfSALKLTNSGGTALvKATAERWEQLT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 296 NLPIYNSFGMTETcSQFLTATPEMLHARPDTVGMPSANVDVKIKN------PNKEgHGELMIKGANVMNGYLYPTDLTGT 369
Cdd:PRK12492 358 GCTIVEGYGLTET-SPVASTNPYGELARLGTVGIPVPGTALKVIDddgnelPLGE-RGELCIKGPQVMKGYWQQPEATAE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 370 F--ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-SES 446
Cdd:PRK12492 436 AldAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVaRDP 515
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446270502 447 DISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12492 516 GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
159-489 |
1.09e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 153.77 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 NLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTN---WLSVLPIYHISGLSV--LLRAVIEGFTVRIV 233
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGceiLIAPLPLYHIYAFTFhcMAMMLIGNHNILIS 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 234 dkfNAEQILTMIKNERITHIS-LVpqTLNWLMQqGLHEPYNLQKILLGGAKLSAT--MietALQY----------NLPIY 300
Cdd:PRK05677 285 ---NPRDLPAMVKELGKWKFSgFV--GLNTLFV-ALCNNEAFRKLDFSALKLTLSggM---ALQLataerwkevtGCAIC 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 301 NSFGMTETcSQFLTATPeMLHARPDTVGMPSANVDVKIKNPNKE----GH-GELMIKGANVMNGYLYPTDLTGTF--ENG 373
Cdd:PRK05677 356 EGYGMTET-SPVVSVNP-SQAIQVGTIGIPVPSTLCKVIDDDGNelplGEvGELCVKGPQVMKGYWQRPEATDEIldSDG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKA 451
Cdd:PRK05677 434 WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGetLTKE 513
|
330 340 350
....*....|....*....|....*....|....*...
gi 446270502 452 QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05677 514 QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
147-491 |
1.11e-40 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 153.84 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 147 KESPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYAS-------------AIGCkeslgfdrDTNWLSVLPIYH 213
Cdd:PLN02574 184 KEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMvelfvrfeasqyeYPGS--------DNVYLAALPMFH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 214 ISGLSVLLRAVIE-GFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQG---LHEPY-NLQKILLGGAKLSATM 288
Cdd:PLN02574 256 IYGLSLFVVGLLSlGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAkgvCGEVLkSLKQVSCGAAPLSGKF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 289 IETALQyNLP---IYNSFGMTETCSQFLTATPEMLHARPDTVGMPSANVDVKIKN--------PNkeGHGELMIKGANVM 357
Cdd:PLN02574 336 IQDFVQ-TLPhvdFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwstgcllpPG--NCGELWIQGPGVM 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 358 NGYLYPTDLTGT--FENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWG 435
Cdd:PLN02574 413 KGYLNNPKATQStiDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446270502 436 QVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PLN02574 493 EIPVAFVVrrQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
39-489 |
2.40e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 152.88 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 39 KRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCTLPLELRGFQIVSLDDIEf 118
Cdd:PRK06710 67 QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIE- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 119 agrDITTNGLLD------NTMG--IQYDTSNETVVPKESPSNIL--------NTSFNL-----DDIASIMFTSGTTGPQK 177
Cdd:PRK06710 146 ---HVIVTRIADflpfpkNLLYpfVQKKQSNLVVKVSESETIHLwnsvekevNTGVEVpcdpeNDLALLQYTGGTTGFPK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 178 AVPQTFRNHYASAI-------GCKESlgfdrDTNWLSVLPIYHISGLSVLLR-AVIEGFTVRIVDKFNAEQILTMIKNER 249
Cdd:PRK06710 223 GVMLTHKNLVSNTLmgvqwlyNCKEG-----EEVVLGVLPFFHVYGMTAVMNlSIMQGYKMVLIPKFDMKMVFEAIKKHK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 250 ITHISLVPQTLNWLMQQGLHEPYNLQKI---LLGGAKLSATMIETALQYNL-PIYNSFGMTEtcSQFLTATPEMLHAR-P 324
Cdd:PRK06710 298 VTLFPGAPTIYIALLNSPLLKEYDISSIracISGSAPLPVEVQEKFETVTGgKLVEGYGLTE--SSPVTHSNFLWEKRvP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 325 DTVGMPSANVDVKIKNPN-----KEGH-GELMIKGANVMNGYL-YPTDLTGTFENGYFNTGDIAEIDHEGYVMIYDRRKD 397
Cdd:PRK06710 376 GSIGVPWPDTEAMIMSLEtgealPPGEiGEIVVKGPQIMKGYWnKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKD 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 398 LIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDT 475
Cdd:PRK06710 456 MIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGteCSEEELNQFARKYLAAYKVPKVYEFRDE 535
|
490
....*....|....
gi 446270502 476 LPYTSTGKLQRNKL 489
Cdd:PRK06710 536 LPKTTVGKILRRVL 549
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
161-486 |
3.71e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 152.23 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDrDTNWLSV-LPIYHISG--LSVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLT-EHDRLCVpVPLYHCFGmvLANLGCMTVGACLVYPNEAFD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQK----ILLGGAKLSATMIETALQYNLP-IYNSFGMTETCS-Q 311
Cdd:PRK12583 280 PLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSlrtgIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSPvS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTATPEMLHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLT--GTFENGYFNTGDIAEID 384
Cdd:PRK12583 360 LQTTAADDLERRVETVGRTQPHLEVKVVDPDGAtvprgEIGELCTRGYSVMKGYWNNPEATaeSIDEDGWMHTGDLATMD 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 385 HEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLA 462
Cdd:PRK12583 440 EQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGhaASEEELREFCKARIA 519
|
330 340
....*....|....*....|....
gi 446270502 463 KYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK12583 520 HFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
24-485 |
3.78e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 152.04 E-value: 3.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 24 SYTYQNLYCEAsllaKRLKAYQQS--------RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQ 95
Cdd:PRK08314 35 AISYRELLEEA----ERLAGYLQQecgvrkgdRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 96 LIFCTLPLELRGFQIVSLDDIEFAgrdITTN--GLLDNTMGIQYDTSNETVVPKESPSNILNTSFN-------------- 159
Cdd:PRK08314 111 VAIVGSELAPKVAPAVGNLRLRHV---IVAQysDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKealaaglappphta 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 160 -LDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK08314 188 gPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMvHSMNAPIYAGATVVLMPRWD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKLSATMIETAL-QYNLPIYNSFGMTETCSQFL 313
Cdd:PRK08314 268 REAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYiggGGAAMPEAVAERLKeLTGLDYVEGYGLTETMAQTH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 314 TATPEmlHARPDTVGMPSANVDVKIKNP--------NKEGhgELMIKGANVMNGYLYPTDLTG----TFEnG--YFNTGD 379
Cdd:PRK08314 348 SNPPD--RPKLQCLGIPTFGVDARVIDPetleelppGEVG--EIVVHGPQVFKGYWNRPEATAeafiEID-GkrFFRTGD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 380 IAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV----SESDISKAQLIA 455
Cdd:PRK08314 423 LGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVlrpeARGKTTEEEIIA 502
|
490 500 510
....*....|....*....|....*....|
gi 446270502 456 YLSQHLAKYKVPKHFEKVDTLPYTSTGKLQ 485
Cdd:PRK08314 503 WAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
164-489 |
6.79e-40 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 150.62 E-value: 6.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 164 ASIMFTSGTTGPQKAV---PQTfRNHYASAIGCKESL-GFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAE 239
Cdd:PRK12406 155 QSMIYTSGTTGHPKGVrraAPT-PEQAAAAEQMRALIyGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQ--QGLHEPYN---LQKILLGGAKLSA----TMIEtalQYNLPIYNSFGMTETcS 310
Cdd:PRK12406 234 ELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDvssLRHVIHAAAPCPAdvkrAMIE---WWGPVIYEYYGSTES-G 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 QFLTATPEMLHARPDTVGMPSANVDVKI----KNPNKEGH-GELMIKGAnVMNGYLY---PTDLTGTFENGYFNTGDIAE 382
Cdd:PRK12406 310 AVTFATSEDALSHPGTVGKAAPGAELRFvdedGRPLPQGEiGEIYSRIA-GNPDFTYhnkPEKRAEIDRGGFITSGDVGY 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVpkLYFVSESD----ISKAQLIAYLS 458
Cdd:PRK12406 389 LDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA--LMAVVEPQpgatLDEADIRAQLK 466
|
330 340 350
....*....|....*....|....*....|.
gi 446270502 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12406 467 ARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
31-489 |
3.13e-39 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 149.79 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 31 YCEASLLAKRLKAYQQS-------RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCtlpL 103
Cdd:PRK07059 51 YGELDELSRALAAWLQSrglakgaRVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVV---L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 104 ElrgfqivslddiEFAGrdiTTNGLLDNT-------------MGIQYDTSNETV--VPKESPSNIL--NTSFNL------ 160
Cdd:PRK07059 128 E------------NFAT---TVQQVLAKTavkhvvvasmgdlLGFKGHIVNFVVrrVKKMVPAWSLpgHVRFNDalaega 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 -----------DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESL--GFDRDT-----NWLSVLPIYHISGLSV--L 220
Cdd:PRK07059 193 rqtfkpvklgpDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLqpAFEKKPrpdqlNFVCALPLYHIFALTVcgL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 221 LRAVIEGFTVRIVdkfNAEQILTMIKNERITHISLVPqTLNWLMQQGLHEP-------YNLQKILLGGAKLSATMIETAL 293
Cdd:PRK07059 273 LGMRTGGRNILIP---NPRDIPGFIKELKKYQVHIFP-AVNTLYNALLNNPdfdkldfSKLIVANGGGMAVQRPVAERWL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 294 QYN-LPIYNSFGMTETcSQFLTATPEMLHARPDTVGMPSANVDVKIKN------PNKEGhGELMIKGANVMNGYLYPTDL 366
Cdd:PRK07059 349 EMTgCPITEGYGLSET-SPVATCNPVDATEFSGTIGLPLPSTEVSIRDddgndlPLGEP-GEICIRGPQVMAGYWNRPDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 367 TG--TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV- 443
Cdd:PRK07059 427 TAkvMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVk 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446270502 444 SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07059 507 KDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
149-486 |
5.39e-39 |
|
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: 147.20 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 149 SPSNILNTSFNlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEG 227
Cdd:cd05914 78 SEAKAIFVSDE-DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFtLLLPLLNG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 228 FTVRIVDKFNAEQILTMIKNErITHISLVPQ----------------TLNWLMQ----------------QGLHEPY--N 273
Cdd:cd05914 157 AHVVFLDKIPSAKIIALAFAQ-VTPTLGVPVplviekifkmdiipklTLKKFKFklakkinnrkirklafKKVHEAFggN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 274 LQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPEMLhaRPDTVGMPSANVDVKIKNPNKEGH-GELMIK 352
Cdd:cd05914 236 IKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRI--RLGSAGKVIDGVEVRIDSPDPATGeGEIIVR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 353 GANVMNGYLYPTDLTGTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISG-GENIYPYQIET--VAKQFPGIS----- 422
Cdd:cd05914 314 GPNVMKGYYKNPEATAEAfdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAkiNNMPFVLESlvvvq 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 423 --DAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKY----KVPKHFEKvdtLPYTSTGKLQR 486
Cdd:cd05914 394 ekKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYkkisKVKIVKEE---FEKTPKGKIKR 460
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
162-489 |
1.10e-38 |
|
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: 146.70 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV--LLRAVIEGFTVRIVDKFNAE 239
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDPSPD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKLSATM---IETALqyNLPIYNSFGMTE--TCSQ 311
Cdd:cd05920 220 AAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLlqvGGARLSPALarrVPPVL--GCTLQQVFGMAEglLNYT 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTATPEMLHArpdTVGMP-SANVDVKI----KNPNKEGH-GELMIKGANVMNGYlY--PTDLTGTF-ENGYFNTGDIAE 382
Cdd:cd05920 298 RLDDPDEVIIH---TQGRPmSPDDEIRVvdeeGNPVPPGEeGELLTRGPYTIRGY-YraPEHNARAFtPDGFYRTGDLVR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-SESDISKAQLIAYLSQH- 460
Cdd:cd05920 374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVlRDPPPSAAQLRRFLRERg 453
|
330 340
....*....|....*....|....*....
gi 446270502 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05920 454 LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
157-489 |
1.41e-38 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 147.59 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 157 SFNLDDIASIMFTSGTTGPQKAVPQTFRNH--YASAIGCKESLGF-DRDTnWLSVLPIYH-------ISGLSVLLRAVIE 226
Cdd:PRK06018 173 TFDENTAAGMCYTSGTTGDPKGVLYSHRSNvlHALMANNGDALGTsAADT-MLPVVPLFHanswgiaFSAPSMGTKLVMP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 GftvrivDKFNAEQILTMIKNERITHISLVPQTlnWLM------QQGLHEPYnLQKILLGGAKLSATMIETALQYNLPIY 300
Cdd:PRK06018 252 G------AKLDGASVYELLDTEKVTFTAGVPTV--WLMllqymeKEGLKLPH-LKMVVCGGSAMPRSMIKAFEDMGVEVR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 301 NSFGMTETC--SQFLTATPEMLHARPD-------TVGMPSANVDVKIKNP-NKE------GHGELMIKGANVMNGYlYPT 364
Cdd:PRK06018 323 HAWGMTEMSplGTLAALKPPFSKLPGDarldvlqKQGYPPFGVEMKITDDaGKElpwdgkTFGRLKVRGPAVAAAY-YRV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 365 DLTGTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVS 444
Cdd:PRK06018 402 DGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQL 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446270502 445 ESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06018 482 KPGetATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
160-489 |
5.28e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 146.34 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 160 LDDIASIMFTSGTTGPQKAVPQTFRNH-YASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFN 237
Cdd:PRK06178 208 LDALAALNYTGGTTGMPKGCEHTQRDMvYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFgLLFPLFSGATLVLLARWD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQ-GLHEpYNLQKILLGGA-----KLS------------ATMIETAlqynlpi 299
Cdd:PRK06178 288 AVAFMAAVERYRVTRTVMLVDNAVELMDHpRFAE-YDLSSLRQVRVvsfvkKLNpdyrqrwraltgSVLAEAA------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 300 ynsFGMTE--TCSQFLTA--TPEM-LHARPDTVGMPSANVDVKIKN-------PNKEgHGELMIKGANVMNGYLYPTDLT 367
Cdd:PRK06178 360 ---WGMTEthTCDTFTAGfqDDDFdLLSQPVFVGLPVPGTEFKICDfetgellPLGA-EGEIVVRTPSLLKGYWNKPEAT 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 G-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPkLYFVS-- 444
Cdd:PRK06178 436 AeALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVP-VAFVQlk 514
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446270502 445 -ESDISKAQLIAYLSQHLAKYKVPKhFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06178 515 pGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
161-489 |
1.03e-37 |
|
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: 143.41 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD-KFNA 238
Cdd:cd05969 89 EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLhPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLMQQG--LHEPYNLQK---ILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQF 312
Cdd:cd05969 169 ESWYGIIERVKVTVWYTAPTAIRMLMKEGdeLARKYDLSSlrfIHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTETGSIM 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 313 LTATPEMlHARPDTVGMPSANVDVKIKNPNKEG-----HGELMIKGA--NVMNGYLY-PTDLTGTFENGYFNTGDIAEID 384
Cdd:cd05969 249 IANYPCM-PIKPGSMGKPLPGVKAAVVDENGNElppgtKGILALKPGwpSMFRGIWNdEERYKNSFIDGWYLTGDLAYRD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 385 HEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQ 459
Cdd:cd05969 328 EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfEPSDELKEEIINFVRQ 407
|
330 340 350
....*....|....*....|....*....|
gi 446270502 460 HLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05969 408 KLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
24-489 |
1.76e-37 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 144.05 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 24 SYTYQNLYCE---ASLLAKRLKAYQQSRVGLYIDNSIQSIIlihaCW--LANIEIAM--INTRLTPNEMTNQMKSIDVQL 96
Cdd:PRK08008 37 RYSYLELNEEinrTANLFYSLGIRKGDKVALHLDNCPEFIF----CWfgLAKIGAIMvpINARLLREESAWILQNSQASL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 97 IFCT---LPL--ELRGFQIVSLDDIEFAGrdiTTNGLLDNTMGIQYDTSNETVVPKESPSniLNTsfnlDDIASIMFTSG 171
Cdd:PRK08008 113 LVTSaqfYPMyrQIQQEDATPLRHICLTR---VALPADDGVSSFTQLKAQQPATLCYAPP--LST----DDTAEILFTSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 172 TTGPQKAVPQT-----FRNHYASAIGCkeslgFDRDTNWLSVLPIYHIS-GLSVLLRAVIEGFTVRIVDKFNAEQILTMI 245
Cdd:PRK08008 184 TTSRPKGVVIThynlrFAGYYSAWQCA-----LRDDDVYLTVMPAFHIDcQCTAAMAAFSAGATFVLLEKYSARAFWGQV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 246 KNERITHISLVPQTLNWLMQQGLHE---PYNLQKILLGgAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTATPEMLH 321
Cdd:PRK08008 259 CKYRATITECIPMMIRTLMVQPPSAndrQHCLREVMFY-LNLSDQEKDAFEErFGVRLLTSYGMTETIVGIIGDRPGDKR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 322 ARPdTVGMPSANVDVKIKNpnKEGH-------GELMIKGA---NVMNGYLYPTDLTG-TFE-NGYFNTGDIAEIDHEGYV 389
Cdd:PRK08008 338 RWP-SIGRPGFCYEAEIRD--DHNRplpageiGEICIKGVpgkTIFKEYYLDPKATAkVLEaDGWLHTGDTGYVDEEGFF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 390 MIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLY--FVSESDISKAQLIAYLSQHLAKYKVP 467
Cdd:PRK08008 415 YFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFvvLNEGETLSEEEFFAFCEQNMAKFKVP 494
|
490 500
....*....|....*....|..
gi 446270502 468 KHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08008 495 SYLEIRKDLPRNCSGKIIKKNL 516
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-489 |
4.11e-37 |
|
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: 141.80 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLG-FDRDTN---------WLSVLpiyhisgLSVLLRAVIEGFTV 230
Cdd:cd05971 88 DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNlFPRDGDlywtpadwaWIGGL-------LDVLLPSLYFGVPV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 231 --RIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQG---LHEPYNLQKILLGGAKLSATMIETAL-QYNLPIYNSFG 304
Cdd:cd05971 161 laHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGeqlKHAQVKLRAIATGGESLGEELLGWAReQFGVEVNEFYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 305 MTEtCSQFLTATPEMLHARPDTVGMPSANVDVKIKN-------PNKEGHGELMIKGANVMNGYLY-PTDLTGTFENGYFN 376
Cdd:cd05971 241 QTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDdngtplpPGEVGEIAVELPDPVAFLGYWNnPSATEKKMAGDWLL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-----SESDISKA 451
Cdd:cd05971 320 TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAR 399
|
330 340 350
....*....|....*....|....*....|....*...
gi 446270502 452 QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05971 400 EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
31-489 |
6.59e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 143.09 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 31 YCEASLLAKRLKAY--------QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLI----- 97
Cdd:PRK08751 53 YREADQLVEQFAAYllgelqlkKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvidn 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 98 FCTLPLelrgfQIVSLDDIefagRDITTNGLLDNTMGIQYDTSNETV--VPKESPSNILNTSFNL--------------- 160
Cdd:PRK08751 133 FGTTVQ-----QVIADTPV----KQVITTGLGDMLGFPKAALVNFVVkyVKKLVPEYRINGAIRFrealalgrkhsmptl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 ----DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGfdrDTNWL--------SVLPIYHISGLSV--LLRAVIE 226
Cdd:PRK08751 204 qiepDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLA---GTGKLeegcevviTALPLYHIFALTAngLVFMKIG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 GFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQ-GLHE-PYNLQKILLGGAKlsATMIETALQYN----LPIY 300
Cdd:PRK08751 281 GCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTpGFDQiDFSSLKMTLGGGM--AVQRSVAERWKqvtgLTLV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 301 NSFGMTETcSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKEGH-----GELMIKGANVMNGYLYPTDLTGTF--ENG 373
Cdd:PRK08751 359 EAYGLTET-SPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLaigeiGELCIKGPQVMKGYWKRPEETAKVmdADG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQL 453
Cdd:PRK08751 438 WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAED 517
|
490 500 510
....*....|....*....|....*....|....*..
gi 446270502 454 I-AYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08751 518 VkAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
166-489 |
6.61e-37 |
|
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: 141.75 E-value: 6.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVPQTF---RNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQIL 242
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLpggPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 243 TMIKNERITHISLVPQTLN--WLMQQGLHEPYN---LQKILLGGAKLSATMIETALQYNLP-IYNSFGMTEtCSQFLTAT 316
Cdd:cd05929 210 RLIERYRVTFAQFVPTMFVrlLKLPEAVRNAYDlssLKRVIHAAAPCPPWVKEQWIDWGGPiIWEYYGGTE-GQGLTIIN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 317 PEMLHARPDTVGMPSANvDVKIKN-------PNKEGhgELMIKGANvmnGYLYPTDLTGT----FENGYFNTGDIAEIDH 385
Cdd:cd05929 289 GEEWLTHPGSVGRAVLG-KVHILDedgnevpPGEIG--EVYFANGP---GFEYTNDPEKTaaarNEGGWSTLGDVGYLDE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYF-----VSESDISKAQLIAYLSQH 460
Cdd:cd05929 363 DGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgADAGTALAEELIAFLRDR 442
|
330 340
....*....|....*....|....*....
gi 446270502 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05929 443 LSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
164-489 |
8.65e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 142.54 E-value: 8.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 164 ASIMFTSGTTGPQKAVPQTFRN---H-YASAIgcKESLGFDRDTNWLSVLPIYHIS--GL--SVLL---RAVIEGftvri 232
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRStvlHaYGAAL--PDAMGLSARDAVLPVVPMFHVNawGLpySAPLtgaKLVLPG----- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 233 vDKFNAEQILTMIKNERITHISLVP----QTLNWLMQQGLHEPyNLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTE 307
Cdd:PRK07008 252 -PDLDGKSLYELIEAERVTFSAGVPtvwlGLLNHMREAGLRFS-TLRRTVIGGSACPPAMIRTFEDeYGVEVIHAWGMTE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 308 ------TC---SQFLTATPEMLHARPDTVGMPSANVDVKIKNPN-KE------GHGELMIKGANVMNGYlYPTDlTGTFE 371
Cdd:PRK07008 330 msplgtLCklkWKHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDgRElpwdgkAFGDLQVRGPWVIDRY-FRGD-ASPLV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 372 NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE--SDIS 449
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRpgAEVT 487
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446270502 450 KAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07008 488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
162-486 |
8.99e-37 |
|
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: 138.55 E-value: 8.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGC-KESLGFDRDTNWLSVLPIYHISGLSVLLRAVIE-GFTVRIVDKFNAE 239
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWL---MQQGLHEPYNLQKILLGGAKLSATMIETALQY-NLPIYNSFGMTET----CSQ 311
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLvseLKSANATVPSLRLIGYGGSRAIAADVRFIEATgLTNTAQVYGLSETgtalCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTATPEMlharpDTVGMPSANVDVKIKNPN-----KEGHGELMIKGANVMNGYLYPTDLTGT-FENGYFNTGDIAEIDH 385
Cdd:cd17635 162 TDDDSIEI-----NAVGRPYPGVDVYLAATDgiagpSASFGTIWIKSPANMLGYWNNPERTAEvLIDGWVNTGDLGERRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQ-LIAYLSQHLA 462
Cdd:cd17635 237 DGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasAELDENAIRaLKHTIRRELE 316
|
330 340
....*....|....*....|....
gi 446270502 463 KYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd17635 317 PYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
161-489 |
1.40e-36 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 142.26 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRN--HYASAIGckESLGF---DRdtnwLSV-LPIYHISGLsVL--LRAVIEGFT-VR 231
Cdd:PRK08315 199 DDPINIQYTSGTTGFPKGATLTHRNilNNGYFIG--EAMKLteeDR----LCIpVPLYHCFGM-VLgnLACVTHGATmVY 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 232 IVDKFNAEQILTMIKNERITHISLVPqTLNWLMqqgLHEP----YNLQK----ILLGGAKLSATMIETALQYNLP-IYNS 302
Cdd:PRK08315 272 PGEGFDPLATLAAVEEERCTALYGVP-TMFIAE---LDHPdfarFDLSSlrtgIMAGSPCPIEVMKRVIDKMHMSeVTIA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 303 FGMTETcS--QFLTATPEMLHARPDTVGMPSANVDVKIKNPNKeGH-------GELMIKGANVMNGYlYpTDLTGTFE-- 371
Cdd:PRK08315 348 YGMTET-SpvSTQTRTDDPLEKRVTTVGRALPHLEVKIVDPET-GEtvprgeqGELCTRGYSVMKGY-W-NDPEKTAEai 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 372 --NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ------VPKlyfv 443
Cdd:PRK08315 424 daDGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEevcawiILR---- 499
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446270502 444 SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08315 500 PGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
7-489 |
2.68e-36 |
|
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: 140.16 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 7 KQAQQNGHHIAITDGQESYTYQNLYCEASLLAK--RLKAYQQSR-VGLYIDNSIQSIILIHACWLAN-----IEIAMint 78
Cdd:cd17655 5 EQAEKTPDHTAVVFEDQTLTYRELNERANQLARtlREKGVGPDTiVGIMAERSLEMIVGILGILKAGgaylpIDPDY--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 79 rltPNEMTNQM-KSIDVQLIFCTLPLELRgfqivslddIEFAGrditTNGLLDNTmgiqyDTSNETVVPKESPSNIlnts 157
Cdd:cd17655 82 ---PEERIQYIlEDSGADILLTQSHLQPP---------IAFIG----LIDLLDED-----TIYHEESENLEPVSKS---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 158 fnlDDIASIMFTSGTTGPQKAVPQTFRN--HYASA------------IGCKESLGFDrdtnwLSVLPIYHisglSVLLRA 223
Cdd:cd17655 137 ---DDLAYVIYTSGSTGKPKGVMIEHRGvvNLVEWankviyqgehlrVALFASISFD-----ASVTEIFA----SLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 224 VIegFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILLGGAKLSATMIET---ALQYNLPIY 300
Cdd:cd17655 205 TL--YIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKiieLFGTNPTIT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 301 NSFGMTETCSQFLTATPEMLHARPDTV--GMPSANVDVKI----KNPNKEG-HGELMIKGANVMNGYLYPTDLTGT---- 369
Cdd:cd17655 283 NAYGPTETTVDASIYQYEPETDQQVSVpiGKPLGNTRIYIldqyGRPQPVGvAGELYIGGEGVARGYLNRPELTAEkfvd 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 370 --FENG--YFNTGDIAE------------IDHEgyVMIYDRRKDLiisgGEniypyqIETVAKQFPGISDAVCVGHPDDT 433
Cdd:cd17655 363 dpFVPGerMYRTGDLARwlpdgnieflgrIDHQ--VKIRGYRIEL----GE------IEARLLQHPDIKEAVVIARKDEQ 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446270502 434 WGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17655 431 GQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
161-491 |
6.13e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 136.71 E-value: 6.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGfdRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD---KFN 237
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG--GPGQWLLALPAHHIAGLQVLVRSVIAGSEPVELDvsaGFD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMI---KNERiTHISLVPQTLNWLMQ--QGLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSqf 312
Cdd:PRK07824 113 PTALPRAVaelGGGR-RYTSLVPMQLAKALDdpAATAALAELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSG-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 313 ltatpemlharpDTV--GMPSANVDVKIKNpnkeghGELMIKGANVMNGYLYPTDLTGTFENGYFNTGDIAEIDhEGYVM 390
Cdd:PRK07824 190 ------------GCVydGVPLDGVRVRVED------GRIALGGPTLAKGYRNPVDPDPFAEPGWFRTDDLGALD-DGVLT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 391 IYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQvpKLYFVSESDISKAQLIAYLSQH----LAKYKV 466
Cdd:PRK07824 251 VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQ--RVVAAVVGDGGPAPTLEALRAHvartLDRTAA 328
|
330 340
....*....|....*....|....*
gi 446270502 467 PKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK07824 329 PRELHVVDELPRRGIGKVDRRALVR 353
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
161-489 |
2.36e-35 |
|
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: 136.82 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASA-IGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKF-N 237
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWpT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKLSATMIETALQYNL-PIYNSFGMTETCSQFL 313
Cdd:cd05919 171 AERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLcvsAGEALPRGLGERWMEHFGgPILDGIGATEVGHIFL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 314 TATPEmlHARPDTVGMPSANVDVKIKNPnkEGH-------GELMIKGANVMNGYLYPTDLT-GTFENGYFNTGDIAEIDH 385
Cdd:cd05919 251 SNRPG--AWRLGSTGRPVPGYEIRLVDE--EGHtippgeeGDLLVRGPSAAVGYWNNPEKSrATFNGGWYRTGDKFCRDA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKA---QLIAYLSQH 460
Cdd:cd05919 327 DGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlkSPAAPQESlarDIHRHLLER 406
|
330 340
....*....|....*....|....*....
gi 446270502 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05919 407 LSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
161-486 |
2.47e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 138.10 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYAS--AIGCKESLGfDRDTNwLSVLPIYHISGL-SVLLRAVIEGFTVRIV--DK 235
Cdd:PRK05852 176 PDDAMIMFTGGTTGLPKMVPWTHANIASSvrAIITGYRLS-PRDAT-VAVMPLYHGHGLiAALLATLASGGAVLLParGR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 FNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYN-----LQKILLGGAKLSAtmiETAL----QYNLPIYNSFGMT 306
Cdd:PRK05852 254 FSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGrkpaaLRFIRSCSAPLTA---ETAQalqtEFAAPVVCAFGMT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 307 ETCSQFLTATPEMLHARPD---TVGMPSANVDVKIKNPNKEGH-------GELMIKGANVMNGYLY-PTDLTGTFENGYF 375
Cdd:PRK05852 331 EATHQVTTTQIEGIGQTENpvvSTGLVGRSTGAQIRIVGSDGLplpagavGEVWLRGTTVVRGYLGdPTITAANFTDGWL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDI--SKAQL 453
Cdd:PRK05852 411 RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAppTAEEL 490
|
330 340 350
....*....|....*....|....*....|...
gi 446270502 454 IAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK05852 491 VQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
14-489 |
2.58e-35 |
|
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: 138.18 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 14 HHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMIN---TRLTPNEMTN 87
Cdd:cd05906 29 TYIDADGSEEFQSYQDLLEDARRLAAGLRQLglrPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvppTYDEPNARLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 88 QMKSIDVQL----IFCTLPL--ELRGfqIVSLDDIEfaGRDITTNGLLDntmgiqyDTSNETVVPKESPsnilntsfnlD 161
Cdd:cd05906 109 KLRHIWQLLgspvVLTDAELvaEFAG--LETLSGLP--GIRVLSIEELL-------DTAADHDLPQSRP----------D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVL-LRAVIEGftvrivdkfnAEQ 240
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLG----------CQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 241 I--------------LTMIKNERIThISLVPQTLNWLMQQGLHE----PYNL---QKILLGGAKLSATMIETALQ----Y 295
Cdd:cd05906 238 VhvpteeiladplrwLDLIDRYRVT-ITWAPNFAFALLNDLLEEiedgTWDLsslRYLVNAGEAVVAKTIRRLLRllepY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 296 NLP---IYNSFGMTETCS--QFLTATPEMLHARPDT---VGMPSANVDVKIKNPNKEGH-----GELMIKGANVMNGYLY 362
Cdd:cd05906 317 GLPpdaIRPAFGMTETCSgvIYSRSFPTYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLpegevGRLQVRGPVVTKGYYN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 363 PTDLTGTF--ENGYFNTGDIAEIDHeGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI--SDAVCVGHPDDTWG-QV 437
Cdd:cd05906 397 NPEANAEAftEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepSFTAAFAVRDPGAEtEE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446270502 438 PKLYFVSESDISKA--QLIAYLSQHLAK-------YKVPkhFEKvDTLPYTSTGKLQRNKL 489
Cdd:cd05906 476 LAIFFVPEYDLQDAlsETLRAIRSVVSRevgvspaYLIP--LPK-EEIPKTSLGKIQRSKL 533
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
17-489 |
1.77e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 135.51 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 17 AITDGQESYTYQNLYCEASLLAKRLK----AYQQSrVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSI 92
Cdd:PRK13383 53 AIIDDDGALSYRELQRATESLARRLTrdgvAPGRA-VGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 93 DVQLIFCtlplelrgfqivsldDIEFAGRDITTN---GLLDNTMGIQYDTSNEtvvPKESPSNILntsfnlddiasIMFT 169
Cdd:PRK13383 132 HISTVVA---------------DNEFAERIAGADdavAVIDPATAGAEESGGR---PAVAAPGRI-----------VLLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 170 SGTTGPQKAVPQtfRNHYASAIGCKESLgFDRDT----NWLSV-LPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTM 244
Cdd:PRK13383 183 SGTTGKPKGVPR--APQLRSAVGVWVTI-LDRTRlrtgSRISVaMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 245 IKNERITHISLVPQTLNWLM----QQGLHEPY-NLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLtATPE 318
Cdd:PRK13383 260 ASLHRADAFTAVPVVLARILelppRVRARNPLpQLRVVMSSGDRLDPTLGQRFMDtYGDILYNGYGSTEVGIGAL-ATPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 319 MLHARPDTVGMPSANVDVKIKNPNKEGHGElMIKGANVMNGYLYPTDLTG----TFENGYFNTGDIAEIDHEGYVMIYDR 394
Cdd:PRK13383 339 DLRDAPETVGKPVAGCPVRILDRNNRPVGP-RVTGRIFVGGELAGTRYTDgggkAVVDGMTSTGDMGYLDNAGRLFIVGR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 395 RKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKYKVPKHFEK 472
Cdd:PRK13383 418 EDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHpgSGVDAAQLRDYLKDRVSRFEQPRDINI 497
|
490
....*....|....*..
gi 446270502 473 VDTLPYTSTGKLQRNKL 489
Cdd:PRK13383 498 VSSIPRNPTGKVLRKEL 514
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
5-484 |
2.07e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 135.55 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:PRK07470 13 LRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARgvrKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 82 PNEMTNQMKSIDVQLIFCTlplelRGFQivslddiEFAGRDITTNGLLDNTMGI---QYDTSNETVVPKESPSNILNTSF 158
Cdd:PRK07470 93 PDEVAYLAEASGARAMICH-----ADFP-------EHAAAVRAASPDLTHVVAIggaRAGLDYEALVARHLGARVANAAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 NLDDIASIMFTSGTTGPQKAVPQT-------FRNHYASAI-GCKESlgfDRDtnwLSVLPIYHISGLSVLLRaVIEGFTV 230
Cdd:PRK07470 161 DHDDPCWFFFTSGTTGRPKAAVLThgqmafvITNHLADLMpGTTEQ---DAS---LVVAPLSHGAGIHQLCQ-VARGAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 231 RIV--DKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYN---LQKILLGGAKLSATMIETAL--------QYnl 297
Cdd:PRK07470 234 VLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDhssLRYVIYAGAPMYRADQKRALaklgkvlvQY-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 298 piynsFGMTEtCSQFLTATPEMLH-------ARPDTVGMPSANVDVKIK----NPNKEGH-GELMIKGANVMNGYL-YPT 364
Cdd:PRK07470 312 -----FGLGE-VTGNITVLPPALHdaedgpdARIGTCGFERTGMEVQIQddegRELPPGEtGEICVIGPAVFAGYYnNPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 365 DLTGTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVS 444
Cdd:PRK07470 386 ANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA 465
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446270502 445 E--SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:PRK07470 466 RdgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
161-489 |
7.87e-34 |
|
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: 132.60 E-value: 7.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIG-CKESLGFDRDTNWLSVLPIYHISGLS-VLLRAVIEGFTVRIVDKFNA 238
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRyAVNVLRLREDDRFVGSPPLAFTFGLGgVLLFPFGVGASGVLLEEATP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLM---QQGLHEPYNLQKILLGGAKLSAtmiETALQYN----LPIYNSFGMTETCSQ 311
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPTAYRAMLahpDAAGPDLSSLRKCVSAGEALPA---ALHRAWKeatgIPIIDGIGSTEMFHI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTATPEmlHARPDTVGMPSANVDVKI----KNPNKEGH-GELMIKGANvmnGYLYPTDLTG--TFENGYFNTGDIAEID 384
Cdd:cd05958 254 FISARPG--DARPGATGKPVPGYEAKVvddeGNPVPDGTiGRLAVRGPT---GCRYLADKRQrtYVQGGWNITGDTYSRD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 385 HEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD-ISKAQLIAYLSQH--- 460
Cdd:cd05958 329 PDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGvIPGPVLARELQDHaka 408
|
330 340 350
....*....|....*....|....*....|
gi 446270502 461 -LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05958 409 hIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
161-489 |
9.86e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 134.20 E-value: 9.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIM--FTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYH------------ISGLSVLLRAVie 226
Cdd:PLN02479 193 DEWQSIAlgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHcngwcftwtlaaLCGTNICLRQV-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 gftvrivdkfNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPY----NLQKILLGGAKLSATMIETALQYNLPIYNS 302
Cdd:PLN02479 271 ----------TAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlplpRVVHVMTAGAAPPPSVLFAMSEKGFRVTHT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 303 FGMTETC--SQFLTATPE----------MLHARPDT--VGMPSANV-DVKIKNP---NKEGHGELMIKGANVMNGYLY-P 363
Cdd:PLN02479 341 YGLSETYgpSTVCAWKPEwdslppeeqaRLNARQGVryIGLEGLDVvDTKTMKPvpaDGKTMGEIVMRGNMVMKGYLKnP 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 364 TDLTGTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV 443
Cdd:PLN02479 421 KANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVT 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446270502 444 SESDISK-------AQLIAYLSQHLAKYKVPKHFeKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02479 501 LKPGVDKsdeaalaEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
162-489 |
1.74e-33 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 133.18 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDR--DTNWLSVLPIYHISGLSVLLRAVIEGF-TVRIVDKFNA 238
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMigQVVTLGLIPFFHIYGITGICCATLRNKgKVVVMSRFEL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQK-----ILLGGAKLSATMIeTALQYNLP---IYNSFGMTE-TC 309
Cdd:PLN02330 265 RTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKlklqaIMTAAAPLAPELL-TAFEAKFPgvqVQEAYGLTEhSC 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 310 SQFLTATPEMLH--ARPDTVGMPSANVDVKIKNPN------KEGHGELMIKGANVMNGYLYPTDLTGTF--ENGYFNTGD 379
Cdd:PLN02330 344 ITLTHGDPEKGHgiAKKNSVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTidEDGWLHTGD 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 380 IAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYL 457
Cdd:PLN02330 424 IGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVinPKAKESEEDILNFV 503
|
330 340 350
....*....|....*....|....*....|..
gi 446270502 458 SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02330 504 AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
166-489 |
3.46e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 131.74 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAV--------PQTFRNHYASaigCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK13391 159 MLYSSGTTGRPKGIkrplpeqpPDTPLPLTAF---LQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFD 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLM-----QQGLHEPYNLQKILLGGAKLSATMIETALQYNLP-IYNSFGMTETCSQ 311
Cdd:PRK13391 236 AEQYLALIEEYGVTHTQLVPTMFSRMLklpeeVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPiIHEYYAATEGLGF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTATPEMLhARPDTVGMPSAnvdvkiknpnkeghGELMIKGANvmnGYLYPTDLTGT--FENG----YFN--------- 376
Cdd:PRK13391 316 TACDSEEWL-AHPGTVGRAMF--------------GDLHILDDD---GAELPPGEPGTiwFEGGrpfeYLNdpaktaear 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 --------TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYF-----V 443
Cdd:PRK13391 378 hpdgtwstVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVqpvdgV 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446270502 444 SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13391 458 DPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-489 |
1.32e-32 |
|
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: 129.72 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 15 HIAITDGQESYTYQNLyCEASL-LAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLtPNEMTNQM- 89
Cdd:cd12116 3 ATAVRDDDRSLSYAEL-DERANrLAARLRARgvgPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADRLRYIl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 90 KSIDVQLIFCTLPLELRGFQI--VSLDDIEFAGRdittnglldntmgiQYDTSNETVVPkespsnilntsfnlDDIASIM 167
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGlpVLLLALAAAAA--------------APAAPRTPVSP--------------DDLAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 168 FTSGTTGPQKAVPQTFRN--HYASAIGckESLGFDRDTNWLSVLPI-YHISGLSVLLrAVIEGFTVRIVDK---FNAEQI 241
Cdd:cd12116 133 YTSGSTGRPKGVVVSHRNlvNFLHSMR--ERLGLGPGDRLLAVTTYaFDISLLELLL-PLLAGARVVIAPRetqRDPEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 LTMIKNERITHISLVPQTLNWLMQQGLHEPYNLqKILLGGAKLSATMIETALQYNLPIYNSFGMTET----CSQFLTATp 317
Cdd:cd12116 210 ARLIEAHSITVMQATPATWRMLLDAGWQGRAGL-TALCGGEALPPDLAARLLSRVGSLWNLYGPTETtiwsTAARVTAA- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 318 emlhARPDTVGMPSANVDVKI----KNPNKEGH-GELMIKGANVMNGYLYPTDLTGT-------FENG--YFNTGDIAEI 383
Cdd:cd12116 288 ----AGPIPIGRPLANTQVYVldaaLRPVPPGVpGELYIGGDGVAQGYLGRPALTAErfvpdpfAGPGsrLYRTGDLVRR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 384 DHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDdtwGQVPKL--YFVSESD--ISKAQLIAYLSQ 459
Cdd:cd12116 364 RADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED---GGDRRLvaYVVLKAGaaPDAAALRAHLRA 440
|
490 500 510
....*....|....*....|....*....|
gi 446270502 460 HLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12116 441 TLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
168-489 |
2.98e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 128.87 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 168 FTSGTTGPQKAV--PQTFRNHYASAIGCKESLGFDR----DTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:PRK08276 147 YSSGTTGRPKGIkrPLPGLDPDEAPGMMLALLGFGMyggpDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 LTMIKNERITHISLVPQTLNWLMQ--QGLHEPYN---LQKILLGGA----KLSATMIEtalqYNLPI-YNSFGMTETCSq 311
Cdd:PRK08276 227 LALIERYRVTHSQLVPTMFVRMLKlpEEVRARYDvssLRVAIHAAApcpvEVKRAMID----WWGPIiHEYYASSEGGG- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 312 FLTATPEMLHARPDTVGMPSANVdVKIKNPNKE-----GHGELMIKganvMNGYL--YPTDLTGTFEN----GYFNTGDI 380
Cdd:PRK08276 302 VTVITSEDWLAHPGSVGKAVLGE-VRILDEDGNelppgEIGTVYFE----MDGYPfeYHNDPEKTAAArnphGWVTVGDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 381 AEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ-----VPKLYFVSESDISKAQLIA 455
Cdd:PRK08276 377 GYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGErvkavVQPADGADAGDALAAELIA 456
|
330 340 350
....*....|....*....|....*....|....
gi 446270502 456 YLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08276 457 WLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
7-489 |
9.05e-32 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 128.20 E-value: 9.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 7 KQAQQNGHHIAI--TDGQESYTYQNLYCEASLLAKRLKA---YQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:PRK05857 22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAqsvSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 82 PNEMTNQMKSIDVQLIfctLPLELRGFQIVSLDDIEFAGRDITTNGLLDNTmgiQYDTSNETVVPKESPSnilntsFNLD 161
Cdd:PRK05857 102 IAAIERFCQITDPAAA---LVAPGSKMASSAVPEALHSIPVIAVDIAAVTR---ESEHSLDAASLAGNAD------QGSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYA-SAIGCKESLGF----DRDTNWlSVLPIYHISGLSVLLRAVIEGFTVrIVDKF 236
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAVLLANRTFFAvPDILQKEGLNWvtwvVGETTY-SPLPATHIGGLWWILTCLMHGGLC-VTGGE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 237 NAEQILTMIKNERITHISLVPQTLNWLMQQ----GLHEPyNLQKILLGGAKLSAT---MIETALQYNLPIYnsfGMTET- 308
Cdd:PRK05857 248 NTTSLLEILTTNAVATTCLVPTLLSKLVSElksaNATVP-SLRLVGYGGSRAIAAdvrFIEATGVRTAQVY---GLSETg 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 CSQFLTATPEMLHARPD--TVGMPSANVDVKIKNPNKEG-----------HGELMIKGANVMNGYLYPTDLTG-TFENGY 374
Cdd:PRK05857 324 CTALCLPTDDGSIVKIEagAVGRPYPGVDVYLAATDGIGptapgagpsasFGTLWIKSPANMLGYWNNPERTAeVLIDGW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 375 FNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLI 454
Cdd:PRK05857 404 VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAAR 483
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446270502 455 AYLSQHLAKYK-------VPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05857 484 ALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
162-489 |
8.21e-31 |
|
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: 125.27 E-value: 8.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVpqtfrNHYASAIGCKESLGFDR--------------DTNWLsvlpiyhISGLSVLLRAVIEG 227
Cdd:cd05928 175 EPMAIYFTSGTTGSPKMA-----EHSHSSLGLGLKVNGRYwldltasdimwntsDTGWI-------KSAWSSLFEPWIQG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 228 FTVRI--VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGL--HEPYNLQKILLGGAKLSATMIET-ALQYNLPIYNS 302
Cdd:cd05928 243 ACVFVhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLssYKFPSLQHCVTGGEPLNPEVLEKwKAQTGLDIYEG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 303 FGMTETCsqFLTATPEMLHARPDTVGMPSANVDVKIKN-------PNKEGHGELMIKGAN---VMNGYL-YPTDLTGTFE 371
Cdd:cd05928 323 YGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDdngnvlpPGTEGDIGIRVKPIRpfgLFSGYVdNPEKTAATIR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 372 NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDIS-- 449
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLsh 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446270502 450 -KAQLIAYLSQHL----AKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05928 481 dPEQLTKELQQHVksvtAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
8-489 |
1.02e-30 |
|
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: 124.24 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLtPNE 84
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAgvgPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL-PAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 85 MTNQMksidvqlifctlpLELRGFQIVsLDDIEFAGRDittNGLLDNTMGIQYDtsnetvvPKESPSNiLNTSFNLDDIA 164
Cdd:cd12117 85 RLAFM-------------LADAGAKVL-LTDRSLAGRA---GGLEVAVVIDEAL-------DAGPAGN-PAVPVSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 165 SIMFTSGTTGPQKAVPQTFRNhyasaigckeSLGFDRDTNWLSVLP---IYHISGLSV------LLRAVIEGFTVRIVDK 235
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRG----------VVRLVKNTNYVTLGPddrVLQTSPLAFdastfeIWGALLNGARLVLAPK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 ---FNAEQILTMIKNERITHISLVPQTLNWLMQQ------GLHEpynlqkILLGGAKLSATMIETALQYN--LPIYNSFG 304
Cdd:cd12117 210 gtlLDPDALGALIAEEGVTVLWLTAALFNQLADEdpecfaGLRE------LLTGGEVVSPPHVRRVLAACpgLRLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 305 MTE--TCSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNkeGH-------GELMIKGANVMNGYLYPTDLTGT------ 369
Cdd:cd12117 284 PTEntTFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDED--GRpvppgvpGELYVGGDGLALGYLNRPALTAErfvadp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 370 FENG---YFnTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSES 446
Cdd:cd12117 362 FGPGerlYR-TGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG 440
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446270502 447 DISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12117 441 ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
16-489 |
3.98e-30 |
|
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: 122.86 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 16 IAITDGQESYTYQNLYCEASLLA---KRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSI 92
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAgalRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 93 DVQLIFCTLPLELRgFQIVSLDDIEFAGRDITTNGLLDNTMGIQYdtsnETVVPKESPS-NILNTSfnLDDIASIMFTSG 171
Cdd:cd05959 101 RARVVVVSGELAPV-LAAALTKSEHTLVVLIVSGGAGPEAGALLL----AELVAAEAEQlKPAATH--ADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 172 TTGPQKAVPQTFRNHYASA-IGCKESLGFDRDTNWLSVLPIYHISGL--SVLLRAVIEGFTVRIVDKFNAEQILTMIKNE 248
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFAYGLgnSLTFPLSVGATTVLMPERPTPAAVFKRIRRY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 249 RITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKLSATMIE--TALqYNLPIYNSFGMTETCSQFLTATPEMLhaR 323
Cdd:cd05959 254 RPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLcvsAGEALPAEVGErwKAR-FGLDILDGIGSTEMLHIFLSNRPGRV--R 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 324 PDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLT-GTFENGYFNTGDIAEIDHEGYVMIYDRRKD 397
Cdd:cd05959 331 YGTTGKPVPGYEVELRDEDGGdvadgEPGELYVRGPSSATMYWNNRDKTrDTFQGEWTRTGDKYVRDDDGFYTYAGRADD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 398 LIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEK 472
Cdd:cd05959 411 MLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALEEELKEFVKDRLAPYKYPRWIVF 490
|
490
....*....|....*..
gi 446270502 473 VDTLPYTSTGKLQRNKL 489
Cdd:cd05959 491 VDELPKTATGKIQRFKL 507
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
161-492 |
7.09e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 121.64 E-value: 7.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLsVL-----LRAvieGFTVRIVDK 235
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGL-VLgvlgpLRI---GNRFVHTGR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 FNAEQIltmiKNERITHISL---VPQTLNWLMQ-QGLHEPYNLQKILLGG-AKLSATMIE--TALQYNLPIyNSFGMTET 308
Cdd:PRK07787 204 PTPEAY----AQALSEGGTLyfgVPTVWSRIAAdPEAARALRGARLLVSGsAALPVPVFDrlAALTGHRPV-ERYGMTET 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 ---CSQFLTATPemlhaRPDTVGMPSANVDVKIKNPNK-------EGHGELMIKGANVMNGYLYPTDLTG-TF-ENGYFN 376
Cdd:PRK07787 279 litLSTRADGER-----RPGWVGLPLAGVETRLVDEDGgpvphdgETVGELQVRGPTLFDGYLNRPDATAaAFtADGWFR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 TGDIAEIDHEGYVMIYDRRK-DLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIA 455
Cdd:PRK07787 354 TGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELID 433
|
330 340 350
....*....|....*....|....*....|....*..
gi 446270502 456 YLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYRG 492
Cdd:PRK07787 434 FVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
155-486 |
1.79e-29 |
|
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: 121.45 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 155 NTSFNLDDIASIMFTSGTTGPQKAVPQTFR---NHYASAIGCKESLGFDR-----DTNWLSVL--PIYH--ISGLSVLlr 222
Cdd:cd05970 179 NSYPCGEDILLVYFSSGTTGMPKMVEHDFTyplGHIVTAKYWQNVREGGLhltvaDTGWGKAVwgKIYGqwIAGAAVF-- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 223 aviegftVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLhEPYNLQKI---LLGGAKLSATMIETALQYN-LP 298
Cdd:cd05970 257 -------VYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLrycTTAGEALNPEVFNTFKEKTgIK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 IYNSFGMTETCSQflTATPEMLHARPDTVGMPSANVDVKIKNPN----KEGH-GELMIKGAN-----VMNGYLYPTDLTG 368
Cdd:cd05970 329 LMEGFGQTETTLT--IATFPWMEPKPGSMGKPAPGYEIDLIDREgrscEAGEeGEIVIRTSKgkpvgLFGGYYKDAEKTA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 369 -TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD 447
Cdd:cd05970 407 eVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKG 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446270502 448 ISKAQ-LIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd05970 487 YEPSEeLKKELQDHVKKvtapYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
81-489 |
1.81e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 121.24 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 81 TPNEMTNQMKSIDVQLIFcTLPL---ELRGFQIVslDDIEFagrdITTNGLLDNTMGIQYDT-SNETVVPKESpsnilnt 156
Cdd:PLN02246 110 TPAEIAKQAKASGAKLII-TQSCyvdKLKGLAED--DGVTV----VTIDDPPEGCLHFSELTqADENELPEVE------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 157 sFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAI----GCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVR 231
Cdd:PLN02246 176 -ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILCVLPMFHIYSLnSVLLCGLRVGAAIL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 232 IVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKI--LLGGAklsATM---IETALQYNLP---IYNSF 303
Cdd:PLN02246 255 IMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIrmVLSGA---APLgkeLEDAFRAKLPnavLGQGY 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 304 GMTET---CSQFLTATPEMLHARPDTVGMPSANVDVKIKNP--------NKEGhgELMIKGANVMNGYLYPTDLTGTF-- 370
Cdd:PLN02246 332 GMTEAgpvLAMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPetgaslprNQPG--EICIRGPQIMKGYLNDPEATANTid 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 371 ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDI 448
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVrsNGSEI 489
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446270502 449 SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02246 490 TEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
161-489 |
8.50e-29 |
|
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: 118.34 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDT-NWLSVLPIYHISGLSVLLRAVIEGFTVRIVD---KF 236
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPdevKL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 237 NAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQ--KILLGG-----AKLSATMIETALQyNLPIYNSFGMTETC 309
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSamRLLIVGsdgckAQDFKTLAARFGQ-GMRIINSYGVTEAT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 310 ---SQFLTATPEMLHARPDTVGMPSANVDVKI----KNPNKEG-HGELMIKGANVMNGYLYPTDLTGT------FENG-- 373
Cdd:cd17650 252 idsTYYEEGRDPLGDSANVPIGRPLPNTAMYVlderLQPQPVGvAGELYIGGAGVARGYLNRPELTAErfvenpFAPGer 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDtwGQVPKL--YFVSESDISKA 451
Cdd:cd17650 332 MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK--GGEARLcaYVVAAATLNTA 409
|
330 340 350
....*....|....*....|....*....|....*...
gi 446270502 452 QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
200-482 |
1.01e-28 |
|
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: 115.86 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 200 DRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL 279
Cdd:cd17636 39 DEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 280 G-GAKLSATMI---ETALQYNLPIYnsfGMTETCSqfLTATPEMLHARPDTVGMPSANVDVKIKNPnkEGH-------GE 348
Cdd:cd17636 119 SpAAPEWNDMAtvdTSPWGRKPGGY---GQTEVMG--LATFAALGGGAIGGAGRPSPLVQVRILDE--DGRevpdgevGE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 349 LMIKGANVMNGYLYPTDLTGT-FENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCV 427
Cdd:cd17636 192 IVARGPTVMAGYWNRPEVNARrTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446270502 428 GHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTG 482
Cdd:cd17636 272 GVPDPRWAQSVKAIVVLKPGasVTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
17-483 |
1.21e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 118.83 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 17 AITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSID 93
Cdd:PRK07798 21 ALVCGDRRLTYAELEERANRLAHYLIAQglgPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 94 VQ-LIF--------CTLPLELRGFQ-IVSLDDiefaGRDittNGLLDNtmGIQYDT-----SNETVVPKESPsnilntsf 158
Cdd:PRK07798 101 AVaLVYerefaprvAEVLPRLPKLRtLVVVED----GSG---NDLLPG--AVDYEDalaagSPERDFGERSP-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 nlDDIAsIMFTSGTTGPQKAV----PQTFR------NHYAS---------AIGCKESLGfdrdTNWLSVLPIYHISGLSV 219
Cdd:PRK07798 164 --DDLY-LLYTGGTTGMPKGVmwrqEDIFRvllggrDFATGepiedeeelAKRAAAGPG----MRRFPAPPLMHGAGQWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 220 LLRAVIEGFTVRI--VDKFNAEQILTMIKNERITHISLV------PqtlnwlMQQGLH--EPYNLQKILL---GGAKLSA 286
Cdd:PRK07798 237 AFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVgdamarP------LLDALEarGPYDLSSLFAiasGGALFSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 287 TmIETALQYNLP---IYNSFGMTETCSQ-FLTATPEMLHARPDTVGM-PSANVDVKIKNPNKEGHGEL-MI-KGANVMNG 359
Cdd:PRK07798 311 S-VKEALLELLPnvvLTDSIGSSETGFGgSGTVAKGAVHTGGPRFTIgPRTVVLDEDGNPVEPGSGEIgWIaRRGHIPLG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 360 YlY--PTDLTGTFE--NG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDT 433
Cdd:PRK07798 390 Y-YkdPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDER 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446270502 434 WGQ-VPKLYFVSE-SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:PRK07798 469 WGQeVVAVVQLREgARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
15-489 |
1.94e-28 |
|
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: 117.58 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 15 HIAITDGQESYTYQNLYCEASLLAKRLK---AYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKS 91
Cdd:cd17656 4 AVAVVFENQKLTYRELNERSNQLARFLRekgVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 92 IDVQLIF----CTLPLELRGFQIVSLDDIEFagrdittnglldntmgiqydtsnetvvpKESPSNIlNTSFNLDDIASIM 167
Cdd:cd17656 84 SGVRVVLtqrhLKSKLSFNKSTILLEDPSIS----------------------------QEDTSNI-DYINNSDDLLYII 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 168 FTSGTTGPQKAVPQTFRNhyasaigCKESLGFDRD-TNWLSVLPIYHISGLSV------LLRAVIEGFTVRIVD---KFN 237
Cdd:cd17656 135 YTSGTTGKPKGVQLEHKN-------MVNLLHFEREkTNINFSDKVLQFATCSFdvcyqeIFSTLLSGGTLYIIReetKRD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLvPQTLnWLMQQGLHE-----PYNLQKILLGGAKL--SATMIETALQYNLPIYNSFGMTET-C 309
Cdd:cd17656 208 VEQLFDLVKRHNIEVVFL-PVAF-LKFIFSEREfinrfPTCVKHIITAGEQLviTNEFKEMLHEHNVHLHNHYGPSEThV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 310 SQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKEGH-----GELMIKGANVMNGYLYPTDLTGT--FENGY------FN 376
Cdd:cd17656 286 VTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQpqgivGELYISGASVARGYLNRQELTAEkfFPDPFdpnermYR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAY 456
Cdd:cd17656 366 TGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREY 445
|
490 500 510
....*....|....*....|....*....|...
gi 446270502 457 LSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17656 446 LAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
161-489 |
3.22e-28 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 117.96 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK--ESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEG----FTVRIVD 234
Cdd:PRK05620 181 TTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRttDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGtplvFPGPDLS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 235 kfnAEQILTMIKNE--RITHisLVPQTLNWLMQQGLHEP---YNLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTET 308
Cdd:PRK05620 261 ---APTLAKIIATAmpRVAH--GVPTLWIQLMVHYLKNPperMSLQEIYVGGSAVPPILIKAWEErYGVDVVHVWGMTET 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 CSQFLTATP------EMLHARPDTVGMPSANVDVKIKNPNK--EGH----GELMIKGANVMNGYLYPTDLTG-----TF- 370
Cdd:PRK05620 336 SPVGTVARPpsgvsgEARWAYRVSQGRFPASLEYRIVNDGQvmESTdrneGEIQVRGNWVTASYYHSPTEEGggaasTFr 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 371 ------------ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVP 438
Cdd:PRK05620 416 gedvedandrftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERP 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446270502 439 KLYFVSESDISKA-----QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05620 496 LAVTVLAPGIEPTretaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
6-491 |
4.16e-28 |
|
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: 116.25 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 6 YKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLkayQQSRVGLyidnsiQSIILIHAcwlaNIEIAMIntrltpnem 85
Cdd:cd17653 4 ERIAAAHPDAVAVESLGGSLTYGELDAASNALANRL---LQLGVVP------GDVVPLLS----DRSLEML--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 86 tnqmksidvqliFCTLPLELRGFQIVSLDDIEFAGRdittnglldntMGIQYDTSNETVvpkespsnILNTSfNLDDIAS 165
Cdd:cd17653 62 ------------VAILAILKAGAAYVPLDAKLPSAR-----------IQAILRTSGATL--------LLTTD-SPDDLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVPQTFRN--HYASA------------IGCKESLGFDrdtnwlsvlpiyhiSGLSVLLRAVIEGFTVR 231
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRGvlNYVSQpparldvgpgsrVAQVLSIAFD--------------ACIGEIFSTLCNGGTLV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 232 IVDkfNAEQILTMIKNERITHISlvPQTLNWLMQQGLhePyNLQKILLGGAKLSATMIETALQyNLPIYNSFGMTE-TCS 310
Cdd:cd17653 176 LAD--PSDPFAHVARTVDALMST--PSILSTLSPQDF--P-NLKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTEcTIS 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 qflTATPEMLHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLT------GTFENG--YFNT 377
Cdd:cd17653 248 ---STMTELLPGQPVTIGKPIPNSTCYILDADLQpvpegVVGEICISGVQVARGYLGNPALTaskfvpDPFWPGsrMYRT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 378 GDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQF-PGISDAVCVGHPDdtwgqvpKLY-FVSESDISKAQLIA 455
Cdd:cd17653 325 GDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAAAIVVNG-------RLVaFVTPETVDVDGLRS 397
|
490 500 510
....*....|....*....|....*....|....*.
gi 446270502 456 YLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd17653 398 ELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
137-489 |
1.26e-27 |
|
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: 115.78 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 137 YDTSNETVVP---KESPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLG--FDRDTNWLSVLPI 211
Cdd:cd17639 61 YATLGEDALIhslNETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 212 YHISGLSV----LLRAVIEGF-TVR-IVDKFNAE-----------------QILTMIK---NERITHISLVPQTLNWL-- 263
Cdd:cd17639 141 AHIFELAAenvcLYRGGTIGYgSPRtLTDKSKRGckgdltefkptlmvgvpAIWDTIRkgvLAKLNPMGGLKRTLFWTay 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 264 ------MQQGLHEPY---------------NLQKILLGGAKLSAtmiETALQYNL---PIYNSFGMTETCSQFLTATPEm 319
Cdd:cd17639 221 qsklkaLKEGPGTPLldelvfkkvraalggRLRYMLSGGAPLSA---DTQEFLNIvlcPVIQGYGLTETCAGGTVQDPG- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 320 lHARPDTVGMPSANVDVKIKNPNKEGH--------GELMIKGANVMNGYLYPTDLTGT--FENGYFNTGDIAEIDHEGYV 389
Cdd:cd17639 297 -DLETGRVGPPLPCCEIKLVDWEEGGYstdkppprGEILIRGPNVFKGYYKNPEKTKEafDGDGWFHTGDIGEFHPDGTL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 390 MIYDRRKDLI-ISGGENIYPYQIETVAKQFPgISDAVCV-GHPDDTW---------GQVPKL---YFVSESD----ISKA 451
Cdd:cd17639 376 KIIDRKKDLVkLQNGEYIALEKLESIYRSNP-LVNNICVyADPDKSYpvaivvpneKHLTKLaekHGVINSEweelCEDK 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446270502 452 QLIAYLSQHLAKYKVPKHFEKVDTLPY---------------TSTGKLQRNKL 489
Cdd:cd17639 455 KLQKAVLKSLAETARAAGLEKFEIPQGvvlldeewtpenglvTAAQKLKRKEI 507
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
5-489 |
2.99e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 114.70 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQqnGHHIAITDGQESYTYQNLYCEASLLAKRL-----KAYQQSRVGLyiDNSIQSIILIHAcwLANIEIAMINTR 79
Cdd:PRK10946 31 LTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLrrqgiKPGDTALVQL--GNVAEFYITFFA--LLKLGVAPVNAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 80 LTPN--EMTNQMKSIDVQLIFC--------------TLPLELRGFQIVSLDDiefagrDITTNGLLDNTMgiqydTSNET 143
Cdd:PRK10946 105 FSHQrsELNAYASQIEPALLIAdrqhalfsdddflnTLVAEHSSLRVVLLLN------DDGEHSLDDAIN-----HPAED 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 144 VVPKESPSnilntsfnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV--LL 221
Cdd:PRK10946 174 FTATPSPA---------DEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSpgAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 222 RAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLN-WLMQ----QGLHEPYNLQKILLGGAKLSATM-------I 289
Cdd:PRK10946 245 GVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSlWLQAiaegGSRAQLASLKLLQVGGARLSETLarripaeL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 290 ETALQynlpiyNSFGMTETCSQF--LTATPEMLHArpdTVGMP-SANVDVKIK----NPNKEGH-GELMIKGANVMNGYl 361
Cdd:PRK10946 325 GCQLQ------QVFGMAEGLVNYtrLDDSDERIFT---TQGRPmSPDDEVWVAdadgNPLPQGEvGRLMTRGPYTFRGY- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 362 Y--PTDLTGTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVP 438
Cdd:PRK10946 395 YksPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKS 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446270502 439 KLYFVSESDISKAQLIAYL-SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK10946 475 CAFLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
8-489 |
4.46e-27 |
|
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: 115.72 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLAN-----IEIAMintr 79
Cdd:COG1020 485 QAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALgvgPGDLVGVCLERSLEMVVALLAVLKAGaayvpLDPAY---- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 80 ltPNEMTNQM-KSIDVQLIFCTLPLELR----GFQIVSLDDIEFAgrdittnglldntmgiQYDTSNETVVPkeSPsnil 154
Cdd:COG1020 561 --PAERLAYMlEDAGARLVLTQSALAARlpelGVPVLALDALALA----------------AEPATNPPVPV--TP---- 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 155 ntsfnlDDIASIMFTSGTTGPQKAVPQTFRN--HYASAIGckESLGFDRDTNWLSVLPIyhiS-GLSV--LLRAVIEGFT 229
Cdd:COG1020 617 ------DDLAYVIYTSGSTGRPKGVMVEHRAlvNLLAWMQ--RRYGLGPGDRVLQFASL---SfDASVweIFGALLSGAT 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 230 VRIVDK---FNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILLGGAKLSATMIETALQY--NLPIYNSFG 304
Cdd:COG1020 686 LVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYG 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 305 MTET--CSQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKE----G-HGELMIKGANVMNGYLYPTDLTGT-FENGYFN 376
Cdd:COG1020 766 PTETtvDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQpvpvGvPGELYIGGAGLARGYLNRPELTAErFVADPFG 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 --------TGDIA------EIDHEGyvmiydrRKD--LIISG-----GEniypyqIETVAKQFPGISDAVCVGHPDdtwG 435
Cdd:COG1020 846 fpgarlyrTGDLArwlpdgNLEFLG-------RADdqVKIRGfrielGE------IEAALLQHPGVREAVVVARED---A 909
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446270502 436 QVPKL---YFVSE--SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG1020 910 PGDKRlvaYVVPEagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
36-431 |
5.34e-27 |
|
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: 114.23 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 36 LLAKRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCTlplelRGFQIVSLDD 115
Cdd:cd05927 22 LRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD-----AGVKVYSLEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 116 IEFAGRDIttnglldntmgiqydtsNETVVPKEspsnilntsfnLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKE 195
Cdd:cd05927 97 FEKLGKKN-----------------KVPPPPPK-----------PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 196 SLG----FDRDTNWLSVLPIYHIsglsvLLRAVIE-----GFTVRIVDKfNAEQILTMIKNERITHISLVPQTLN----- 261
Cdd:cd05927 149 ILEilnkINPTDVYISYLPLAHI-----FERVVEAlflyhGAKIGFYSG-DIRLLLDDIKALKPTVFPGVPRVLNriydk 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 262 -------------WLMQQGL-HEPYNLQK---------------------------ILLGGAKLSATmIETALQYNL--P 298
Cdd:cd05927 223 ifnkvqakgplkrKLFNFALnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPE-VLEFLRVALgcP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 IYNSFGMTETCS-QFLTATPEMlhaRPDTVGMPSANVDVKIKN-PNKE-------GHGELMIKGANVMNGYLYPTDLT-G 368
Cdd:cd05927 302 VLEGYGQTECTAgATLTLPGDT---SVGHVGGPLPCAEVKLVDvPEMNydakdpnPRGEVCIRGPNVFSGYYKDPEKTaE 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446270502 369 TF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAKQFPGISDA-----------VCVGHPD 431
Cdd:cd05927 379 ALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIfvygdslksflVAIVVPD 454
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-489 |
6.83e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 113.68 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 1 MDFW--LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAM 75
Cdd:PRK06164 10 DTLAslLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQgvrRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 76 INTRLTPNE--------------MTNQMKSIDVQLIFCTLP----LELRGFQIVslddiefagrDITTNGLLDNTMGiqy 137
Cdd:PRK06164 90 VNTRYRSHEvahilgrgrarwlvVWPGFKGIDFAAILAAVPpdalPPLRAIAVV----------DDAADATPAPAPG--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 138 DTSNETVVPKESPSNILNTSFNLDDIASIMFT-SGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISG 216
Cdd:PRK06164 157 ARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 217 LSVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQ-GLHEPYNLQKiLLGGAKLSATMIE---TA 292
Cdd:PRK06164 237 FSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTaGERADFPSAR-LFGFASFAPALGElaaLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 293 LQYNLPIYNSFGMTETCSQFL--TATPEMLHaRPDTVGMP-SANVDVKIKNPNKEG------HGELMIKGANVMNGYLYP 363
Cdd:PRK06164 316 RARGVPLTGLYGSSEVQALVAlqPATDPVSV-RIEGGGRPaSPEARVRARDPQDGAllpdgeSGEIEIRAPSLMRGYLDN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 364 TDLTGT--FENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDtwGQVPKLY 441
Cdd:PRK06164 395 PDATARalTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTVPVA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446270502 442 FVSESDISKAQ---LIAYLSQHLAKYKVPKHFEKVDTLPYTSTG---KLQRNKL 489
Cdd:PRK06164 473 FVIPTDGASPDeagLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
16-489 |
1.12e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 112.79 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 16 IAITDGQESYTYQNLYCEASLLAKRLK---AYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSI 92
Cdd:PRK13390 16 VIVAETGEQVSYRQLDDDSAALARVLYdagLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 93 DVQLIFCTL-----------PLELRgfqivslddIEFAGRditTNGLLDntmgiqYDTSNETVVPK--ESPSNilntsfn 159
Cdd:PRK13390 96 GARVLVASAaldglaakvgaDLPLR---------LSFGGE---IDGFGS------FEAALAGAGPRltEQPCG------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 160 lddiASIMFTSGTTGPQKAVPQTFRNHYASAIG------CKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIV 233
Cdd:PRK13390 151 ----AVMLYSSGTTGFPKGIQPDLPGRDVDAPGdpivaiARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 234 DKFNAEQILTMIKNERITHISLVPQTLNWLMQ-----QGLHEPYNLQKILLGGAKLSATMIETALQYNLPI-YNSFGMTE 307
Cdd:PRK13390 227 KRFDAQATLGHVERYRITVTQMVPTMFVRLLKldadvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIvYEYYSSTE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 308 TCSQFLTATPEMLhARPDTVGMpSANVDVKIknPNKEGH-------GELMIKGANVMNGYLYPTDLTGTFENG----YFN 376
Cdd:PRK13390 307 AHGMTFIDSPDWL-AHPGSVGR-SVLGDLHI--CDDDGNelpagriGTVYFERDRLPFRYLNDPEKTAAAQHPahpfWTT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWG-QVPKLYFVSE----SDISKA 451
Cdd:PRK13390 383 VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGeQVKAVIQLVEgirgSDELAR 462
|
490 500 510
....*....|....*....|....*....|....*...
gi 446270502 452 QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13390 463 ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
151-484 |
2.00e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 113.48 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 151 SNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGF- 228
Cdd:PRK08633 772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVtLWLPLLEGIk 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 229 TVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKILL---GGAKL-SATMIETALQYNLPIYNSFG 304
Cdd:PRK08633 852 VVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLvvaGAEKLkPEVADAFEEKFGIRILEGYG 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 305 MTET-------CSQFLTATPEMLHA-RPDTVGMPSANVDVKIKNPN-----KEGH-GELMIKGANVMNGYLYPTDLTG-- 368
Cdd:PRK08633 932 ATETspvasvnLPDVLAADFKRQTGsKEGSVGMPLPGVAVRIVDPEtfeelPPGEdGLILIGGPQVMKGYLGDPEKTAev 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 369 ---TFENGYFNTGDIAEIDHEGYVMIYDR--RKDLIisGGENIYPYQIE-TVAKQFPGISDAVCV-GHPDDTWG-QVPKL 440
Cdd:PRK08633 1012 ikdIDGIGWYVTGDKGHLDEDGFLTITDRysRFAKI--GGEMVPLGAVEeELAKALGGEEVVFAVtAVPDEKKGeKLVVL 1089
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446270502 441 YFVSESDISKAQLIAyLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:PRK08633 1090 HTCGAEDVEELKRAI-KESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
26-425 |
2.46e-26 |
|
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: 110.43 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 26 TYQNLYCEASLLAKRLKAY----QQSRVGLYIDNSIQSIILIHACWLAN-----IEIAMintrltPNEMTNQM-KSIDVQ 95
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAggvgPGDRVAVLLERSAELVVAILAVLKAGaayvpLDPAY------PAERLAFIlEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 96 LIFCTLPLELRGFQIVSLDdiefagrdittnGLLDNTMGIQYDTSNETVVPKESPSNilntsfnlDDIASIMFTSGTTGP 175
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPV------------ILLDPLELAALDDAPAPPPPDAPSGP--------DDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 176 QKAVPQTFR---NHYASAIGCKESLGFDRdtnWLSVLPIYHisGLSV--LLRAVIEGFTVRIVD----KFNAEQILTMIK 246
Cdd:TIGR01733 135 PKGVVVTHRslvNLLAWLARRYGLDPDDR---VLQFASLSF--DASVeeIFGALLAGATLVVPPedeeRDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 247 NERITHISLVPQTLNWLMQQGLHEPYNLQKILLGGAKLSATMIETALQ--YNLPIYNSFGMTET---CSQFLTATPEMLH 321
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRArgPGARLINLYGPTETtvwSTATLVDPDDAPR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 322 ARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLT----------GTFENGYFNTGDIAEIDHE 386
Cdd:TIGR01733 290 ESPVPIGRPLANTRLYVLDDDLRpvpvgVVGELYIGGPGVARGYLNRPELTaerfvpdpfaGGDGARLYRTGDLVRYLPD 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446270502 387 GYVMIYDRRKDLI-ISG-----GEniypyqIETVAKQFPGISDAV 425
Cdd:TIGR01733 370 GNLEFLGRIDDQVkIRGyrielGE------IEAALLRHPGVREAV 408
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-483 |
5.81e-26 |
|
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: 108.62 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIAsIMFTSGTTGPQKAVpqTFRNH--YASAIGckeSLGFDR-----------------DTNWLSVLPIYHISGLSVLL 221
Cdd:cd05924 4 DDLY-ILYTGGTTGMPKGV--MWRQEdiFRMLMG---GADFGTgeftpsedahkaaaaaaGTVMFPAPPLMHGTGSWTAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 222 RAVIEGFTVRIVD-KFNAEQILTMIKNERITHISLV------PqTLNWLMQQGLHEPYNLQKILLGGAKLSATMIET--A 292
Cdd:cd05924 78 GGLLGGQTVVLPDdRFDPEEVWRTIEKHKVTSMTIVgdamarP-LIDALRDAGPYDLSSLFAISSGGALLSPEVKQGllE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 293 LQYNLPIYNSFGMTETCSQFLTATPEMLH-ARPDTVGMPSANV---DVKIKNPNKEGHGELMIKGaNVMNGYLYPTDLTG 368
Cdd:cd05924 157 LVPNITLVDAFGSSETGFTGSGHSAGSGPeTGPFTRANPDTVVlddDGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 369 -TFE--NG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ--VPKLY 441
Cdd:cd05924 236 eTFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQevVAVVQ 315
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446270502 442 FVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:cd05924 316 LREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
161-488 |
2.25e-25 |
|
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: 108.60 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRN--HYASAIGCKESLGF-DRdtnWLSVLPIYHISGLS----VLLRAVIEGFTvriv 233
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHANllHQIRSLSDIVPPQPgDR---FLSILPIWHSYERSaeyfIFACGCSQAYT---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 234 dkfnaeQILTM---IKNERITHISLVP---QTLNWLMQQGLHEPYNLQKILLGGAkLSATMIETAL-------QY----- 295
Cdd:cd17640 161 ------SIRTLkddLKRVKPHYIVSVPrlwESLYSGIQKQVSKSSPIKQFLFLFF-LSGGIFKFGIsgggalpPHvdtff 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 296 ---NLPIYNSFGMTETcSQFLTATpemLHARP--DTVGMPSANVDVKIKNPN------KEGHGELMIKGANVMNGYLYPT 364
Cdd:cd17640 234 eaiGIEVLNGYGLTET-SPVVSAR---RLKCNvrGSVGRPLPGTEIKIVDPEgnvvlpPGEKGIVWVRGPQVMKGYYKNP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 365 DLTGTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDLII-SGGENIYPYQIETVAKQFPGISDAVCVGH----------PD 431
Cdd:cd17640 310 EATSKVldSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQdqkrlgalivPN 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446270502 432 ----DTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKY----KVPKHFEKVDTL-----PY------TSTGKLQRNK 488
Cdd:cd17640 390 feelEKWAKESGVKLANDrsQLLASKKVLKLYKNEIKDEisnrPGFKSFEQIAPFalleePFiengemTQTMKIKRNV 467
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
9-489 |
3.23e-25 |
|
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: 107.72 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 9 AQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLAnieiamintrltpnem 85
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLgldAGDPVVVYGHKSPDAIAAFLAALKA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 86 tnqmksidvqlifctlplelrGFQIVSLDDIEFAGRdittnglldntmgiqydtsNETVVPKESPSNILNTSfnlDDIAS 165
Cdd:cd05945 65 ---------------------GHAYVPLDASSPAER-------------------IREILDAAKPALLIADG---DDNAY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVPQTFRN--HYASAI------------GCKESLGFDrdtnwLSVLPIYHisglsvllrAVIEGFTVR 231
Cdd:cd05945 102 IIFTSGSTGRPKGVQISHDNlvSFTNWMlsdfplgpgdvfLNQAPFSFD-----LSVMDLYP---------ALASGATLV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 232 IVDK---FNAEQILTMIKNERITHISLVPQTLNWLMQQGL----HEPyNLQKILLGGAKLSATMIEtALQYNLP---IYN 301
Cdd:cd05945 168 PVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTftpeSLP-SLRHFLFCGEVLPHKTAR-ALQQRFPdarIYN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 302 SFGMTET---CSQFlTATPEMLHA-RPDTVGMPSANVDVKIKN----PNKEGH-GELMIKGANVMNGYLYPTDLTGTF-- 370
Cdd:cd05945 246 TYGPTEAtvaVTYI-EVTPEVLDGyDRLPIGYAKPGAKLVILDedgrPVPPGEkGELVISGPSVSKGYLNNPEKTAAAff 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 371 -ENGY--FNTGDIAEIDHEGYVmIYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE- 445
Cdd:cd05945 325 pDEGQraYRTGDLVRLEADGLL-FYRGRLDFQVKlNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKp 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446270502 446 -SDISKAQLI-AYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05945 404 gAEAGLTKAIkAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
150-489 |
3.49e-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: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 150 PSNILNTSfnlDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLsvlpIYHISG--LSV--LLRAVI 225
Cdd:cd17643 85 PSLLLTDP---DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdFSVweIWGALL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 226 EGFTVRIVDKFNA---EQILTMIKNERITHISLVPQTLNWLMQ---QGLHEPYNLQKILLGGAKLSATMIET-ALQYNLP 298
Cdd:cd17643 158 HGGRLVVVPYEVArspEDFARLLRDEGVTVLNQTPSAFYQLVEaadRDGRDPLALRYVIFGGEALEAAMLRPwAGRFGLD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 ---IYNSFGMTETC--SQFLTATPEMLHARPDTV---GMPSANVDVKIKNPNKE---GHGELMIKGANVMNGYLYPTDLT 367
Cdd:cd17643 238 rpqLVNMYGITETTvhVTFRPLDAADLPAAAASPigrPLPGLRVYVLDADGRPVppgVVGELYVSGAGVARGYLGRPELT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 GT------FENG---YFNTGDIA------EIDHEGyvmiydRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDD 432
Cdd:cd17643 318 AErfvanpFGGPgsrMYRTGDLArrlpdgELEYLG------RADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446270502 433 TWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17643 392 PGDTRLVAYVVadDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-491 |
4.53e-24 |
|
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: 104.52 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DRDTNWLSVLP------IYHISG------LSVLLRAvieG 227
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLrPEDSFWNAADPgwayglYYAITGplalghPTILLEG---G 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 228 FTVrivdkfnaEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYN----LQKILLGGAKLSATMIE-TALQYNLPIYNS 302
Cdd:cd05973 165 FSV--------ESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARpkgrLRRVSSAGEPLTPEVIRwFDAALGVPIHDH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 303 FGMTE----TCSQFLTATPemLHARPDTVGMPSANVDVKIKNPNKEGHGELMIKGANVMNGYL-----YPTDLTGTFENG 373
Cdd:cd05973 237 YGQTElgmvLANHHALEHP--VHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrgYQLPDTPAIDGG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-----SESDI 448
Cdd:cd05973 315 YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgghEGTPA 394
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446270502 449 SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05973 395 LADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
7-489 |
6.26e-24 |
|
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: 104.35 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 7 KQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKA---YQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRlTPN 83
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRArgvGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA-YPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 84 EMTNQMKSiDVQLIFCTLPLELRGfqivslddiEFAGRDITtnGLLDNTMGIQYDTSNETVVPKespsnilntsfNLDDI 163
Cdd:cd17651 82 ERLAFMLA-DAGPVLVLTHPALAG---------ELAVELVA--VTLLDQPGAAAGADAEPDPAL-----------DADDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 164 ASIMFTSGTTGPQKAVPQTFRN-------HYASAIGCKE-------SLGFDrdtnwLSVLPIyhisgLSVLLRA---VIE 226
Cdd:cd17651 139 AYVIYTSGSTGRPKGVVMPHRSlanlvawQARASSLGPGartlqfaGLGFD-----VSVQEI-----FSTLCAGatlVLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 GFTVRivdkFNAEQILTMIKNERITHISLVPQTLNWLMQQGLH---EPYNLQKILLGGAKLSATMIETALQYNLP---IY 300
Cdd:cd17651 209 PEEVR----TDPPALAAWLDEQRISRVFLPTVALRALAEHGRPlgvRLAALRYLLTGGEQLVLTEDLREFCAGLPglrLH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 301 NSFGMTETcsQFLTA--TPEMLHARPDT--VGMPSANVDVKIKNPNKE----GH-GELMIKGANVMNGYLYPTDLT---- 367
Cdd:cd17651 285 NHYGPTET--HVVTAlsLPGDPAAWPAPppIGRPIDNTRVYVLDAALRpvppGVpGELYIGGAGLARGYLNRPELTaerf 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 --GTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV 443
Cdd:cd17651 363 vpDPFVPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446270502 444 S--ESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17651 443 GdpEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
273-428 |
7.38e-24 |
|
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: 104.75 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 273 NLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPEMLhaRPDTVGMPSANVDVKIKNPNKEGHGELMIK 352
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAY--RLLSCGKALPGCKTKIHNPDADGIGEICFW 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 353 GANVMNGYLYPTDLT--GTFENGYFNTGDIAEIDHEGYVMIYDRRKDLII-SGGENIYPYQIE-TVAKQFPGISDAVCVG 428
Cdd:cd05933 399 GRHVFMGYLNMEDKTeeAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIEdAVKKELPIISNAMLIG 478
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
26-483 |
1.52e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 104.66 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 26 TYQNLYCEASLLAKRLKAY--QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCT--- 100
Cdd:PRK06814 660 TYRKLLTGAFVLGRKLKKNtpPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSraf 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 101 --------LPLEL-RGFQIVSLDDIEfagrdiTTNGLLDNTMGIQYDTSNETVVPKESPsnilntsfnlDDIASIMFTSG 171
Cdd:PRK06814 740 iekarlgpLIEALeFGIRIIYLEDVR------AQIGLADKIKGLLAGRFPLVYFCNRDP----------DDPAVILFTSG 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 172 TTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTV---------RIVDKF----N 237
Cdd:PRK06814 804 SEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGgLVLPLLSGVKVflypsplhyRIIPELiydtN 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AeQIL----TMIKN-ERITHislvpqtlnwlmqqglhePYN---LQKILLGGAKLSATMIET-ALQYNLPIYNSFGMTET 308
Cdd:PRK06814 884 A-TILfgtdTFLNGyARYAH------------------PYDfrsLRYVFAGAEKVKEETRQTwMEKFGIRILEGYGVTET 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 CSQFLTATPemLHARPDTVGMPSANVDVKI-KNPNKEGHGELMIKGANVMNGYLYpTDLTGTFE---NGYFNTGDIAEID 384
Cdd:PRK06814 945 APVIALNTP--MHNKAGTVGRLLPGIEYRLePVPGIDEGGRLFVRGPNVMLGYLR-AENPGVLEppaDGWYDTGDIVTID 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 385 HEGYVMIYDRRKDLIISGGENIYPYQIETVAKQF-PGISDAVcVGHPDDTWGQVPKLyFVSESDISKAQLIAYLSQH-LA 462
Cdd:PRK06814 1022 EEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAA-VSIPDARKGERIIL-LTTASDATRAAFLAHAKAAgAS 1099
|
490 500
....*....|....*....|.
gi 446270502 463 KYKVPKHFEKVDTLPYTSTGK 483
Cdd:PRK06814 1100 ELMVPAEIITIDEIPLLGTGK 1120
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
162-489 |
2.13e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 103.30 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:PRK06155 181 DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGF 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 LTMIKNERITHISLVPQTLNWLMQQ--GLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPEm 319
Cdd:PRK06155 261 WPAVRRHGATVTYLLGAMVSILLSQpaRESDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGS- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 320 lhARPDTVGMPSANVDVKIKNPNKEG-----HGELMIKGAN---VMNGYL-YPTDLTGTFENGYFNTGDIAEIDHEGYVM 390
Cdd:PRK06155 340 --QRPGSMGRLAPGFEARVVDEHDQElpdgePGELLLRADEpfaFATGYFgMPEKTVEAWRNLWFHTGDRVVRDADGWFR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 391 IYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKYKVPK 468
Cdd:PRK06155 418 FVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRdgTALEPVALVRHCEPRLAYFAVPR 497
|
330 340
....*....|....*....|.
gi 446270502 469 HFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06155 498 YVEFVAALPKTENGKVQKFVL 518
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
15-489 |
2.52e-23 |
|
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: 102.48 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 15 HIAITDGQESYTYQNLYCEASLLAKRLKA----YQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLtPNEMtnqmk 90
Cdd:cd17648 3 RVAVVYGDKRLTYRELNERANRLAHYLLSvaeiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSY-PDER----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 91 sidVQLIFctlplelrgfqivslddiefagrdittnglldntmgiqYDTSNETVVPkespsnilntsfNLDDIASIMFTS 170
Cdd:cd17648 77 ---IQFIL--------------------------------------EDTGARVVIT------------NSTDLAYAIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 171 GTTGPQKAVPQTFRnhyaSAIGCKESL-----GFDRDTNWLSVLPIYhISGLSV--LLRAVIEGFTVRIVD---KFNAEQ 240
Cdd:cd17648 104 GTTGKPKGVLVEHG----SVVNLRTSLseryfGRDNGDEAVLFFSNY-VFDFFVeqMTLALLNGQKLVVPPdemRFDPDR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 241 ILTMIKNERITHISLVPQTLNwlmQQGLHEPYNLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETcSQFLTATPEM 319
Cdd:cd17648 179 FYAYINREKVTYLSGTPSVLQ---QYDLARLPHLKRVDAAGEEFTAPVFEKLRSrFAGLIINAYGPTET-TVTNHKRFFP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 320 LHARPD-TVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLTGT--FENGY--------------FNT 377
Cdd:cd17648 255 GDQRFDkSLGRPVRNTKCYVLNDAMKrvpvgAVGELYLGGDGVARGYLNRPELTAErfLPNPFqteqerargrnarlYKT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 378 GDIAEIDHEGYVMiYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKL-----YFVSESD-ISK 450
Cdd:cd17648 335 GDLVRWLPSGELE-YLGRNDFQVKiRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkylvgYYLPEPGhVPE 413
|
490 500 510
....*....|....*....|....*....|....*....
gi 446270502 451 AQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17648 414 SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
162-491 |
4.67e-23 |
|
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: 102.12 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTGPQKAVPQTFRNHY--ASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAV-IEGFTVRIVDKFNA 238
Cdd:cd05915 154 AACGMAYTTGTTGLPKGVVYSHRALVlhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATlVGAKQVLPGPRLDP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLM--QQGLHE--PYNLQkILLGGAKLSATMIETALQYNLPIYNSFGMTE-----TC 309
Cdd:cd05915 234 ASLVELFDGEGVTFTAGVPTVWLALAdyLESTGHrlKTLRR-LVVGGSAAPRSLIARFERMGVEVRQGYGLTEtspvvVQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 310 SQFL---TATPE----MLHAR--------------PDTVGMPSANVDVKIknpnkeghgeLMIKGANVMNGYLYPTDLT- 367
Cdd:cd05915 313 NFVKshlESLSEeeklTLKAKtglpiplvrlrvadEEGRPVPKDGKALGE----------VQLKGPWITGGYYGNEEATr 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 -GTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYF-VSE 445
Cdd:cd05915 383 sALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvPRG 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446270502 446 SDISKAQLIAYLSQHLAKYK-VPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05915 463 EKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
161-489 |
7.57e-23 |
|
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: 101.39 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISG-LSVLLRAVIEGFTVrivdkFNAE 239
Cdd:cd05932 137 EQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLV-----AFAE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMI---KNERITHISLVPQTlnW-LMQQGLHEPYNLQK--ILL---------------------------GGAKLSA 286
Cdd:cd05932 212 SLDTFVedvQRARPTLFFSVPRL--WtKFQQGVQDKIPQQKlnLLLkipvvnslvkrkvlkglgldqcrlagcGSAPVPP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 287 TMIETALQYNLPIYNSFGMTETCSQFLTATPemLHARPDTVGMPSANVDVKIKNpnkegHGELMIKGANVMNG-YLYPTD 365
Cdd:cd05932 290 ALLEWYRSLGLNILEAYGMTENFAYSHLNYP--GRDKIGTVGNAGPGVEVRISE-----DGEILVRSPALMMGyYKDPEA 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 366 LTGTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAKQFPGIsDAVCV---GHPDDTWGQVPKL 440
Cdd:cd05932 363 TAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRV-EMVCVigsGLPAPLALVVLSE 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446270502 441 YFVSESDIS-KAQLIAYLSQHLAkyKVPKHFEK---------------VDTLPYTSTGKLQRNKL 489
Cdd:cd05932 442 EARLRADAFaRAELEASLRAHLA--RVNSTLDSheqlagivvvkdpwsIDNGILTPTLKIKRNVL 504
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
161-489 |
1.82e-22 |
|
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: 99.75 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQtfrNHYASAIGCKESLGFDRDTNWLSVLPIYHIS---GLSVLLRAVIEGFTVRIVDK-- 235
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAV---SHGPLAAHCQATAERYGLTPGDRELQFASFNfdgAHEQLLPPLICGACVVLRPDel 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 -FNAEQILTMIKNERITHISLVP----QTLNWLMQQGLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETcs 310
Cdd:cd17649 171 wASADELAEMVRELGVTVLDLPPaylqQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEA-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 qflTATPEMLHARPDT----VGMP--------SANVDVKIKNPNKEGH-GELMIKGANVMNGYLYPTDLTGT-------F 370
Cdd:cd17649 249 ---TVTPLVWKCEAGAaragASMPigrplggrSAYILDADLNPVPVGVtGELYIGGEGLARGYLGRPELTAErfvpdpfG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 371 ENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKlYFVSESDI 448
Cdd:cd17649 326 APGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVA-YVVLRAAA 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446270502 449 SKAQLIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17649 405 AQPELRAQLRTALRAslpdYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
154-489 |
1.10e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.47 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 154 LNTSFNLD--DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVR 231
Cdd:PRK12467 647 HNPEVALDpdNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLH 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 232 IVDK---FNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE-PYNLQKILLGGAKLSATMIET--ALQYNLPIYNSFGM 305
Cdd:PRK12467 727 LLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAlPRPQRALVCGGEALQVDLLARvrALGPGARLINHYGP 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 306 TETC--SQFLTATPEMLHARPDTVGMPSANVDVKI----KNPNKEG-HGELMIKGANVMNGYLYPTDLTGTF-------E 371
Cdd:PRK12467 807 TETTvgVSTYELSDEERDFGNVPIGQPLANLGLYIldhyLNPVPVGvVGELYIGGAGLARGYHRRPALTAERfvpdpfgA 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 372 NG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ-----VPKLYFVS 444
Cdd:PRK12467 887 DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQlvaylVPAAVADG 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446270502 445 -ESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12467 967 aEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-491 |
1.10e-21 |
|
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: 97.25 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDR-DTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD--KFN 237
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPgDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNyaRFD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHE-PYNLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTA 315
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASfDVKLREVVGAGEPLNPEVIEQVRRaWGLTIRDGYGQTETTALVGNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 316 TPEMLhaRPDTVGMPSANVDVKI----KNPNKEGHGELMI---KGANVMNGYLY-PTDLTGTFENGYFNTGDIAEIDHEG 387
Cdd:cd05974 245 PGQPV--KAGSMGRPLPGYRVALldpdGAPATEGEVALDLgdtRPVGLMKGYAGdPDKTAHAMRGGYYRTGDIAMRDEDG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLA 462
Cdd:cd05974 323 YLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyEPSPETALEIFRFSRERLA 402
|
330 340
....*....|....*....|....*....
gi 446270502 463 KYKVPKHFEKVDtLPYTSTGKLQRNKLYR 491
Cdd:cd05974 403 PYKRIRRLEFAE-LPKTISGKIRRVELRR 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-489 |
2.38e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.02 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLtPNE 84
Cdd:PRK12316 520 QVERTPEAPALAFGEETLDYAELNRRANRLAHALIERgvgPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY-PAE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 85 MTNQM-KSIDVQLIFC------TLPLElRGFQIVSLDDI--EFAGRdittnglldntmgiqydtsnetvvPKESPSniln 155
Cdd:PRK12316 599 RLAYMlEDSGVQLLLSqshlgrKLPLA-AGVQVLDLDRPaaWLEGY------------------------SEENPG---- 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 156 TSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIV-- 233
Cdd:PRK12316 650 TELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAap 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 234 -DKFNAEQILTMIKNERITHISLVPQTLNWLMQ-QGLHEPYNLQKILLGGAKLSATMIETALQyNLP---IYNSFGMTET 308
Cdd:PRK12316 730 gDHRDPAKLVELINREGVDTLHFVPSMLQAFLQdEDVASCTSLRRIVCSGEALPADAQEQVFA-KLPqagLYNLYGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 CSQFLTATPEMLHARPDTVGMPSANVDVKI----KNPNKEG-HGELMIKGANVMNGYLYPTDLTGT------FENG--YF 375
Cdd:PRK12316 809 AIDVTHWTCVEEGGDSVPIGRPIANLACYIldanLEPVPVGvLGELYLAGRGLARGYHGRPGLTAErfvpspFVAGerMY 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPddtwGQVPKLYFVSESD--ISKAQL 453
Cdd:PRK12316 889 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEggDWREAL 964
|
490 500 510
....*....|....*....|....*....|....*.
gi 446270502 454 IAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12316 965 KAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-491 |
3.58e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNE 84
Cdd:PRK12316 3066 QVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERgvgPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 85 MTNQMKSIDVQLIFCTLPLELRGFQIVSLDDIEFAGRDITTNGLLDNTMGiqydtsnetvvpkespsnilntsfnlDDIA 164
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMP--------------------------ENLA 3199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 165 SIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNA---EQI 241
Cdd:PRK12316 3200 YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWrdpALL 3279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 242 LTMIKNERITHISLVPQTLNWLMQQ-GLHEPYNLQKILLGGAKLSATMIETALQyNLPIYNSFGMTETCSQFLTATPEML 320
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLEEeDAHRCTSLKRIVCGGEALPADLQQQVFA-GLPLYNLYGPTEATITVTHWQCVEE 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 321 HARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYLYPTDLTGT------FENG--YFNTGDIAEIDHEG 387
Cdd:PRK12316 3359 GKDAVPIGRPIANRACYILDGSLEpvpvgALGELYLGGEGLARGYHNRPGLTAErfvpdpFVPGerLYRTGDLARYRADG 3438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVghpdDTWGQVPKLYFVSESDISKAQ--LIAYLSQHLAKYK 465
Cdd:PRK12316 3439 VIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLReaLKAHLKASLPEYM 3514
|
490 500
....*....|....*....|....*.
gi 446270502 466 VPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK12316 3515 VPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-491 |
4.42e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.46 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNE 84
Cdd:PRK12467 1583 QAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALgvgPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER 1662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 85 MTNQMKSIDVQLIFCTLPLELR-----GFQIVSLDDIefagrdittNGLLDNtmgiqYDTSNETVVPkeSPSNIlntsfn 159
Cdd:PRK12467 1663 LAYMIEDSGIELLLTQSHLQARlplpdGLRSLVLDQE---------DDWLEG-----YSDSNPAVNL--APQNL------ 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 160 lddiASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWL---------SVLPIYH--ISGLSVLLRAVIEgf 228
Cdd:PRK12467 1721 ----AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLqftsfafdvSVWELFWplINGARLVIAPPGA-- 1794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 229 tvrivdKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLH--EPYNLQKILLGGAKLSATMIETALQyNLP---IYNSF 303
Cdd:PRK12467 1795 ------HRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQveHPLSLRRVVCGGEALEVEALRPWLE-RLPdtgLFNLY 1867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 304 GMTET--------CSQfltATPEMLHARPdtVGMPSANVDVKIK----NPNKEG-HGELMIKGANVMNGYLYPTDLT--- 367
Cdd:PRK12467 1868 GPTETavdvthwtCRR---KDLEGRDSVP--IGQPIANLSTYILdaslNPVPIGvAGELYLGGVGLARGYLNRPALTaer 1942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 ------GTFENGYFNTGDIAE------------IDHEgyVMIYDRRKDLiisgGEniypyqIETVAKQFPGISDAVCVGH 429
Cdd:PRK12467 1943 fvadpfGTVGSRLYRTGDLARyradgvieylgrIDHQ--VKIRGFRIEL----GE------IEARLREQGGVREAVVIAQ 2010
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446270502 430 pDDTWGQ------VPKLYFVSESDI----SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK12467 2011 -DGANGKqlvayvVPTDPGLVDDDEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
8-489 |
6.31e-20 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 92.11 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLAnieiamintrltpne 84
Cdd:cd17644 9 QVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLgvkSESLVGICVERSLEMIIGLLAILKA--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 85 mtnqmksidvqlifctlplelrGFQIVSLDdiefagrdittnglldntmgIQYDTSNETVVPKESPSNILNTsfNLDDIA 164
Cdd:cd17644 74 ----------------------GGAYVPLD--------------------PNYPQERLTYILEDAQISVLLT--QPENLA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 165 SIMFTSGTTGPQKAV---PQTFRNHYASAI-----------GCKESLGFDrdtnwLSVLPIYH--ISGLSVLLRAViEGF 228
Cdd:cd17644 110 YVIYTSGSTGKPKGVmieHQSLVNLSHGLIkeygitssdrvLQFASIAFD-----VAAEEIYVtlLSGATLVLRPE-EMR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 229 tvrivdkFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE----PYNLQKILLGGAKLSATMIET---ALQYNLPIYN 301
Cdd:cd17644 184 -------SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStidlPSSLRLVIVGGEAVQPELVRQwqkNVGNFIQLIN 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 302 SFGMTE-----TCSQFLTATPEMLHARPdtVGMPSANVDVKIKNPNK-----EGHGELMIKGANVMNGYLYPTDLT---- 367
Cdd:cd17644 257 VYGPTEatiaaTVCRLTQLTERNITSVP--IGRPIANTQVYILDENLqpvpvGVPGELHIGGVGLARGYLNRPELTaekf 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 ------GTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLY 441
Cdd:cd17644 335 ishpfnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446270502 442 FV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17644 415 IVphYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
161-489 |
1.28e-19 |
|
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: 91.22 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRdtnWLSVLPIYHIS-GLSV--LLRAVIEGFTVRIVDkfN 237
Cdd:cd12115 105 DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE---LAGVLASTSICfDLSVfeLFGPLATGGKVVLAD--N 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHePYNLQKILLGGAKLSATMIETaLQYNLP---IYNSFGMTETcSQFLT 314
Cdd:cd12115 180 VLALPDLPAAAEVTLINTVPSAAAELLRHDAL-PASVRVVNLAGEPLPRDLVQR-LYARLQverVVNLYGPSED-TTYST 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 ATPEMLHA-RPDTVGMPSANVDVKI----KNPNKEG-HGELMIKGANVMNGYLYPTDLTGT------FENG--YFNTGDI 380
Cdd:cd12115 257 VAPVPPGAsGEVSIGRPLANTQAYVldraLQPVPLGvPGELYIGGAGVARGYLGRPGLTAErflpdpFGPGarLYRTGDL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 381 AEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE--SDISKAQLIAYLS 458
Cdd:cd12115 337 VRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLG 416
|
330 340 350
....*....|....*....|....*....|.
gi 446270502 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12115 417 TRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
160-486 |
2.91e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 90.72 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 160 LDDIASIMFTSGTTG-P------QKAVPQtfrnHYASAigcKESLGF-DRDTNWLSVLPIYhISGLSV-----LLRAVie 226
Cdd:PRK04319 204 REDGAILHYTSGSTGkPkgvlhvHNAMLQ----HYQTG---KYVLDLhEDDVYWCTADPGW-VTGTSYgifapWLNGA-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 gftVRIVD--KFNAEQILTMIKNERITHISLVPQTLNWLMQQG--LHEPYN---LQKILLGGAKLSATMIETALQ-YNLP 298
Cdd:PRK04319 274 ---TNVIDggRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddLVKKYDlssLRHILSVGEPLNPEVVRWGMKvFGLP 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 IYNSFGMTETCSQFLTATPEMlHARPDTVGMPSANVDVKI-------KNPNKEGhgELMIKGA--NVMNGYLY-PTDLTG 368
Cdd:PRK04319 351 IHDNWWMTETGGIMIANYPAM-DIKPGSMGKPLPGIEAAIvddqgneLPPNRMG--NLAIKKGwpSMMRGIWNnPEKYES 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 369 TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLyFVS---- 444
Cdd:PRK04319 428 YFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKA-FVAlrpg 506
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446270502 445 --ESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK04319 507 yePSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
166-486 |
3.63e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 89.33 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVPQTFRN------HYASAIGCKEslgfdrDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFNA 238
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEidreieAYNEALNCEQ------DETPIVACPVTHSYGLiCGVLAALTRGSKPVIITNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERiTHISLVPQTLNWLMQQGLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTET-CsqfLTATP 317
Cdd:PRK08308 180 KFALNILRNTP-QHILYAVPLMLHILGRLLPGTFQFHAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAgC---VSICP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 318 EMlhARPDTVGMPSANVDVKIkNPNKEGHGELMIKganvmngylyptdlTGTFEngyFNTGDIAEIDHEGYVMIYDRRKD 397
Cdd:PRK08308 256 DM--KSHLDLGNPLPHVSVSA-GSDENAPEEIVVK--------------MGDKE---IFTKDLGYKSERGTLHFMGRMDD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 398 LIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLP 477
Cdd:PRK08308 316 VINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIP 395
|
....*....
gi 446270502 478 YTSTGKLQR 486
Cdd:PRK08308 396 KNANGKVSR 404
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
161-489 |
7.72e-19 |
|
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: 88.85 E-value: 7.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNA-- 238
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELlp 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 -EQILTMIKNERITHISLVPQTLNWLMQQGLHEpynLQKILLGGAKLSATMIETALQYNLpIYNSFGMTET--CSQFLTA 315
Cdd:cd17652 173 gEPLADLLREHRITHVTLPPAALAALPPDDLPD---LRTLVVAGEACPAELVDRWAPGRR-MINAYGPTETtvCATMAGP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 316 TPEMlhaRPDTVGMPSANVDVKIKNPNKE----G-HGELMIKGANVMNGYLYPTDLT---------GTFENGYFNTGDIA 381
Cdd:cd17652 249 LPGG---GVPPIGRPVPGTRVYVLDARLRpvppGvPGELYIAGAGLARGYLNRPGLTaerfvadpfGAPGSRMYRTGDLA 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 382 EIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQ 459
Cdd:cd17652 326 RWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAE 405
|
330 340 350
....*....|....*....|....*....|
gi 446270502 460 HLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17652 406 RLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
161-486 |
3.42e-18 |
|
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: 87.29 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFT---------V 230
Cdd:cd05931 149 DDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLiGGLLTPLYSGGPsvlmspaafL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 231 RivdkfNAEQILTMIKNERITHiSLVP-----QTLNWLMQQGLhEPYNLQ--KILLGGAK--LSATM---IETALQYNLP 298
Cdd:cd05931 229 R-----RPLRWLRLISRYRATI-SAAPnfaydLCVRRVRDEDL-EGLDLSswRVALNGAEpvRPATLrrfAEAFAPFGFR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 ---IYNSFGMTETC-------------SQFLTATPEMLHARPDT-----------VGMPSANVDVKIKNPN-----KEGH 346
Cdd:cd05931 302 peaFRPSYGLAEATlfvsggppgtgpvVLRVDRDALAGRAVAVAaddpaarelvsCGRPLPDQEVRIVDPEtgrelPDGE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 347 -GELMIKGANVMNGYLYPTDLT-GTF-------ENGYFNTGDIAEIdHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQ 417
Cdd:cd05931 382 vGEIWVRGPSVASGYWGRPEATaETFgalaatdEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 418 FPG---ISDAVCVGHPDDtwgQVPKLYFVSESDISK-----AQLIAYLSQHLAK-YKVPKH---FEKVDTLPYTSTGKLQ 485
Cdd:cd05931 461 AHPalrPGCVAAFSVPDD---GEERLVVVAEVERGAdpadlAAIAAAIRAAVAReHGVAPAdvvLVRPGSIPRTSSGKIQ 537
|
.
gi 446270502 486 R 486
Cdd:cd05931 538 R 538
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
106-429 |
4.61e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.02 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 106 RGFQIVSLDDIEFagrdITTNGLLDNTMGIQYDTSNETVVPKESPSNIlnTSFNLDDIASIMFTSGTTGPQKAVPQTFRN 185
Cdd:PRK12582 171 RALAALDLLDVTV----VHVTGPGEGIASIAFADLAATPPTAAVAAAI--AAITPDTVAKYLFTSGSTGMPKAVINTQRM 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 186 HYASAIGCKESLGFDRDT------NWlsvLPIYHISGLSVLLRAV-IEGFTVRIVD-KFNAEQILTMIKNER---ITHIS 254
Cdd:PRK12582 245 MCANIAMQEQLRPREPDPpppvslDW---MPWNHTMGGNANFNGLlWGGGTLYIDDgKPLPGMFEETIRNLReisPTVYG 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 255 LVPQTLNWL---MQQ--GLHEPY--NLQKILLGGAKLS----ATMIETALQ---YNLPIYNSFGMTETcsqflTATPEML 320
Cdd:PRK12582 322 NVPAGYAMLaeaMEKddALRRSFfkNLRLMAYGGATLSddlyERMQALAVRttgHRIPFYTGYGATET-----APTTTGT 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 321 H---ARPDTVGMPSANVDVKIKnPNKEGHgELMIKGANVMNGYLYPTDLTG-TF-ENGYFNTGDIAE-IDHEGYV--MIY 392
Cdd:PRK12582 397 HwdtERVGLIGLPLPGVELKLA-PVGDKY-EVRVKGPNVTPGYHKDPELTAaAFdEEGFYRLGDAARfVDPDDPEkgLIF 474
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446270502 393 DRR--KDLIISGGE--NIYPYQIETVAKQFPGISDAVCVGH 429
Cdd:PRK12582 475 DGRvaEDFKLSTGTwvSVGTLRPDAVAACSPVIHDAVVAGQ 515
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
5-484 |
5.70e-18 |
|
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: 86.86 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 5 LYKQAQQNGHHIA-ITDGQE-----SYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAM 75
Cdd:cd17634 59 LDRHLRENGDRTAiIYEGDDtsqsrTISYRELHREVCRFAGTLLDLgvkKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 76 INTRLTPNEMTNQMKSIDVQLIfctlplelrgfqiVSLDDIEFAGRDITTNGLLDNTMGIQYdTSNETVV---------- 145
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLL-------------ITADGGVRAGRSVPLKKNVDDALNPNV-TSVEHVIvlkrtgsdid 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 146 -----------------PKESPSNIlntsfNLDDIASIMFTSGTTGPQKAV-----------PQTFRNHYASAIG----C 193
Cdd:cd17634 205 wqegrdlwwrdliakasPEHQPEAM-----NAEDPLFILYTSGTTGKPKGVlhttggylvyaATTMKYVFDYGPGdiywC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 194 KESLGFDRDTNWLSVLPIyhISGLSVLLravIEGftvrIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLH--EP 271
Cdd:cd17634 280 TADVGWVTGHSYLLYGPL--ACGATTLL---YEG----VPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDaiEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 272 YNLQKI-LLGGA------KLSATMIETALQYNLPIYNSFGMTETCSQFLTATP--EMLHARPDT---VGMPSANVDVKiK 339
Cdd:cd17634 351 TDRSSLrILGSVgepinpEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPgaIELKAGSATrpvFGVQPAVVDNE-G 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 340 NPNKEGH-GELMIkGANVMNGYL--------YPTDLTGTFENGYFnTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQ 410
Cdd:cd17634 430 HPQPGGTeGNLVI-TDPWPGQTRtlfgdherFEQTYFSTFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAE 507
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446270502 411 IETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:cd17634 508 IESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVlnhgvEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
161-489 |
8.83e-18 |
|
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: 85.79 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQK--AVPQT--------FRNHY----ASAIGCKESLGFDrdtnwLSV----LPIyhISGLSVLLr 222
Cdd:cd17646 138 DNLAYVIYTSGSTGRPKgvMVTHAgivnrllwMQDEYplgpGDRVLQKTPLSFD-----VSVwelfWPL--VAGARLVV- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 223 AVIEGFTvrivdkfNAEQILTMIKNERITHISLVPQTLNWLMQQ-GLHEPYNLQKILLGGAKLSATMIETALQ-YNLPIY 300
Cdd:cd17646 210 ARPGGHR-------DPAYLAALIREHGVTTCHFVPSMLRVFLAEpAAGSCASLRRVFCSGEALPPELAARFLAlPGAELH 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 301 NSFGMTEtcsqfltATPEMLH--ARPDT------VGMPSANVDVKIKNPnkEGH-------GELMIKGANVMNGYLYPTD 365
Cdd:cd17646 283 NLYGPTE-------AAIDVTHwpVRGPAetpsvpIGRPVPNTRLYVLDD--ALRpvpvgvpGELYLGGVQLARGYLGRPA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 366 LTGT------FENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQV 437
Cdd:cd17646 354 LTAErfvpdpFGPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAAR 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446270502 438 PKLYFVSESD---ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17646 434 LVGYVVPAAGaagPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
161-489 |
1.28e-17 |
|
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: 85.29 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWL---------SVLPIyhisgLSVLLRavieGFTVR 231
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfasytfdvSILEI-----FTTLAA----GGCLC 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 232 I---VDKFN--AEQILTMikneRITHISLVPQTLNWLMQQGLhePyNLQKILLGGAKLSATMIET-ALQYNLpiYNSFGM 305
Cdd:cd05918 177 IpseEDRLNdlAGFINRL----RVTWAFLTPSVARLLDPEDV--P-SLRTLVLGGEALTQSDVDTwADRVRL--INAYGP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 306 TEtCSQFLTATPEMLHARPDTVGMPSANVD--VKIKNPNKEGH----GELMIKGANVMNGYLYPTDLT------------ 367
Cdd:cd05918 248 AE-CTIAATVSPVVPSTDPRNIGRPLGATCwvVDPDNHDRLVPigavGELLIEGPILARGYLNDPEKTaaafiedpawlk 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 --GTFENGYF-NTGDIAEIDHEGyVMIYDRRKD--LIISG-----GEniypyqIE-TVAKQFPGISD------------- 423
Cdd:cd05918 327 qeGSGRGRRLyRTGDLVRYNPDG-SLEYVGRKDtqVKIRGqrvelGE------IEhHLRQSLPGAKEvvvevvkpkdgss 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446270502 424 -----AVCVGHPDDTWGQVPKLYFVSESD---ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05918 400 spqlvAFVVLDGSSSGSGDGDSLFLEPSDefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
161-486 |
1.91e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 85.05 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTN-WLSVLPIYH----ISGLSVLLRAVIEGFTVRIVDk 235
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDvMVSWLPLFHdmgmVGFLTVPMYFGAELVKVTPMD- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 FNAEQIL--TMIKNERIThISLVPqtlNW--------LMQQGLHEPYNLQ--KILLGGAKL--SATM---IETALQYNLP 298
Cdd:PRK07768 231 FLRDPLLwaELISKYRGT-MTAAP---NFayallarrLRRQAKPGAFDLSslRFALNGAEPidPADVedlLDAGARFGLR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 ---IYNSFGMTET------------------CSQFLTAT-----PEMLHARP-DTVGMPSANVDVKI-----KNPNKEGH 346
Cdd:PRK07768 307 peaILPAYGMAEAtlavsfspcgaglvvdevDADLLAALrravpATKGNTRRlATLGPPLPGLEVRVvdedgQVLPPRGV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 347 GELMIKGANVMNGYLyptDLTGTF----ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI- 421
Cdd:PRK07768 387 GVIELRGESVTPGYL---TMDGFIpaqdADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVr 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446270502 422 -SDAVCV----GHPDDTWGQVPKLYFVSESDISKA---QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK07768 464 pGNAVAVrldaGHSREGFAVAVESNAFEDPAEVRRirhQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRR 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
146-489 |
5.19e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.62 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 146 PKESPSNILNTsfnlDDIASIMFTSGTTGPQKAVP---QTFRNH---YASAIGC--------KESLGFDrdtnwLSVLPI 211
Cdd:PRK12316 4683 PAHDPAVRLHP----DNLAYVIYTSGSTGRPKGVAvshGSLVNHlhaTGERYELtpddrvlqFMSFSFD-----GSHEGL 4753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 212 YH--ISGLSVLLRAViegftvrivDKFNAEQILTMIKNERITHISLVPQTLNWLMQ--QGLHEPYNLQKILLGGAKLSAT 287
Cdd:PRK12316 4754 YHplINGASVVIRDD---------SLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEhaERDGEPPSLRVYCFGGEAVAQA 4824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 288 MIETALQ--YNLPIYNSFGMTETcsqflTATPEMLHARPDT--------VGMPSANVDVKI----KNPNKEGH-GELMIK 352
Cdd:PRK12316 4825 SYDLAWRalKPVYLFNGYGPTET-----TVTVLLWKARDGDacgaaympIGTPLGNRSGYVldgqLNPLPVGVaGELYLG 4899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 353 GANVMNGYLYPTDLT---------GTFENGYFNTGDIAEIDHEGyVMIYDRRKD-------LIISGGEniypyqIETVAK 416
Cdd:PRK12316 4900 GEGVARGYLERPALTaerfvpdpfGAPGGRLYRTGDLARYRADG-VIDYLGRVDhqvkirgFRIELGE------IEARLR 4972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 417 QFPGISDAVCVGHPDDTWGQ-----VPKLYFVSESDISKA----QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRN 487
Cdd:PRK12316 4973 EHPAVREAVVIAQEGAVGKQlvgyvVPQDPALADADEAQAelrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
..
gi 446270502 488 KL 489
Cdd:PRK12316 5053 AL 5054
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
162-491 |
8.01e-17 |
|
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: 82.79 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 162 DIASIMFTSGTTG-PQKAVPQTFRNHYASAIGCKESLGFDRDTNWlSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFNAE 239
Cdd:cd05940 82 DAALYIYTSGTTGlPKAAIISHRRAWRGGAFFAGSGGALPSDVLY-TCLPLYHSTALIVGWSACLaSGATLVIRKKFSAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 240 QILTMIKNERITHISLVPQTLNWLMQQGLHE---PYNLQKILlgGAKLSATMIETAL-QYNLP-IYNSFGMTETCSQFLT 314
Cdd:cd05940 161 NFWDDIRKYQATIFQYIGELCRYLLNQPPKPterKHKVRMIF--GNGLRPDIWEEFKeRFGVPrIAEFYAATEGNSGFIN 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 atpemLHARPDTVG---------MPSANV--DVKIKNP--NKEGH---------GELM--IKGANVMNGYLYPTD----- 365
Cdd:cd05940 239 -----FFGKPGAIGrnpsllrkvAPLALVkyDLESGEPirDAEGRcikvprgepGLLIsrINPLEPFDGYTDPAAtekki 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 366 LTGTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHP-DDTWGQ--VPKL 440
Cdd:cd05940 314 LRDVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRagMAAI 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446270502 441 YFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05940 394 VLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
161-483 |
1.29e-16 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 82.84 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSV-LLRAVIEGFTV--------- 230
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPLLTGAEVflypsplhy 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 231 RIVDKFNAEQILTMI--------KNERITHislvpqtlnwlmqqglhePYN---LQKILLGGAKLSATMIETAL-QYNLP 298
Cdd:PRK08043 445 RIVPELVYDRNCTVLfgtstflgNYARFAN------------------PYDfarLRYVVAGAEKLQESTKQLWQdKFGLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 IYNSFGMTEtCSQFLTATPEMLhARPDTVGMPSANVDVK-IKNPNKEGHGELMIKGANVMNGYLY---------PT--DL 366
Cdd:PRK08043 507 ILEGYGVTE-CAPVVSINVPMA-AKPGTVGRILPGMDARlLSVPGIEQGGRLQLKGPNIMNGYLRvekpgvlevPTaeNA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 367 TGTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLyFVSES 446
Cdd:PRK08043 585 RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVL-FTTDS 663
|
330 340 350
....*....|....*....|....*....|....*...
gi 446270502 447 DISKAQLIAYLSQH-LAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:PRK08043 664 ELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
161-433 |
1.39e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 82.84 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIG-CKES--LGFDRDTNwLSVLPIYHISGLSVLLRAVIEGFTVRIVDK-- 235
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPlCKHSifKKYNPKTH-LSYLPISHIYERVIAYLSFMLGGTINIWSKdi 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 -----------------------------------------FNAEQILTMIKN----------ERITHISL-VPQTLNwl 263
Cdd:PTZ00342 383 nyfskdiynskgnilagvpkvfnriytnimteinnlpplkrFLVKKILSLRKSnnnggfskflEGITHISSkIKDKVN-- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 264 mqqglhePyNLQKILLGGAKLSATMI-ETALQYNLPIYNSFGMTETCSQFLTAtpemlHAR---PDTVGMP-SANVDVKI 338
Cdd:PTZ00342 461 -------P-NLEVILNGGGKLSPKIAeELSVLLNVNYYQGYGLTETTGPIFVQ-----HADdnnTESIGGPiSPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 339 K---------NPNKeghGELMIKGANVMNGYLYPTDLT-GTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENI 406
Cdd:PTZ00342 528 RtwetykatdTLPK---GELLIKSDSIFSGYFLEKEQTkNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYI 604
|
330 340
....*....|....*....|....*..
gi 446270502 407 YPYQIETVAKQFPGISDavCVGHPDDT 433
Cdd:PTZ00342 605 ETDMLNNLYSQISFINF--CVVYGDDS 629
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-486 |
2.03e-16 |
|
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: 81.55 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 15 HIAITDGQESYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDNSIQ------SIILIHACWLanieiamintrltpnem 85
Cdd:cd12114 3 ATAVICGDGTLTYGELAERARRVAGALKAAgvrPGDLVAVTLPKGPEqvvavlGILAAGAAYV----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 86 tnqmkSIDVQLifctlPLElRGFQIVSLDDIEFAgrdiTTNGLLDNTMGIQYDTSNETVVPKESPSNILNTSFNLDDIAS 165
Cdd:cd12114 66 -----PVDIDQ-----PAA-RREAILADAGARLV----LTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSV------LPIYHISGLsvlLRAvieGFTVRIVD---KF 236
Cdd:cd12114 131 VIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALsslsfdLSVYDIFGA---LSA---GATLVLPDearRR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 237 NAEQILTMIKNERITHISLVPQ----TLNWLMQQGLHEPyNLQKILLGG----AKLSATMieTALQYNLPIYNSFGMTET 308
Cdd:cd12114 205 DPAHWAELIERHGVTLWNSVPAllemLLDVLEAAQALLP-SLRLVLLSGdwipLDLPARL--RALAPDARLISLGGATEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 309 C--SQFLTATPEMLHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYL---------YPTDLTGtfeN 372
Cdd:cd12114 282 SiwSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRGRdcpdwVPGELWIGGRGVALGYLgdpeltaarFVTHPDG---E 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 373 GYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTwgqVPKL--YFVSESD--- 447
Cdd:cd12114 359 RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG---GKRLaaFVVPDNDgtp 435
|
490 500 510
....*....|....*....|....*....|....*....
gi 446270502 448 ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd12114 436 IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
161-429 |
2.61e-16 |
|
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: 81.32 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDT-----NWlsvLPIYHISGLSVLLRAVI-EGFTVRIVD 234
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppvlvDW---LPWNHTFGGNHNFNLVLyNGGTLYIDD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 235 -KFNAEQILTMIKNER---ITHISLVPQTLNWLMQ-----QGLHEPY--NLQKILLGGAKLSATMIEtALQ--------Y 295
Cdd:cd05921 242 gKPMPGGFEETLRNLReisPTVYFNVPAGWEMLVAalekdEALRRRFfkRLKLMFYAGAGLSQDVWD-RLQalavatvgE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 296 NLPIYNSFGMTETCSQFLTATpeMLHARPDTVGMPSANVDVKIKnPNkEGHGELMIKGANVMNGYLYPTDLTG-TF-ENG 373
Cdd:cd05921 321 RIPMMAGLGATETAPTATFTH--WPTERSGLIGLPAPGTELKLV-PS-GGKYEVRVKGPNVTPGYWRQPELTAqAFdEEG 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446270502 374 YFNTGD---IAEIDHEGYVMIYDRR--KDLIISGGE--NIYPYQIETVAKQFPGISDAVCVGH 429
Cdd:cd05921 397 FYCLGDaakLADPDDPAKGLVFDGRvaEDFKLASGTwvSVGPLRARAVAACAPLVHDAVVAGE 459
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-486 |
2.85e-16 |
|
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: 81.38 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 24 SYTYQNLYCEASLLAKRLKAY---QQSRVGLYIDnSIQSIILIhacWLANIEIAMINTRL----TPNEMTNQMKSIDVQL 96
Cdd:cd05968 91 TLTYGELLYEVKRLANGLRALgvgKGDRVGIYLP-MIPEIVPA---FLAVARIGGIVVPIfsgfGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 97 IFCTLPLELRGFQIVSLDDIEFAGRDITT--------NGLLDNTMGIQYDTSNETVVPKESPSNILNTSfnlDDIASIMF 168
Cdd:cd05968 167 LITADGFTRRGREVNLKEEADKACAQCPTvekvvvvrHLGNDFTPAKGRDLSYDEEKETAGDGAERTES---EDPLMIIY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 169 TSGTTGPQKAvpqTFRNHYASAIGCKESLGFDRDTN------WLSVLPiyHISGLSVLLRAVIEGFTVRIVDKF----NA 238
Cdd:cd05968 244 TSGTTGKPKG---TVHVHAGFPLKAAQDMYFQFDLKpgdlltWFTDLG--WMMGPWLIFGGLILGATMVLYDGApdhpKA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLMQQGLH-----------------EPYNLQKILLggaklsatMIETALQYNLPIYN 301
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPRGDApvnahdlsslrvlgstgEPWNPEPWNW--------LFETVGKGRNPIIN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 302 SFGMTET-----CSQFLTATPEMLHARPdTVGMPSANVDVKiKNPNKEGHGEL--------MIKG-----ANVMNGYLyp 363
Cdd:cd05968 391 YSGGTEIsggilGNVLIKPIKPSSFNGP-VPGMKADVLDES-GKPARPEVGELvllapwpgMTRGfwrdeDRYLETYW-- 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 364 tdltGTFENGYFNtGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV 443
Cdd:cd05968 467 ----SRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVV 541
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446270502 444 -----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd05968 542 lkpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
161-429 |
3.05e-16 |
|
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: 81.32 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNhyasAIG-CKESLGFD---RDTNWLSVLPIYHI-SGLSVLLRAVIEGFTVRIVDK 235
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGN----FLGhCAAYLAADplgPGDEYVSVLPLPWIgEQMYSVGQALVCGFIVNFPEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 ----------------FNA----EQILTMIK---------------------------NERITHISLVPQTLNWLMQQGL 268
Cdd:cd17641 234 petmmedlreigptfvLLPprvwEGIAADVRarmmdatpfkrfmfelgmklglraldrGKRGRPVSLWLRLASWLADALL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 269 HEPY-------NLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSqFLTATPEMlHARPDTVGMPSANVDVKIKNp 341
Cdd:cd17641 314 FRPLrdrlgfsRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAG-AYTVHRDG-DVDPDTVGVPFPGTEVRIDE- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 342 nkegHGELMIKGANVMNGYLYPTDLTGT--FENGYFNTGDIAEIDHEGYVMIYDRRKDL-IISGGENIYPYQIETVAKQF 418
Cdd:cd17641 391 ----VGEILVRSPGVFVGYYKNPEATAEdfDEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFS 466
|
330
....*....|.
gi 446270502 419 PGISDAVCVGH 429
Cdd:cd17641 467 PYIAEAVVLGA 477
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
26-406 |
8.77e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 79.86 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 26 TYQNLYCEASLLAKRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCTLPLEL 105
Cdd:PRK06334 47 SYNQVRKAVIALATKVSKYPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 106 RGFQIVSlDDIEFAGR-----DITTNGLLDNTMGIQYDTSnetvVPKESPSNILNTS-FNLDDIASIMFTSGTTGPQKAV 179
Cdd:PRK06334 127 HLAQTHG-EDAEYPFSliymeEVRKELSFWEKCRIGIYMS----IPFEWLMRWFGVSdKDPEDVAVILFTSGTEKLPKGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 180 PQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIV-DKFNAEQILTMIKNERITHISLVP 257
Cdd:PRK06334 202 PLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLSGVPVVFAyNPLYPKKIVEMIDEAKVTFLGSTP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 258 QTLNWLM----QQGLHEPyNLQKILLGGAKLSATMIETALQY--NLPIYNSFGMTEtCSQFLTATPEMLHARPDTVGMPS 331
Cdd:PRK06334 282 VFFDYILktakKQESCLP-SLRFVVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTE-CSPVITINTVNSPKHESCVGMPI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 332 ANVDVKI-----KNPNKEGH-GELMIKGANVMNGYLYPTDLTGTFENG---YFNTGDIAEIDHEGYVMIYDRRKDLIISG 402
Cdd:PRK06334 360 RGMDVLIvseetKVPVSSGEtGLVLTRGTSLFSGYLGEDFGQGFVELGgetWYVTGDLGYVDRHGELFLKGRLSRFVKIG 439
|
....
gi 446270502 403 GENI 406
Cdd:PRK06334 440 AEMV 443
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
26-489 |
8.95e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 80.24 E-value: 8.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 26 TYQNLYCEASLLAKRLKAYQQ---SRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIF---- 98
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAepgSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFvqdk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 99 ---------CTLPLELRGfqIVSLDDIEFAGRDITTNglldntMGIQ-YDTSNETVVPKESPSNILNTSFNldDIASIMF 168
Cdd:PLN02430 158 kikellepdCKSAKRLKA--IVSFTSVTEEESDKASQ------IGVKtYSWIDFLHMGKENPSETNPPKPL--DICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 169 TSGTTGPQKAVPQTFRNHYASAIG---CKESlgFD----RDTNWLSVLPIYHI-----------SGLSV----------- 219
Cdd:PLN02430 228 TSGTSGDPKGVVLTHEAVATFVRGvdlFMEQ--FEdkmtHDDVYLSFLPLAHIldrmieeyffrKGASVgyyhgdlnalr 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 220 ---------LLRAVIEGFTvRIVDKF-NAEQILTMIKneRITHISLVPQTLNWlMQQGLHEPY----------------- 272
Cdd:PLN02430 306 ddlmelkptLLAGVPRVFE-RIHEGIqKALQELNPRR--RLIFNALYKYKLAW-MNRGYSHKKaspmadflafrkvkakl 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 273 --NLQKILLGGAKLSaTMIETALQYNLPIY--NSFGMTETCSQFLTATPE---MLharpDTVGMPSANVDVKIKNPNKEG 345
Cdd:PLN02430 382 ggRLRLLISGGAPLS-TEIEEFLRVTSCAFvvQGYGLTETLGPTTLGFPDemcML----GTVGAPAVYNELRLEEVPEMG 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 346 H--------GELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVA 415
Cdd:PLN02430 457 YdplgepprGEICVRGKCLFSGYYKNPELTEeVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVY 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 416 KQFPGISD-------------AVCVGHPDDT--W----GQVPKLYFVSESDISKAQLIAYLSQHLAKYKVpKHFEKV--- 473
Cdd:PLN02430 537 GQNPIVEDiwvygdsfksmlvAVVVPNEENTnkWakdnGFTGSFEELCSLPELKEHILSELKSTAEKNKL-RGFEYIkgv 615
|
570 580
....*....|....*....|....*
gi 446270502 474 --DTLPY-------TSTGKLQRNKL 489
Cdd:PLN02430 616 ilETKPFdverdlvTATLKKRRNNL 640
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
7-489 |
1.89e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 78.76 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 7 KQAQQNGHHIAITDGQESYTYQnlycEASLLAKRLKAYQQSR-------VGLYIDNSIQSIilihACWLANIEI----AM 75
Cdd:PRK08279 45 EAAARHPDRPALLFEDQSISYA----ELNARANRYAHWAAARgvgkgdvVALLMENRPEYL----AAWLGLAKLgavvAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 76 INTRLTPNEMTNQMKSIDVQLI---------FCTLPLELRGFQIVSLDDiefAGRDITTNGLLD-NTMGIQYDTSNetvv 145
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLivgeelveaFEEARADLARPPRLWVAG---GDTLDDPEGYEDlAAAAAGAPTTN---- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 146 pKESPSNILntsfnLDDIASIMFTSGTTGPQKAVPQTfrnHY---ASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLR 222
Cdd:PRK08279 190 -PASRSGVT-----AKDTAFYIYTSGTTGLPKAAVMS---HMrwlKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 223 AVI-EGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE---PYNLQKILlgGAKLSATMIETALQY--- 295
Cdd:PRK08279 261 SVLaAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPtdrDHRLRLMI--GNGLRPDIWDEFQQRfgi 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 296 ------------NLPIYNSFGMTETCSqfLTATPEMLHAR-----PDTvGMPsanvdvkIKNPN-------KEGHGEL-- 349
Cdd:PRK08279 339 prilefyaasegNVGFINVFNFDGTVG--RVPLWLAHPYAivkydVDT-GEP-------VRDADgrcikvkPGEVGLLig 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 350 MIKGANVMNGYlypTD--------LTGTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFP 419
Cdd:PRK08279 409 RITDRGPFDGY---TDpeasekkiLRDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFP 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 420 GISDAVcvghpddTWG-QVP-----------KLYFVSESDIskAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRN 487
Cdd:PRK08279 486 GVEEAV-------VYGvEVPgtdgragmaaiVLADGAEFDL--AALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKV 556
|
..
gi 446270502 488 KL 489
Cdd:PRK08279 557 DL 558
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
159-489 |
1.54e-14 |
|
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: 75.67 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 NLDDIASIMFTSGTTGPQKAVPQTFRN--------HYASAIGCKE------SLGFDRdtnwlSVLPIY-HISGlsvllra 223
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNlvnlcewhRPYFGVTPADkslvyaSFSFDA-----SAWEIFpHLTA------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 224 vieGFTVRIVD---KFNAEQILTMIKNERIThISLVP-QTLNWLMQQglhEPYNLQKILLGGAKLsatmiETALQYNLPI 299
Cdd:cd17645 170 ---GAALHVVPserRLDLDALNDYFNQEGIT-ISFLPtGAAEQFMQL---DNQSLRVLLTGGDKL-----KKIERKGYKL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 300 YNSFGMTEtCSQFLTATPEMLHARPDTVGMPSANVDVKIKNPN----KEG-HGELMIKGANVMNGYLYPTDLTGT----- 369
Cdd:cd17645 238 VNNYGPTE-NTVVATSFEIDKPYANIPIGKPIDNTRVYILDEAlqlqPIGvAGELCIAGEGLARGYLNRPELTAEkfivh 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 370 -FENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSES 446
Cdd:cd17645 317 pFVPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446270502 447 DISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17645 397 EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
411-483 |
1.79e-14 |
|
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: 68.34 E-value: 1.79e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446270502 411 IETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
161-489 |
1.84e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 76.75 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTfrnHYASAigckESLGFDRDTnwlsvlpiYHISGLSVLLRAVIEGFTVRIVDKF---- 236
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNT---HAALA----ERLQWMQAT--------YALDDSDVLMQKAPISFDVSVWECFwpli 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 237 --------------NAEQILTMIKNERITHISLVPQtlnwLMQQGLHEP-----YNLQKILLGGAKLSATMIETALQyNL 297
Cdd:PRK05691 1338 tgcrlvlagpgehrDPQRIAELVQQYGVTTLHFVPP----LLQLFIDEPlaaacTSLRRLFSGGEALPAELRNRVLQ-RL 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 298 P---IYNSFGMTETCsqfLTATpeMLHARPDT-----VGMPSANVDVKIK----NPNKEG-HGELMIKGANVMNGYLYPT 364
Cdd:PRK05691 1413 PqvqLHNRYGPTETA---INVT--HWQCQAEDgerspIGRPLGNVLCRVLdaelNLLPPGvAGELCIGGAGLARGYLGRP 1487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 365 DLT---------GTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHpDDTWG 435
Cdd:PRK05691 1488 ALTaerfvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAG 1566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446270502 436 QVPKLYFVSE--SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05691 1567 AQLVGYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
161-489 |
2.36e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.84 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIG-CKESLGFDRDTNWLSVLPIYHISGL--SVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAIHRHADPLTFVDAmCRKALRLTPEDTGLCSARMYFAYGLgnSVWFPLATGGSAVINSAPVT 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHEPY-NLQKILLGGAKLSATMIETALQY--NLPIYNSFGMTETCSQFLT 314
Cdd:PRK06060 225 PEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFrSLRCVVSAGEALELGLAERLMEFfgGIPILDGIGSTEVGQTFVS 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 ATPEmlHARPDTVGMPSANVDVKIKNPNKE-----GHGELMIKGANVMNGYL-YPTDLtgtFEN-GYFNTGDIAEIDHEG 387
Cdd:PRK06060 305 NRVD--EWRLGTLGRVLPPYEIRVVAPDGTtagpgVEGDLWVRGPAIAKGYWnRPDSP---VANeGWLDTRDRVCIDSDG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSES----DISKAQLI-AYLSQHLA 462
Cdd:PRK06060 380 WVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgatiDGSVMRDLhRGLLNRLS 459
|
330 340
....*....|....*....|....*..
gi 446270502 463 KYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06060 460 AFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
335-488 |
3.84e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.66 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 335 DVKIKNPNKEGHGELMI-----KGANVMNGYLYPTDLTGTFE-NGYFNTGDIAEIdHEGYVMIYDRRKDLIISGGENIYP 408
Cdd:PRK09192 395 EIEIRNEAGMPLPERVVghicvRGPSLMSGYFRDEESQDVLAaDGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWP 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 409 YQIETVAKQFPGI--SDAVCVGHPDDTWGQVPKLYFVSESDI-SKAQLIAYLSQHL-AKYKVPKHFEKV--DTLPYTSTG 482
Cdd:PRK09192 474 QDIEWIAEQEPELrsGDAAAFSIAQENGEKIVLLVQCRISDEeRRGQLIHALAALVrSEFGVEAAVELVppHSLPRTSSG 553
|
....*.
gi 446270502 483 KLQRNK 488
Cdd:PRK09192 554 KLSRAK 559
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
166-492 |
4.84e-14 |
|
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: 74.66 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQK-----------AVPQTFRNHYasaiGCKESLGF--DRDTNW-----LSVL-PIYHisGLSVLLravIE 226
Cdd:cd05967 235 ILYTSGTTGKPKgvvrdngghavALNWSMRNIY----GIKPGDVWwaASDVGWvvghsYIVYgPLLH--GATTVL---YE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 GFTVRIVDkfnAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPY-------NLQKILLGGAKLSATMIETALQ-YNLP 298
Cdd:cd05967 306 GKPVGTPD---PGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikkydlsSLRTLFLAGERLDPPTLEWAENtLGVP 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 IYNSFGMTETCSQfLTATP---EMLHARPDTVGMPSANVDVKIKNPNKE--GHGELmikGANVMNGYLYPTDLTGTFEN- 372
Cdd:cd05967 383 VIDHWWQTETGWP-ITANPvglEPLPIKAGSPGKPVPGYQVQVLDEDGEpvGPNEL---GNIVIKLPLPPGCLLTLWKNd 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 373 ------------GYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKL 440
Cdd:cd05967 459 erfkklylskfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLG 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446270502 441 YFVSESDISKA------QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRN---KLYRG 492
Cdd:cd05967 539 LVVLKEGVKITaeelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRtlrKIADG 599
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
164-489 |
5.12e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 164 ASIMFTSGTTGPQKAVpqtFRNHYASAIGCKE-----------------SLGFDRDTNWLSVlPIyhISGLSVLLRAviE 226
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGV---VVSHGEIAMHCQAvierfgmraddcelhfySINFDAASERLLV-PL--LCGARVVLRA--Q 2407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 GftvrivdKFNAEQILTMIKNERITHISLVP----QTLNWLMQQGLHEPYNLqkILLGGAKLSA---TMIETALQYNLpI 299
Cdd:PRK05691 2408 G-------QWGAEEICQLIREQQVSILGFTPsygsQLAQWLAGQGEQLPVRM--CITGGEALTGehlQRIRQAFAPQL-F 2477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 300 YNSFGMTETCSQFLTA-TPEMLhaRPDTVGMPSANV---------DVKIKNPNKEGHGELMIKGANVMNGYLYPTDLTG- 368
Cdd:PRK05691 2478 FNAYGPTETVVMPLAClAPEQL--EEGAASVPIGRVvgarvayilDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAe 2555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 369 -----TFE-NG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHpDDTWGQVPKL 440
Cdd:PRK05691 2556 rfvadPFAaDGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAG 2634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446270502 441 YFVSE----SDISKAQL----IAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05691 2635 YLVSAvagqDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
161-464 |
7.44e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.78 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYA--SAIgcKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNA 238
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAqiEAL--REDYGIEPGEIDLPTFPLFALFGPALGMTSVIPDMDPTRPATVDP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPY---NLQKILLGGAKLSATMIE---TALQYNLPIYNSFGMTE----- 307
Cdd:PRK09274 252 AKLFAAIERYGVTNLFGSPALLERLGRYGEANGIklpSLRRVISAGAPVPIAVIErfrAMLPPDAEILTPYGATEalpis 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 308 --TCSQFLTATPEMLHARPDT-VGMPSANVDVKI----KNPNKEGH----------GELMIKGANVMNGYLYPTDLT--- 367
Cdd:PRK09274 332 siESREILFATRAATDNGAGIcVGRPVDGVEVRIiaisDAPIPEWDdalrlatgeiGEIVVAGPMVTRSYYNRPEATrla 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 ------GTFengYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTwGQVPKLy 441
Cdd:PRK09274 412 kipdgqGDV---WHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVL- 486
|
330 340
....*....|....*....|....*..
gi 446270502 442 fVSESD----ISKAQLIAYLSQHLAKY 464
Cdd:PRK09274 487 -CVELEpgvaCSKSALYQELRALAAAH 512
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
321-486 |
3.06e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.72 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 321 HARpdtVGMPSANVDVKIKNP------NKEGHGELMIKGANVMNGYLYPTDLTgtfENGYFNTGDIAEIDHEGYVmIYDR 394
Cdd:PRK05851 344 HAV---LGNPIPGMEVRISPGdgaagvAGREIGEIEIRGASMMSGYLGQAPID---PDDWFPTGDLGYLVDGGLV-VCGR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 395 RKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSE---SDISKAQliAYLSQHLAKY--KVPKH 469
Cdd:PRK05851 417 AKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEfrgPDEAGAR--SEVVQRVASEcgVVPSD 494
|
170
....*....|....*....
gi 446270502 470 --FEKVDTLPYTSTGKLQR 486
Cdd:PRK05851 495 vvFVAPGSLPRTSSGKLRR 513
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
161-489 |
1.53e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 70.07 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQK--AVPQT--------FRNHY----ASAIGCKESLGFDRDTnWLSVLPIyhISGlSVLLRAVIE 226
Cdd:PRK10252 598 HHTAYIIFTSGSTGRPKgvMVGQTaivnrllwMQNHYpltaDDVVLQKTPCSFDVSV-WEFFWPF--IAG-AKLVMAEPE 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 GFTvrivdkfNAEQILTMIKNERITHISLVPQTL----NWLMQQGLHEPY-NLQKILLGGAKLSATMIETALQ-YNLPIY 300
Cdd:PRK10252 674 AHR-------DPLAMQQFFAEYGVTTTHFVPSMLaafvASLTPEGARQSCaSLRQVFCSGEALPADLCREWQQlTGAPLH 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 301 NSFGMTE---------TCSQFLTATPemlhARPDTVGMPSANVDVKI----KNPNKEG-HGELMIKGANVMNGYLYPTDL 366
Cdd:PRK10252 747 NLYGPTEaavdvswypAFGEELAAVR----GSSVPIGYPVWNTGLRIldarMRPVPPGvAGDLYLTGIQLAQGYLGRPDL 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 367 T------GTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAV---CV-GHPDDTW 434
Cdd:PRK10252 823 TasrfiaDPFAPGerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthaCViNQAAATG 902
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446270502 435 GQVPKL--YFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK10252 903 GDARQLvgYLVSQSGlpLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
161-489 |
2.84e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 68.94 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYH----ISGLSVllrAVIEGFTVRIVDKF 236
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHsnavMAGWAV---ALAAGASIALRRKF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 237 NAEQILTMIKNERITHISLVPQTLNWLM--QQGLHEPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFlT 314
Cdd:PRK07867 229 SASGFLPDVRRYGATYANYVGKPLSYVLatPERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGVAI-T 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 ATPEmlhARPDTVGMPSAnvDVKIKNPN------------------KEGHGELM-IKGANVMNGYLYPTDLTGT-FENGY 374
Cdd:PRK07867 308 RTPD---TPPGALGPLPP--GVAIVDPDtgtecppaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAErMRGGV 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 375 FNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWG-QV-PKLYFVSESDISKAQ 452
Cdd:PRK07867 383 YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGdQVmAALVLAPGAKFDPDA 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 446270502 453 LIAYLSQH--LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07867 463 FAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-464 |
3.16e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 68.26 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF---DRDtnwLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIrpgEVD---LATFPLFALFGPALGLTSVIPDMDPTRPARAD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLN----WLMQQGLHEPyNLQKILLGGAKLSATMIET---ALQYNLPIYNSFGMTETCS 310
Cdd:cd05910 162 PQKLVGAIRQYGVSIVFGSPALLErvarYCAQHGITLP-SLRRVLSAGAPVPIALAARlrkMLSDEAEILTPYGATEALP 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 QFLTATPEMLHAR---PDT-----VGMPSANVDVKI--------------KNPNKEGHGELMIKGANVMNGYLYPTDLTG 368
Cdd:cd05910 241 VSSIGSRELLATTtaaTSGgagtcVGRPIPGVRVRIieiddepiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVATA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 369 -----TFENGYFN-TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI--SDAVCVGHPDdtwGQVPKL 440
Cdd:cd05910 321 lakidDNSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVrrSALVGVGKPG---CQLPVL 397
|
330 340
....*....|....*....|....*.
gi 446270502 441 YFVSESDISK--AQLIAYLSQHLAKY 464
Cdd:cd05910 398 CVEPLPGTITprARLEQELRALAKDY 423
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
9-489 |
3.46e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.38 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 9 AQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAYQ---QSRVGLYIDNSIQSIILIHACWLANIEIAMINTRlTPNEM 85
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKlpdKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS-SPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 86 TNQMKSI-DVQLIFCT--LPLELRGFQIVSLDDIEfagrdittnglldntmgiqydtsnETVVPKESPSniLNTSFNLDD 162
Cdd:PRK04813 91 IEMIIEVaKPSLIIATeeLPLEILGIPVITLDELK------------------------DIFATGNPYD--FDHAVKGDD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 163 IASIMFTSGTTGPQKAVP------QTFRNHYASAIGCKES--------LGFDrdtnwLSVLPIYH--ISG--LSVLLRAV 224
Cdd:PRK04813 145 NYYIIFTSGTTGKPKGVQishdnlVSFTNWMLEDFALPEGpqflnqapYSFD-----LSVMDLYPtlASGgtLVALPKDM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 225 IEGFtvrivdkfnaEQILTMIKNERIT---------HISLVPQTLNwlmqqGLHEPyNLQKILLGGAKLSAtmiETA--L 293
Cdd:PRK04813 220 TANF----------KQLFETLPQLPINvwvstpsfaDMCLLDPSFN-----EEHLP-NLTHFLFCGEELPH---KTAkkL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 294 QYNLP---IYNSFGMTETCSQfLTA---TPEMLHARPD-TVGMPSAnvDVKIKNPNKEGH-------GELMIKGANVMNG 359
Cdd:PRK04813 281 LERFPsatIYNTYGPTEATVA-VTSieiTDEMLDQYKRlPIGYAKP--DSPLLIIDEEGTklpdgeqGEIVISGPSVSKG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 360 YLYPTDLTG---TFENGY--FNTGDIAEIDHEgyVMIYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCVghPDDT 433
Cdd:PRK04813 358 YLNNPEKTAeafFTFDGQpaYHTGDAGYLEDG--LLFYQGRIDFQIKlNGYRIELEEIEQNLRQSSYVESAVVV--PYNK 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446270502 434 WGQVPKLY---------FVSESDISKAqLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK04813 434 DHKVQYLIayvvpkeedFEREFELTKA-IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
276-421 |
3.89e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 68.51 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 276 KILLGGAKLSATMIETALQY--NLPIYNSFGMTETCSQFLTATPEMLHARpDTVGMPSANVDVKIKN-PNKE-------G 345
Cdd:PLN02614 389 RIILSGAAPLASHVESFLRVvaCCHVLQGYGLTESCAGTFVSLPDELDML-GTVGPPVPNVDIRLESvPEMEydalastP 467
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446270502 346 HGELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAKQFPGI 421
Cdd:PLN02614 468 RGEICIRGKTLFSGYYKREDLTKeVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAV 545
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
159-491 |
6.11e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 67.51 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 NLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIV--DK 235
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLiAFHLAPLIAGMNQYLMptRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 236 FNAEQILTMIK--NERITHISLVPQTLNWLMQQGLHEPYN------LQKILLGGAKLSATMIETALQ----YNL------ 297
Cdd:cd05908 184 FIRRPILWLKKasEHKATIVSSPNFGYKYFLKTLKPEKANdwdlssIRMILNGAEPIDYELCHEFLDhmskYGLkrnail 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 298 PIY----NSFGMTETCSQFLTATPEMLH-------------------ARPDTVGMPSANVDVKIKNPNKEG-----HGEL 349
Cdd:cd05908 264 PVYglaeASVGASLPKAQSPFKTITLGRrhvthgepepevdkkdsecLTFVEVGKPIDETDIRICDEDNKIlpdgyIGHI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 350 MIKGANVMNGYLYPTDLTGTF--ENGYFNTGDIAEIdHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISD---A 424
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKVftDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELgrvV 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 425 VCVGHPDDTwgqvpklyfvSESDISKAQLIAYLSQHLAKY--KVPKHFEK-----------VDTLPYTSTGKLQRNKLYR 491
Cdd:cd05908 423 ACGVNNSNT----------RNEEIFCFIEHRKSEDDFYPLgkKIKKHLNKrggwqinevlpIRRIPKTTSGKVKRYELAQ 492
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
135-489 |
8.80e-12 |
|
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: 67.07 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 135 IQYDTSNETVVPKESPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHI 214
Cdd:cd05937 61 INYNLSGDPLIHCLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 215 SGLSVLLRAVI-EGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMqQGLHEPYNLQK--ILLGGAKLSATMIET 291
Cdd:cd05937 141 TAAFLGACNCLmSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLL-STPPSPYDRDHkvRVAWGNGLRPDIWER 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 292 ALQ-YNLPI----YNS----FGMTETCSQFLTATPEMLHA--------------RPDTvgmpsaNVDVKIKNPNK----- 343
Cdd:cd05937 220 FRErFNVPEigefYAAtegvFALTNHNVGDFGAGAIGHHGlirrwkfenqvvlvKMDP------ETDDPIRDPKTgfcvr 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 344 ---EGHGELM--IKGANV--MNGYLYPTD------LTGTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYP 408
Cdd:cd05937 294 apvGEPGEMLgrVPFKNReaFQGYLHNEDatesklVRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVST 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 409 YQIETVAKQFPGISDAVCVG----HPDdtwGQVPKLYF------VSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPY 478
Cdd:cd05937 374 TEVADVLGAHPDIAEANVYGvkvpGHD---GRAGCAAItleessAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVAT 450
|
410
....*....|.
gi 446270502 479 TSTGKLQRNKL 489
Cdd:cd05937 451 TDNHKQQKGVL 461
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
146-491 |
9.65e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 146 PKESPSNILNTsfnlDDIASIMFTSGTTGPQKAVP--------------QTFRNHYASAIGCKESLGFD-RDTNWLSVLp 210
Cdd:PRK12316 2135 PDTAPAVQLAG----ENLAYVIYTSGSTGLPKGVAvshgalvahcqaagERYELSPADCELQFMSFSFDgAHEQWFHPL- 2209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 211 iyhISGLSVLLRAViegftvrivDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE--PYNLQKILLGGAKLSATM 288
Cdd:PRK12316 2210 ---LNGARVLIRDD---------ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFGGEAVPAAS 2277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 289 IETALQYNLPIY--NSFGMTETcsqflTATPEMLHARPDTvgmPSANVDVKIKNP--NKEGH--------------GELM 350
Cdd:PRK12316 2278 LRLAWEALRPVYlfNGYGPTEA-----VVTPLLWKCRPQD---PCGAAYVPIGRAlgNRRAYildadlnllapgmaGELY 2349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 351 IKGANVMNGYLYPTDLTGT------FENG---YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI 421
Cdd:PRK12316 2350 LGGEGLARGYLNRPGLTAErfvpdpFSASgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAV 2429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446270502 422 SDAVCVGHpDDTWGQVPKLYFVSES--DISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK12316 2430 REAVVVAQ-DGASGKQLVAYVVPDDaaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
296-486 |
1.11e-11 |
|
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: 67.20 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 296 NLPIYNSFGMTETCSQFLTATPEMLHARPDTVGMPSANVDVKIKNPN-----KEGHGELMIKGAnvmngylYPTDLTGT- 369
Cdd:cd05966 381 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEgneveGEVEGYLVIKRP-------WPGMARTIy 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 370 -----FENGYFN-------TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQV 437
Cdd:cd05966 454 gdherYEDTYFSkfpgyyfTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEA 533
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446270502 438 PKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd05966 534 IYAFVTlkdgeEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
118-489 |
2.69e-11 |
|
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: 65.78 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 118 FAGRDITTNGLldNTMGIQYDTSNETVVPKESPSNILNTSfnlddIASIMFTSGTTG-PQKAVPQTFRNHYASAIgcKES 196
Cdd:cd05938 108 YLSHTSNTEGV--ISLLDKVDAASDEPVPASLRAHVTIKS-----PALYIYTSGTTGlPKAARISHLRVLQCSGF--LSL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 197 LGFDRDTNWLSVLPIYHISGLSVLLRAVIE-GFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQ 275
Cdd:cd05938 179 CGVTADDVIYITLPLYHSSGFLLGIGGCIElGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 276 KILLG-GAKLSATMIETALQY--NLPIYNSFGMTETCSQFLTATpemlhARPDTVGMPSA-----------NVDVKIKNP 341
Cdd:cd05938 259 KVRLAiGNGLRADVWREFLRRfgPIRIREFYGSTEGNIGFFNYT-----GKIGAVGRVSYlykllfpfeliKFDVEKEEP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 342 --NKEGH------GE--LMIKGANVMN---GYLYPTDLT------GTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLII 400
Cdd:cd05938 334 vrDAQGFcipvakGEpgLLVAKITQQSpflGYAGDKEQTekkllrDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 401 SGGENIYPYQIETVAKQFPGISDA----VCV-GHPddtwGQVP----KLYFVSESDISKaqLIAYLSQHLAKYKVPKHFE 471
Cdd:cd05938 414 WKGENVATTEVADVLGLLDFLQEVnvygVTVpGHE----GRIGmaavKLKPGHEFDGKK--LYQHVREYLPAYARPRFLR 487
|
410
....*....|....*...
gi 446270502 472 KVDTLPYTSTGKLQRNKL 489
Cdd:cd05938 488 IQDSLEITGTFKQQKVRL 505
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
161-379 |
4.48e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 65.29 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDT-----NWLsvlPIYHISGLSVLLRAVIE-GFTVRIVD 234
Cdd:PRK08180 209 DTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppvlvDWL---PWNHTFGGNHNLGIVLYnGGTLYIDD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 235 -KFNAEQILTMIKNERitHIS-----LVPQtlNWLM-------QQGLHEPY--NLQKILLGGAKLSAT-------MIETA 292
Cdd:PRK08180 286 gKPTPGGFDETLRNLR--EISptvyfNVPK--GWEMlvpalerDAALRRRFfsRLKLLFYAGAALSQDvwdrldrVAEAT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 293 LQYNLPIYNSFGMTETCSQFLTATPEMlhARPDTVGMPSANVDVKIKnPNkEGHGELMIKGANVMNGYLYPTDLTGT-F- 370
Cdd:PRK08180 362 CGERIRMMTGLGMTETAPSATFTTGPL--SRAGNIGLPAPGCEVKLV-PV-GGKLEVRVKGPNVTPGYWRAPELTAEaFd 437
|
....*....
gi 446270502 371 ENGYFNTGD 379
Cdd:PRK08180 438 EEGYYRSGD 446
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
14-489 |
2.88e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 62.35 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 14 HHIAITDGQESYTYQNLYCE----ASLLAKRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQM 89
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEaaarAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 90 KSIDVQLIFCT---LP----LELRGFQIVSLDDIEFAGRdITTNGLLdntmgiqydTSNETVVPkespsnilntsfnlDD 162
Cdd:PRK13388 96 RRADCQLLVTDaehRPlldgLDLPGVRVLDVDTPAYAEL-VAAAGAL---------TPHREVDA--------------MD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 163 IASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDR-DTNWLSvLPIYH----ISGLSVllrAVIEGFTVRIVDKFN 237
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRdDVCYVS-MPLFHsnavMAGWAP---AVASGAAVALPAKFS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLH--EPYNLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLT- 314
Cdd:PRK13388 228 ASGFLDDVRRYGATYFNYVGKPLAYILATPERpdDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVRe 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 315 -ATPEMLHAR---------PDTVGM-PSANVDV--KIKNPNkEGHGELMIK-GANVMNGYLYPTDLTGT-FENGYFNTGD 379
Cdd:PRK13388 308 pGTPPGSIGRgapgvaiynPETLTEcAVARFDAhgALLNAD-EAIGELVNTaGAGFFEGYYNNPEATAErMRHGMYWSGD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 380 IAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWG-QVPKLYFVSE-SDISKAQLIAYL 457
Cdd:PRK13388 387 LAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGdQVMAALVLRDgATFDPDAFAAFL 466
|
490 500 510
....*....|....*....|....*....|....
gi 446270502 458 S--QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13388 467 AaqPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
45-414 |
3.00e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 62.42 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 45 QQSRVGLYIDNSIQSIILIHACW-LANIEIAMINTrLTPNEMTNQMKSIDVQLIFC---TLPLELrGF--QIVSLddief 118
Cdd:PLN02736 102 KGACVGLYFINRPEWLIVDHACSaYSYVSVPLYDT-LGPDAVKFIVNHAEVAAIFCvpqTLNTLL-SClsEIPSV----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 119 agRDITTNGLLDNTMGIQYDTSNETVVPK---ESPSNILNTSF---NLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIG 192
Cdd:PLN02736 175 --RLIVVVGGADEPLPSLPSGTGVEIVTYsklLAQGRSSPQPFrppKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 193 CKESLGFDRDTNWLSVLPIYHI----SGLSVLLRAVIEGF----TVRIVDKFNA--EQILTMIKN--ERI-THISLVPQT 259
Cdd:PLN02736 253 SSLSTKFYPSDVHISYLPLAHIyervNQIVMLHYGVAVGFyqgdNLKLMDDLAAlrPTIFCSVPRlyNRIyDGITNAVKE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 260 LNWLMQQGLHEPYNLQK-------------------------------ILLGGAKLSATMIE-TALQYNLPIYNSFGMTE 307
Cdd:PLN02736 333 SGGLKERLFNAAYNAKKqalengknpspmwdrlvfnkikaklggrvrfMSSGASPLSPDVMEfLRICFGGRVLEGYGMTE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 308 TcSQFLTATPE----MLHarpdtVGMPSANVDVKIKNPNKEGH---------GELMIKGANVMNGYLYPTDLTGTF--EN 372
Cdd:PLN02736 413 T-SCVISGMDEgdnlSGH-----VGSPNPACEVKLVDVPEMNYtsedqpyprGEICVRGPIIFKGYYKDEVQTREVidED 486
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446270502 373 GYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETV 414
Cdd:PLN02736 487 GWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
153-398 |
3.34e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 62.30 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 153 ILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESL-----GFDRDTNWLSVLPIYHISGLSV----LLRA 223
Cdd:PTZ00216 256 PLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndligPPEEDETYCSYLPLAHIMEFGVtnifLARG 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 224 VIEGF-TVR-IVDKF----------------NAEQILTMIKneRITHISLVP-------------QT-LNWLMqQGLHEP 271
Cdd:PTZ00216 336 ALIGFgSPRtLTDTFarphgdltefrpvfliGVPRIFDTIK--KAVEAKLPPvgslkrrvfdhayQSrLRALK-EGKDTP 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 272 Y---------------NLQKILLGGAKLSAtmiETALQYNL---PIYNSFGMTETCS----QFltaTPEMlhaRPDTVGM 329
Cdd:PTZ00216 413 YwnekvfsapravlggRVRAMLSGGGPLSA---ATQEFVNVvfgMVIQGWGLTETVCcggiQR---TGDL---EPNAVGQ 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446270502 330 PSANVDVKI------KNPNK-EGHGELMIKGANVMNGYLYPTDLTGTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDL 398
Cdd:PTZ00216 484 LLKGVEMKLldteeyKHTDTpEPRGEILLRGPFLFKGYYKQEELTREVldEDGWFHTGDVGSIAANGTLRIIGRVKAL 561
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
24-489 |
5.72e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 58.25 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 24 SYTYQNLYCEASLLAKRLKAYQQSR---VGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVqliFCT 100
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEeraIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHV---SYL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 101 LplelrgfqivslddiefagrditTNGLLDNtmgiqydtSNETVVPKESPSNILnTSFNLddiASIMFTSGTTGPQK--A 178
Cdd:cd17654 93 L-----------------------QNKELDN--------APLSFTPEHRHFNIR-TDECL---AYVIHTSGTTGTPKivA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 179 VP-QTFRNHYASAigCKESLGFDRDTNWLSVLPIYHISGLSVLLrAVIEGFTVRIVD---KFNAEQILTMI-KNERITHI 253
Cdd:cd17654 138 VPhKCILPNIQHF--RSLFNITSEDILFLTSPLTFDPSVVEIFL-SLSSGATLLIVPtsvKVLPSKLADILfKRHRITVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 254 SLVPQTLNWLMQQGLHEPY-----NLQKILLGGAKL-SATMIETALQY--NLPIYNSFGMTETCSQFLTATPEMLHArPD 325
Cdd:cd17654 215 QATPTLFRRFGSQSIKSTVlsatsSLRVLALGGEPFpSLVILSSWRGKgnRTRIFNIYGITEVSCWALAYKVPEEDS-PV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 326 TVGMPSANVDVKIK-NPNKEGHGELMIKGANvmNGYLYPTDLTGTFENGYfNTGDIAEIDhEGYVMIYDRRKDLIISGGE 404
Cdd:cd17654 294 QLGSPLLGTVIEVRdQNGSEGTGQVFLGGLN--RVCILDDEVTVPKGTMR-ATGDFVTVK-DGELFFLGRKDSQIKRRGK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 405 NIYPYQIETVAKQFPGIsDAVCVGHPDDtwgQVPKLYFVSESdiSKAQLIAYLSQH-LAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:cd17654 370 RINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGES--SSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGK 443
|
....*.
gi 446270502 484 LQRNKL 489
Cdd:cd17654 444 VDKSEL 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
159-491 |
1.30e-08 |
|
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: 57.05 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 159 NLDDIASIMFTSGTTG-PQKAVPQTFRnHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLL-RAVIEGFTVRIVDKF 236
Cdd:cd05939 102 NFRDKLFYIYTSGTTGlPKAAVIVHSR-YYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVgQALLHGSTVVIRKKF 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 237 NAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYNLQKI-LLGGAKLSATMIETALQ-YNLP-IYNSFGMTE-TCS-- 310
Cdd:cd05939 181 SASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVrLAVGNGLRPQIWEQFVRrFGIPqIGEFYGATEgNSSlv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 311 ---------QFLTATPEMLH------ARPDTV---------------GMPSANVD-VKIKNPNKEGHGELMiKGANvmNG 359
Cdd:cd05939 261 nidnhvgacGFNSRILPSVYpirlikVDEDTGelirdsdglcipcqpGEPGLLVGkIIQNDPLRRFDGYVN-EGAT--NK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 360 YLYptdlTGTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHpddtwgQV 437
Cdd:cd05939 338 KIA----RDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV------EV 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446270502 438 P----KLYFVSESDISKAQLIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05939 408 PgvegRAGMAAIVDPERKVDLDRFSAVLAKslppYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
161-422 |
1.81e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 56.77 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESL-----GFDRDTNWLSVLPIYHI-----------SGLSV----- 219
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLkvtdrVATEEDSYFSYLPLAHVydqvietycisKGASIgfwqg 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 220 LLRAVIEGFTV----------RIVDKFNAeQILTMIKNERITHISLVPQTLNWL---MQQGL--HEPYNL---------- 274
Cdd:PLN02861 300 DIRYLMEDVQAlkptifcgvpRVYDRIYT-GIMQKISSGGMLRKKLFDFAYNYKlgnLRKGLkqEEASPRldrlvfdkik 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 275 ------QKILLGGAKLSATMIETALQYN--LPIYNSFGMTETCSQFLTATPEMLhARPDTVGMPSANVDVKIKNPNKEGH 346
Cdd:PLN02861 379 eglggrVRLLLSGAAPLPRHVEEFLRVTscSVLSQGYGLTESCGGCFTSIANVF-SMVGTVGVPMTTIEARLESVPEMGY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 347 --------GELMIKGANVMNGYLYPTDLTG-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAK 416
Cdd:PLN02861 458 dalsdvprGEICLRGNTLFSGYHKRQDLTEeVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYS 537
|
....*.
gi 446270502 417 QFPGIS 422
Cdd:PLN02861 538 RCPLIA 543
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
45-399 |
2.63e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 56.28 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 45 QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMTNQMKSIDVQLIFCTlPLELRGFQIVSlDDIEFAGRDIT 124
Cdd:PLN02387 130 KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD-SKQLKKLIDIS-SQLETVKRVIY 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 125 TNGLLDNTMGIQYDTSNETV-----VPKESPSNILNTSFNL-DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESL- 197
Cdd:PLN02387 208 MDDEGVDSDSSLSGSSNWTVssfseVEKLGKENPVDPDLPSpNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVp 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 198 GFDRDTNWLSVLPIYHISGL---SVLLR---AVIEGFTVRIVD-----KFNAEQILTMIKNeriTHISLVPQTL------ 260
Cdd:PLN02387 288 KLGKNDVYLAYLPLAHILELaaeSVMAAvgaAIGYGSPLTLTDtsnkiKKGTKGDASALKP---TLMTAVPAILdrvrdg 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 261 -----------------------------NWLMQQGLHEPY---------------NLQKILLGGAKLSA-TMIETALQY 295
Cdd:PLN02387 365 vrkkvdakgglakklfdiaykrrlaaiegSWFGAWGLEKLLwdalvfkkiravlggRIRFMLSGGAPLSGdTQRFINICL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 296 NLPIYNSFGMTETCSQFLTATPEmlharpDT----VGMPSANVDVKIKNPNKEGH---------GELMIKGANVMNGYL- 361
Cdd:PLN02387 445 GAPIGQGYGLTETCAGATFSEWD------DTsvgrVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFk 518
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446270502 362 --------YPTDltgtfENG--YFNTGDIAEIDHEGYVMIYDRRKDLI 399
Cdd:PLN02387 519 nqektdevYKVD-----ERGmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
160-423 |
3.13e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 55.54 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 160 LDDIASIMFTSGTTGPQKAVPQTFR--NHYASAIG-CKESLGFDRDTnwlsvlpIYHIS--------GLSVL--LRAVie 226
Cdd:COG1541 82 LEEIVRIHASSGTTGKPTVVGYTRKdlDRWAELFArSLRAAGVRPGD-------RVQNAfgyglftgGLGLHygAERL-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 227 GFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLM----QQGLH-EPYNLQKILLGGAKLSATM---IETALqyNLP 298
Cdd:COG1541 153 GATVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAevaeEEGIDpRDLSLKKGIFGGEPWSEEMrkeIEERW--GIK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 299 IYNSFGMTETCSQFLTATPEM--LHARPD----TVgmpsanVDVKIKNPNKEGH-GELMIkganvmngylypTDLTgtfE 371
Cdd:COG1541 231 AYDIYGLTEVGPGVAYECEAQdgLHIWEDhflvEI------IDPETGEPVPEGEeGELVV------------TTLT---K 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446270502 372 NGY----FNTGDIAEIDHE----GYVM-----IYDRRKDLIISGGENIYPYQIETVAKQFPGISD 423
Cdd:COG1541 290 EAMplirYRTGDLTRLLPEpcpcGRTHprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGP 354
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
145-417 |
1.24e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 54.35 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 145 VPKESPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGL-SVLLRA 223
Cdd:PRK07769 164 VPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLiTVLLPA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 224 VIEGFT--------VRIVDKFNAEqiLTMIKNERITHISLVPQ-TLNWLMQQGL---HEP----YNLQKILLGGAKLSAT 287
Cdd:PRK07769 244 LLGHYItfmspaafVRRPGRWIRE--LARKPGGTGGTFSAAPNfAFEHAAARGLpkdGEPpldlSNVKGLLNGSEPVSPA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 288 MI----ETALQYNLP---IYNSFGMTETcSQFLTATPEMLHAR---------------------PDTVGMPSAN------ 333
Cdd:PRK07769 322 SMrkfnEAFAPYGLPptaIKPSYGMAEA-TLFVSTTPMDEEPTviyvdrdelnagrfvevpadaPNAVAQVSAGkvgvse 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 334 ----VDVKIKNPNKEGH-GELMIKGANVMNGY------------------LYPTDLTGTFENG-YFNTGDIAeIDHEGYV 389
Cdd:PRK07769 401 waviVDPETASELPDGQiGEIWLHGNNIGTGYwgkpeetaatfqnilksrLSESHAEGAPDDAlWVRTGDYG-VYFDGEL 479
|
330 340
....*....|....*....|....*...
gi 446270502 390 MIYDRRKDLIISGGENIYPYQIETVAKQ 417
Cdd:PRK07769 480 YITGRVKDLVIIDGRNHYPQDLEYTAQE 507
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
368-486 |
1.61e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 53.99 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 GTFENGYFnTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESD 447
Cdd:PRK00174 479 STFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGG 557
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446270502 448 ISK-AQLIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK00174 558 EEPsDELRKELRNWVRKeigpIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
145-419 |
1.88e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.51 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 145 VPKESPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DRDTNWLSVLPIYHISGLSVL-LR 222
Cdd:PRK12476 177 IPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLlDRNTHGVSWLPLYHDMGLSMIgFP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 223 AVIEGFTVRIVDKFNAEQILTMIK--NERITHISLVPQTLN----WLMQQGLHEP---YNLQKILL--GGAKLSATMIET 291
Cdd:PRK12476 257 AVYGGHSTLMSPTAFVRRPQRWIKalSEGSRTGRVVTAAPNfayeWAAQRGLPAEgddIDLSNVVLiiGSEPVSIDAVTT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 292 ---AL-QYNLP---IYNSFGMTETCSQFLTATP-----------EML---HARPDTVGMPSANVDVK-----------IK 339
Cdd:PRK12476 337 fnkAFaPYGLPrtaFKPSYGIAEATLFVATIAPdaepsvvyldrEQLgagRAVRVAADAPNAVAHVScgqvarsqwavIV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 340 NPNKE-----GH-GELMIKGANVMNGYL-YPTDLTGTFEN-------------------GYFNTGDIA-EIDHEGYVMiy 392
Cdd:PRK12476 417 DPDTGaelpdGEvGEIWLHGDNIGRGYWgRPEETERTFGAklqsrlaegshadgaaddgTWLRTGDLGvYLDGELYIT-- 494
|
330 340
....*....|....*....|....*...
gi 446270502 393 DRRKDLIISGGENIYPYQIE-TVAKQFP 419
Cdd:PRK12476 495 GRIADLIVIDGRNHYPQDIEaTVAEASP 522
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
165-486 |
1.98e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 47.04 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 165 SIMFTSGTTGPQKAVPQT-------FRNHYASAIGCKESLGFDRDTN--WLSvlpiYHiSGL--SVLLRAVIEGFTVRIV 233
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSngphlvgLKYYWRSIIEKDIPTVVFSHSSigWVS----FH-GFLygSLSLGNTFVMFEGGII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 234 DKFNAEQ-ILTMIKNERITHISLVPQTLNWLMQ-----QGLHEPY---NLQKILLGGAKLSATM---IETALqyNLPIYN 301
Cdd:PTZ00237 333 KNKHIEDdLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYdlsNLKEIWCGGEVIEESIpeyIENKL--KIKSSR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 302 SFGMTET-CSQFLTAtpEMLHARPDTVGMPSANVDVKIKNPNKEGHGELMIkGANVMNGYLYPTDLTGTFEN-------- 372
Cdd:PTZ00237 411 GYGQTEIgITYLYCY--GHINIPYNATGVPSIFIKPSILSEDGKELNVNEI-GEVAFKLPMPPSFATTFYKNdekfkqlf 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 373 ----GYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFV----- 443
Cdd:PTZ00237 488 skfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVlkqdq 567
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446270502 444 SESDIS----KAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PTZ00237 568 SNQSIDlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
166-486 |
2.48e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 46.87 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 166 IMFTSGTTGPQKAVpQTFRNHYASAIGCKESLGFD----------RDTNWL---SVLpIYH--ISGLSVLLravIEGFTV 230
Cdd:PRK10524 238 ILYTSGTTGKPKGV-QRDTGGYAVALATSMDTIFGgkagetffcaSDIGWVvghSYI-VYAplLAGMATIM---YEGLPT 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 231 R--------IVDKFnaeqiltmikneRITHISLVPQTLNWLMQQGL-----HEPYNLQKILLGGAKL---SATMIETALq 294
Cdd:PRK10524 313 RpdagiwwrIVEKY------------KVNRMFSAPTAIRVLKKQDPallrkHDLSSLRALFLAGEPLdepTASWISEAL- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 295 yNLPIYNSFGMTETCSQFLTATP--EMLHARPDTVGMPSANVDVKIKNpnkEGHGELMI---KGANVMNGYLYPTDLT-- 367
Cdd:PRK10524 380 -GVPVIDNYWQTETGWPILAIARgvEDRPTRLGSPGVPMYGYNVKLLN---EVTGEPCGpneKGVLVIEGPLPPGCMQtv 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 368 ----GTFENGYF--------NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWG 435
Cdd:PRK10524 456 wgddDRFVKTYWslfgrqvySTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKG 535
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446270502 436 QVPkLYFVSESDISK-----------AQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK10524 536 QVA-VAFVVPKDSDSladrearlaleKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
298-489 |
1.45e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 44.50 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 298 PIYNSFGMTETCSQFLTATPEMLHARPDTVGMP-----SANVDVKIKNPNKEGHGELMIKGA-----NVMNG--YLYPTD 365
Cdd:PLN02654 427 PISDTWWQTETGGFMITPLPGAWPQKPGSATFPffgvqPVIVDEKGKEIEGECSGYLCVKKSwpgafRTLYGdhERYETT 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 366 LTGTFEnGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQ-----VPKL 440
Cdd:PLN02654 507 YFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQgiyafVTLV 585
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446270502 441 YFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02654 586 EGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
347-432 |
5.93e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 42.24 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 347 GELMIKGANVMNGYLYPTDLT-------------GTFENGYFNTGDIAEIdHEGYVMIYDRRKDLIISGGENIYPYQIE- 412
Cdd:PRK05850 398 GEIWVHGDNVAAGYWQKPEETertfgatlvdpspGTPEGPWLRTGDLGFI-SEGELFIVGRIKDLLIVDGRNHYPDDIEa 476
|
90 100
....*....|....*....|
gi 446270502 413 TVAKQFPGISDAVCVghPDD 432
Cdd:PRK05850 477 TIQEITGGRVAAISV--PDD 494
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
347-489 |
6.60e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 347 GELMIKGANVMNGYL----------YPTDLTGTFENGYfNTGDIAE------------IDHEgyVMIYDRRKDLiisgGE 404
Cdd:PRK05691 4067 GELCVAGTGVGRGYVgdplrtalafVPHPFGAPGERLY-RTGDLARrrsdgvleyvgrIDHQ--VKIRGYRIEL----GE 4139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446270502 405 niypyqIETVAKQFPGISDAVcVGHPDDTWGQVPKLYFV-SESDISKAQLIAYLSQHL----AKYKVPKHFEKVDTLPYT 479
Cdd:PRK05691 4140 ------IEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVpHQTVLAQGALLERIKQRLraelPDYMVPLHWLWLDRLPLN 4212
|
170
....*....|
gi 446270502 480 STGKLQRNKL 489
Cdd:PRK05691 4213 ANGKLDRKAL 4222
|
|
| COG4495 |
COG4495 |
Uncharacterized conserved protein, DUF4176 domain [Function unknown]; |
343-389 |
9.87e-03 |
|
Uncharacterized conserved protein, DUF4176 domain [Function unknown];
Pssm-ID: 443583 Cd Length: 97 Bit Score: 35.71 E-value: 9.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446270502 343 KEGHGELMI-------KGANVMNGY---LYPTDLTGTFENGYFNTGDIAEIDHEGYV 389
Cdd:COG4495 17 KGGTKKLMIigriqqnEGEETIFDYvgcPYPEGNVGPEKTYLFNHEDIDEVVFEGYE 73
|
|
| |
