|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-518 |
0e+00 |
|
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: 617.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 46 CQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNI 125
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 126 SKPKIIFTDADHYDKLYSATSAF--KPEIILTTGTKDGVLSIQDLLAPT-KTEFFYQPTPLKEGPSQTVAILTSSGTTGM 202
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELgpKDKIIVLDDKPDGVLSIEDLLSPTlGEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 203 PKAVCISNDILTQETVFVNGY--------DTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAaDYFVYLVSKYSITY 274
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFlygndgsnDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDS-ELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 275 ALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGFIVFN--HGHLKLTAAGN 352
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVnpDGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 353 PLPGIQVKIVDDDGNQ-LGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKW 431
Cdd:cd05911 320 LLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 432 KGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDiQKQLRAGVQFADEIP 511
Cdd:cd05911 400 KGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVAS-YKQLRGGVVFVDEIP 478
|
....*..
gi 21356947 512 QNHNGKV 518
Cdd:cd05911 479 KSASGKI 485
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
52-531 |
3.23e-92 |
|
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: 289.02 E-value: 3.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKII 131
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 132 FTdadhydklysatsafkpeiilttgtkdgvlsiqdllaptkteffyqptplkegpsqtVAILTSSGTTGMPKAVcisnd 211
Cdd:COG0318 101 VT---------------------------------------------------------ALILYTSGTTGRPKGV----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 212 ILTQETVFVNGY-----------DTIFISASLDWITGLWATIFSTV-NGCTRIISSKPFAADyFVYLVSKYSITYALIPP 279
Cdd:COG0318 119 MLTHRNLLANAAaiaaalgltpgDVVLVALPLFHVFGLTVGLLAPLlAGATLVLLPRFDPER-VLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 280 EHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSsYGMTEVGFIVF----NHGHLKLTAAGNPLP 355
Cdd:COG0318 198 TMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEG-YGLTETSPVVTvnpeDPGERRPGSVGRPLP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 356 GIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT-KAMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGL 434
Cdd:COG0318 277 GVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATaEAFRD--GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 435 QMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNH 514
Cdd:COG0318 355 NVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARY-KVPRR-VEFVDELPRTA 432
|
490
....*....|....*..
gi 21356947 515 NGKVVRRYARDLFVALS 531
Cdd:COG0318 433 SGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
189-518 |
4.67e-85 |
|
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: 266.84 E-value: 4.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 189 QTVAILTSSGTTGMPKAVCISN-DILTQ-----ETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTrIISSKPFAADY 262
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrNLLAAaaalaASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGT-VVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 263 FVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKlAPNGVLNSSYGMTEVGFIVF-- 340
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVAtg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 341 --NHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATkAMQDEEGWFHTGDMGYFDEDDY 418
Cdd:cd04433 159 ppDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 419 LYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIQK 498
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKV 317
|
330 340
....*....|....*....|
gi 21356947 499 QLRagVQFADEIPQNHNGKV 518
Cdd:cd04433 318 PRR--VVFVDALPRTASGKI 335
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
35-521 |
1.08e-79 |
|
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: 258.32 E-value: 1.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 35 FKNMRNWPKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYImptaVACFFH----GTPFQSA 110
Cdd:cd05904 12 FLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEF----PVAFLAvlslGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 111 NPILEESTLKHLYNISKPKIIFTDADHYDKLysatSAFKPEIILTTGTKDGVLSIQDLLAPTKtefFYQPTPLKEGPSQT 190
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFTTAELAEKL----ASLALPVVLLDSAEFDSLSFSDLLFEAD---EAEPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 191 VAILTSSGTTGMPKAVCISN-DILTQETVFVNGYDTIFISAS-------LDWITGLWATIFSTV-NGCTRIISSKpFAAD 261
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHrNLIAMVAQFVAGEGSNSDSEDvflcvlpMFHIYGLSSFALGLLrLGATVVVMPR-FDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 262 YFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGFIV-- 339
Cdd:cd05904 240 ELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVam 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 340 ---FNHGHLKLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDE 415
Cdd:cd05904 320 cfaPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 416 DDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRL-P 494
Cdd:cd05904 400 DGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVaP 479
|
490 500
....*....|....*....|....*..
gi 21356947 495 diQKQLRAgVQFADEIPQNHNGKVVRR 521
Cdd:cd05904 480 --YKKVRK-VAFVDAIPKSPSGKILRK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
23-526 |
9.65e-79 |
|
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: 256.68 E-value: 9.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 23 PFKP--ETSLGRIIFKNMRNW---PKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNT-TYIMPT 96
Cdd:cd17642 7 PFYPleDGTAGEQLHKAMKRYasvPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSlQFFLPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 97 aVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKLYSATSAFK--PEIILTTGTKD--GVLS----IQDL 168
Cdd:cd17642 87 -IAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKiiKTIIILDSKEDykGYQClytfITQN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 169 LAPTKTEFFYQPtPLKEGPSQTVAILTSSGTTGMPKAVcisndILTQETV---FVNGYDTIFISASLDWITGLWATIFST 245
Cdd:cd17642 166 LPPGFNEYDFKP-PSFDRDEQVALIMNSSGSTGLPKGV-----QLTHKNIvarFSHARDPIFGNQIIPDTAILTVIPFHH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 246 VNGCT----------RIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVE 315
Cdd:cd17642 240 GFGMFttlgylicgfRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 316 RVKKLAPNGVLNSSYGMTEV--GFIVFNHGHLKLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIVHNGFSWNGYFADP 392
Cdd:cd17642 320 AVAKRFKLPGIRQGYGLTETtsAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 393 EATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALV 472
Cdd:cd17642 400 EATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 21356947 473 VREDNATLTAQQVIDHVAKRLPDiQKQLRAGVQFADEIPQNHNGKVVRRYARDL 526
Cdd:cd17642 480 VLEAGKTMTEKEVMDYVASQVST-AKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
2-521 |
1.53e-63 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 216.39 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 2 SKLPcsyDAEnkiwkgIPQNNPfkpetsLGRIIFKNMRNWPKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKD 81
Cdd:PLN02246 12 SKLP---DIY------IPNHLP------LHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 82 IIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKLYSATSAFKPEIILTTGTKDG 161
Cdd:PLN02246 77 VVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 162 VLSIQDLLAPTKTEFfyqpTPLKEGPSQTVAILTSSGTTGMPKAVCISNDIL----TQET------VFVNGYDTIFISAS 231
Cdd:PLN02246 157 CLHFSELTQADENEL----PEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLvtsvAQQVdgenpnLYFHSDDVILCVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 232 LDWITGLWATIFSTVN-GCTRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMT 310
Cdd:PLN02246 233 MFHIYSLNSVLLCGLRvGAAILIMPK-FEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 311 QATVERVKKLAPNGVLNSSYGMTEVGFIVfnhgHLKLTAAGNPLP-----------GIQVKIVD-DDGNQLGVNQTGEII 378
Cdd:PLN02246 312 KELEDAFRAKLPNAVLGQGYGMTEAGPVL----AMCLAFAKEPFPvksgscgtvvrNAELKIVDpETGASLPRNQPGEIC 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 379 VHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:PLN02246 388 IRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356947 459 VYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPdIQKQLRAgVQFADEIPQNHNGKVVRR 521
Cdd:PLN02246 468 MKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVV-FYKRIHK-VFFVDSIPKAPSGKILRK 528
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
52-518 |
1.57e-63 |
|
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: 213.63 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKII 131
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 132 FTDadhydklysatsafkpeiilttgtkdgvlsiqdllaptkteffyqptplkegpsqTVAILTSSGTTGMPKAVcisnd 211
Cdd:cd17631 97 FDD-------------------------------------------------------LALLMYTSGTTGRPKGA----- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 212 ILTQETVFVNGYDTI-----------FISASLDWITGLWATIFSTV-NGCTRIISSKpFAADYFVYLVSKYSITYALIPP 279
Cdd:cd17631 117 MLTHRNLLWNAVNALaaldlgpddvlLVVAPLFHIGGLGVFTLPTLlRGGTVVILRK-FDPETVLDLIERHRVTSFFLVP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 280 EHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKklAPNGVLNSSYGMTEVGFIVF---NHGHL-KLTAAGNPLP 355
Cdd:cd17631 196 TMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQ--ARGVKFVQGYGMTETSPGVTflsPEDHRrKLGSAGRPVF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 356 GIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT-KAMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGL 434
Cdd:cd17631 274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATaAAFRD--GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 435 QMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPD--IQKQlragVQFADEIPQ 512
Cdd:cd17631 352 NVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARykIPKS----VEFVDALPR 427
|
....*.
gi 21356947 513 NHNGKV 518
Cdd:cd17631 428 NATGKI 433
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
48-432 |
8.68e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 211.40 E-value: 8.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 48 ISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISK 127
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 128 PKIIFTDADHY-DKLYSATSAFKPEIILTTGTKDGVLSIQDLLAPTKTEFFYQPTPLKEGPSQTVAILTSSGTTGMPKAV 206
Cdd:pfam00501 94 AKVLITDDALKlEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 207 CIS-----NDILTQETVF-----VNGYDTIFISASLDWITGL-WATIFSTVNGCTRIISSK--PFAADYFVYLVSKYSIT 273
Cdd:pfam00501 174 MLThrnlvANVLSIKRVRprgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGfpALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 274 YALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSsYGMTEVGFIVFNHG-----HLKLT 348
Cdd:pfam00501 254 VLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNG-YGLTETTGVVTTPLpldedLRSLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 349 AAGNPLPGIQVKIVDDD-GNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKE 427
Cdd:pfam00501 333 SVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKD 412
|
....*
gi 21356947 428 VLKWK 432
Cdd:pfam00501 413 QIKLG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
29-525 |
7.51e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 208.89 E-value: 7.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 29 SLGRIIFKNMRNWPKNVcqISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTtyimPTAVACFFhGTPFQ 108
Cdd:PRK06187 7 TIGRILRHGARKHPDKE--AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNS----HEYLEAYF-AVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 109 SA--NPI---LEESTLKHLYNISKPKIIFTDAD---HYDKLYSATSAFKPEIILTTGTKDG----VLSIQDLLApTKTEF 176
Cdd:PRK06187 80 GAvlHPInirLKPEEIAYILNDAEDRVVLVDSEfvpLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLA-AASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 177 FYQPTPlkeGPSQTVAILTSSGTTGMPKAVCISNDILTQETVFVNGY------DTIFISASLDWITGLWATIFSTVNGCT 250
Cdd:PRK06187 159 FDFPDI---DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWlklsrdDVYLVIVPMFHVHAWGLPYLALMAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 251 RIISsKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLnSSY 330
Cdd:PRK06187 236 QVIP-RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLV-QGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 331 GMTEVGFIV----FNHGHL----KLTAAGNPLPGIQVKIVDDDGNQLGVN--QTGEIIVHNGfsWN--GYFADPEAT-KA 397
Cdd:PRK06187 314 GMTETSPVVsvlpPEDQLPgqwtKRRSAGRPLPGVEARIVDDDGDELPPDggEVGEIIVRGP--WLmqGYWNRPEATaET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 398 MQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDN 477
Cdd:PRK06187 392 IDG--GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 21356947 478 ATLTAQQVIDHVAKRLPD--IQKQLRagvqFADEIPQNHNGKVVRRYARD 525
Cdd:PRK06187 470 ATLDAKELRAFLRGRLAKfkLPKRIA----FVDELPRTSVGKILKRVLRE 515
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
53-521 |
9.91e-61 |
|
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: 207.42 E-value: 9.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 53 GVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIF 132
Cdd:cd05936 22 GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 133 TDadhydklysatsafkpeiilttgtkdgvLSIQDLLAPTKTEFFYQPTPlkegPSQTVAILTSSGTTGMPKAVcisndI 212
Cdd:cd05936 102 VA----------------------------VSFTDLLAAGAPLGERVALT----PEDVAVLQYTSGTTGVPKGA-----M 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 213 LTQETVFVNGYDTIFISASLDW-------------ITGLWATIF-STVNGCTRIISSKPFAADyFVYLVSKYSITyaLIP 278
Cdd:cd05936 145 LTHRNLVANALQIKAWLEDLLEgddvvlaalplfhVFGLTVALLlPLALGATIVLIPRFRPIG-VLKEIRKHRVT--IFP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 279 --PEHCCSLLDCPTATPEKLGSLtKLNFGGG-RMTQATVERVKKLApNGVLNSSYGMTEVGFIV-FNH--GHLKLTAAGN 352
Cdd:cd05936 222 gvPTMYIALLNAPEFKKRDFSSL-RLCISGGaPLPVEVAERFEELT-GVPIVEGYGLTETSPVVaVNPldGPRKPGSIGI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 353 PLPGIQVKIVDDDGNQLGVNQTGEIIV--HNGFSwnGYFADPEAT-KAMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVL 429
Cdd:cd05936 300 PLPGTEVKIVDDDGEELPPGEVGELWVrgPQVMK--GYWNRPEETaEAFVD--GWLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 430 KWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADE 509
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGY-KVPRQ-VEFRDE 453
|
490
....*....|..
gi 21356947 510 IPQNHNGKVVRR 521
Cdd:cd05936 454 LPKSAVGKILRR 465
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-534 |
4.43e-59 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 204.83 E-value: 4.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 4 LPCSYDAENkIWKGIPQNNPFKPETSLGRIIFKNMRNWPKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDII 83
Cdd:PLN02330 5 IQKQEDNEH-IFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 84 GISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKLYSATSafkPEIILTTGTKDGVL 163
Cdd:PLN02330 84 VVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGL---PVIVLGEEKIEGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 164 SIQDLL-APTKTeffyQPTPLKEGPSQT--VAILTSSGTTGMPKAVCISNDILTQ---ETVFVNGYDTIFISASLDWIT- 236
Cdd:PLN02330 161 NWKELLeAADRA----GDTSDNEEILQTdlCALPFSSGTTGISKGVMLTHRNLVAnlcSSLFSVGPEMIGQVVTLGLIPf 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 237 ----GLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLtKLNfggGRMTQA 312
Cdd:PLN02330 237 fhiyGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKL-KLQ---AIMTAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 313 T------VERVKKLAPNGVLNSSYGMTEVGFIVFNHGH-------LKLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEII 378
Cdd:PLN02330 313 AplapelLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDpekghgiAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 379 VHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:PLN02330 393 VRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVP 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356947 459 VYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRRYARDLFVALSKKN 534
Cdd:PLN02330 473 LPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHY-KKVRV-VQFVDSIPKSLSGKIMRRLLKEKMLSINKAN 546
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
38-525 |
2.37e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 202.06 E-value: 2.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 38 MRNWPKNVCQISDS---------EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMptaVACFfhGTpfQ 108
Cdd:PRK07656 4 WMTLPELLARAARRfgdkeayvfGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWV---IAAL--GA--L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 109 SA-------NPILEESTLKHLYNISKPKIIFTDADHYDKLYSATSAF---KPEIILTTGT----KDGVLSIQDLLAPTKT 174
Cdd:PRK07656 77 KAgavvvplNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpalEHVVICETEEddphTEKMKTFTDFLAAGDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 175 EFFYQPTplkeGPSQTVAILTSSGTTGMPKAV------CISN-----DILTQE----TVFVN------GYdTIFISASLd 233
Cdd:PRK07656 157 AERAPEV----DPDDVADILFTSGTTGRPKGAmlthrqLLSNaadwaEYLGLTegdrYLAANpffhvfGY-KAGVNAPL- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 234 witglwatifstVNGCTRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQAT 313
Cdd:PRK07656 231 ------------MRGATILPLPV-FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 314 VERVKKLAPNGVLNSSYGMTEV-GFIVFN--HGHLKLTA--AGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHnGFS-WNG 387
Cdd:PRK07656 298 LERFESELGVDIVLTGYGLSEAsGVTTFNrlDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVR-GPNvMKG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 388 YFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDV 467
Cdd:PRK07656 377 YYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356947 468 PGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:PRK07656 457 GKAYVVLKPGAELTEEELIAYCREHLAKY-KVPRS-IEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
48-521 |
7.60e-57 |
|
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: 197.53 E-value: 7.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 48 ISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTtyiMPTAVAcfFHGTPFQSA-----NPILEESTLKHL 122
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNG---LEFVVA--FLAAARAGAvvaplNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 123 YNISKPKIIFTDADHYDKLYSATSAFKPEII---LTTGTKDGVLSIQDL--LAPTKTEFFYQPTPLkegPSQTVAILTSS 197
Cdd:cd05926 82 LADLGSKLVLTPKGELGPASRAASKLGLAILelaLDVGVLIRAPSAESLsnLLADKKNAKSEGVPL---PDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 198 GTTGMPKAVCISN-DILTQETVFVNGY-----DTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYS 271
Cdd:cd05926 159 GTTGRPKGVPLTHrNLAASATNITNTYkltpdDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 272 IT-YALIPPEHCCsLLDCPTATPEKlgSLTKLNF---GGGRMTQATVERVKKLAPNGVLnSSYGMTEVGFIV----FNHG 343
Cdd:cd05926 239 ATwYTAVPTIHQI-LLNRPEPNPES--PPPKLRFirsCSASLPPAVLEALEATFGAPVL-EAYGMTEAAHQMtsnpLPPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 344 HLKLTAAGNPLpGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTD 423
Cdd:cd05926 315 PRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 424 RKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPD--IQKQlr 501
Cdd:cd05926 394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAfkVPKK-- 471
|
490 500
....*....|....*....|
gi 21356947 502 agVQFADEIPQNHNGKVVRR 521
Cdd:cd05926 472 --VYFVDELPKTATGKIQRR 489
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
52-530 |
2.77e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 191.30 E-value: 2.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKII 131
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 132 FTDADHYDKLYSATSAFKPEIIL------TTGTKDGVLSIQDLLAPTkteffYQPTPLKEGPSQTVA-ILTSSGTTGMPK 204
Cdd:PRK08316 113 LVDPALAPTAEAALALLPVDTLIlslvlgGREAPGGWLDFADWAEAG-----SVAEPDVELADDDLAqILYTSGTESLPK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 AVCISNDILTQE---TVFVNGYDT---------IFISASLDWITGLWATIfstvnGCTRIISSKPfAADYFVYLVSKYSI 272
Cdd:PRK08316 188 GAMLTHRALIAEyvsCIVAGDMSAddiplhalpLYHCAQLDVFLGPYLYV-----GATNVILDAP-DPELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 273 TYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGFI--VFNHG-HL-KLT 348
Cdd:PRK08316 262 TSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAPLatVLGPEeHLrRPG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 349 AAGNPLPGIQVKIVDDDGNQLGVNQTGEIiVHNG-FSWNGYFADPEATK-AMQDeeGWFHTGDMGYFDEDDYLYMTDRKK 426
Cdd:PRK08316 342 SAGRPVLNVETRVVDDDGNDVAPGEVGEI-VHRSpQLMLGYWDDPEKTAeAFRG--GWFHSGDLGVMDEEGYITVVDRKK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 427 EVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLP--DIQKQlragV 504
Cdd:PRK08316 419 DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAgfKVPKR----V 494
|
490 500
....*....|....*....|....*.
gi 21356947 505 QFADEIPQNHNGKVVRRYARDLFVAL 530
Cdd:PRK08316 495 IFVDELPRNPSGKILKRELRERYAGA 520
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
50-521 |
2.12e-52 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 187.24 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 50 DSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGIsarnttyIMP----TAV---ACFFHGTPFQSANPILEESTLKHL 122
Cdd:COG0365 34 DGEERTLTYAELRREVNRFANALRALGVKKGDRVAI-------YLPnipeAVIamlACARIGAVHSPVFPGFGAEALADR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 123 YNISKPKIIFTDADHY--DKLYSATSAF--------KPEIILTTG------TKDGVLSIQDLLAPTKTEFFYQPTPlkeg 186
Cdd:COG0365 107 IEDAEAKVLITADGGLrgGKVIDLKEKVdealeelpSLEHVIVVGrtgadvPMEGDLDWDELLAAASAEFEPEPTD---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISN-DILTQ---ETVFVNGY---DTIFISASLDWITGLWATIFST-VNGCTRIIS-SKP 257
Cdd:COG0365 183 ADDPLFILYTSGTTGKPKGVVHTHgGYLVHaatTAKYVLDLkpgDVFWCTADIGWATGHSYIVYGPlLNGATVVLYeGRP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 258 FA--ADYFVYLVSKYSITYalippeHCCSlldcPTA----------TPEK--LGSLTKLNFGGGRMTQATVERVKKLApn 323
Cdd:COG0365 263 DFpdPGRLWELIEKYGVTV------FFTA----PTAiralmkagdePLKKydLSSLRLLGSAGEPLNPEVWEWWYEAV-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 324 GV-LNSSYGMTEVG--FIVFNHGH-LKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGF--SWNGYFADPEATKA 397
Cdd:COG0365 331 GVpIVDGWGQTETGgiFISNLPGLpVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 398 --MQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVRE 475
Cdd:COG0365 411 tyFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLK 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 21356947 476 DNATLT---AQQVIDHVAKRL-----PDIqkqlragVQFADEIPQNHNGKVVRR 521
Cdd:COG0365 491 PGVEPSdelAKELQAHVREELgpyayPRE-------IEFVDELPKTRSGKIMRR 537
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
4-529 |
6.78e-51 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 183.12 E-value: 6.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 4 LPCSYDAENKIW--KGIPQNNPFKPETSLGRIIFKNmRNWPKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSR-GLDHK 80
Cdd:PLN02574 14 PPFWYSPETGIYssKHPPVPLPSDPNLDAVSFIFSH-HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 81 DIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKLysatSAFKPEIILTTGT-- 158
Cdd:PLN02574 93 DVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKL----SPLGVPVIGVPENyd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 159 -KDGVLSIQDLLAPTKTEFFYQPTPLKeGPSQTVAILTSSGTTGMPKAVCIS--NDILTQETvFVN---------GYDTI 226
Cdd:PLN02574 169 fDSKRIEFPKFYELIKEDFDFVPKPVI-KQDDVAAIMYSSGTTGASKGVVLThrNLIAMVEL-FVRfeasqyeypGSDNV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 227 FISA-SLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSIT-YALIPPEHCCSLLDCPTATPEKLGSLTKLNF 304
Cdd:PLN02574 247 YLAAlPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVThFPVVPPILMALTKKAKGVCGEVLKSLKQVSC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 305 GGGRMTQATVERVKKLAPNGVLNSSYGMTE---VGFIVFNHGHL-KLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIV 379
Cdd:PLN02574 327 GAAPLSGKFIQDFVQTLPHVDFIQGYGMTEstaVGTRGFNTEKLsKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 380 HNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGV 459
Cdd:PLN02574 407 QGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAV 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 460 YDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIQKQLRagVQFADEIPQNHNGKVVRRYARDLFVA 529
Cdd:PLN02574 487 PDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRK--VVFVQSIPKSPAGKILRRELKRSLTN 554
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
67-524 |
3.03e-48 |
|
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: 173.40 E-value: 3.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 67 RIAQQLKSRGLDHKD-IIGISARNTTYImPTAVACFFHGTP----FQSANPILEESTLKHLYNISKPKIIFTDADHYDKL 141
Cdd:cd05922 5 AAASALLEAGGVRGErVVLILPNRFTYI-ELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 142 YSATSAfkpeiiltTGTKDGVLSIQDLLAPTKteffyqPTPLKE-GPSQTVAILTSSGTTGMPKAVCISNDILTQETVFV 220
Cdd:cd05922 84 RDALPA--------SPDPGTVLDADGIRAARA------SAPAHEvSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 221 NGY------DTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSIT-YALIPPEHccSLLDCPTATP 293
Cdd:cd05922 150 AEYlgitadDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATgLAGVPSTY--AMLTRLGFDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 294 EKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE----VGFIVFNHGHLKLTAAGNPLPGIQVKIVDDDGNQL 369
Cdd:cd05922 228 AKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEatrrMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 370 GVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELP 449
Cdd:cd05922 308 PPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 450 EVKRVCVIGVyDETQGDVPGALVVREDNATLTAqqVIDHVAKRLPdiQKQLRAGVQFADEIPQNHNGKVVRRYAR 524
Cdd:cd05922 388 LIIEAAAVGL-PDPLGEKLALFVTAPDKIDPKD--VLRSLAERLP--PYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
30-521 |
1.04e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 173.96 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 30 LGRIIFKNMRNWPKNVCQIsDSEGvEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPF-- 107
Cdd:PRK07788 51 FAGLVAHAARRAPDRAALI-DERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIil 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 108 ---QSANPILEESTLKHlynisKPKIIFTDaDHYDKLYSATSAFKPEIILTTGTKD-------GVLSIQDLLAPTKTEFF 177
Cdd:PRK07788 129 lntGFSGPQLAEVAARE-----GVKALVYD-DEFTDLLSALPPDLGRLRAWGGNPDddepsgsTDETLDDLIAGSSTAPL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 178 yqPTPLKEGPSqtvaILTSSGTTGMPKAVCISN--------DILTQETVFVNGydTIFISASLDWITGLWATIFSTVNGC 249
Cdd:PRK07788 203 --PKPPKPGGI----VILTSGTTGTPKGAPRPEpsplaplaGLLSRVPFRAGE--TTLLPAPMFHATGWAHLTLAMALGS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 250 TRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEK--LGSLTKLNFGGGRMTQATVERV-KKLAPngVL 326
Cdd:PRK07788 275 TVVLRRR-FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKydTSSLKIIFVSGSALSPELATRAlEAFGP--VL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 327 NSSYGMTEVGF-IVFNHGHLKL--TAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYfADPeATKAMQDeeG 403
Cdd:PRK07788 352 YNLYGSTEVAFaTIATPEDLAEapGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY-TDG-RDKQIID--G 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQ 483
Cdd:PRK07788 428 LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDED 507
|
490 500 510
....*....|....*....|....*....|....*...
gi 21356947 484 QVIDHVAKRLPDiQKQLRAgVQFADEIPQNHNGKVVRR 521
Cdd:PRK07788 508 AIKDYVRDNLAR-YKVPRD-VVFLDELPRNPTGKVLKR 543
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
172-521 |
3.99e-47 |
|
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: 169.45 E-value: 3.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 172 TKTEFFYQPTPLKEGPSQTVAILTSSGTTGMPKAVCIS------NDILTQETVFVNGYDTIFISASLDWITGLWATIFST 245
Cdd:cd05912 61 TPNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTfgnhwwSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 246 VNGCTRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLD-CPTATPEklgSLTKLNFGGGRMTQATVERVKKLapNG 324
Cdd:cd05912 141 IYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQRLLEiLGEGYPN---NLRCILLGGGPAPKPLLEQCKEK--GI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 325 VLNSSYGMTEVG--FIVFN--HGHLKLTAAGNPLPGIQVKIVDDDGNQLGVnqtGEIIVHNGFSWNGYFADPEATKAMQd 400
Cdd:cd05912 215 PVYQSYGMTETCsqIVTLSpeDALNKIGSAGKPLFPVELKIEDDGQPPYEV---GEILLKGPNVTKGYLNRPDATEESF- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 401 EEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREdnATL 480
Cdd:cd05912 291 ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPI 368
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21356947 481 TAQQVIDHVAKRLP--DIQKQlragVQFADEIPQNHNGKVVRR 521
Cdd:cd05912 369 SEEELIAYCSEKLAkyKVPKK----IYFVDELPRTASGKLLRH 407
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-521 |
1.43e-46 |
|
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: 168.24 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 53 GVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTtyimPTAVACFFH----GTPFQSANPILEESTLKHLYNISKP 128
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNC----PEFLFAWFAlaklGAVLVPINTALRGDELAYIIDHSGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 129 KIIFTDadhydklysatsafkpeiilttgtkdgvlsiqdllaptkteffyqptplkegpsqTVAILTSSGTTGMPKAVCI 208
Cdd:cd05934 77 QLVVVD-------------------------------------------------------PASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 209 SNDILT---QETVFVNGY---DTIFISASLDWITGLWATIFSTV-NGCTRIISSKpFAADYFVYLVSKYSITYA-LIPPe 280
Cdd:cd05934 102 THANLTfagYYSARRFGLgedDVYLTVLPLFHINAQAVSVLAALsVGATLVLLPR-FSASRFWSDVRRYGATVTnYLGA- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 281 hCCSLLdcpTATPEKLgsltklnfgggRMTQATVeRVKKLAPN------------GV-LNSSYGMTEVGFIVFN--HGHL 345
Cdd:cd05934 180 -MLSYL---LAQPPSP-----------DDRAHRL-RAAYGAPNppelheefeerfGVrLLEGYGMTETIVGVIGprDEPR 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 346 KLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSW---NGYFADPEAT-KAMqdEEGWFHTGDMGYFDEDDYLYM 421
Cdd:cd05934 244 RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWgffKGYYNMPEATaEAM--RNGWFHTGDLGYRDADGFFYF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 422 TDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDiqKQLR 501
Cdd:cd05934 322 VDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY--FKVP 399
|
490 500
....*....|....*....|
gi 21356947 502 AGVQFADEIPQNHNGKVVRR 521
Cdd:cd05934 400 RYIRFVDDLPKTPTEKVAKA 419
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
162-521 |
2.72e-45 |
|
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: 164.96 E-value: 2.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 162 VLSIQDLLAPTKTEFFyqptpLKEGPSQTVAILTS----------SGTTGMPKAV------CISNDILTQETVFVNGYDT 225
Cdd:cd05935 53 VVPINPMLKERELEYI-----LNDSGAKVAVVGSElddlalipytSGTTGLPKGCmhthfsAAANALQSAVWTGLTPSDV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 226 IFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFG 305
Cdd:cd05935 128 ILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 306 GGRMTQATVERVKKLApnGV-LNSSYGMTE-VGFIVFN-HGHLKLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIVHN 381
Cdd:cd05935 208 GAPMPPAVAEKLLKLT--GLrFVEGYGLTEtMSQTHTNpPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 382 GFSWNGYFADPEAT-KAMQDEEG--WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:cd05935 286 PQIFKGYWNRPEETeESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 459 VYDETQGDVPGALVV--REDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRR 521
Cdd:cd05935 366 VPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAREQMAAY-KYPRE-VEFVDELPRSASGKILWR 428
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
284-520 |
3.28e-44 |
|
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: 159.36 E-value: 3.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 284 SLLDCPTATPEKLGSLTKLnfgGGRMTQATVERVKKLAPnGVLNSSYGMTEV-GFIVFNHGHLKLTAAGNPLPGIQVKIV 362
Cdd:cd17637 101 NLLDAAEKSGVDLSSLRHV---LGLDAPETIQRFEETTG-ATFWSLYGQTETsGLVTLSPYRERPGSAGRPGPLVRVRIV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 363 DDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATkAMQDEEGWFHTGDMGYFDEDDYLYMTDRK--KEVLKWKGLQMWPAE 440
Cdd:cd17637 177 DDNDRPVPAGETGEIVVRGPLVFQGYWNLPELT-AYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 441 VEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIQKQLRagVQFADEIPQNHNGKVVR 520
Cdd:cd17637 256 VEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKPRY--VVFVEALPKTADGSIDR 333
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
53-525 |
1.95e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 161.21 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 53 GVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANpileestlkhlYNISKPKIIF 132
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN-----------YRLAADEVAY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 133 TDADHYDKLYSATSAFkpEIILTTGTKDGVLsiqDLLAPTKTEFFYQP----TPLK-EGPSQTVAILTSSGTTGMPKAVC 207
Cdd:PRK06145 94 ILGDAGAKLLLVDEEF--DAIVALETPKIVI---DAAAQADSRRLAQGgleiPPQAaVAPTDLVRLMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 208 ISND--------------ILTQETVFVNGYDTIFISASLDWITGLWatifstVNGCTRIisSKPFAADYFVYLVSKYSIT 273
Cdd:PRK06145 169 HSYGnlhwksidhvialgLTASERLLVVGPLYHVGAFDLPGIAVLW------VGGTLRI--HREFDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 274 YALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEV--GFIVFNHGHL--KLTA 349
Cdd:PRK06145 241 CAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETcsGDTLMEAGREieKIGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 350 AGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATkAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVL 429
Cdd:PRK06145 321 TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKT-AEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 430 KWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIQ--KQLRagvqFA 507
Cdd:PRK06145 400 ISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKvpRQLK----VR 475
|
490
....*....|....*...
gi 21356947 508 DEIPQNHNGKVVRRYARD 525
Cdd:PRK06145 476 DELPRNPSGKVLKRVLRD 493
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
188-525 |
3.64e-43 |
|
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: 159.04 E-value: 3.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 188 SQTVAILTSSGTTGMPKAVCISNDILTQETVFVNGY------DTIFISASLDWITGLWATIFSTVN-GCTRI-ISSKPFA 259
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWlglrpdDIHWNIADPGWAKGAWSSFFGPWLlGATVFvYEGPRFD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 260 ADYFVYLVSKYSITyalippehccSLLDCPTA--------TPE-KLGSLTKLNFGGGRMTQATVERVK-KLAPNgvLNSS 329
Cdd:cd05972 161 AERILELLERYGVT----------SFCGPPTAyrmlikqdLSSyKFSHLRLVVSAGEPLNPEVIEWWRaATGLP--IRDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVFNHGHLKLT--AAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHngFSWN----GYFADPEATKAmQDEEG 403
Cdd:cd05972 229 YGQTETGLTVGNFPDMPVKpgSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIK--LPPPglflGYVGDPEKTEA-SIRGD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLT-- 481
Cdd:cd05972 306 YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSee 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 21356947 482 -AQQVIDHVAKRL-----PDIqkqlragVQFADEIPQNHNGKVVRRYARD 525
Cdd:cd05972 386 lAEELQGHVKKVLapykyPRE-------IEFVEELPKTISGKIRRVELRD 428
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
166-524 |
1.33e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 159.38 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 166 QDLLAPTKTeffYQPTPLKEG--PSQTVAILTSSGTTGMPKAVCISNDILTQETVFvngydtifISASLDW---ITGLWA 240
Cdd:PRK06188 147 VDLLAAAAK---FGPAPLVAAalPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI--------QLAEWEWpadPRFLMC 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 241 TIFSTVNGCT---------RIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQ 311
Cdd:PRK06188 216 TPLSHAGGAFflptllrggTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 312 AT-VERVKKLAPngVLNSSYGMTEVGFIVF-----NHGHLK---LTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNG 382
Cdd:PRK06188 296 VRlAEAIERFGP--IFAQYYGQTEAPMVITylrkrDHDPDDpkrLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 383 FSWNGYFADPEAT-KAMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYD 461
Cdd:PRK06188 374 LVMDGYWNRPEETaEAFRD--GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPD 451
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 462 ETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIQ--KQlragVQFADEIPQNHNGKVVRRYAR 524
Cdd:PRK06188 452 EKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHapKQ----VDFVDSLPLTALGKPDKKALR 512
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-520 |
3.95e-42 |
|
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: 153.43 E-value: 3.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVcISNDILT-------QETVFVNGYDTIFISASLDWITGLWATIF-STVNGCTrIISSKPFAADYFV 264
Cdd:cd17638 5 IMFTSGTTGRSKGV-MCAHRQTlraaaawADCADLTEDDRYLIINPFFHTFGYKAGIVaCLLTGAT-VVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 265 YLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGFIVF---- 340
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMcrpg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 341 NHGHLKLTAAGNPLPGIQVKIVDDdgnqlgvnqtGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLY 420
Cdd:cd17638 163 DDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 421 MTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQL 500
Cdd:cd17638 233 ITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANY-KVP 311
|
330 340
....*....|....*....|
gi 21356947 501 RAgVQFADEIPQNHNGKVVR 520
Cdd:cd17638 312 RF-VRFLDELPRNASGKVMK 330
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-521 |
5.54e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 156.66 E-value: 5.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 38 MRNWPKNVCQISDS------EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNT--TY--IMptavACFFHG--T 105
Cdd:PRK03640 4 MPNWLKQRAFLTPDrtaiefEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGmeMIlvIH----ALQQLGavA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 106 PFQSANPILEEST--LKHlyniSKPKIIFTDADHYDKLYSATSAfkpeiilttgtkdgvlSIQDLLAPTKTEFFYQPT-P 182
Cdd:PRK03640 80 VLLNTRLSREELLwqLDD----AEVKCLITDDDFEAKLIPGISV----------------KFAELMNGPKEEAEIQEEfD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 183 LkegpSQTVAILTSSGTTGMPKAVcisndiltQETvfvngYDTIFISA---SLD--------W--------ITGLWATIF 243
Cdd:PRK03640 140 L----DEVATIMYTSGTTGKPKGV--------IQT-----YGNHWWSAvgsALNlglteddcWlaavpifhISGLSILMR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 244 STVNGCTriisskpfaadyfVYLVSKYS---ITYALIppEHCCSLLDCPTATPEKLgsLTKL-------NF-----GGGR 308
Cdd:PRK03640 203 SVIYGMR-------------VVLVEKFDaekINKLLQ--TGGVTIISVVSTMLQRL--LERLgegtypsSFrcmllGGGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 309 MTQATVERVK-KLAPngvLNSSYGMTEVGF-IV---FNHGHLKLTAAGNPLPGIQVKIVDDdGNQLGVNQTGEIIVHNGF 383
Cdd:PRK03640 266 APKPLLEQCKeKGIP---VYQSYGMTETASqIVtlsPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 384 SWNGYFADPEATK-AMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDE 462
Cdd:PRK03640 342 VTKGYLNREDATReTFQD--GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356947 463 TQGDVPGALVVREdnATLTAQQVIDHVAKRLP--DIQKQlragVQFADEIPQNHNGKVVRR 521
Cdd:PRK03640 420 KWGQVPVAFVVKS--GEVTEEELRHFCEEKLAkyKVPKR----FYFVEELPRNASGKLLRH 474
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
305-525 |
1.22e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 157.23 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 305 GGGRMTQATVERVKKLAPNGVLnSSYGMTEVGFIV-FN-HGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNG 382
Cdd:PRK05677 334 GGMALQLATAERWKEVTGCAIC-EGYGMTETSPVVsVNpSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 383 FSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDE 462
Cdd:PRK05677 413 QVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDE 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356947 463 TQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:PRK05677 493 KSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGY-KVPKA-VEFRDELPTTNVGKILRRELRD 553
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
56-518 |
2.44e-41 |
|
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: 154.08 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 56 VTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTda 135
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 136 dhydklysatsafkpeiilttgtkdgvlsiqdllaptkTEFFYQPTPLKEgPSQTVAILTSSGTTGMPKAVCISNDILTQ 215
Cdd:cd05903 80 --------------------------------------PERFRQFDPAAM-PDAVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 216 ETVF------VNGYDTIFISASLDWITG-LWATIFSTVNGCTRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLDC 288
Cdd:cd05903 121 SIRQyaerlgLGPGDVFLVASPMAHQTGfVYGFTLPLLLGAPVVLQDI-WDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 289 PTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLnSSYGMTEVGFIVFN----HGHLKLTAAGNPLPGIQVKIVDD 364
Cdd:cd05903 200 VEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVC-SAYGSTECPGAVTSitpaPEDRRLYTDGRPLPGVEIKVVDD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 365 DGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAmQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAV 444
Cdd:cd05903 279 TGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-AAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDL 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 445 IDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRlpDIQKQ-LRAGVQFADEIPQNHNGKV 518
Cdd:cd05903 358 LLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQ--GVAKQyWPERLVHVDDLPRTPSGKV 430
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-525 |
6.36e-41 |
|
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: 154.71 E-value: 6.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 50 DSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPT--AVACFfhGTPFQSANPILEESTLKHLYNISK 127
Cdd:cd12119 20 EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELyyAVPGM--GAVLHTINPRLFPEQIAYIINHAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 128 PKIIFTDADHYDKLYSATSAFKP---EIILTTGTK------DGVLSIQDLLAPTKTEFFYqpTPLKEGpsQTVAILTSSG 198
Cdd:cd12119 98 DRVVFVDRDFLPLLEAIAPRLPTvehVVVMTDDAAmpepagVGVLAYEELLAAESPEYDW--PDFDEN--TAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 199 TTGMPKAVCISNDILTQETVFVNGYDTIFISASlDWITGL--------WATIFSTV-NGCTRIISSKPFAADYFVYLVSK 269
Cdd:cd12119 174 TTGNPKGVVYSHRSLVLHAMAALLTDGLGLSES-DVVLPVvpmfhvnaWGLPYAAAmVGAKLVLPGPYLDPASLAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 270 YSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLapnGV-LNSSYGMTEVG----FIVFNHGH 344
Cdd:cd12119 253 EGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER---GVrVIHAWGMTETSplgtVARPPSEH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 345 LKLTAA---------GNPLPGIQVKIVDDDGNQL---GVNQtGEIIVHNGFSWNGYFADPEATKAMqDEEGWFHTGDMGY 412
Cdd:cd12119 330 SNLSEDeqlalrakqGRPVPGVELRIVDDDGRELpwdGKAV-GELQVRGPWVTKSYYKNDEESEAL-TEDGWLRTGDVAT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 413 FDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKR 492
Cdd:cd12119 408 IDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADK 487
|
490 500 510
....*....|....*....|....*....|....*...
gi 21356947 493 -----LPDiqkqlraGVQFADEIPQNHNGKVVRRYARD 525
Cdd:cd12119 488 vakwwLPD-------DVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
48-525 |
6.58e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 154.29 E-value: 6.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 48 ISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISK 127
Cdd:PRK08276 4 IMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 128 PKIIFTDADHYD---KLYSATSAFKPEIILTTGTKDGVLSIQDLLAPtkteffyQPTPLKEGPSQTVAILTSSGTTGMPK 204
Cdd:PRK08276 84 AKVLIVSAALADtaaELAAELPAGVPLLLVVAGPVPGFRSYEEALAA-------QPDTPIADETAGADMLYSSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 AVCIS---NDILTQETVFV--------NGYDTIFIS-------ASLDWITglwatiFSTVNGCTRIISSKpFAADYFVYL 266
Cdd:PRK08276 157 GIKRPlpgLDPDEAPGMMLallgfgmyGGPDSVYLSpaplyhtAPLRFGM------SALALGGTVVVMEK-FDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 267 VSKYSITYALIPPEHCCSLLDCPTATPEK--LGSLTklnfgggRMTQAT----VErVKK-----LAPngVLNSSYGMTEV 335
Cdd:PRK08276 230 IERYRVTHSQLVPTMFVRMLKLPEEVRARydVSSLR-------VAIHAAapcpVE-VKRamidwWGP--IIHEYYASSEG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 336 GFIVFNHGHLKLT---AAGNPLPGiQVKIVDDDGNQLGVNQTGEIIVHNG---FSwngYFADPEATKAMQDEEGWFHTGD 409
Cdd:PRK08276 300 GGVTVITSEDWLAhpgSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDgypFE---YHNDPEKTAAARNPHGWVTVGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 410 MGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLT---AQQVI 486
Cdd:PRK08276 376 VGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGdalAAELI 455
|
490 500 510
....*....|....*....|....*....|....*....
gi 21356947 487 DHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:PRK08276 456 AWLRGRLAHY-KCPRS-IDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
186-520 |
1.10e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 153.48 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 186 GPSQTVAILTSSGTTGMPKAVcisndILTQETVFVNGYDTIF-----------ISASLDWITGLWATIFSTVNGCTRIIS 254
Cdd:PRK06839 147 NESASFIICYTSGTTGKPKGA-----VLTQENMFWNALNNTFaidltmhdrsiVLLPLFHIGGIGLFAFPTLFAGGVIIV 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 255 SKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGrmtQATVERVKKLAPNGVL-NSSYGMT 333
Cdd:PRK06839 222 PRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGA---PCPEELMREFIDRGFLfGQGFGMT 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 334 EVGFIVF----NHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT-KAMQDeeGWFHTG 408
Cdd:PRK06839 299 ETSPTVFmlseEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATeETIQD--GWLCTG 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 409 DMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDH 488
Cdd:PRK06839 377 DLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEH 456
|
330 340 350
....*....|....*....|....*....|..
gi 21356947 489 VAKRLPdiQKQLRAGVQFADEIPQNHNGKVVR 520
Cdd:PRK06839 457 CRLFLA--KYKIPKEIVFLKELPKNATGKIQK 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
110-521 |
1.37e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 153.96 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 110 ANPILEESTLKHLYNISKPKIIFTDADHYDKL----------------YSATSAFKPEII----------LTTGTKDGVL 163
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqYSDYLPAEPEIAvpawlraeppLQALAPGGVV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 164 SIQDLLAPTkteffYQPTPLKEGPsQTVAILT-SSGTTGMPKAvCISndilTQETVFVNgydtifISASLDW-------- 234
Cdd:PRK08314 171 AWKEALAAG-----LAPPPHTAGP-DDLAVLPyTSGTTGVPKG-CMH----THRTVMAN------AVGSVLWsnstpesv 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 235 ---------ITG----LWATIFStvnGCTRIISS---KPFAADyfvyLVSKYSITYALIPPEHCCSLLDCPTATPEKLGS 298
Cdd:PRK08314 234 vlavlplfhVTGmvhsMNAPIYA---GATVVLMPrwdREAAAR----LIERYRVTHWTNIPTMVVDFLASPGLAERDLSS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 299 LTKLNFGGGRMTQATVERVKKLApnGV-LNSSYGMTE-VGFIVFN-HGHLKLTAAGNPLPGIQVKIVD-DDGNQLGVNQT 374
Cdd:PRK08314 307 LRYIGGGGAAMPEAVAERLKELT--GLdYVEGYGLTEtMAQTHSNpPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 375 GEIIVHNGFSWNGYFADPEAT-KAMQDEEG--WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEV 451
Cdd:PRK08314 385 GEIVVHGPQVFKGYWNRPEATaEAFIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356947 452 KRVCVIGVYDETQGDVPGALVVREDNA--TLTAQQVID----HVAK-RLPDIqkqlragVQFADEIPQNHNGKVVRR 521
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAwareHMAAyKYPRI-------VEFVDSLPKSGSGKILWR 534
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
59-531 |
9.62e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 151.85 E-value: 9.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 59 GQALTWA------IRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIF 132
Cdd:PRK07786 40 GNTTTWRelddrvAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 133 TDADHYDkLYSATSAFKP--EIILTTG--TKDGVLSIQDLLAPTKteffyQPTPLKEGPSQTVA-ILTSSGTTGMPKAVC 207
Cdd:PRK07786 120 TEAALAP-VATAVRDIVPllSTVVVAGgsSDDSVLGYEDLLAEAG-----PAHAPVDIPNDSPAlIMYTSGTTGRPKGAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 208 ISNDILTQET---VFVNGYDTI----FISASLDWITGLWATIFSTVNGCTRII-SSKPFAADYFVYLVSKYSITYALIPP 279
Cdd:PRK07786 194 LTHANLTGQAmtcLRTNGADINsdvgFVGVPLFHIAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVLEAEKVTGIFLVP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 280 EHCCSLLDCPTATPEKLgSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGFIVF----NHGHLKLTAAGNPLP 355
Cdd:PRK07786 274 AQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCmllgEDAIRKLGSVGKVIP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 356 GIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATkAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQ 435
Cdd:PRK07786 353 TVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEAT-AEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGEN 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 436 MWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALV-VREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNH 514
Cdd:PRK07786 432 IYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLARY-KHPKA-LEIVDALPRNP 509
|
490
....*....|....*..
gi 21356947 515 NGKVVRRYARDLFVALS 531
Cdd:PRK07786 510 AGKVLKTELRERYGACV 526
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
330-521 |
2.52e-39 |
|
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: 148.59 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVFN--HGHLKLTAAGNPLPGIQVKIVDDDGNQ-LGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFH 406
Cdd:cd05941 244 YGMTEIGMALSNplDGERRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 407 TGDMGYFDEDDYLYMTDRKK-EVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNA-TLTAQQ 484
Cdd:cd05941 324 TGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEE 403
|
170 180 190
....*....|....*....|....*....|....*....
gi 21356947 485 VIDHVAKRLP--DIQKQLRagvqFADEIPQNHNGKVVRR 521
Cdd:cd05941 404 LKEWAKQRLApyKRPRRLI----LVDELPRNAMGKVNKK 438
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
54-532 |
7.09e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 148.42 E-value: 7.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 54 VEVTFGQALTWAI------RIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISK 127
Cdd:PRK09088 15 VDLALGRRWTYAEldalvgRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 128 PKIIFTDADhydklysatsafkpeiiLTTGTKDGVlSIQDLLAPTKTEffyQPTPLKEGPSQTVA-ILTSSGTTGMPKAV 206
Cdd:PRK09088 95 PRLLLGDDA-----------------VAAGRTDVE-DLAAFIASADAL---EPADTPSIPPERVSlILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 207 CISNDILTQETV-F-----VNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYS--ITYALIP 278
Cdd:PRK09088 154 MLSERNLQQTAHnFgvlgrVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAlgITHYFCV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 279 PEHCCSLLDCPTATPEKLGSLTKLnFGGGRMTQATVERvKKLAPNGVLNSSYGMTEVGfIVFNHG------HLKLTAAGN 352
Cdd:PRK09088 234 PQMAQAFRAQPGFDAAALRHLTAL-FTGGAPHAAEDIL-GWLDDGIPMVDGFGMSEAG-TVFGMSvdcdviRAKAGAAGI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 353 PLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWK 432
Cdd:PRK09088 311 PTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 433 GLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPdiQKQLRAGVQFADEIPQ 512
Cdd:PRK09088 391 GENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLA--KYKVPKHLRLVDALPR 468
|
490 500
....*....|....*....|
gi 21356947 513 NHNGKVVRRYARDLFVALSK 532
Cdd:PRK09088 469 TASGKLQKARLRDALAAGRK 488
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
67-526 |
9.19e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 148.65 E-value: 9.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 67 RIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKLySATS 146
Cdd:PRK07470 44 ALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHA-AAVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 147 AFKPEI--ILTTGTKDGVLSIQDLLA--------PTKTE------FFYqptplkegpsqtvailtSSGTTGMPKAVcisn 210
Cdd:PRK07470 123 AASPDLthVVAIGGARAGLDYEALVArhlgarvaNAAVDhddpcwFFF-----------------TSGTTGRPKAA---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 211 dILTQETV-FV------------NGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSITYALI 277
Cdd:PRK07470 182 -VLTHGQMaFVitnhladlmpgtTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSERFDPAEVWALVERHRVTNLFT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 278 PPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVER-VKKLAPngVLNSSYGMTEV-GFIVF--NHGH-------LK 346
Cdd:PRK07470 261 VPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRaLAKLGK--VLVQYFGLGEVtGNITVlpPALHdaedgpdAR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 347 LTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT-KAMQDeeGWFHTGDMGYFDEDDYLYMTDRK 425
Cdd:PRK07470 339 IGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANaKAFRD--GWFRTGDLGHLDARGFLYITGRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 426 KEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPdiQKQLRAGVQ 505
Cdd:PRK07470 417 SDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVA--RYKLPKRFF 494
|
490 500
....*....|....*....|.
gi 21356947 506 FADEIPQNHNGKVVRRYARDL 526
Cdd:PRK07470 495 FWDALPKSGYGKITKKMVREE 515
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
13-518 |
4.21e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 147.50 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 13 KIW-KGIPQnnpfKPETSLGRI-IFKNMRNWPKnvcqiSDSEGVEVTF-GQALTWA------IRIAQQLKSRGLDHKDII 83
Cdd:PRK06178 16 AAWpAGIPR----EPEYPHGERpLTEYLRAWAR-----ERPQRPAIIFyGHVITYAeldelsDRFAALLRQRGVGAGDRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 84 GISARNTtyimPTAVACFFH----GTPFQSANPILEESTLKHLYNISKPKIIFTdadhYDKLYSATSAFKPEI----ILT 155
Cdd:PRK06178 87 AVFLPNC----PQFHIVFFGilklGAVHVPVSPLFREHELSYELNDAGAEVLLA----LDQLAPVVEQVRAETslrhVIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 156 TGTKD-----------GVLSIQDLLAPTKTEFFY------QPTPLKEGPSQTVAILT-SSGTTGMPK------------- 204
Cdd:PRK06178 159 TSLADvlpaeptlplpDSLRAPRLAAAGAIDLLPalractAPVPLPPPALDALAALNyTGGTTGMPKgcehtqrdmvyta 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 -AVCISNDILTQETVFVNgYDTIFisasldWI----TGLwatIFSTVNGCTRIISSKpFAADYFVYLVSKYSITYALIPP 279
Cdd:PRK06178 239 aAAYAVAVVGGEDSVFLS-FLPEF------WIagenFGL---LFPLFSGATLVLLAR-WDAVAFMAAVERYRVTRTVMLV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 280 EHCCSLLDCPTATPEKLGSLTKLNfgggrmtqaTVERVKKLAPN----------GVL-NSSYGMTEV----GFIV-FNHG 343
Cdd:PRK06178 308 DNAVELMDHPRFAEYDLSSLRQVR---------VVSFVKKLNPDyrqrwraltgSVLaEAAWGMTEThtcdTFTAgFQDD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 344 HLKLTAA----GNPLPGIQVKIVD-DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQdEEGWFHTGDMGYFDEDDY 418
Cdd:PRK06178 379 DFDLLSQpvfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 419 LYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRL----- 493
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMavykv 537
|
570 580
....*....|....*....|....*
gi 21356947 494 PDIqkqlragvQFADEIPQNHNGKV 518
Cdd:PRK06178 538 PEI--------RIVDALPMTATGKV 554
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
179-525 |
5.45e-38 |
|
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: 145.60 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 179 QPTPLKEGPSQTVAILTSSGTTGMPKAV-----CISNDILTQ---ETVFVNGYDTIFIS-ASLDWITGLWATIFSTVNGC 249
Cdd:cd05929 116 SPETPIEDEAAGWKMLYSGGTTGRPKGIkrglpGGPPDNDTLmaaALGFGPGADSVYLSpAPLYHAAPFRWSMTALFMGG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 250 TRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEK--LGSLTKLNFGGGRMTQATVERVKKLAPNgVLN 327
Cdd:cd05929 196 TLVLMEK-FDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAydLSSLKRVIHAAAPCPPWVKEQWIDWGGP-IIW 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 328 SSYGMTE-VGFIVFNhGHLKLT---AAGNPLPGiQVKIVDDDGNQLGVNQTGEIIVHNGFSWNgYFADPEATKAMQDEEG 403
Cdd:cd05929 274 EYYGGTEgQGLTIIN-GEEWLThpgSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNA---TL 480
Cdd:cd05929 351 WSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTA 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 21356947 481 TAQQVIDHVAKRLPDiQKQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:cd05929 431 LAEELIAFLRDRLSR-YKCPRS-IEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
196-525 |
2.01e-36 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 142.32 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 196 SSGTTGMPKAVCISN-----------DILTQETVFVNGYDTIFISASLDWITGLWAT--IFSTVNGCTRIISSkPFAADY 262
Cdd:PRK08751 216 TGGTTGVAKGAMLTHrnlvanmqqahQWLAGTGKLEEGCEVVITALPLYHIFALTANglVFMKIGGCNHLISN-PRDMPG 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 263 FVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLtKLNFGGGRMTQATV-ERVKKLApnGV-LNSSYGMTEVG-FIV 339
Cdd:PRK08751 295 FVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSL-KMTLGGGMAVQRSVaERWKQVT--GLtLVEAYGLTETSpAAC 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 340 FNHGHLKL--TAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDD 417
Cdd:PRK08751 372 INPLTLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQG 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 418 YLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNAtLTAQQVIDHVAKRLPDIq 497
Cdd:PRK08751 452 FVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA-LTAEDVKAHARANLTGY- 529
|
330 340
....*....|....*....|....*...
gi 21356947 498 KQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:PRK08751 530 KQPRI-IEFRKELPKTNVGKILRRELRD 556
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-518 |
5.02e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 137.41 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCisndiLTQETVFVNGY-----------DTIFISASLDWITGLWATIFSTVN-GCTRIIS 254
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGAT-----LTHHNIVNNGYfigerlglteqDRLCIPVPLFHCFGSVLGVLACLThGATMVFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 255 SKPFAAdyfvylvskySITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFG-----GGRMTQATV--ERVKKLApnGVLN 327
Cdd:cd05917 76 SPSFDP----------LAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDlsslrTGIMAGAPCppELMKRVI--EVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 328 -----SSYGMTEVGFIVFNHG-----HLKLTAAGNPLPGIQVKIVDDDGN-QLGVNQTGEIIVHnGFS-WNGYFADPEAT 395
Cdd:cd05917 144 mkdvtIAYGMTETSPVSTQTRtddsiEKRVNTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIR-GYSvMKGYWNDPEKT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 396 KAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVRE 475
Cdd:cd05917 223 AEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLK 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21356947 476 DNATLTAQQVIDHVAKRLPDiQKQLRAgVQFADEIPQNHNGKV 518
Cdd:cd05917 303 EGAELTEEDIKAYCKGKIAH-YKVPRY-VFFVDEFPLTVSGKI 343
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
48-532 |
5.86e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 141.04 E-value: 5.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 48 ISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIgisarntTYIMPT-------AVACFFHGTPFQSANPILEESTLK 120
Cdd:PRK06087 42 VVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRV-------AFQLPGwceftiiYLACLKVGAVSVPLLPSWREAELV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 121 HLYNISKPKIIFTDAdhydklYSATSAFKPEIILTTG---TKDGVLSIqDLLAPTKTEFFYQP-----TPLKEGPSQT-- 190
Cdd:PRK06087 115 WVLNKCQAKMFFAPT------LFKQTRPVDLILPLQNqlpQLQQIVGV-DKLAPATSSLSLSQiiadyEPLTTAITTHgd 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 191 --VAILTSSGTTGMPKAVCIS-NDILTQETVFVNGY-----DTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADY 262
Cdd:PRK06087 188 elAAVLFTSGTEGLPKGVMLThNNILASERAYCARLnltwqDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 263 FVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGG----GRMTQATVERVKKLApngvlnSSYGMTE-VGF 337
Cdd:PRK06087 268 CLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGttipKKVARECQQRGIKLL------SVYGSTEsSPH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 338 IVFNHGH-LKLTAA--GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFD 414
Cdd:PRK06087 342 AVVNLDDpLSRFMHtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 415 EDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVV-REDNATLTAQQVI-----DH 488
Cdd:PRK06087 422 EAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHSLTLEEVVaffsrKR 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 21356947 489 VAKRL-PDiqkqlraGVQFADEIPQNHNGKvVRRY--ARDLFVALSK 532
Cdd:PRK06087 502 VAKYKyPE-------HIVVIDKLPRTASGK-IQKFllRKDIMRRLTQ 540
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
301-534 |
6.31e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 140.96 E-value: 6.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 301 KLNFGGGRMTQATV-ERVKKLAPNGVLnSSYGMTEVGFIV--FNHGHLKLTAA-GNPLPGIQVKIVDDDGNQLGVNQTGE 376
Cdd:PRK08974 328 KLSVGGGMAVQQAVaERWVKLTGQYLL-EGYGLTECSPLVsvNPYDLDYYSGSiGLPVPSTEIKLVDDDGNEVPPGEPGE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 377 IIVHNGFSWNGYFADPEATKAMQdEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCV 456
Cdd:PRK08974 407 LWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 457 IGVYDETQGDVPGALVVREDnATLTAQQVIDHVAKRLP--DIQKQlragVQFADEIPQNHNGKVVRRYARDLFVALSKKN 534
Cdd:PRK08974 486 VGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTgyKVPKL----VEFRDELPKSNVGKILRRELRDEARAKVDNK 560
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
53-518 |
3.19e-35 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 138.74 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 53 GVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIF 132
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 133 TDADHYDKLYSAtsafkpeiilttgtKDGVLSIQDLL----AP---TKTEFFYQPTP-LKEG-------PSQTVAILTSS 197
Cdd:PRK06155 124 VEAALLAALEAA--------------DPGDLPLPAVWlldaPAsvsVPAGWSTAPLPpLDAPapaaavqPGDTAAILYTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 198 GTTGMPKAVCISN------DILTQETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKpFAADYFVYLVSKY- 270
Cdd:PRK06155 190 GTTGPSKGVCCPHaqfywwGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPR-FSASGFWPAVRRHg 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 271 -SITYALippEHCCSLLDCPTATPEKLGSLTKLNFGGG---RMTQATVERVkklapnGV-LNSSYGMTEVGFIVF-NHGH 344
Cdd:PRK06155 269 aTVTYLL---GAMVSILLSQPARESDRAHRVRVALGPGvpaALHAAFRERF------GVdLLDGYGSTETNFVIAvTHGS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 345 LKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNG--FSW-NGYFADPEAT-KAMQDEegWFHTGDMGYFDEDDYLY 420
Cdd:PRK06155 340 QRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepFAFaTGYFGMPEKTvEAWRNL--WFHTGDRVVRDADGWFR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 421 MTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLP--DIQK 498
Cdd:PRK06155 418 FVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAyfAVPR 497
|
490 500
....*....|....*....|
gi 21356947 499 QLRagvqFADEIPQNHNGKV 518
Cdd:PRK06155 498 YVE----FVAALPKTENGKV 513
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
330-511 |
4.29e-35 |
|
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: 134.35 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEV-GFIVFNH-GHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQdEEGWFHT 407
Cdd:cd17636 143 YGQTEVmGLATFAAlGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 408 GDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVID 487
Cdd:cd17636 222 NDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIE 301
|
170 180
....*....|....*....|....
gi 21356947 488 HVAKRLPDIQKQlrAGVQFADEIP 511
Cdd:cd17636 302 HCRARIASYKKP--KSVEFADALP 323
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-525 |
1.53e-34 |
|
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: 135.25 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 55 EVTFGQALTWAIRIAQQLKSRGLDHKDIIGIsarnttYIMPTAVACFFHGTPFQSAnpileestlkhLYNISKPKIIFTD 134
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGV------FLSQGPECAIAHIAILRSG-----------AIAVPLFALFGPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 135 ADHYDKLYSATSAfkpeiILTTGTKDgvlsiqdllaptkteffyqptplkegPSQtvaILTSSGTTGMPKAVC------- 207
Cdd:cd05971 69 ALEYRLSNSGASA-----LVTDGSDD--------------------------PAL---IIYTSGTTGPPKGALhahrvll 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 208 --ISNDILTQEtVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIIS--SKPFAADYFVYLVSKYSITYALIPPehcc 283
Cdd:cd05971 115 ghLPGVQFPFN-LFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVTTAFLPP---- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 284 SLLDCPTATPEKLG----SLTKLNFGG---GRMTQATVERVKKLApngvLNSSYGMTEVGFIVFNHGHL---KLTAAGNP 353
Cdd:cd05971 190 TALKMMRQQGEQLKhaqvKLRAIATGGeslGEELLGWAREQFGVE----VNEFYGQTECNLVIGNCSALfpiKPGSMGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 354 LPGIQVKIVDDDGNQLGVNQTGEIIVH--NGFSWNGYFADPEATKAmQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKW 431
Cdd:cd05971 266 IPGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEK-KMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 432 KGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVRedNATLTAQQVI-----DHVAKRLPdiQKQLRAGVQF 506
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVL--NPGETPSDALareiqELVKTRLA--AHEYPREIEF 420
|
490
....*....|....*....
gi 21356947 507 ADEIPQNHNGKVVRRYARD 525
Cdd:cd05971 421 VNELPRTATGKIRRRELRA 439
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
65-529 |
5.55e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 134.83 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 65 AIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHG---TPFQ-SANPilEEstLKHLYNISKPKIIFTDADHYDK 140
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGayaVPVNwHFKP--EE--IAYILEDSGARVLIAHADLLHG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 141 LYSATSA--------FKPEIILTTGTKDGVLSiqdllAPTKT---EFFYQPTPLKEGP--SQTVAILTSSGTTGMPKAVC 207
Cdd:PRK12406 97 LASALPAgvtvlsvpTPPEIAAAYRISPALLT-----PPAGAidwEGWLAQQEPYDGPpvPQPQSMIYTSGTTGHPKGVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 208 ISNDILTQETVFVNGYDTIF--ISASLDWITG-LWAT------IFSTVNGCTRIISSKpFAADYFVYLVSKYSITYALIP 278
Cdd:PRK12406 172 RAAPTPEQAAAAEQMRALIYglKPGIRALLTGpLYHSapnaygLRAGRLGGVLVLQPR-FDPEELLQLIERHRITHMHMV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 279 PEHCCSLLDCPTATPEKLgSLTKLNF--GGGRMTQATVER--VKKLAPngVLNSSYGMTEVGFIVFNHGHLKLT---AAG 351
Cdd:PRK12406 251 PTMFIRLLKLPEEVRAKY-DVSSLRHviHAAAPCPADVKRamIEWWGP--VIYEYYGSTESGAVTFATSEDALShpgTVG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 352 NPLPGIQVKIVDDDGNQLGVNQTGEIIVH-NGFSWNGYFADPEATKAMqDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLK 430
Cdd:PRK12406 328 KAAPGAELRFVDEDGRPLPQGEIGEIYSRiAGNPDFTYHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMVI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 431 WKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPD--IQKQlragVQFAD 508
Cdd:PRK12406 407 SGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGykVPKH----IEIMA 482
|
490 500
....*....|....*....|.
gi 21356947 509 EIPQNHNGKVVRRYARDLFVA 529
Cdd:PRK12406 483 ELPREDSGKIFKRRLRDPYWA 503
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
188-520 |
7.70e-34 |
|
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: 131.23 E-value: 7.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 188 SQTVAILTSSGTTGMPKAVCISN-------DILTQETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAA 260
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANktffavpDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 261 DYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVeRVKKLAPNGVLNSSYGMTEVG---F 337
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADV-RFIEATGLTNTAQVYGLSETGtalC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 338 IVFNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATkAMQDEEGWFHTGDMGYFDEDD 417
Cdd:cd17635 160 LPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERT-AEVLIDGWVNTGDLGERREDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 418 YLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVR---EDNATLTAQqvIDHVAKRLP 494
Cdd:cd17635 239 FLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDENAIRAL--KHTIRRELE 316
|
330 340
....*....|....*....|....*.
gi 21356947 495 diQKQLRAGVQFADEIPQNHNGKVVR 520
Cdd:cd17635 317 --PYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
65-520 |
1.33e-33 |
|
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: 132.57 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 65 AIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDadhydklysa 144
Cdd:TIGR01923 9 AAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 145 tSAFKPEIILTtgtkdgvLSIQDLLAPtktefFYQPTPLKEGPS--QTVAILTSSGTTGMPKAVCIS------NDILTQE 216
Cdd:TIGR01923 79 -SLLEEKDFQA-------DSLDRIEAA-----GRYETSLSASFNmdQIATLMFTSGTTGKPKAVPHTfrnhyaSAVGSKE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 217 TVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKpFAAdyFVYLVSKYSITYALIPPEHCCSLLDcPTATPEkl 296
Cdd:TIGR01923 146 NLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDK-FNQ--LLEMIANERVTHISLVPTQLNRLLD-EGGHNE-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 297 gSLTKLNFGGGrmtQATVERVKKLAPNGV-LNSSYGMTEVG--FIVFNHGHLK-LTAAGNPLPGIQVKIVDDdgNQLGVn 372
Cdd:TIGR01923 220 -NLRKILLGGS---AIPAPLIEEAQQYGLpIYLSYGMTETCsqVTTATPEMLHaRPDVGRPLAGREIKIKVD--NKEGH- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 373 qtGEIIVHNGFSWNGYFADPEATKAMqDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVK 452
Cdd:TIGR01923 293 --GEIMVKGANLMKGYLYQGELTPAF-EQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356947 453 RVCVIGVYDETQGDVPGALVVRE---DNATLTAqQVIDHVAK-RLPdiqkqlrAGVQFADEIPQNHNGKVVR 520
Cdd:TIGR01923 370 EAVVVPKPDAEWGQVPVAYIVSEsdiSQAKLIA-YLTEKLAKyKVP-------IAFEKLDELPYNASGKILR 433
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
49-529 |
1.58e-33 |
|
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: 133.95 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 49 SDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKD-IIGISARNTTYImpTAV-ACFFHG------TPFqsANPILEESTLK 120
Cdd:cd05906 33 ADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDsVILQFDDNEDFI--PAFwACVLAGfvpaplTVP--PTYDEPNARLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 121 HLYNISK----PKIIfTDAdhydklySATSAFKPEIILTTGTKDGVLSIQDLLAPTKTEFFYQPTPlkEGPsqtVAILTS 196
Cdd:cd05906 109 KLRHIWQllgsPVVL-TDA-------ELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRP--DDL---ALLMLT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 197 SGTTGMPKAVCISN-DILTQE--TVFVNGY--DTIFIS-ASLDWITGL-WATIFSTVNGCTRI-ISSKPFAAD--YFVYL 266
Cdd:cd05906 176 SGSTGFPKAVPLTHrNILARSagKIQHNGLtpQDVFLNwVPLDHVGGLvELHLRAVYLGCQQVhVPTEEILADplRWLDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 267 VSKYSITYALIPP---EHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVER-VKKLAPNG----VLNSSYGMTEVGF- 337
Cdd:cd05906 256 IDRYRVTITWAPNfafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRlLRLLEPYGlppdAIRPAFGMTETCSg 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 338 IVFNH--------GHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGD 409
Cdd:cd05906 336 VIYSRsfptydhsQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 410 MGYFDeDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKR--VCVIGVYDETQGDVPGALV-----VREDNATLTA 482
Cdd:cd05906 416 LGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFfvpeyDLQDALSETL 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 483 QQVIDHVAKR--------LPdIQKqlragvqfaDEIPQNHNGKVVRRYARDLFVA 529
Cdd:cd05906 495 RAIRSVVSREvgvspaylIP-LPK---------EEIPKTSLGKIQRSKLKAAFEA 539
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
97-525 |
2.69e-33 |
|
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: 132.97 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 97 AVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTD---ADHYDKLYSATSAFKPEIILTTGTKDGVLSIQDLLAPTK 173
Cdd:cd05928 84 NVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSdelAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNEAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 174 TEFfyqpTPLKEGPSQTVAILTSSGTTGMPKAVCISNDILTQETVFVNGY-------DTIFISASLDWITGLWATIFST- 245
Cdd:cd05928 164 TEH----HCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYwldltasDIMWNTSDTGWIKSAWSSLFEPw 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 246 VNGCTRIISSKP-FAADYFVYLVSKYSITyalippeHCCSlldCPTA---------TPEKLGSLTKLNFGGGRMTQATVE 315
Cdd:cd05928 240 IQGACVFVHHLPrFDPLVILKTLSSYPIT-------TFCG---APTVyrmlvqqdlSSYKFPSLQHCVTGGEPLNPEVLE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 316 RVKKLApnGV-LNSSYGMTEVGFIVFNHGHLKLTAA--GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNG----FS-WNG 387
Cdd:cd05928 310 KWKAQT--GLdIYEGYGQTETGLICANFKGMKIKPGsmGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpFGlFSG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 388 YFADPEATKAMqdEEGWFH-TGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGD 466
Cdd:cd05928 388 YVDNPEKTAAT--IRGDFYlTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGE 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 467 VPGALVV------REDNATLTAqQVIDHVaKRLPDIQKQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:cd05928 466 VVKAFVVlapqflSHDPEQLTK-ELQQHV-KSVTAPYKYPRK-VEFVQELPKTVTGKIQRNELRD 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
55-523 |
2.55e-32 |
|
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: 129.80 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 55 EVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYiMPTAvacfFHGTPFQSANPI-----LEESTLKHLYNISKPK 129
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVD-FPTA----FLGAIRAGIVPVpvntlLTPDDYAYYLEDSRAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 130 IIFTDADHYDKLYSATSAFKPE---IILTTG--TKDGVLSIQDLLAPTKTEFfyqpTPLKEGPSQTVAILTSSGTTGMPK 204
Cdd:cd05959 104 VVVVSGELAPVLAAALTKSEHTlvvLIVSGGagPEAGALLLAELVAAEAEQL----KPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 -AVCISNDILTQETVFVNGY------DTIFISASLDWITGLW-ATIFSTVNGCTRII-SSKPFAADYFVYLVS-KYSITY 274
Cdd:cd05959 180 gVVHLHADIYWTAELYARNVlgiredDVCFSAAKLFFAYGLGnSLTFPLSVGATTVLmPERPTPAAVFKRIRRyRPTVFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 275 ALipPEHCCSLLDCPTATPEKLGSLtKLNFGGGRMTQATV-ERVKKLAPNGVLNSsYGMTEVGFIVFNH--GHLKLTAAG 351
Cdd:cd05959 260 GV--PTLYAAMLAAPNLPSRDLSSL-RLCVSAGEALPAEVgERWKARFGLDILDG-IGSTEMLHIFLSNrpGRVRYGTTG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 352 NPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKA-MQDEegWFHTGDMGYFDEDDYLYMTDRKKEVLK 430
Cdd:cd05959 336 KPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDtFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 431 WKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVV---REDNATLTAQQVIDHVAKRLPDiQKQLRaGVQFA 507
Cdd:cd05959 414 VSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpGYEDSEALEEELKEFVKDRLAP-YKYPR-WIVFV 491
|
490
....*....|....*.
gi 21356947 508 DEIPQNHNGKvVRRYA 523
Cdd:cd05959 492 DELPKTATGK-IQRFK 506
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
330-530 |
2.67e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 129.61 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVFN--HGHLKLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIVH--NGFSwnGYFADPEATKAMQDEEGW 404
Cdd:PRK07514 301 YGMTETNMNTSNpyDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKgpNVFK--GYWRMPEKTAEEFRADGF 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 405 FHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQ 484
Cdd:PRK07514 379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAA 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21356947 485 VIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRRYARDLFVAL 530
Cdd:PRK07514 459 ILAALKGRLARF-KQPKR-VFFVDELPRNTMGKVQKNLLREQYADL 502
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
298-525 |
5.08e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 129.76 E-value: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 298 SLTKLNFGGGRMTQATV-ERVKKLAPNGVLnSSYGMTEVGFIV----FNHGHLKLTAaGNPLPGIQVKIVDDDGNQLGVN 372
Cdd:PRK07059 327 SKLIVANGGGMAVQRPVaERWLEMTGCPIT-EGYGLSETSPVAtcnpVDATEFSGTI-GLPLPSTEVSIRDDDGNDLPLG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 373 QTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVK 452
Cdd:PRK07059 405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356947 453 RVCVIGVYDETQGDVPGALVVREDNAtLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:PRK07059 485 EVAAVGVPDEHSGEAVKLFVVKKDPA-LTEEDVKAFCKERLTNY-KRPKF-VEFRTELPKTNVGKILRRELRD 554
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
186-521 |
5.30e-32 |
|
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: 128.78 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 186 GPSQTVAILTSSGTTGMPKAVCISND--------ILTQETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKP 257
Cdd:cd05923 148 EPEQPAFVFYTSGTTGLPKGAVIPQRaaesrvlfMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 258 FAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSsYGMTEVgf 337
Cdd:cd05923 228 FDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEA-- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 338 ivFNHGHLKLTAAGNPL-PGI--QVKIVDDDGNQ---LGVNQTGEIIV--HNGFSWNGYFADPEATkAMQDEEGWFHTGD 409
Cdd:cd05923 305 --MNSLYMRDARTGTEMrPGFfsEVRIVRIGGSPdeaLANGEEGELIVaaAADAAFTGYLNQPEAT-AKKLQDGWYRTGD 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 410 MGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDnATLTAQQvIDHV 489
Cdd:cd05923 382 VGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-GTLSADE-LDQF 459
|
330 340 350
....*....|....*....|....*....|....
gi 21356947 490 --AKRLPDIqKQLRAGVqFADEIPQNHNGKVVRR 521
Cdd:cd05923 460 crASELADF-KRPRRYF-FLDELPKNAMNKVLRR 491
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
48-529 |
7.36e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 128.66 E-value: 7.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 48 ISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISK 127
Cdd:PRK13391 17 IMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 128 PKIIFTDADHYD---KLYSATSAFKPEIIL-TTGTKDGVLSIQDLLAPtkteffYQPTPLKEGPSQTvAILTSSGTTGMP 203
Cdd:PRK13391 97 ARALITSAAKLDvarALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAG------LPATPIADESLGT-DMLYSSGTTGRP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 204 KAV---CISNDILTQETVF-----VNGY--DTIFIS-ASLDWITGLWATIFSTVNGCTRIISSKpFAADYFVYLVSKYSI 272
Cdd:PRK13391 170 KGIkrpLPEQPPDTPLPLTaflqrLWGFrsDMVYLSpAPLYHSAPQRAVMLVIRLGGTVIVMEH-FDAEQYLALIEEYGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 273 TYALIPPEHCCSLLDCPTATPEK--LGSLTKLNFGGGRMTQATVER-VKKLAPngVLNSSYGMTE-VGFIVFN-HGHL-K 346
Cdd:PRK13391 249 THTQLVPTMFSRMLKLPEEVRDKydLSSLEVAIHAAAPCPPQVKEQmIDWWGP--IIHEYYAATEgLGFTACDsEEWLaH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 347 LTAAGNPLPGIqVKIVDDDGNQLGVNQTGEIIVHNGFSWNgYFADPEATKAMQDEEG-WFHTGDMGYFDEDDYLYMTDRK 425
Cdd:PRK13391 327 PGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 426 KEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLT---AQQVIDHVAKRLPDiQKQLRA 502
Cdd:PRK13391 405 AFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSR-QKCPRS 483
|
490 500
....*....|....*....|....*..
gi 21356947 503 gVQFADEIPQNHNGKVVRRYARDLFVA 529
Cdd:PRK13391 484 -IDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
186-521 |
7.79e-32 |
|
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: 127.64 E-value: 7.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 186 GPSQTVAILTSSGTTGMPKAVCISNDILT------QETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRII--SSKP 257
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVnlllwmQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVlpEEVR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 258 FAADYFVYLVSKYSITYALIPPEHCCSLLDcpTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGF 337
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQ--ELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 338 IV--FNHGHLKLTAA----GNPLPGIQVKIVDDDGNQLGVNQTGEIIVH-NGFSwNGYFADPEATKA------MQDEEGW 404
Cdd:cd05930 249 DAtyYRVPPDDEEDGrvpiGRPIPNTRVYVLDENLRPVPPGVPGELYIGgAGLA-RGYLNRPELTAErfvpnpFGPGERM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 405 FHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQ 484
Cdd:cd05930 328 YRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEE 407
|
330 340 350
....*....|....*....|....*....|....*...
gi 21356947 485 VIDHVAKRLPDIqkqLR-AGVQFADEIPQNHNGKVVRR 521
Cdd:cd05930 408 LRAHLAERLPDY---MVpSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
53-521 |
8.61e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 129.00 E-value: 8.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 53 GVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTtyimPTAVACFF----HGTPFQSANPILEESTLKHLYNISKP 128
Cdd:PRK06710 47 GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNC----PQAVIGYYgtllAGGIVVQTNPLYTERELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 129 KIIFTDADHYDKLYSATSAFKPEIILTTGTKDGVLSIQDLLAP-------------TKTEFFYQPTPLKE---------- 185
Cdd:PRK06710 123 KVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPfvqkkqsnlvvkvSESETIHLWNSVEKevntgvevpc 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 186 GPSQTVAILT-SSGTTGMPKAVCISNDILTQETVF--------VNGYDTIFISASLDWITGLWATI-FSTVNGCTRIISS 255
Cdd:PRK06710 203 DPENDLALLQyTGGTTGFPKGVMLTHKNLVSNTLMgvqwlyncKEGEEVVLGVLPFFHVYGMTAVMnLSIMQGYKMVLIP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 256 KpFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLApNGVLNSSYGMTEV 335
Cdd:PRK06710 283 K-FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVT-GGKLVEGYGLTES 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 336 GFIVFNHGHLKLTAAGN---PLPGIQVKIVD-DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQdEEGWFHTGDMG 411
Cdd:PRK06710 361 SPVTHSNFLWEKRVPGSigvPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 412 YFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNaTLTAQQVIDHVAK 491
Cdd:PRK06710 440 YMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEG-TECSEEELNQFAR 518
|
490 500 510
....*....|....*....|....*....|
gi 21356947 492 RLPDIQKQLRAgVQFADEIPQNHNGKVVRR 521
Cdd:PRK06710 519 KYLAAYKVPKV-YEFRDELPKTTVGKILRR 547
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-518 |
1.13e-31 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 128.63 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 55 EVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKII--- 131
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLvvp 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 132 --FTDADH---YDKLYSATSAFKpEIILTTGtkDGVLSIQDLLAPTKTEffYQP------TPLKEGPSQTVAILTSSGTT 200
Cdd:PRK13295 135 ktFRGFDHaamARRLRPELPALR-HVVVVGG--DGADSFEALLITPAWE--QEPdapailARLRPGPDDVTQLIYTSGTT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 201 GMPKAV------CISNDILTQETVFVNGYDTIFISASLDWITG-LWATIFSTVNGCTRIISSKpFAADYFVYLVSKYSIT 273
Cdd:PRK13295 210 GEPKGVmhtantLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAVLQDI-WDPARAAELIRTEGVT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 274 YALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLnSSYGMTEVGFIVFNH----GHLKLTA 349
Cdd:PRK13295 289 FTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIV-SAWGMTENGAVTLTKlddpDERASTT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 350 AGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKamQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVL 429
Cdd:PRK13295 368 DGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISGRSKDVI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 430 KWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVID-----HVAKR-LPDiqkqlRAG 503
Cdd:PRK13295 446 IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEflkaqKVAKQyIPE-----RLV 520
|
490
....*....|....*
gi 21356947 504 VQfaDEIPQNHNGKV 518
Cdd:PRK13295 521 VR--DALPRTPSGKI 533
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
196-520 |
2.93e-31 |
|
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: 123.28 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 196 SSGTTGMPKAVCISND-----ILTQETVF-VNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKpFAADYFVYLVSK 269
Cdd:cd17633 8 TSGTTGLPKAYYRSERswiesFVCNEDLFnISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK-FNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 270 YSITYALIPPEHCCSLLDcpTATPEklgSLTKLNFGGGRMTQATVER-VKKLAPNGVLNSSYGMTEVGFIV--FNHGHLK 346
Cdd:cd17633 87 YNATVIYLVPTMLQALAR--TLEPE---SKIKSIFSSGQKLFESTKKkLKNIFPKANLIEFYGTSELSFITynFNQESRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 347 LTAAGNPLPGIQVKIVDDDGNQLGvnqtgEIIVHNGFSWNGYFADPEATKamqdeEGWFHTGDMGYFDEDDYLYMTDRKK 426
Cdd:cd17633 162 PNSVGRPFPNVEIEIRNADGGEIG-----KIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRES 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 427 EVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREdnaTLTAQQVIDHVAKRLP--DIQKQLragv 504
Cdd:cd17633 232 DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLTYKQLKRFLKQKLSryEIPKKI---- 304
|
330
....*....|....*.
gi 21356947 505 QFADEIPQNHNGKVVR 520
Cdd:cd17633 305 IFVDSLPYTSSGKIAR 320
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-473 |
5.07e-31 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 127.14 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 26 PETSLGRIIFKNMRNWPKNVCQISDSEG--VEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFH 103
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 104 G---TP-FQSANPilEEstLKHLYNISKPKIIFT-DADHYDKLYSATSAFK--PEIIL----TTGTKDGVLSIQDLLA-- 170
Cdd:COG1022 89 GavtVPiYPTSSA--EE--VAYILNDSGAKVLFVeDQEQLDKLLEVRDELPslRHIVVldprGLRDDPRLLSLDELLAlg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 171 -PTKTEFFYQPTPLKEGPSQTVAILTSSGTTGMPKAVCISND-ILTQetvfVNGYDTIF-ISAS--------LDWITGLW 239
Cdd:COG1022 165 rEVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRnLLSN----ARALLERLpLGPGdrtlsflpLAHVFERT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 240 ATIFSTVNGCT--------------------------------------RIISSKPF-----------AADYFVYLVSKY 270
Cdd:COG1022 241 VSYYALAAGATvafaespdtlaedlrevkptfmlavprvwekvyagiqaKAEEAGGLkrklfrwalavGRRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 271 SITYALIPPeHccSLLDcptatpeklgsltKLNFG------GGRMtqatvervkKLAPNG------------------VL 326
Cdd:COG1022 321 SPSLLLRLK-H--ALAD-------------KLVFSklrealGGRL---------RFAVSGgaalgpelarffralgipVL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 327 NSsYGMTEV-GFIVFNH-GHLKLTAAGNPLPGIQVKIVDDdgnqlgvnqtGEIIVH--NGFSwnGYFADPEATKAMQDEE 402
Cdd:COG1022 376 EG-YGLTETsPVITVNRpGDNRIGTVGPPLPGVEVKIAED----------GEILVRgpNVMK--GYYKNPEATAEAFDAD 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356947 403 GWFHTGDMGYFDEDDYLYMTDRKKEVLKW-KGLQMWPAEVEAVIDELPEVKRVCVIGvydetQG-DVPGALVV 473
Cdd:COG1022 443 GWLHTGDIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVVG-----DGrPFLAALIV 510
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
284-526 |
9.27e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 126.09 E-value: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 284 SLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLnSSYGMTEVGFIVFN--HGHL-KLTAAGNPLPGIQVK 360
Cdd:PRK12492 320 ALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIV-EGYGLTETSPVASTnpYGELaRLGTVGIPVPGTALK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 361 IVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAE 440
Cdd:PRK12492 399 VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 441 VEAVIDELPEVKRVCVIGVYDETQGDVPGALVVRED------------NATLTAQQVIDHVAKRlpdiqkqlragvqfaD 508
Cdd:PRK12492 479 IEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDpglsveelkaycKENFTGYKVPKHIVLR---------------D 543
|
250
....*....|....*...
gi 21356947 509 EIPQNHNGKVVRRYARDL 526
Cdd:PRK12492 544 SLPMTPVGKILRRELRDI 561
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
193-526 |
9.86e-31 |
|
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: 126.28 E-value: 9.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVCISND------ILTQETVFVNGYDTIFISAS-LDWITGLWATIFST-VNGCTRII-SSKPFA---A 260
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGghavalNWSMRNIYGIKPGDVWWAASdVGWVVGHSYIVYGPlLHGATTVLyEGKPVGtpdP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 261 DYFVYLVSKYSITyalippehccSLLDCPTA-------TPE-------KLGSLTKLNFGGGRMTQATVERVKKLAPNGVL 326
Cdd:cd05967 315 GAFWRVIEKYQVN----------ALFTAPTAirairkeDPDgkyikkyDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 327 NSsYGMTEVGFIV------FNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVH----NGFSwNGYFADPEATK 396
Cdd:cd05967 385 DH-WWQTETGWPItanpvgLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKlplpPGCL-LTLWKNDERFK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 397 A--MQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVR 474
Cdd:cd05967 463 KlyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVL 542
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 475 EDNATLTAQQvidhvakrlpdIQKQLRAGVQ-------------FADEIPQNHNGKVVRRYARDL 526
Cdd:cd05967 543 KEGVKITAEE-----------LEKELVALVReqigpvaafrlviFVKRLPKTRSGKILRRTLRKI 596
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
146-526 |
9.89e-31 |
|
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: 124.54 E-value: 9.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 146 SAFKPEII---LTTGTKDGVLSIQDLLAPTKTEffyqpTPLkegpsqtvAILTSSGTTGMPKAVCISNDILTQET----- 217
Cdd:cd05969 57 SAFGPEAIrdrLENSEAKVLITTEELYERTDPE-----DPT--------LLHYTSGTTGTPKGVLHVHDAMIFYYftgky 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 218 VFVNGYDTIF-ISASLDWITGLWATIFST-VNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSL--LDCPTATP 293
Cdd:cd05969 124 VLDLHPDDIYwCTADPGWVTGTVYGIWAPwLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmkEGDELARK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 294 EKLGSLTKLNFGGGRMT-QATVERVKKLapNGVLNSSYGMTEVGFIVFNH---GHLKLTAAGNPLPGIQVKIVDDDGNQL 369
Cdd:cd05969 204 YDLSSLRFIHSVGEPLNpEAIRWGMEVF--GVPIHDTWWQTETGSIMIANypcMPIKPGSMGKPLPGVKAAVVDENGNEL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 370 GVNQTGEI------------IVHNGFSWNGYFADpeatkamqdeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMW 437
Cdd:cd05969 282 PPGTKGILalkpgwpsmfrgIWNDEERYKNSFID-----------GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 438 PAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVV-----------REDNATLTAQQVIDHVAKRlpdiqkqlraGVQF 506
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfepsdelKEEIINFVRQKLGAHVAPR----------EIEF 420
|
410 420
....*....|....*....|..
gi 21356947 507 ADEIPQNHNGKVVRRY--ARDL 526
Cdd:cd05969 421 VDNLPKTRSGKIMRRVlkAKEL 442
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
185-505 |
1.46e-30 |
|
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: 123.86 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 185 EGPSQTVAILTSSGTTGMPKAVCISNDILTQETVfvNGYDTIFISA------------SLDWITGLWATIFStvNGCTRI 252
Cdd:cd05907 84 EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNAL--ALAERLPATEgdrhlsflplahVFERRAGLYVPLLA--GARIYF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 253 ISS-KPFAADyfvylVSKYSITYALIPP---EHCCSLLDCPTATPEK--------LGSLTKLNFGGGRMTQATVERVKKL 320
Cdd:cd05907 160 ASSaETLLDD-----LSEVRPTVFLAVPrvwEKVYAAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFRAL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 321 apnGV-LNSSYGMTEVGFIVF-NHGH-LKLTAAGNPLPGIQVKIVDDdgnqlgvnqtGEIIVHNGFSWNGYFADPEATKA 397
Cdd:cd05907 235 ---GIpVYEGYGLTETSAVVTlNPPGdNRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 398 MQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKW-KGLQMWPAEVEAVIDELPEVKRVCVIGvyDetQGDVPGALVV-RE 475
Cdd:cd05907 302 ALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG--D--GRPFLVALIVpDP 377
|
330 340 350
....*....|....*....|....*....|....*
gi 21356947 476 DNATLTAQQVIDHVAKRL-----PDIQKQLRAGVQ 505
Cdd:cd05907 378 EALEAWAEEHGIAYTDVAelaanPAVRAEIEAAVE 412
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
62-518 |
1.74e-30 |
|
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: 124.33 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 62 LTWA------IRIAQQLKSRGLDHKDIIGISARNTtyimPTAVACFFhGTPFQSA--NPI---LEESTLKHLYNISKPKI 130
Cdd:cd12118 30 YTWRqtydrcRRLASALAALGISRGDTVAVLAPNT----PAMYELHF-GVPMAGAvlNALntrLDAEEIAFILRHSEAKV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 131 IFTDadhydklysatSAFKPEiilttgtkdgvlsiqDLLAPTKTEFFYQPtPLKEgpSQTVAILTSSGTTGMPKAVcisn 210
Cdd:cd12118 105 LFVD-----------REFEYE---------------DLLAEGDPDFEWIP-PADE--WDPIALNYTSGTTGRPKGV---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 211 dILTQETVFVNGYDTIFISA---------SLD------WiTGLWA-TIFSTVNGCTRIISSKPfaadyfVY-LVSKYSIT 273
Cdd:cd12118 152 -VYHHRGAYLNALANILEWEmkqhpvylwTLPmfhcngW-CFPWTvAAVGGTNVCLRKVDAKA------IYdLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 274 yalippeHCCS-------LLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLapNGVLNSSYGMTEV-GFIVF----- 340
Cdd:cd12118 224 -------HFCGaptvlnmLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL--GFDVTHVYGLTETyGPATVcawkp 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 341 --NHGHLKLTAAGNPLPGI------QVKIVDDDGNQL----GVnQTGEIIVHNGFSWNGYFADPEAT-KAMQDeeGWFHT 407
Cdd:cd12118 295 ewDELPTEERARLKARQGVryvgleEVDVLDPETMKPvprdGK-TIGEIVFRGNIVMKGYLKNPEATaEAFRG--GWFHS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 408 GDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVID 487
Cdd:cd12118 372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIA 451
|
490 500 510
....*....|....*....|....*....|...
gi 21356947 488 HVAKRLPD--IQKQlragVQFaDEIPQNHNGKV 518
Cdd:cd12118 452 FCREHLAGfmVPKT----VVF-GELPKTSTGKI 479
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
50-521 |
2.15e-30 |
|
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: 123.51 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 50 DSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQsanPIleestlkhlyNISKPK 129
Cdd:cd05945 11 VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYV---PL----------DASSPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 130 iiftdadhyDKLYSATSAFKPEIILTTGTkdgvlsiqdllaptktEFFYqptplkegpsqtvaILTSSGTTGMPKAVCIS 209
Cdd:cd05945 78 ---------ERIREILDAAKPALLIADGD----------------DNAY--------------IIFTSGSTGRPKGVQIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 210 ND-------------ILTQETVFVNGYDTIFISASLDWITGLwatifstVNGCTRIISSKPFAADY---FVYLvSKYSIT 273
Cdd:cd05945 119 HDnlvsftnwmlsdfPLGPGDVFLNQAPFSFDLSVMDLYPAL-------ASGATLVPVPRDATADPkqlFRFL-AEHGIT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 274 YALIPPE--HCCSLLdcPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE----VGFIVFN----HG 343
Cdd:cd05945 191 VWVSTPSfaAMCLLS--PTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEatvaVTYIEVTpevlDG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 344 HLKLTAaGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT-KAMQDEEG--WFHTGDMGYFDEDDYLY 420
Cdd:cd05945 269 YDRLPI-GYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTaAAFFPDEGqrAYRTGDLVRLEADGLLF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 421 MTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVI-DHVAKRLPD--IQ 497
Cdd:cd05945 348 YRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIkAELAERLPPymIP 427
|
490 500
....*....|....*....|....
gi 21356947 498 KQLRAgvqfADEIPQNHNGKVVRR 521
Cdd:cd05945 428 RRFVY----LDELPLNANGKIDRK 447
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
55-520 |
1.05e-29 |
|
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: 121.41 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 55 EVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTD 134
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 135 ADhydklysatsafkpeiilttgtkdgvlsiqdllaptkteffyqptplkegpsqTVAILT-SSGTTGMPKAVCISN--- 210
Cdd:cd05919 90 AD-----------------------------------------------------DIAYLLySSGTTGPPKGVMHAHrdp 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 211 ----DILTQETVFVNGYDTIFISASLDWITGLW-ATIFSTVNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSL 285
Cdd:cd05919 117 llfaDAMAREALGLTPGDRVFSSAKMFFGYGLGnSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 286 LDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSsYGMTEVGFIVFNH--GHLKLTAAGNPLPGIQVKIVD 363
Cdd:cd05919 197 LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDG-IGATEVGHIFLSNrpGAWRLGSTGRPVPGYEIRLVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 364 DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAmQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEA 443
Cdd:cd05919 276 EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRA-TFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 444 VIDELPEVKRVCVIGVYDETQGDVPGALVVREDNAT---LTAQQVIDHVAKRLPdIQKQLRAgVQFADEIPQNHNGKVVR 520
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeSLARDIHRHLLERLS-AHKVPRR-IAFVDELPRTATGKLQR 432
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
186-521 |
1.17e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 122.56 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 186 GPSQTVAILTSSGTTGMPKAVCISN--DILTQETVF----VNGYDTIFISASLDWITGLWATIFSTVNGCTrIISSKPFA 259
Cdd:PRK13382 194 TGRKGRVILLTSGTTGTPKGARRSGpgGIGTLKAILdrtpWRAEEPTVIVAPMFHAWGFSQLVLAASLACT-IVTRRRFD 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 260 ADYFVYLVSKYSITYALIPPEHCCSLLDCPtatPEKLG--SLTKLNF---GGGRMTQATVER-VKKLAPngVLNSSYGMT 333
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDLP---AEVRNrySGRSLRFaaaSGSRMRPDVVIAfMDQFGD--VIYNNYNAT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 334 EVGFI-VFNHGHLKLT--AAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYfaDPEATKAMQDeeGWFHTGDM 410
Cdd:PRK13382 348 EAGMIaTATPADLRAApdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDV 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 411 GYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVA 490
Cdd:PRK13382 424 GYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVR 503
|
330 340 350
....*....|....*....|....*....|.
gi 21356947 491 KRLPDiQKQLRAgVQFADEIPQNHNGKVVRR 521
Cdd:PRK13382 504 DNLAN-YKVPRD-IVVLDELPRGATGKILRR 532
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
49-522 |
1.70e-29 |
|
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: 121.01 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 49 SDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTtyimPTAVACFFHGTPFQS-ANPILEEST---LKHLYN 124
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENR----PEWGIAFFAIWTYGAiAVPILAEFTadeVHHILN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 125 ISKPKIIFTDADHYDKLYSATSAfkpeiilTTGTKDGVLSIQDLLApTKTEFFYQPTPLKEGpSQTVAILTSSGTTGMpk 204
Cdd:cd05914 77 HSEAKAIFVSDEDDVALINYTSG-------TTGNSKGVMLTYRNIV-SNVDGVKEVVLLGKG-DKILSILPLHHIYPL-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 avcisndILTQETVFVNGYDTIFisasLDWITGLWATIFSTVNGCTRIISSKPfaadyfvYLVSKYSITYALipPEHCCS 284
Cdd:cd05914 146 -------TFTLLLPLLNGAHVVF----LDKIPSAKIIALAFAQVTPTLGVPVP-------LVIEKIFKMDII--PKLTLK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 285 LLDCPTATPEKLGSLTKLNF----------------GGGRMTQATVERVKKLapNGVLNSSYGMTEVGFIV-FNH-GHLK 346
Cdd:cd05914 206 KFKFKLAKKINNRKIRKLAFkkvheafggnikefviGGAKINPDVEEFLRTI--GFPYTIGYGMTETAPIIsYSPpNRIR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 347 LTAAGNPLPGIQVKIVDDDGNqlgvNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKK 426
Cdd:cd05914 284 LGSAGKVIDGVEVRIDSPDPA----TGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 427 EV-LKWKGLQMWPAEVEAVIDELPEV---------KRVCVIGVYDETQGDVPgALVVREDNATLTaQQVIDHVAKRLPDI 496
Cdd:cd05914 360 EMiVLSSGKNIYPEEIEAKINNMPFVleslvvvqeKKLVALAYIDPDFLDVK-ALKQRNIIDAIK-WEVRDKVNQKVPNY 437
|
490 500
....*....|....*....|....*.
gi 21356947 497 QKQLRAGVQFaDEIPQNHNGKvVRRY 522
Cdd:cd05914 438 KKISKVKIVK-EEFEKTPKGK-IKRF 461
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
314-524 |
2.84e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 120.65 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 314 VERVKKLAPNGVLNSSYGMTEVGFIVFNH---GHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFA 390
Cdd:PRK07638 270 KEKIKNIFPYAKLYEFYGASELSFVTALVdeeSERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 391 DPEATKAMqDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGA 470
Cdd:PRK07638 350 GGVLAREL-NADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVA 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21356947 471 LVvrEDNAtlTAQQVIDHVAKRLPDIQKQLRagVQFADEIPQNHNGKVVRRYAR 524
Cdd:PRK07638 429 II--KGSA--TKQQLKSFCLQRLSSFKIPKE--WHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
190-534 |
5.13e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 120.65 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 190 TVAILTSSGTTGMPKAVcisndILTQETVFVNGYdtiFISASLdwitGL---------------WATIFSTVnGCTRIIS 254
Cdd:PRK12583 203 PINIQYTSGTTGFPKGA-----TLSHHNILNNGY---FVAESL----GLtehdrlcvpvplyhcFGMVLANL-GCMTVGA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 255 SKPFAADYFVYLvskysITYALIPPEHCCSLLDCPTA------TPEK----LGSLTKLNFGGGRMTQATVERVKKLAPNG 324
Cdd:PRK12583 270 CLVYPNEAFDPL-----ATLQAVEEERCTALYGVPTMfiaeldHPQRgnfdLSSLRTGIMAGAPCPIEVMRRVMDEMHMA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 325 VLNSSYGMTEVGFIVFNHG-----HLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQ 399
Cdd:PRK12583 345 EVQIAYGMTETSPVSLQTTaaddlERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESI 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 400 DEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNAT 479
Cdd:PRK12583 425 DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHA 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356947 480 LTAQQVIDHVAKRLP--DIQKQLRagvqFADEIPQNHNGKVVRRYARDLFVALSKKN 534
Cdd:PRK12583 505 ASEEELREFCKARIAhfKVPRYFR----FVDEFPMTVTGKVQKFRMREISIEELALP 557
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
157-521 |
5.72e-29 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.17 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 157 GTKDGVLSIQDLLAPTKTEFFYQPtPLKegPSQTVAILTSSGTTGMPKAVcisndILTQETVFVNGYDTifisaslDWIT 236
Cdd:PRK08008 145 PADDGVSSFTQLKAQQPATLCYAP-PLS--TDDTAEILFTSGTTSRPKGV-----VITHYNLRFAGYYS-------AWQC 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 237 GLWA---------------------TIFSTvnGCTRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEK 295
Cdd:PRK08008 210 ALRDddvyltvmpafhidcqctaamAAFSA--GATFVLLEK-YSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 296 LGSLTKLNFgggRMTQATVERVKKLAPNGV-LNSSYGMTE--VGFIV-FNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGV 371
Cdd:PRK08008 287 QHCLREVMF---YLNLSDQEKDAFEERFGVrLLTSYGMTEtiVGIIGdRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 372 NQTGEIIVHN--GFS-WNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDEL 448
Cdd:PRK08008 364 GEIGEICIKGvpGKTiFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356947 449 PEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:PRK08008 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKF--KVPSYLEIRKDLPRNCSGKIIKK 514
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
54-509 |
1.04e-28 |
|
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: 119.50 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 54 VEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFT 133
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 134 DA-DHYDklysatsAFKPeiilttGTKDGVLSIQdLLAPTKTEFFYQ-------PTPLKE----GPSQTVAILTSSGTTG 201
Cdd:cd05932 85 GKlDDWK-------AMAP------GVPEGLISIS-LPPPSAANCQYQwddliaqHPPLEErptrFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 202 MPKAVCISNDILTQ------ETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIIsskpFAA--DYFVYLVSKYSIT 273
Cdd:cd05932 151 QPKGVMLTFGSFAWaaqagiEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVA----FAEslDTFVEDVQRARPT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 274 ----------------YALIPPEHCCSLLDCPTatpekLGSLTK--------------LNFGGGRMTQATVERVKKLAPN 323
Cdd:cd05932 227 lffsvprlwtkfqqgvQDKIPQQKLNLLLKIPV-----VNSLVKrkvlkglgldqcrlAGCGSAPVPPALLEWYRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 324 gvLNSSYGMTE-VGFIVFNH-GHLKLTAAGNPLPGIQVKIVDDdgnqlgvnqtGEIIVHNGFSWNGYFADPEATKAMQDE 401
Cdd:cd05932 302 --ILEAYGMTEnFAYSHLNYpGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 402 EGWFHTGDMGYFDEDDYLYMTDRKKEVLKW-KGLQMWPAEVEAVIDELPEVKRVCVIGvydETQGDvPGALVV------- 473
Cdd:cd05932 370 DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG---SGLPA-PLALVVlseearl 445
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 21356947 474 REDNATLTA-----QQVIDHVAKRLpDIQKQLRAGVQFADE 509
Cdd:cd05932 446 RADAFARAEleaslRAHLARVNSTL-DSHEQLAGIVVVKDP 485
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
160-525 |
2.98e-28 |
|
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: 118.37 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 160 DGVLSIQDLLAPTkTEFFYQPTPLKEGPSQTVAILT-SSGTTGMPKAVCISN-----DILTQ---ETVFVNG-YDTIfis 229
Cdd:cd05970 157 EGWIDFRKLIKNA-SPDFERPTANSYPCGEDILLVYfSSGTTGMPKMVEHDFtyplgHIVTAkywQNVREGGlHLTV--- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 230 ASLDWITGLWATIFST-VNGCTRII-SSKPFAADYFVYLVSKYSITYALIPPEhCCSLLDCPTATPEKLGSLTKLNFGGG 307
Cdd:cd05970 233 ADTGWGKAVWGKIYGQwIAGAAVFVyDYDKFDPKALLEKLSKYGVTTFCAPPT-IYRFLIREDLSRYDLSSLRYCTTAGE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 308 RMTQATVERVKKLApnGV-LNSSYGMTEVGFIV--FNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHN--- 381
Cdd:cd05970 312 ALNPEVFNTFKEKT--GIkLMEGFGQTETTLTIatFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTskg 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 382 ---GFsWNGYFADPEAT-KAMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVI 457
Cdd:cd05970 390 kpvGL-FGGYYKDAEKTaEVWHD--GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356947 458 GVYDETQGDVPGALVVRedNATLTAQQVI-----DHVaKRLPDIQKQLRAgVQFADEIPQNHNGKVVRRYARD 525
Cdd:cd05970 467 GVPDPIRGQVVKATIVL--AKGYEPSEELkkelqDHV-KKVTAPYKYPRI-VEFVDELPKTISGKIRRVEIRE 535
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
57-521 |
3.93e-28 |
|
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: 117.94 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 57 TFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGtpfqsANPIL-----EESTLKHLYNISKPKII 131
Cdd:COG1021 52 SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG-----AIPVFalpahRRAEISHFAEQSEAVAY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 132 FTDADH----YDKLYSATSAFKPEI--ILTTGTKDGVLSIQDLLAPTKTEFFYQPTPlkegpsQTVAILT-SSGTTGMPK 204
Cdd:COG1021 127 IIPDRHrgfdYRALARELQAEVPSLrhVLVVGDAGEFTSLDALLAAPADLSEPRPDP------DDVAFFQlSGGTTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 AvcI-------------SNDI--LTQETVFV-------NgydtiFISASldwiTGLWATIFstVNGCTrIISSKPfAADY 262
Cdd:COG1021 201 L--IprthddylysvraSAEIcgLDADTVYLaalpaahN-----FPLSS----PGVLGVLY--AGGTV-VLAPDP-SPDT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 263 FVYLVSKYSITY-ALIPPeHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKlAPNGVLNSSYGMTEvGFIVFN 341
Cdd:COG1021 266 AFPLIERERVTVtALVPP-LALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRP-ALGCTLQQVFGMAE-GLVNYT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 342 H----GHLKLTAAGNPL-PGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDED 416
Cdd:COG1021 343 RlddpEEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 417 DYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVReDNATLTAQQVIDHVAKR---- 492
Cdd:COG1021 423 GYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRRFLRERglaa 501
|
490 500 510
....*....|....*....|....*....|.
gi 21356947 493 --LPDiqkqlRagVQFADEIPQNHNGKVVRR 521
Cdd:COG1021 502 fkLPD-----R--LEFVDALPLTAVGKIDKK 525
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
146-524 |
4.26e-28 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 116.85 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 146 SAFKPEII-LTTGTKDGVLSIQDLLAPTKteffyqptpLKEGPsqtVAILTSSGTTGMPKAVCISNDILT------QETV 218
Cdd:cd05973 57 TAFGPKAIeHRLRTSGARLVVTDAANRHK---------LDSDP---FVMMFTSGTTGLPKGVPVPLRALAafgaylRDAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 219 FVNGYDTIFISASLDWITGLWATIFSTV-NGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKL- 296
Cdd:cd05973 125 DLRPEDSFWNAADPGWAYGLYYAITGPLaLGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPk 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 297 GSLTKLNFGGGRMTqATVERVKKLAPNGVLNSSYGMTEVGFIVFNHGHL----KLTAAGNPLPGIQVKIVDDDGNQLGVN 372
Cdd:cd05973 205 GRLRRVSSAGEPLT-PEVIRWFDAALGVPIHDHYGQTELGMVLANHHALehpvHAGSAGRAMPGWRVAVLDDDGDELGPG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 373 QTG--EIIVHNG--FSWNGYFADPEATKAmqdeEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDEL 448
Cdd:cd05973 284 EPGrlAIDIANSplMWFRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEH 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356947 449 PEVKRVCVIGVYDETQGDVPGALVV-RE--DNATLTAQQVIDHVAKRLPdIQKQLRAgVQFADEIPQNHNGKVVRRYAR 524
Cdd:cd05973 360 PAVAEAAVIGVPDPERTEVVKAFVVlRGghEGTPALADELQLHVKKRLS-AHAYPRT-IHFVDELPKTPSGKIQRFLLR 436
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
330-521 |
6.04e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 113.55 E-value: 6.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTE--VGFIVFNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVN--QTGEIIVHNGFSWNGYFADPEATKAMQDEEGWF 405
Cdd:PRK07787 273 YGMTEtlITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGWF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 406 HTGDMGYFDEDDYLYMTDRKK-EVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNAtlTAQQ 484
Cdd:PRK07787 353 RTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV--AADE 430
|
170 180 190
....*....|....*....|....*....|....*..
gi 21356947 485 VIDHVAKRLpDIQKQLRAgVQFADEIPQNHNGKVVRR 521
Cdd:PRK07787 431 LIDFVAQQL-SVHKRPRE-VRFVDALPRNAMGKVLKK 465
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
50-518 |
2.13e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 113.51 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 50 DSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNT--TYI-----MPTAVACffhgtpfqSANPILEESTLKHL 122
Cdd:PRK07529 53 LDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLpeTHFalwggEAAGIAN--------PINPLLEPEQIAEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 123 YNISKPKIIFT-----DADHYDKLYSA------------------TSAFKPEIILTTGTK--DGVLSIQDLLAPTKTEFF 177
Cdd:PRK07529 125 LRAAGAKVLVTlgpfpGTDIWQKVAEVlaalpelrtvvevdlaryLPGPKRLAVPLIRRKahARILDFDAELARQPGDRL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 178 YQPTPLkeGPSQTVAILTSSGTTGMPKAV--CISNDI----LTQETVFVNGYDTIFISASLDWITGLWATIFSTV-NGCT 250
Cdd:PRK07529 205 FSGRPI--GPDDVAAYFHTGGTTGMPKLAqhTHGNEVanawLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLaRGAH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 251 RIISS-----KPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEkLGSLtKLNFGGGR-MTQATVERVKKLApnG 324
Cdd:PRK07529 283 VVLATpqgyrGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVDGHD-ISSL-RYALCGAApLPVEVFRRFEAAT--G 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 325 V-LNSSYGMTEVGFIV---FNHGHLKLTAAGNPLPGIQVKIV--DDDGNQL---GVNQTGEIIVHNGFSWNGYfADPEAT 395
Cdd:PRK07529 359 VrIVEGYGLTEATCVSsvnPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIAGPNVFSGY-LEAAHN 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 396 KAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVRE 475
Cdd:PRK07529 438 KGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLK 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 21356947 476 DNATLTAQQVIDHVAKRLPDiqkqlRAGV----QFADEIPQNHNGKV 518
Cdd:PRK07529 518 PGASATEAELLAFARDHIAE-----RAAVpkhvRILDALPKTAVGKI 559
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
57-456 |
3.18e-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: 110.82 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 57 TFGQALTWAIRIAQQLKSR-GLDHKDIIGISARNTTYIMPTAVACFFHG---TPFQSANP------ILEEStlkhlynis 126
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGaayVPLDPAYPaerlafILEDA--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 127 KPKIIFTDADHYDKLYSATsafkPEIILTTGTKdgVLSIQDLLAPTkteffyqPTPLKEGPSQTVAILTSSGTTGMPKAV 206
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLV----LPVILLDPLE--LAALDDAPAPP-------PPDAPSGPDDLAYVIYTSGSTGRPKGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 207 CISND-ILTQETVFVNGY-----DTIFISASLDWITGLWATIFSTVNGCTRII----SSKPFAADYFvYLVSKYSITYAL 276
Cdd:TIGR01733 139 VVTHRsLVNLLAWLARRYgldpdDRVLQFASLSFDASVEEIFGALLAGATLVVppedEERDDAALLA-ALIAEHPVTVLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 277 IPPehccSLLD-CPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE----VGFIVFNHGHLKLTAA- 350
Cdd:TIGR01733 218 LTP----SLLAlLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTEttvwSTATLVDPDDAPRESPv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 --GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHN-GFSwNGYFADPEATK--------AMQDEEGWFHTGDMGYFDEDDYL 419
Cdd:TIGR01733 294 piGRPLANTRLYVLDDDLRPVPVGVVGELYIGGpGVA-RGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNL 372
|
410 420 430
....*....|....*....|....*....|....*..
gi 21356947 420 YMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCV 456
Cdd:TIGR01733 373 EFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
193-527 |
3.76e-25 |
|
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: 105.88 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVCISNDILT------QETVFVNGYDTIFISASLDWITGL----------WATIFSTVNGCTRiiSSK 256
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLasaaglHSRLGFGGGDSWLLSLPLYHVGGLailvrsllagAELVLLERNQALA--EDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 257 PFAADYFVYLVskysityalipPEHCCSLLDCPtATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLnsSYGMTEVG 336
Cdd:cd17630 83 APPGVTHVSLV-----------PTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYT--TYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 337 FIVFNH--GHLKLTAAGNPLPGIQVKIVDDdgnqlgvnqtGEIIVHNGFSWNGYFADPEATKAmqDEEGWFHTGDMGYFD 414
Cdd:cd17630 149 SQVATKrpDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPEF--NEDGWFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 415 EDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLtaQQVIDHVAKRLP 494
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP--AELRAWLKDKLA 294
|
330 340 350
....*....|....*....|....*....|....*
gi 21356947 495 DIQ--KQLRagvqFADEIPQNHNGKVVRRYARDLF 527
Cdd:cd17630 295 RFKlpKRIY----PVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
156-533 |
6.80e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 108.55 E-value: 6.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 156 TGTKDGVLSIQDLLAPTKTEFFYQPTPLKEGPSQTVAILTSSGTTGMPKAVcisndILTQETVFVNgydtifISASLDWI 235
Cdd:PRK05605 187 TGPAPGTVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGA-----QLTHRNLFAN------AAQGKAWV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 236 TGLwatifstVNGCTRIISSKPFAADYFVYLVSKYSI----TYALIPPEHCCSLLDC-----PTATP------------- 293
Cdd:PRK05605 256 PGL-------GDGPERVLAALPMFHAYGLTLCLTLAVsiggELVLLPAPDIDLILDAmkkhpPTWLPgvpplyekiaeaa 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 294 -EKLGSLTKLNFG-GGRMT--QATVERVKKLApNGVLNSSYGMTEVGFIVFNH---GHLKLTAAGNPLPGIQVKIVD--D 364
Cdd:PRK05605 329 eERGVDLSGVRNAfSGAMAlpVSTVELWEKLT-GGLLVEGYGLTETSPIIVGNpmsDDRRPGYVGVPFPDTEVRIVDpeD 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 365 DGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQdEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAV 444
Cdd:PRK05605 408 PDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEV 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 445 IDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAGVQFaDEIPQNHNGKVVRRYAR 524
Cdd:PRK05605 487 LREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRY-KVPRRFYHV-DELPRDQLGKVRRREVR 564
|
....*....
gi 21356947 525 DLFVALSKK 533
Cdd:PRK05605 565 EELLEKLGA 573
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
29-531 |
8.39e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 109.24 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 29 SLGRIIFKNMRNWPKNVCqISDSEGVEVTFGQALTWAIRIAQQLKsRGLDHKDIIGIsarnttyIMPTAV-------ACF 101
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLA-VADSTGGELSYGKALTGALALARLLK-RELKDEENVGI-------LLPPSVagalanlALL 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 102 FHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKL----YSATSAFKPEIIL------TTGTKDGVLS-IQDLLA 170
Cdd:PRK08633 687 LAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLknkgFDLELPENVKVIYledlkaKISKVDKLTAlLAARLL 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 171 PTKT-EFFYQPTPlkeGPSQTVAILTSSGTTGMPKAVCISND-ILTQ----ETVF-VNGYDTIFISASLDWITGLWATIF 243
Cdd:PRK08633 767 PARLlKRLYGPTF---KPDDTATIIFSSGSEGEPKGVMLSHHnILSNieqiSDVFnLRNDDVILSSLPFFHSFGLTVTLW 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 244 -STVNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLtklnfgggRMTQATVERVKKLAP 322
Cdd:PRK08633 844 lPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASL--------RLVVAGAEKLKPEVA 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 323 NGVLN-------SSYGMTE-------------VGFIVFNHGHlKLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIVHN 381
Cdd:PRK08633 916 DAFEEkfgirilEGYGATEtspvasvnlpdvlAADFKRQTGS-KEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGG 994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 382 GFSWNGYFADPEATKAM---QDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGlQMWPaeVEAVIDELPEV-----KR 453
Cdd:PRK08633 995 PQVMKGYLGDPEKTAEVikdIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGG-EMVP--LGAVEEELAKAlggeeVV 1071
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356947 454 VCVIGVYDETQGDvpgALVVREDNATLTAQQVIDHVAK-RLPDIQKQLRAgVQfADEIPQNHNGKVVRRYARDLFVALS 531
Cdd:PRK08633 1072 FAVTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRY-FK-VEALPLLGSGKLDLKGLKELALALL 1145
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-524 |
1.62e-24 |
|
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: 105.16 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVC---------------------ISNDILTQETVfVNGYDTIFISASLDWITGLWATIFSTVNGCTR 251
Cdd:cd05924 8 ILYTGGTTGMPKGVMwrqedifrmlmggadfgtgefTPSEDAHKAAA-AAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 252 IISSKPFAADYFVYLVSKYSITYALI-------PpehccsLLDC-PTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPN 323
Cdd:cd05924 87 VLPDDRFDPEEVWRTIEKHKVTSMTIvgdamarP------LIDAlRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 324 GVLNSSYGMTEVGFIVFNHGHLKLTAAG---NPLPGIQVkiVDDDGNQLGVNQTGE-IIVHNGFSWNGYFADPEATKAM- 398
Cdd:cd05924 161 ITLVDAFGSSETGFTGSGHSAGSGPETGpftRANPDTVV--LDDDGRVVPPGSGGVgWIARRGHIPLGYYGDEAKTAETf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 399 --QDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVRED 476
Cdd:cd05924 239 peVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLRE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 21356947 477 NATLTAQQVIDHVAKRLP--DIQKQlragVQFADEIPQNHNGKVVRRYAR 524
Cdd:cd05924 319 GAGVDLEELREHCRTRIAryKLPKQ----VVFVDEIERSPAGKADYRWAK 364
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
38-527 |
1.67e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.14 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 38 MRNWPKNVCQISDS---------------EG--VEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVAC 100
Cdd:PRK06018 5 MQDWPLLCHRIIDHaarihgnrevvtrsvEGpiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 101 FFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADH---YDKLYSATSAFKPEIILTTG------TKDGVLSIQDLLAP 171
Cdd:PRK06018 85 MGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTFvpiLEKIADKLPSVERYVVLTDAahmpqtTLKNAVAYEEWIAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 172 TKTEFFYqptplKEGPSQTVAILT-SSGTTGMPKAVCISNDILTQETVFVNGYDTIFISASlDWI--------TGLWATI 242
Cdd:PRK06018 165 ADGDFAW-----KTFDENTAAGMCyTSGTTGDPKGVLYSHRSNVLHALMANNGDALGTSAA-DTMlpvvplfhANSWGIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 243 FSTVNGCTRIISSKPFAADYFVY-LVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLA 321
Cdd:PRK06018 239 FSAPSMGTKLVMPGAKLDGASVYeLLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 322 PNGVlnSSYGMTE------VGFIVFNHGHLKLTA-------AGNPLPGIQVKIVDDDGNQL---GvNQTGEIIVHNGFSW 385
Cdd:PRK06018 319 VEVR--HAWGMTEmsplgtLAALKPPFSKLPGDArldvlqkQGYPPFGVEMKITDDAGKELpwdG-KTFGRLKVRGPAVA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 386 NGYFadpEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQG 465
Cdd:PRK06018 396 AAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWD 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356947 466 DVPGALVVREDNATLTAQQVIDH----VAK-RLPDiqkqlraGVQFADEIPQNHNGKVVRRYARDLF 527
Cdd:PRK06018 473 ERPLLIVQLKPGETATREEILKYmdgkIAKwWMPD-------DVAFVDAIPHTATGKILKTALREQF 532
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
68-477 |
2.04e-24 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 106.81 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 68 IAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHG---TP------FQSANP----------ILEESTLK---HLYNI 125
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGgivAPlnyrwsFEEAKSamllvrpvmlVTDETCSSwyeELQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 126 SKPKI---IFTDADHYDKLYSATSAFKPEIILTtgtkdgvlsiqdlLAPTKTEFFYqptplKEGPSQTVAILTSSGTTGM 202
Cdd:PLN02860 125 RLPSLmwqVFLESPSSSVFIFLNSFLTTEMLKQ-------------RALGTTELDY-----AWAPDDAVLICFTSGTTGR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 203 PKAVCISNDILTQET---VFVNGY---DTIFISASLDWITGLWATIFSTVNGCTRIISSKpFAADYFVYLVSKYSITYAL 276
Cdd:PLN02860 187 PKGVTISHSALIVQSlakIAIVGYgedDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPK-FDAKAALQAIKQHNVTSMI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 277 IPPEHCCSLLDcPTATPEK---LGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE----VGFIVFN-------- 341
Cdd:PLN02860 266 TVPAMMADLIS-LTRKSMTwkvFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacssLTFMTLHdptlespk 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 342 ------------HGHLKL-TAAGNPLPGIQVKIVDDDGNQlgvnqTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTG 408
Cdd:PLN02860 345 qtlqtvnqtkssSVHQPQgVCVGKPAPHVELKIGLDESSR-----VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTG 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356947 409 DMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDN 477
Cdd:PLN02860 420 DIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDG 488
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-518 |
3.63e-24 |
|
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: 103.71 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAV--CISNDILTQETVFVNGY----DTIFISASLDWITGLWATIFS-TVNGCTRIISS---- 255
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAqhTHSNEVYNAWMLALNSLfdpdDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAGpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 256 -KPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATpeKLGSLtKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE 334
Cdd:cd05944 81 rNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNA--DISSL-RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 335 VGFIV---FNHGHLKLTAAGNPLPGIQVKIV--DDDGNQL---GVNQTGEIIVHNGFSWNGYFaDPEATKAMQDEEGWFH 406
Cdd:cd05944 158 ATCLVavnPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVADGWLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 407 TGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVI 486
Cdd:cd05944 237 TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 21356947 487 DHVAKRLPDiqkqlRAGVQFA----DEIPQNHNGKV 518
Cdd:cd05944 317 AWARDHVPE-----RAAVPKHievlEELPVTAVGKV 347
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
39-524 |
3.65e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 105.86 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 39 RNWPKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEEST 118
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 119 LKHLYNISKPKIIFTDAdHYDKLYSATSAFKPEIILTTGTKDGVLSIQDLLAPTKTeffyqptPLKEGPSQTVaILTSSG 198
Cdd:PRK13390 88 ADYIVGDSGARVLVASA-ALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGP-------RLTEQPCGAV-MLYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 199 TTGMPKA-----------------VCISN---DILTQETVFVNGydTIFISASLDWITGLWATifstvnGCTRIISSKPF 258
Cdd:PRK13390 159 TTGFPKGiqpdlpgrdvdapgdpiVAIARafyDISESDIYYSSA--PIYHAAPLRWCSMVHAL------GGTVVLAKRFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 259 AADYFVYlVSKYSITYALIPPEHCCSLL--DCPTATPEKLGSLTKLNFGGG----RMTQATVERvkkLAPngVLNSSYGM 332
Cdd:PRK13390 231 AQATLGH-VERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAApcpvDVKHAMIDW---LGP--IVYEYYSS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 333 TEV-GFIVFNHGHL--KLTAAGNPLPGiQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEG--WFHT 407
Cdd:PRK13390 305 TEAhGMTFIDSPDWlaHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 408 GDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGA---LVVREDNATLTAQQ 484
Cdd:PRK13390 384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAviqLVEGIRGSDELARE 463
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 21356947 485 VIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGKVVRRYAR 524
Cdd:PRK13390 464 LIDYTRSRIAHY-KAPRS-VEFVDELPRTPTGKLVKGLLR 501
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
49-529 |
5.18e-24 |
|
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: 105.78 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 49 SDSEGVEVTFGQALTWAIRIAQQLKSRGLdHKDIIGISARNTTYIMPTAVACFFHG---TPFQSANPIleeSTLKHLYNI 125
Cdd:cd05931 18 EGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGaiaVPLPPPTPG---RHAERLAAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 126 ---SKPKIIFTDADHYDklysatsAFKPEIILTTGTKDGVLSIQDLLAPTKTEffyqPTPLKEGPSQTVAILT-SSGTTG 201
Cdd:cd05931 94 ladAGPRVVLTTAAALA-------AVRAFAASRPAAGTPRLLVVDLLPDTSAA----DWPPPSPDPDDIAYLQyTSGSTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 202 MPKAVCISND-ILTQETVFVNGY----DTIFISasldWI-----TGLWATIFSTV-NGCTRIISSkPFAadyFVY----- 265
Cdd:cd05931 163 TPKGVVVTHRnLLANVRQIRRAYgldpGDVVVS----WLplyhdMGLIGGLLTPLySGGPSVLMS-PAA---FLRrplrw 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 266 --LVSKYSITYALIPP---EHCCSlldcpTATPEKLGS--LTKLNF---GGGRMTQATVER-VKKLAPNG----VLNSSY 330
Cdd:cd05931 235 lrLISRYRATISAAPNfayDLCVR-----RVRDEDLEGldLSSWRValnGAEPVRPATLRRfAEAFAPFGfrpeAFRPSY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 331 GMTE----VGFIVFNHGHL------------------------KLTAAGNPLPGIQVKIVDDDGNQ-LGVNQTGEIIVHN 381
Cdd:cd05931 310 GLAEatlfVSGGPPGTGPVvlrvdrdalagravavaaddpaarELVSCGRPLPDQEVRIVDPETGReLPDGEVGEIWVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 382 GFSWNGYFADPEATKAM------QDEEGWFHTGDMGYFDeDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKR-- 453
Cdd:cd05931 390 PSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpg 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 454 -VCVIGVYDEtqgDVPGALVVREDNATLTaqqvidhvAKRLPDIQKQLRA------GVQFAD-------EIPQNHNGKVV 519
Cdd:cd05931 469 cVAAFSVPDD---GEERLVVVAEVERGAD--------PADLAAIAAAIRAavarehGVAPADvvlvrpgSIPRTSSGKIQ 537
|
570
....*....|
gi 21356947 520 RRYARDLFVA 529
Cdd:cd05931 538 RRACRAAYLD 547
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
34-527 |
1.36e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 104.31 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 34 IFKNMRNWPKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHG--------- 104
Cdd:PRK07768 8 MYANARTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGasltmlhqp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 105 TPfQSANPILEESTLKHLYNISKPKIIFTDAdhYDklySATSAFKPEIILttgtkdgVLSIQDLLAPTKTEffyqPTPLK 184
Cdd:PRK07768 88 TP-RTDLAVWAEDTLRVIGMIGAKAVVVGEP--FL---AAAPVLEEKGIR-------VLTVADLLAADPID----PVETG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 185 EGpsqTVAILT-SSGTTGMPKAVCIsndilTQETVFVNGYdTIFISASLDWITGL---WATIFS--------TVN---GC 249
Cdd:PRK07768 151 ED---DLALMQlTSGSTGSPKAVQI-----THGNLYANAE-AMFVAAEFDVETDVmvsWLPLFHdmgmvgflTVPmyfGA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 250 TRI-ISSKPFAADYFVY--LVSKY--SITYAlipPEHCCSLLDCPTATPEKLGS--LTKLNF---GGGRMTQATVER-VK 318
Cdd:PRK07768 222 ELVkVTPMDFLRDPLLWaeLISKYrgTMTAA---PNFAYALLARRLRRQAKPGAfdLSSLRFalnGAEPIDPADVEDlLD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 319 KLAPNGvLNSS-----YGMTE----VGFIVFNHG------HLKLTAA------------------GNPLPGIQVKIVDDD 365
Cdd:PRK07768 299 AGARFG-LRPEailpaYGMAEatlaVSFSPCGAGlvvdevDADLLAAlrravpatkgntrrlatlGPPLPGLEVRVVDED 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 366 GNQLGVNQTGEIIVHnGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVI 445
Cdd:PRK07768 378 GQVLPPRGVGVIELR-GESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 446 DELPEVKRVCVIGV-YDETQGDVPGALVV----REDNATLT------AQQVIDHVAKRlPDIQKQLRAGvqfadEIPQNH 514
Cdd:PRK07768 457 ARVEGVRPGNAVAVrLDAGHSREGFAVAVesnaFEDPAEVRrirhqvAHEVVAEVGVR-PRNVVVLGPG-----SIPKTP 530
|
570
....*....|...
gi 21356947 515 NGKVVRRYARDLF 527
Cdd:PRK07768 531 SGKLRRANAAELV 543
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
167-519 |
1.44e-23 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 104.58 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 167 DLLAPTKTEFfyQPTPLkeGPSQTVAILTSSGTTGMPKAVCISND--ILTQETVFVNGYD-----TIFISASLDWITG-L 238
Cdd:cd17634 215 DLIAKASPEH--QPEAM--NAEDPLFILYTSGTTGKPKGVLHTTGgyLVYAATTMKYVFDygpgdIYWCTADVGWVTGhS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 239 WATIFSTVNGCTRII-SSKPF--AADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEK--LGSLTKLNFGGGRMTQAT 313
Cdd:cd17634 291 YLLYGPLACGATTLLyEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGtdRSSLRILGSVGEPINPEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 314 VE-RVKKLAPNG--VLNSSYGMTEVGFIVFN---HGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVhnGFSWNG 387
Cdd:cd17634 371 YEwYWKKIGKEKcpVVDTWWQTETGGFMITPlpgAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVI--TDPWPG 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 388 ----YFADPEA--TKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYD 461
Cdd:cd17634 449 qtrtLFGDHERfeQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPH 528
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356947 462 ETQGDVPGALVV----REDNATLtAQQVIDHVAKRL-----PDIqkqlragVQFADEIPQNHNGKVV 519
Cdd:cd17634 529 AIKGQAPYAYVVlnhgVEPSPEL-YAELRNWVRKEIgplatPDV-------VHWVDSLPKTRSGKIM 587
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
184-524 |
4.07e-23 |
|
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: 101.79 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 184 KEGPSQTVAILT-SSGTTGMPKAVC--ISNDILTQETVFVNGY-----DTIFISASLDWITGLWAT-IFSTVNGCTRIIS 254
Cdd:cd05958 92 ALTASDDICILAfTSGTTGAPKATMhfHRDPLASADRYAVNVLrlredDRFVGSPPLAFTFGLGGVlLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 255 SKPFAADYFVyLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSsYGMTE 334
Cdd:cd05958 172 EEATPDLLLS-AIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDG-IGSTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 335 VG--FIVFNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVhNGFSWNGYFADPEATKAMQDeeGWFHTGDMGY 412
Cdd:cd05958 250 MFhiFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV-RGPTGCRYLADKRQRTYVQG--GWNITGDTYS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 413 FDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNAT---LTAQQVIDHv 489
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpVLARELQDH- 405
|
330 340 350
....*....|....*....|....*....|....*
gi 21356947 490 AKRLPDIQKQLRAgVQFADEIPQNHNGKVVRRYAR 524
Cdd:cd05958 406 AKAHIAPYKYPRA-IEFVTELPRTATGKLQRFALR 439
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3-533 |
5.61e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 102.65 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 3 KLPCSYDAENKIWKGIPQNNPFKPET--SLGRIIFKNMRNWPKNVCQISdsEGVEVTFGQALTWAIRIAQQLKSRGLDHK 80
Cdd:PRK08279 10 RLPRRLPDLPGILRGLKRTALITPDSkrSLGDVFEEAAARHPDRPALLF--EDQSISYAELNARANRYAHWAAARGVGKG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 81 DIIGISARNTtyimPTAVACFFhGTPFQSA-----NPILEESTLKHLYNISKPKIIFTDADHYDKLYSATSAFKPEI--- 152
Cdd:PRK08279 88 DVVALLMENR----PEYLAAWL-GLAKLGAvvallNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPrlw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 153 ILTTGTKDGVLSIQDLLAPTKTeffyQPTPLKEGPSQTVA------ILTSsGTTGMPKAVCIS-NDILTQETVFV----- 220
Cdd:PRK08279 163 VAGGDTLDDPEGYEDLAAAAAG----APTTNPASRSGVTAkdtafyIYTS-GTTGLPKAAVMShMRWLKAMGGFGgllrl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 221 NGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLT 300
Cdd:PRK08279 238 TPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 301 KLnFGGG-------RMTQAT-VERVKKLapngvlnssYGMTE--VGFI-VFNhghlKLTAAGN-PLPGI-QVKIV----- 362
Cdd:PRK08279 318 LM-IGNGlrpdiwdEFQQRFgIPRILEF---------YAASEgnVGFInVFN----FDGTVGRvPLWLAhPYAIVkydvd 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 363 ------DDDGN--QLGVNQTGEII--VHNGFSWNGYfADPEATKA--MQD--EEG--WFHTGDMGYFDEDDYLYMTDRKK 426
Cdd:PRK08279 384 tgepvrDADGRciKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKkiLRDvfKKGdaWFNTGDLMRDDGFGHAQFVDRLG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 427 EVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVydetqgDVPG--------ALVVReDNATLTAQQVIDHVAKRLPDiqk 498
Cdd:PRK08279 463 DTFRWKGENVATTEVENALSGFPGVEEAVVYGV------EVPGtdgragmaAIVLA-DGAEFDLAALAAHLYERLPA--- 532
|
570 580 590
....*....|....*....|....*....|....*
gi 21356947 499 qlragvqfadeipqnhngkvvrrYARDLFVALSKK 533
Cdd:PRK08279 533 -----------------------YAVPLFVRLVPE 544
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
51-527 |
6.29e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 102.27 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 51 SEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKI 130
Cdd:PRK05852 39 ADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 131 IFTDADHYDKLYSATSAFKPEIIL---TTGTKDGVLSIQ--DLLAPTKTeffyQPTPLKEGPSQTVaILTSSGTTGMPKA 205
Cdd:PRK05852 119 VLIDADGPHDRAEPTTRWWPLTVNvggDSGPSGGTLSVHldAATEPTPA----TSTPEGLRPDDAM-IMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 206 VCISN-DILTQETVFVNGY-----DTIFISASLDWITGLWATIFSTV--NGCTRIISSKPFAADYFVYLVSKYSIT-YAL 276
Cdd:PRK05852 194 VPWTHaNIASSVRAIITGYrlsprDATVAVMPLYHGHGLIAALLATLasGGAVLLPARGRFSAHTFWDDIKAVGATwYTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 277 IPPEHCCsLLDCPTATPEKLGSlTKLNF---GGGRMTQATVERVKK--LAPngVLnSSYGMTEVGFIV-------FNHGH 344
Cdd:PRK05852 274 VPTIHQI-LLERAATEPSGRKP-AALRFirsCSAPLTAETAQALQTefAAP--VV-CAFGMTEATHQVtttqiegIGQTE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 345 LKLTAAG--NPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATkAMQDEEGWFHTGDMGYFDEDDYLYMT 422
Cdd:PRK05852 349 NPVVSTGlvGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTIT-AANFTDGWLRTGDLGSLSAAGDLSIR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 423 DRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqkQLRA 502
Cdd:PRK05852 428 GRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAF--EIPA 505
|
490 500
....*....|....*....|....*
gi 21356947 503 GVQFADEIPQNHNGKVVRRYARDLF 527
Cdd:PRK05852 506 SFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
330-488 |
2.79e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 100.27 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVFNHG-----HLKLTAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIVHnGFS-WNGYFADPEATKAMQDEE 402
Cdd:PRK08315 348 YGMTETSPVSTQTRtddplEKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCTR-GYSvMKGYWNDPEKTAEAIDAD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 403 GWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTA 482
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE 506
|
....*.
gi 21356947 483 QQVIDH 488
Cdd:PRK08315 507 EDVRDF 512
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
55-417 |
5.56e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 99.74 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 55 EVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPIL-----EESTLKHLYNISKPK 129
Cdd:PRK12582 80 KVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshDHAKLKHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 130 IIFT-DADHYDKLYSATSAFKPEIILTTGTKDG--VLSIQDLLAPTKTEFFYQP----TPlkegpsQTVA-ILTSSGTTG 201
Cdd:PRK12582 160 VVFAqSGAPFARALAALDLLDVTVVHVTGPGEGiaSIAFADLAATPPTAAVAAAiaaiTP------DTVAkYLFTSGSTG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 202 MPKAV-----CISNDILTQETVFVNGYDTIfISASLDWITglWATIFS--------TVNGCTRIISS-KPFAADYFVYLV 267
Cdd:PRK12582 234 MPKAVintqrMMCANIAMQEQLRPREPDPP-PPVSLDWMP--WNHTMGgnanfnglLWGGGTLYIDDgKPLPGMFEETIR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 268 SKYSI--TYALIPPEHCCSLLDCPTATPEKLGSLTK----LNFGGGRMTQATVERVKKLA--PNG---VLNSSYGMTEV- 335
Cdd:PRK12582 311 NLREIspTVYGNVPAGYAMLAEAMEKDDALRRSFFKnlrlMAYGGATLSDDLYERMQALAvrTTGhriPFYTGYGATETa 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 336 GFIVFNHGHLKLTA-AGNPLPGIQVKIVdDDGNQLGVNQTGEIIVhngfswNGYFADPEATKAMQDEEGWFHTGDMGYF- 413
Cdd:PRK12582 391 PTTTGTHWDTERVGlIGLPLPGVELKLA-PVGDKYEVRVKGPNVT------PGYHKDPELTAAAFDEEGFYRLGDAARFv 463
|
....
gi 21356947 414 DEDD 417
Cdd:PRK12582 464 DPDD 467
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
52-521 |
1.03e-21 |
|
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: 98.12 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKII 131
Cdd:cd17646 20 EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 132 FTDADHYDKLYSatsafkpeiilttGTKDGVLSIQDLLAPTKTeffyqPTPLKEGPSQTVAILTSSGTTGMPKAVC---- 207
Cdd:cd17646 100 LTTADLAARLPA-------------GGDVALLGDEALAAPPAT-----PPLVPPRPDNLAYVIYTSGSTGRPKGVMvtha 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 208 -ISNDILTQETVF-VNGYDTIFISASLDWITGLWAtIFSTVNGCTRIISSKPFA---ADYFVYLVSKYSITYALIPPehc 282
Cdd:cd17646 162 gIVNRLLWMQDEYpLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARLVVARPGGhrdPAYLAALIREHGVTTCHFVP--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 283 cSLLD--CPTATPEKLGSLTKLNFGGGRMTQATVERVKKLaPNGVLNSSYGMTEVgfiVFNHGHLKLTAA--------GN 352
Cdd:cd17646 238 -SMLRvfLAEPAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEA---AIDVTHWPVRGPaetpsvpiGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 353 PLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKA--MQDeegWF-------HTGDMGYFDED---DYLY 420
Cdd:cd17646 313 PVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAErfVPD---PFgpgsrmyRTGDLARWRPDgalEFLG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 421 MTDrkkEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIgVYDETQGD--VPGALVVREDNATLTAQQVIDHVAKRLPDiqK 498
Cdd:cd17646 390 RSD---DQVKIRGFRVEPGEIEAALAAHPAVTHAVVV-ARAAPAGAarLVGYVVPAAGAAGPDTAALRAHLAERLPE--Y 463
|
490 500
....*....|....*....|...
gi 21356947 499 QLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd17646 464 MVPAAFVVLDALPLTANGKLDRA 486
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
351-529 |
1.13e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 98.54 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMqDEEGWFHTGDMGYFdEDDYLYMTDRKKEVLK 430
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYL-LDGYLYITGRAKDLII 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 431 WKGLQMWPAEVEAVIDELPEVKR--VCVIGVYDETqGDVPGALVVREDNATLTAQQVIDHVAKRLpdiqkQLRAGVQFAD 508
Cdd:PRK09192 466 INGRNIWPQDIEWIAEQEPELRSgdAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALV-----RSEFGVEAAV 539
|
170 180
....*....|....*....|....*..
gi 21356947 509 E------IPQNHNGKVVRRYARDLFVA 529
Cdd:PRK09192 540 ElvpphsLPRTSSGKLSRAKAKKRYLS 566
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
175-518 |
1.24e-21 |
|
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: 97.78 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 175 EFFYQPTPLKEGPSQ-TVAI-LTSSGTTGMPKAVCISND-------------ILTQETVF--VNGYDTIFISASLDWITG 237
Cdd:cd05920 124 GFDHRALARELAESIpEVALfLLSGGTTGTPKLIPRTHNdyaynvrasaevcGLDQDTVYlaVLPAAHNFPLACPGVLGT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 238 LWAtifstvnGCTRIISSKPFAADYFVyLVSKYSITY-ALIPPehCCSL-LDCPTATPEKLGSLTKLNFGGGRMTQATVE 315
Cdd:cd05920 204 LLA-------GGRVVLAPDPSPDAAFP-LIEREGVTVtALVPA--LVSLwLDAAASRRADLSSLRLLQVGGARLSPALAR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 316 RVKKlAPNGVLNSSYGMTEvGFIVFNH----GHLKLTAAGNPL-PGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFA 390
Cdd:cd05920 274 RVPP-VLGCTLQQVFGMAE-GLLNYTRlddpDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 391 DPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGA 470
Cdd:cd05920 352 APEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 21356947 471 LVVREDNAtLTAQQVIDHVAKR------LPDiqkqlraGVQFADEIPQNHNGKV 518
Cdd:cd05920 432 FVVLRDPP-PSAAQLRRFLRERglaaykLPD-------RIEFVDSLPLTAVGKI 477
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
56-417 |
1.37e-21 |
|
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: 98.27 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 56 VTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPIL-----EESTLKHLYNISKPKI 130
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqDLAKLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 131 IFT-DADHYDKLYSATSAFKPEIILTTGTKDG--VLSIQDLLAPTKT----EFFYQPTPlkegpsQTVA-ILTSSGTTGM 202
Cdd:cd05921 106 VFAqDAAPFARALAAIFPLGTPLVVSRNAVAGrgAISFAELAATPPTaavdAAFAAVGP------DTVAkFLFTSGSTGL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 203 PKAVCISNDILTQETVFVNGYDTIF---ISASLDWITglWATIFST--------VNGCTRIISS-KPFAADYFVYLVSKY 270
Cdd:cd05921 180 PKAVINTQRMLCANQAMLEQTYPFFgeePPVLVDWLP--WNHTFGGnhnfnlvlYNGGTLYIDDgKPMPGGFEETLRNLR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 271 SIT---YALIPPEH---CCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGV-----LNSSYGMTEVG-FI 338
Cdd:cd05921 258 EISptvYFNVPAGWemlVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVATVgeripMMAGLGATETApTA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 339 VFNHGhlKLTAAGN---PLPGIQVKIVDDDGNQlgvnqtgEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYF-D 414
Cdd:cd05921 338 TFTHW--PTERSGLiglPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLaD 408
|
...
gi 21356947 415 EDD 417
Cdd:cd05921 409 PDD 411
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
178-459 |
1.48e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 98.05 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 178 YQPTPLKegPSQTVAILTSSGTTGMPKAVCISNDILTqetvfvngydtifisASLDWITGLWA--------------TIF 243
Cdd:PRK09274 166 FPMADLA--PDDMAAILFTSGSTGTPKGVVYTHGMFE---------------AQIEALREDYGiepgeidlptfplfALF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 244 STVNGCTRII----SSKPFAAD--YFVYLVSKYSITY-----ALIPPehccsLLDCPTATPEKLGSLTKLNFGGGRMTQA 312
Cdd:PRK09274 229 GPALGMTSVIpdmdPTRPATVDpaKLFAAIERYGVTNlfgspALLER-----LGRYGEANGIKLPSLRRVISAGAPVPIA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 313 TVERVKKLAPNGV-LNSSYGMTEVGFIVFNHGHLKLTAA------------GNPLPGIQVKIVD---------DDGNQLG 370
Cdd:PRK09274 304 VIERFRAMLPPDAeILTPYGATEALPISSIESREILFATraatdngagicvGRPVDGVEVRIIAisdapipewDDALRLA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 371 VNQTGEIIVHNGFSWNGYFADPEATKA--MQDEEG--WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVID 446
Cdd:PRK09274 384 TGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFN 463
|
330
....*....|...
gi 21356947 447 ELPEVKRVCVIGV 459
Cdd:PRK09274 464 THPGVKRSALVGV 476
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
41-521 |
2.16e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 97.37 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 41 WPKNVCQISDSEGVEVTFGQALTWAIriAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLK 120
Cdd:PRK13383 48 WPGRTAIIDDDGALSYRELQRATESL--ARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 121 HLYNISKPKIIFTDADHYDKLysatsafkpeiiltTGTKDGVLSIqDLLAPTKTEFFYQPtplKEGPSQTVAILTSsGTT 200
Cdd:PRK13383 126 AALRAHHISTVVADNEFAERI--------------AGADDAVAVI-DPATAGAEESGGRP---AVAAPGRIVLLTS-GTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 201 GMPKAVCISNDILTQETVFVNGYDTIF------ISASLDWITGL-WATIFSTVNGCTRIISSKPFAADYFVYLVSKYSIT 273
Cdd:PRK13383 187 GKPKGVPRAPQLRSAVGVWVTILDRTRlrtgsrISVAMPMFHGLgLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRAD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 274 YALIPPEHCCSLLDCPTATPEK--LGSLTKLNFGGGRMTQATVERVKKlAPNGVLNSSYGMTEVGFivfnhGHLKLTA-- 349
Cdd:PRK13383 267 AFTAVPVVLARILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMD-TYGDILYNGYGSTEVGI-----GALATPAdl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 350 ------AGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADpeATKAMQDeeGWFHTGDMGYFDEDDYLYMTD 423
Cdd:PRK13383 341 rdapetVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVD--GMTSTGDMGYLDNAGRLFIVG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 424 RKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIQkQLRaG 503
Cdd:PRK13383 417 REDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFE-QPR-D 494
|
490
....*....|....*...
gi 21356947 504 VQFADEIPQNHNGKVVRR 521
Cdd:PRK13383 495 INIVSSIPRNPTGKVLRK 512
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
160-526 |
3.45e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 96.89 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 160 DGVLSIQDLLAPTKTEFFYQPTPLKEGpsqtvAILT-SSGTTGMPK-AVCISNDILTQetvFVNGY-------DTIF-IS 229
Cdd:PRK04319 181 PGTLDFNALMEQASDEFDIEWTDREDG-----AILHyTSGSTGKPKgVLHVHNAMLQH---YQTGKyvldlheDDVYwCT 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 230 ASLDWITGLWATIFST-VNGCTRIISSKPFAADYFVYLVSKYSIT--YAlippehccslldCPTATpeklgsltklnfgg 306
Cdd:PRK04319 253 ADPGWVTGTSYGIFAPwLNGATNVIDGGRFSPERWYRILEDYKVTvwYT------------APTAI-------------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 307 gRM-TQATVERVKK---------------LAPNGV----------LNSSYGMTEVGFIV---FNHGHLKLTAAGNPLPGI 357
Cdd:PRK04319 307 -RMlMGAGDDLVKKydlsslrhilsvgepLNPEVVrwgmkvfglpIHDNWWMTETGGIMianYPAMDIKPGSMGKPLPGI 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 358 QVKIVDDDGNQLGVNQTGEI------------IVHNGFSWNGYFADpeatkamqdeeGWFHTGDMGYFDEDDYLYMTDRK 425
Cdd:PRK04319 386 EAAIVDDQGNELPPNRMGNLaikkgwpsmmrgIWNNPEKYESYFAG-----------DWYVSGDSAYMDEDGYFWFQGRV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 426 KEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQ---QVIDHVAKRLPdiqkqlrA 502
Cdd:PRK04319 455 DDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLG-------A 527
|
410 420 430
....*....|....*....|....*....|.
gi 21356947 503 GV-----QFADEIPQNHNGKVVRRY--ARDL 526
Cdd:PRK04319 528 HAapreiEFKDKLPKTRSGKIMRRVlkAWEL 558
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
50-520 |
7.21e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 95.73 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 50 DSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHG---------TPFQSANPILEestlk 120
Cdd:PRK04813 22 DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvdvsSPAERIEMIIE----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 121 hlynISKPKIIFtdadhydklysATSAFKPEIiltTGTKdgVLSIQDLlaptKTEFFYQPTPLKEGPSQ---TVAILTSS 197
Cdd:PRK04813 97 ----VAKPSLII-----------ATEELPLEI---LGIP--VITLDEL----KDIFATGNPYDFDHAVKgddNYYIIFTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 198 GTTGMPKAVCISNDILTQetvFVNgydtifisasldWITGLwatiFSTVNGcTRIISSKPFAADYFV------------- 264
Cdd:PRK04813 153 GTTGKPKGVQISHDNLVS---FTN------------WMLED----FALPEG-PQFLNQAPYSFDLSVmdlyptlasggtl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 265 YLVSKYSIT-----YALIP----------P---EHCcsLLDcPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVL 326
Cdd:PRK04813 213 VALPKDMTAnfkqlFETLPqlpinvwvstPsfaDMC--LLD-PSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 327 NSSYGMTEVGFIVfnhGHLKLT----AAGNPLP------GIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATK 396
Cdd:PRK04813 290 YNTYGPTEATVAV---TSIEITdemlDQYKRLPigyakpDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 397 A---MQDEEGWFHTGDMGYFDeDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVV 473
Cdd:PRK04813 367 EaffTFDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 474 -----REDNATLTaQQVIDHVAKRLPDI---QKQLragvqFADEIPQNHNGKVVR 520
Cdd:PRK04813 446 pkeedFEREFELT-KAIKKELKERLMEYmipRKFI-----YRDSLPLTPNGKIDR 494
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
55-526 |
9.93e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 95.34 E-value: 9.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 55 EVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACF-FHGTPFqSANPILEESTLKHLYNISKPKIIFT 133
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFkARAVPV-NVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 134 DADHYDK---LYSATSAFKPEIILTTGTKD----GVLSIQDLLAPTKTEffyqpTPLKEGPSQTVAILTSSGTTGMPKAV 206
Cdd:PRK07798 107 EREFAPRvaeVLPRLPKLRTLVVVEDGSGNdllpGAVDYEDALAAGSPE-----RDFGERSPDDLYLLYTGGTTGMPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 207 cisndILTQETVFV---NGYD-----------------------TIFISASLDWITGLWATIFSTVNGCTRIISSKP-FA 259
Cdd:PRK07798 182 -----MWRQEDIFRvllGGRDfatgepiedeeelakraaagpgmRRFPAPPLMHGAGQWAAFAALFSGQTVVLLPDVrFD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 260 ADYFVYLVSKYSITYALI-------PpehccsLLDC-PTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYG 331
Cdd:PRK07798 257 ADEVWRTIEREKVNVITIvgdamarP------LLDAlEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 332 MTEVGFIVFNHGHLKLTAAGNPL--PGIQVKIVDDDGNQL--GVNQTGeIIVHNGFSWNGYFADPEATKAM---QDEEGW 404
Cdd:PRK07798 331 SSETGFGGSGTVAKGAVHTGGPRftIGPRTVVLDEDGNPVepGSGEIG-WIARRGHIPLGYYKDPEKTAETfptIDGVRY 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 405 FHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQ 484
Cdd:PRK07798 410 AIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21356947 485 VIDHVAKRLpdiqkqlrAG------VQFADEIPQNHNGKVVRRYARDL 526
Cdd:PRK07798 490 LRAHCRSSL--------AGykvpraIWFVDEVQRSPAGKADYRWAKEQ 529
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
167-521 |
1.17e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 95.13 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 167 DLLAPTKTEFFYQPTPlkeGPSQTVAILTSSGTTGMPKAVcisndILTQETVFVNGY-----------DTIFISASL--- 232
Cdd:PRK07867 134 DELAAHRDAEPPFRVA---DPDDLFMLIFTSGTSGDPKAV-----RCTHRKVASAGVmlaqrfglgpdDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 233 -----DWITGLWAtifstvnGCTRIISSKpFAADYFVYLVSKYSITYALIPPEHCCSLLdcptATPEKLG----SLTKL- 302
Cdd:PRK07867 206 navmaGWAVALAA-------GASIALRRK-FSASGFLPDVRRYGATYANYVGKPLSYVL----ATPERPDdadnPLRIVy 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 303 -NFGGGRMTQATVERVKKLAPNGvlnssYGMTEVGFIVFNHGHLKLTAAGNPLPGIQV-----------KIVDDDGNQLG 370
Cdd:PRK07867 274 gNEGAPGDIARFARRFGCVVVDG-----FGSTEGGVAITRTPDTPPGALGPLPPGVAIvdpdtgtecppAEDADGRLLNA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 371 VNQTGEIIVHNGFSW-NGYFADPEATKA-MQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDEL 448
Cdd:PRK07867 349 DEAIGELVNTAGPGGfEGYYNDPEADAErMRG--GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRY 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356947 449 PEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRlPDI-QKQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:PRK07867 427 PDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQ-PDLgPKQWPSYVRVCAELPRTATFKVLKR 499
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
193-527 |
1.77e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 92.80 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVCISNDILTqetvfvngydtifisASLD-----------W--------ITGLWATIFSTVNGCTRII 253
Cdd:PRK07824 40 VVATSGTTGTPKGAMLTAAALT---------------ASADathdrlggpgqWllalpahhIAGLQVLVRSVIAGSEPVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 254 S--SKPFAADYFVYLVSKYSI--TYALIPPEHCCSLLDCPTATpEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVlnSS 329
Cdd:PRK07824 105 LdvSAGFDPTALPRAVAELGGgrRYTSLVPMQLAKALDDPAAT-AALAELDAVLVGGGPAPAPVLDAAAAAGINVV--RT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEV-GFIVFNhghlkltaaGNPLPGIQVKIVDddgnqlgvnqtGEIIVHNGFSWNGYfADPEATKAMQdEEGWFHTG 408
Cdd:PRK07824 182 YGMSETsGGCVYD---------GVPLDGVRVRVED-----------GRIALGGPTLAKGY-RNPVDPDPFA-EPGWFRTD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 409 DMGYFDeDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDH 488
Cdd:PRK07824 240 DLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAH 318
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21356947 489 VAKRLPDIQ--KQLRagvqFADEIPQNHNGKVVRRYARDLF 527
Cdd:PRK07824 319 VARTLDRTAapRELH----VVDELPRRGIGKVDRRALVRRF 355
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
345-526 |
1.88e-20 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 94.94 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 345 LKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNgfSWNGY----FADPEATKA--MQDEEGWFHTGDMGYFDEDDY 418
Cdd:cd05966 407 LKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKR--PWPGMartiYGDHERYEDtyFSKFPGYYFTGDGARRDEDGY 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 419 LYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLT---AQQVIDHVAKRL-- 493
Cdd:cd05966 485 YWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIgp 564
|
170 180 190
....*....|....*....|....*....|....*.
gi 21356947 494 ---PDIqkqlragVQFADEIPQNHNGKVVRRYARDL 526
Cdd:cd05966 565 iatPDK-------IQFVPGLPKTRSGKIMRRILRKI 593
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
179-521 |
1.94e-20 |
|
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: 94.26 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 179 QPTPLKEGPSQTVAILTSSGTTGMPKAVCISND-----ILTQETVF-VNGYDTIFISASLDW------ITGLWATifstv 246
Cdd:cd12114 117 PPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRaalntILDINRRFaVGPDDRVLALSSLSFdlsvydIFGALSA----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 247 nGCTRIISSKPFAAD--YFVYLVSKYSITY-----ALIPpehccSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKK 319
Cdd:cd12114 192 -GATLVLPDEARRRDpaHWAELIERHGVTLwnsvpALLE-----MLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 320 LAPNGVLNSSYGMTEVGF------IVFNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEI-IVHNGFSwNGYFADP 392
Cdd:cd12114 266 LAPDARLISLGGATEASIwsiyhpIDEVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELwIGGRGVA-LGYLGDP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 393 EATKA----MQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVP 468
Cdd:cd12114 345 ELTAArfvtHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLA 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21356947 469 GALVVREDNATLTAQQVIDHVAKRLPDIQKQLRagVQFADEIPQNHNGKVVRR 521
Cdd:cd12114 425 AFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSR--VIALEALPLTANGKVDRA 475
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
50-526 |
2.59e-20 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 93.94 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 50 DSEGVEVTFGQALTWAIRIAQQLKsRGLDHKDIIGIsarnttyIMPTAVACF--FHGTPFQSANPIL-----EESTLKHL 122
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALARKLA-KMTKEGENVGV-------MLPPSAGGAlaNFALALSGKVPVMlnytaGLRELRAC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 123 YNISKPKIIFTDADHYDKL---YSATSAFKPEIIL------TTGTKDGVLSIQDLLAPTKTEFFYQPTPLKEgPSQTVAI 193
Cdd:cd05909 74 IKLAGIKTVLTSKQFIEKLklhHLFDVEYDARIVYledlraKISKADKCKAFLAGKFPPKWLLRIFGVAPVQ-PDDPAVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 194 LTSSGTTGMPKAVCISN-DILTQE----TVFVNGYDTIFISA-----SLDWITGLWATIFStvnGCTRIISSKPFAADYF 263
Cdd:cd05909 153 LFTSGSEGLPKGVVLSHkNLLANVeqitAIFDPNPEDVVFGAlpffhSFGLTGCLWLPLLS---GIKVVFHPNPLDYKKI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 264 VYLVSKYSITYalippehccsLLDCPT--------ATPEKLGSLTKLNFGGGRMTQATVERVKKLApnGV-LNSSYGMTE 334
Cdd:cd05909 230 PELIYDKKATI----------LLGTPTflrgyaraAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF--GIrILEGYGTTE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 335 VGFIV--------FNHGhlkltAAGNPLPGIQVKIVD-DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQdEEGWF 405
Cdd:cd05909 298 CSPVIsvntpqspNKEG-----TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 406 HTGDMGYFDEDDYLYMTDRKKEVLKWKGlQMWPAE-VEAVIDE-LPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQ 483
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGRLSRFAKIAG-EMVSLEaIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLN 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 21356947 484 QVIDHVAkrLPDIQKQlrAGVQFADEIPQNHNGKVVRRYARDL 526
Cdd:cd05909 451 DILKNAG--ISNLAKP--SYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
183-521 |
3.11e-20 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 93.20 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 183 LKEGPSQTVAILTSSGTTGMPKAVCISNDILTQETVFVNGY------DTI--FISASLD-----WITGLwatifstVNGC 249
Cdd:cd17649 89 LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERygltpgDRElqFASFNFDgaheqLLPPL-------ICGA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 250 TRIISSKPFA--ADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKL-GSLTKLNFGGGRMtqaTVERVKKLAPNGV- 325
Cdd:cd17649 162 CVVLRPDELWasADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRpPSLRLYIFGGEAL---SPELLRRWLKAPVr 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 326 LNSSYGMTE--VGFIVFnHGHLKLTAA------GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKA 397
Cdd:cd17649 239 LFNAYGPTEatVTPLVW-KCEAGAARAgasmpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 398 --MQD---EEG--WFHTGDMGYFDED---DYLYMTDRKkevLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDV 467
Cdd:cd17649 318 rfVPDpfgAPGsrLYRTGDLARWRDDgviEYLGRVDHQ---VKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 468 PGALVVREDNA-TLTAQQVIDHVAKRLPDiqKQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd17649 395 VAYVVLRAAAAqPELRAQLRTALRASLPD--YMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
26-520 |
5.68e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 93.15 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 26 PETSLGRIIfKNMRNWPKNVCqISDSEGV-EVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARN--TTYImpTAVACFF 102
Cdd:PRK05857 13 PSTVLDRVF-EQARQQPEAIA-LRRCDGTsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNgpETYL--SVLACAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 103 HGTPFQSANPILEESTLKHLYNISKPKIIF------TDADHYDKLYSATSAFKPEIILTTGTKDGVLSIQdllaptktef 176
Cdd:PRK05857 89 LGAIAVMADGNLPIAAIERFCQITDPAAALvapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAA---------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 177 fYQPTPLKEGPSQTVAILTSSGTTGMPKAVCISN-------DILTQETV----FVNGyDTIFISASLDWITGLWATIFST 245
Cdd:PRK05857 159 -SLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANrtffavpDILQKEGLnwvtWVVG-ETTYSPLPATHIGGLWWILTCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 246 VNGCTrIISSKPFAADYFVYLVSKYSITYALIP---PEHCCSLLDCPTATPeklgSLTKLNFGGGRMTQATVERVKKlap 322
Cdd:PRK05857 237 MHGGL-CVTGGENTTSLLEILTTNAVATTCLVPtllSKLVSELKSANATVP----SLRLVGYGGSRAIAADVRFIEA--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 323 NGVLNSS-YGMTEVGFIVF-------NHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHnGFSWN-------G 387
Cdd:PRK05857 309 TGVRTAQvYGLSETGCTALclptddgSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSASF-GTLWIkspanmlG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 388 YFADPEATKAMQdEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDV 467
Cdd:PRK05857 388 YWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAL 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 21356947 468 PG-ALVVREDNATLTAQQVIDHVAKRLPDIQKQLR--AGVQFADEIPQNHNGKVVR 520
Cdd:PRK05857 467 VGlAVVASAELDESAARALKHTIAARFRRESEPMArpSTIVIVTDIPRTQSGKVMR 522
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
57-528 |
7.19e-20 |
|
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: 92.94 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 57 TFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVAC---------FFHGTPFQSANPILEESTLKHLYN--- 124
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVariggivvpIFSGFGKEAAATRLQDAEAKALITadg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 125 -ISKPKIIfTDADHYDKLYSATSAFKPEIILTTGTKDGVLSIQDLLAPTKTEFFYQPTPLKEGPSQTVAILTSSGTTGMP 203
Cdd:cd05968 173 fTRRGREV-NLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 204 KAvCI----------SNDILTQETVfVNGyDTIFISASLDWITGLWATIFSTVNGCTRII----SSKPfAADYFVYLVSK 269
Cdd:cd05968 252 KG-TVhvhagfplkaAQDMYFQFDL-KPG-DLLTWFTDLGWMMGPWLIFGGLILGATMVLydgaPDHP-KADRLWRMVED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 270 YSITYALIPPEHCCSLLDCPTAtPEKLGSLTKLNFGGGRMTQATVE------RVKKLAPNGVLNSSyGMTEV-GFIVFNH 342
Cdd:cd05968 328 HEITHLGLSPTLIRALKPRGDA-PVNAHDLSSLRVLGSTGEPWNPEpwnwlfETVGKGRNPIINYS-GGTEIsGGILGNV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 343 --GHLKLTAAGNPLPGIQVKIVDDDGNQLgVNQTGEIIVHNgfSW----NGYFADPE---ATKAMQDEEGWFHtGDMGYF 413
Cdd:cd05968 406 liKPIKPSSFNGPVPGMKADVLDESGKPA-RPEVGELVLLA--PWpgmtRGFWRDEDrylETYWSRFDNVWVH-GDFAYY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 414 DEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTA-------QQVI 486
Cdd:cd05968 482 DEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalaeelmERVA 561
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 21356947 487 DHVAKRL-PDiqkqlraGVQFADEIPQNHNGKVVRRYARDLFV 528
Cdd:cd05968 562 DELGKPLsPE-------RILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
21-530 |
8.08e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 92.77 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 21 NNPFKPETSLGR----------IIFKNMR-NWPknvcqisdsegvevtfgQALTWAIRIAQQLKSRGLDHKDIIGISARN 89
Cdd:PLN03102 11 NVPLTPITFLKRasecypnrtsIIYGKTRfTWP-----------------QTYDRCCRLAASLISLNITKNDVVSVLAPN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 90 TTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDadhydklysatSAFKP---EIILTTGTKDG----- 161
Cdd:PLN03102 74 TPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD-----------RSFEPlarEVLHLLSSEDSnlnlp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 162 VLSIQDLLAPTKT---EFFYQ-------PTPLK-------EGPSQTVAILTSSGTTGMPKAVCISNdiltqetvfvNGYD 224
Cdd:PLN03102 143 VIFIHEIDFPKRPsseELDYEcliqrgePTPSLvarmfriQDEHDPISLNYTSGTTADPKGVVISH----------RGAY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 225 TIFISASLDWITG-----LWATIFSTVNG---------------CTRIISSKPFAADyfvylVSKYSITYALIPPEHCCS 284
Cdd:PLN03102 213 LSTLSAIIGWEMGtcpvyLWTLPMFHCNGwtftwgtaarggtsvCMRHVTAPEIYKN-----IEMHNVTHMCCVPTVFNI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 285 LLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNgvLNSSYGMTE-VGFIVF-----------NHGHLKLTAAGN 352
Cdd:PLN03102 288 LLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQ--VMHAYGLTEaTGPVLFcewqdewnrlpENQQMELKARQG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 353 ----PLPGIQVK------IVDDDGNQLGvnqtgEIIVHNGFSWNGYFADPEAT-KAMQdeEGWFHTGDMGYFDEDDYLYM 421
Cdd:PLN03102 366 vsilGLADVDVKnketqeSVPRDGKTMG-----EIVIKGSSIMKGYLKNPKATsEAFK--HGWLNTGDVGVIHPDGHVEI 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 422 TDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATlTAQQVIDHVAKRLPDIQKQLR 501
Cdd:PLN03102 439 KDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGET-TKEDRVDKLVTRERDLIEYCR 517
|
570 580 590
....*....|....*....|....*....|....*...
gi 21356947 502 AG---------VQFADEIPQNHNGKVVRRYARDLFVAL 530
Cdd:PLN03102 518 ENlphfmcprkVVFLQELPKNGNGKILKPKLRDIAKGL 555
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
183-473 |
1.17e-19 |
|
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: 91.65 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 183 LKEGPSQTVAILTSSGTTGMPKAVCISNDILTQETVFVN-----GYDTIFISasldwITGLW------ATIFSTVNGCTR 251
Cdd:cd17640 83 VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSdivppQPGDRFLS-----ILPIWhsyersAEYFIFACGCSQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 252 IISSKPFAADYF-----VYLVSK---YSITYALIPPEHCCSlldcpTATPEKLG----SLTKLNF---GGGRMTQaTVER 316
Cdd:cd17640 158 AYTSIRTLKDDLkrvkpHYIVSVprlWESLYSGIQKQVSKS-----SPIKQFLFlfflSGGIFKFgisGGGALPP-HVDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 317 VKKLAPNGVLNSsYGMTEVGFIVF--NHGHLKLTAAGNPLPGIQVKIVDDDGNQ-LGVNQTGEIIVHNGFSWNGYFADPE 393
Cdd:cd17640 232 FFEAIGIEVLNG-YGLTETSPVVSarRLKCNVRGSVGRPLPGTEIKIVDPEGNVvLPPGEKGIVWVRGPQVMKGYYKNPE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 394 ATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKE--VLKwKGLQMWPAEVEAVIDELPEVKRVCVIGvYDETQgdvPGAL 471
Cdd:cd17640 311 ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG-QDQKR---LGAL 385
|
..
gi 21356947 472 VV 473
Cdd:cd17640 386 IV 387
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
56-524 |
1.34e-19 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 92.40 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 56 VTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDA 135
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 136 DHYDKLYSATsAFKPEIILTTGTKDGvlsiqdllaPTKteffYQPTplkEGPSQTVAILTSsGTTGMPKAVCISN----- 210
Cdd:PRK06060 111 ALRDRFQPSR-VAEAAELMSEAARVA---------PGG----YEPM---GGDALAYATYTS-GTTGPPKAAIHRHadplt 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 211 --DILTQETVFVNGYDTIFISASLDWITGLWATI-FSTVNGCTRIISSKPFAADYFVYLVSKY--SITYALipPEHCCSL 285
Cdd:PRK06060 173 fvDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVwFPLATGGSAVINSAPVTPEAAAILSARFgpSVLYGV--PNFFARV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 286 LDcpTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVG--FIVFNHGHLKLTAAGNPLPGIQVKIVD 363
Cdd:PRK06060 251 ID--SCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGqtFVSNRVDEWRLGTLGRVLPPYEIRVVA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 364 DDGNQLGVNQTGEIIVHNGFSWNGYFADPEAtkaMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEA 443
Cdd:PRK06060 329 PDGTTAGPGVEGDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVER 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 444 VIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTaQQVIDHVAKRLPDIQKQLRAGVQFA--DEIPQNHNGKVVRR 521
Cdd:PRK06060 406 LIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATID-GSVMRDLHRGLLNRLSAFKVPHRFAvvDRLPRTPNGKLVRG 484
|
...
gi 21356947 522 YAR 524
Cdd:PRK06060 485 ALR 487
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
177-473 |
3.29e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 90.96 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 177 FYQPTPLKEgpSQTVAILTSSGTTGMPKAVCISND------ILTQETVFVNGYDTIFIS-ASLDWITGLWATIFSTVNGC 249
Cdd:PTZ00237 245 FYEYVPVES--SHPLYILYTSGTTGNSKAVVRSNGphlvglKYYWRSIIEKDIPTVVFShSSIGWVSFHGFLYGSLSLGN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 250 TRI-----ISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDC-PTATPEK----LGSLTKLNFGGGRMTQATVERVK- 318
Cdd:PTZ00237 323 TFVmfeggIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdPEATIIRskydLSNLKEIWCGGEVIEESIPEYIEn 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 319 --KLAPNGVlnssYGMTEVGFI-VFNHGHLKLT--AAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVH----NGFSWNGYF 389
Cdd:PTZ00237 403 klKIKSSRG----YGQTEIGITyLYCYGHINIPynATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmpPSFATTFYK 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 390 ADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPG 469
Cdd:PTZ00237 479 NDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPI 558
|
....
gi 21356947 470 ALVV 473
Cdd:PTZ00237 559 GLLV 562
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
130-521 |
3.56e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 90.86 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 130 IIFTDADHYDKLysATSAFKPEIILTTGTKDgvlsIQDLLAPTKTEffyqpTPLKE-GPSQTVAILTSSGTTGMPKAVCI 208
Cdd:PRK13388 102 LLVTDAEHRPLL--DGLDLPGVRVLDVDTPA----YAELVAAAGAL-----TPHREvDAMDPFMLIFTSGTTGAPKAVRC 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 209 SndiltQETVFVNGY-----------DTIFISASL---DWITGLWATIFstVNGCT----RIISSKPFAAD-------YF 263
Cdd:PRK13388 171 S-----HGRLAFAGRalterfgltrdDVCYVSMPLfhsNAVMAGWAPAV--ASGAAvalpAKFSASGFLDDvrrygatYF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 264 VYlVSKySITYALIPPEHccslldcptatPEKLGSLTKLNFGggrmTQATVERVKKLAPN-GV-LNSSYGMTEVGFIVFN 341
Cdd:PRK13388 244 NY-VGK-PLAYILATPER-----------PDDADNPLRVAFG----NEASPRDIAEFSRRfGCqVEDGYGSSEGAVIVVR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 342 HGHLKLTAAGNPLPGIQ-----------VKIVDDDGNQLGVNQT-GEIIVHNG---FSwnGYFADPEAT-KAMQDeeGWF 405
Cdd:PRK13388 307 EPGTPPGSIGRGAPGVAiynpetltecaVARFDAHGALLNADEAiGELVNTAGagfFE--GYYNNPEATaERMRH--GMY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 406 HTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGD-VPGALVVREDnATLTAQQ 484
Cdd:PRK13388 383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDqVMAALVLRDG-ATFDPDA 461
|
410 420 430
....*....|....*....|....*....|....*...
gi 21356947 485 VIDHVAKRlPDIQKQLRAG-VQFADEIPQNHNGKVVRR 521
Cdd:PRK13388 462 FAAFLAAQ-PDLGTKAWPRyVRIAADLPSTATNKVLKR 498
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
187-521 |
5.45e-19 |
|
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: 89.67 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISNDILT-----QETVF-VNGYD--TIFISASLDWitGLWATIFSTVNGCTRIISSKPF 258
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLalfaaTQRWFgFNEDDvwTLFHSYAFDF--SVWEIWGALLHGGRLVVVPYEV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 259 A--ADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVER--VKKLAPNGVLNSSYGMTE 334
Cdd:cd17643 170 ArsPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPwaGRFGLDRPQLVNMYGITE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 335 ----VGFIVFNHGHLKLTAA---GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPE--ATKAMQDEEG-- 403
Cdd:cd17643 250 ttvhVTFRPLDAADLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPEltAERFVANPFGgp 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 ---WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATL 480
Cdd:cd17643 330 gsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAA 409
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21356947 481 TAQQVIDHVAKRLPDiqKQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd17643 410 DIAELRALLKELLPD--YMVPARYVPLDALPLTVNGKLDRA 448
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
52-521 |
1.09e-18 |
|
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: 88.80 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTtyimPTAVACFF-------HGTPFQSANPileESTLKHLYN 124
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERS----PELVVALLavlkagaAYVPLDPELP---AERLAFMLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 125 ISKPKIIFTDAdhydklysaTSAFKPEIILTTGTKDGVLSIQDLLAPtkteffyqPTPLkeGPSQTVAILTSSGTTGMPK 204
Cdd:cd12117 92 DAGAKVLLTDR---------SLAGRAGGLEVAVVIDEALDAGPAGNP--------AVPV--SPDDLAYVMYTSGSTGRPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 AVCISN-DI--LTQETVFV--NGYDTIFISASLDWITG---LWATIfstVNGCTRIISSK--PFAADYFVYLVSKYSITY 274
Cdd:cd12117 153 GVAVTHrGVvrLVKNTNYVtlGPDDRVLQTSPLAFDAStfeIWGAL---LNGARLVLAPKgtLLDPDALGALIAEEGVTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 275 ALIppehccslldcpTAT---------PEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE---------VG 336
Cdd:cd12117 230 LWL------------TAAlfnqladedPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnttfttshvVT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 337 FIVFNHGHLKLtaaGNPLPGIQVKIVDDDGNQLGVNQTGEI-IVHNGFSwNGYFADPEATKA------MQDEEGWFHTGD 409
Cdd:cd12117 298 ELDEVAGSIPI---GRPIANTRVYVLDEDGRPVPPGVPGELyVGGDGLA-LGYLNRPALTAErfvadpFGPGERLYRTGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 410 MGYFDED---DYLYMTDRKkevLKWKGLQMWPAEVEAVIDELPEVKRVCVIgVYDETQGD---VpgALVVREdnATLTAQ 483
Cdd:cd12117 374 LARWLPDgrlEFLGRIDDQ---VKIRGFRIELGEIEAALRAHPGVREAVVV-VREDAGGDkrlV--AYVVAE--GALDAA 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 21356947 484 QVIDHVAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd12117 446 ELRAFLRERLPAY--MVPAAFVVLDELPLTANGKVDRR 481
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
57-532 |
3.97e-18 |
|
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: 87.02 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 57 TFGQALTWAIRIAQQLKSRGLDHKDIIGISARN---TTYIMPTAVACffhGTPFQSANPILEESTLKHLYNISKPKIIFT 133
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENrpeYVLLWLGLVKI---GAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 134 DADHYdklysatsafkpeiilttgtkdgvlsiqdllaptkteffyqptplkegpsqtvaILTSsGTTGMPKAVCISNDIL 213
Cdd:cd05940 82 DAALY------------------------------------------------------IYTS-GTTGLPKAAIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 214 TQETVFVNGY------DTIFISASLDWITGL---WATifSTVNGCTRIISSKpFAADYFVYLVSKYSITYALIPPEHCCS 284
Cdd:cd05940 107 WRGGAFFAGSggalpsDVLYTCLPLYHSTALivgWSA--CLASGATLVIRKK-FSASNFWDDIRKYQATIFQYIGELCRY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 285 LLDCPTATPEKLGSLTKLnFGGG-R-------MTQATVERVKKLapngvlnssYGMTE--VGFI-VFNhghlKLTAAG-N 352
Cdd:cd05940 184 LLNQPPKPTERKHKVRMI-FGNGlRpdiweefKERFGVPRIAEF---------YAATEgnSGFInFFG----KPGAIGrN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 353 PLPGIQV---KIV-----------DDDG--NQLGVNQTGEIIVHNGFSWN--GYFaDPEAT--KAMQD--EEG--WFHTG 408
Cdd:cd05940 250 PSLLRKVaplALVkydlesgepirDAEGrcIKVPRGEPGLLISRINPLEPfdGYT-DPAATekKILRDvfKKGdaWFNTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 409 DMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVydetqgDVPG--------ALVVREdNATL 480
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGV------QVPGtdgragmaAIVLQP-NEEF 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21356947 481 TAQQVIDHVAKRLPdiqkqlragvqfadeipqnhngkvvrRYARDLFVALSK 532
Cdd:cd05940 402 DLSALAAHLEKNLP--------------------------GYARPLFLRLQP 427
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-521 |
4.03e-18 |
|
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: 88.38 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGI----SARnttyiMPTAV-------ACFfhgTPFQSANP------IL 114
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVclerSLE-----MVVALlavlkagAAY---VPLDPAYPaerlayML 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 115 EEStlkhlynisKPKIIFTDADHYDKLysatSAFKPEIILTTGTKDGVLSIQDLLAPTkteffyqptplkeGPSQTVAIL 194
Cdd:COG1020 570 EDA---------GARLVLTQSALAARL----PELGVPVLALDALALAAEPATNPPVPV-------------TPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 195 TSSGTTGMPKAVCIS-----NDILTQETVF-VNGYDTI--FISASLDwiTGLWAtIFST-VNGCTRIISSKPFAAD--YF 263
Cdd:COG1020 624 YTSGSTGRPKGVMVEhralvNLLAWMQRRYgLGPGDRVlqFASLSFD--ASVWE-IFGAlLSGATLVLAPPEARRDpaAL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 264 VYLVSKYSITYALIPPEHCCSLLDcptATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE--VGFIVFN 341
Cdd:COG1020 701 AELLARHRVTVLNLTPSLLRALLD---AAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTEttVDSTYYE 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 342 HGHLKLTAA----GNPLPGIQVKIVDDDGNQLGVNQTGEIivhngfsW-------NGYFADPEATKA-------MQDEEG 403
Cdd:COG1020 778 VTPPDADGGsvpiGRPIANTRVYVLDAHLQPVPVGVPGEL-------YiggaglaRGYLNRPELTAErfvadpfGFPGAR 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 WFHTGDMGYFDED---DYLymtDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIgVYDETQGDVP-GALVVREDNAT 479
Cdd:COG1020 851 LYRTGDLARWLPDgnlEFL---GRADDQVKIRGFRIELGEIEAALLQHPGVREAVVV-AREDAPGDKRlVAYVVPEAGAA 926
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21356947 480 LTAQQVIDHVAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:COG1020 927 AAAALLRLALALLLPPY--MVPAAVVLLLPLPLTGNGKLDRL 966
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
332-526 |
4.56e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 87.50 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 332 MTEVGFIVFNH--G--HLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNgfSWNGY----FADPE-------ATk 396
Cdd:PRK00174 404 QTETGGIMITPlpGatPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKD--PWPGMmrtiYGDHErfvktyfST- 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 397 amqdEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVV--- 473
Cdd:PRK00174 481 ----FKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkg 556
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356947 474 -REDNATLtAQQVIDHVAKRL-----PDIqkqlragVQFADEIPQNHNGKVVRRYARDL 526
Cdd:PRK00174 557 gEEPSDEL-RKELRNWVRKEIgpiakPDV-------IQFAPGLPKTRSGKIMRRILRKI 607
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
186-521 |
6.97e-18 |
|
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: 86.22 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 186 GPSQTVAILTSSGTTGMPKAVCISNDILTQetvFVNGYDTIFisaSLDWITGLWAT-----------IFST--VNGCTRI 252
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAA---FLQWAAAAF---SAEELAGVLAStsicfdlsvfeLFGPlaTGGKVVL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 253 ISSkpfaadyfvylvskysityALIPPEH----CCSLLD-CPTATPEKL------GSLTKLNFGGGRMTQATVERVKKLA 321
Cdd:cd12115 177 ADN-------------------VLALPDLpaaaEVTLINtVPSAAAELLrhdalpASVRVVNLAGEPLPRDLVQRLYARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 322 PNGVLNSSYGMTEVG----FIVFNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKA 397
Cdd:cd12115 238 QVERVVNLYGPSEDTtystVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 398 ------MQDEEGWFHTGDMGYFDED---DYLYMTDRKkevLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVP 468
Cdd:cd12115 318 rflpdpFGPGARLYRTGDLVRWRPDgllEFLGRADNQ---VKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21356947 469 GALVVREDNATLTAQQVIDHVAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd12115 395 VAYIVAEPGAAGLVEDLRRHLGTRLPAY--MVPSRFVRLDALPLTPNGKIDRS 445
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
330-458 |
9.84e-18 |
|
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: 86.32 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVFNH--GHLKLTAAGNPLPGIQVKIvdddgnqlgvNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHT 407
Cdd:cd17641 355 YGQTELAGAYTVHrdGDVDPDTVGVPFPGTEVRI----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHT 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 21356947 408 GDMGYFDEDDYLYMTDRKKEVLKW-KGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:cd17641 425 GDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
440-517 |
1.26e-17 |
|
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: 77.20 E-value: 1.26e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356947 440 EVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFADEIPQNHNGK 517
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPY-AVPKE-VVFVDELPKTRSGK 76
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
330-484 |
1.28e-17 |
|
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: 85.73 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEV--GFIVFNHGHLKLTAAGNPLPGIQVKIVD-DDGNQL--GVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGW 404
Cdd:cd17639 281 YGLTETcaGGTVQDPGDLETGRVGPPLPCCEIKLVDwEEGGYStdKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 405 FHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAE-VEAVIDELPEVKRVCVIGVYDETQgdvPGALVV-REDNATLTA 482
Cdd:cd17639 361 FHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEkLESIYRSNPLVNNICVYADPDKSY---PVAIVVpNEKHLTKLA 437
|
..
gi 21356947 483 QQ 484
Cdd:cd17639 438 EK 439
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
192-525 |
1.28e-17 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 85.05 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 192 AILTSsGTTGMPKAVCISNDILTQETVFVNGYDTI--------FISASLDWITGlwaTIFSTV-NGCTRII--SSKPFAA 260
Cdd:cd17653 110 IIFTS-GSTGIPKGVMVPHRGVLNYVSQPPARLDVgpgsrvaqVLSIAFDACIG---EIFSTLcNGGTLVLadPSDPFAH 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 261 DyfvylvsKYSITYALIPPehccSLLDcpTATPEKLGSLTKLNFGGGRMTQATVERvkkLAPNGVLNSSYGMTEVGFIVF 340
Cdd:cd17653 186 V-------ARTVDALMSTP----SILS--TLSPQDFPNLKTIFLGGEAVPPSLLDR---WSPGRRLYNAYGPTECTISST 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 341 nHGHL---KLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT----KAMQDEEGW--FHTGDMG 411
Cdd:cd17653 250 -MTELlpgQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTaskfVPDPFWPGSrmYRTGDYG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 412 YFDEDDYLYMTDRKKEVLKWKGLQM-WPAEVEAVIDELPEVKRVCVIGVydetqGDVPGALVVREDNATLTAQQVIdhvA 490
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRInLEEIEEVVLQSQPEVTQAAAIVV-----NGRLVAFVTPETVDVDGLRSEL---A 400
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21356947 491 KRLPdiqkqlragvQFA--------DEIPQNHNGKVVRRYARD 525
Cdd:cd17653 401 KHLP----------SYAvpdriialDSFPLTANGKVDRKALRE 433
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
349-521 |
4.58e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 84.02 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 349 AAGNPL-PGIQVKIVD-DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDED-DYLYMTdRK 425
Cdd:PRK06164 350 GGGRPAsPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDgQFVYQT-RM 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 426 KEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVydETQGD-VPGALVVREDNATLTAQQVIDHVAKRLPDIqkQLRAGV 504
Cdd:PRK06164 429 GDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASPDEAGLMAACREALAGF--KVPARV 504
|
170
....*....|....*....
gi 21356947 505 QFADEIP--QNHNGKVVRR 521
Cdd:PRK06164 505 QVVEAFPvtESANGAKIQK 523
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
187-458 |
1.48e-16 |
|
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: 82.79 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISNDILTqetvfvngYDTIFISASLDW----------------------ITGLWATIFs 244
Cdd:cd05933 149 PNQCCTLIYTSGTTGMPKGVMLSHDNIT--------WTAKAASQHMDLrpatvgqesvvsylplshiaaqILDIWLPIK- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 245 tVNGCT----------------RIISSKPFAADYFVY------LVSKYSITYAL-----------------------IPP 279
Cdd:cd05933 220 -VGGQVyfaqpdalkgtlvktlREVRPTAFMGVPRVWekiqekMKAVGAKSGTLkrkiaswakgvgletnlklmggeSPS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 280 EHCCSLLDCPTATP--EKLG--SLTKLNFGGGRMTQATVERVkkLAPNGVLNSSYGMTEVG--FIVFNHGHLKLTAAGNP 353
Cdd:cd05933 299 PLFYRLAKKLVFKKvrKALGldRCQKFFTGAAPISRETLEFF--LSLNIPIMELYGMSETSgpHTISNPQAYRLLSCGKA 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 354 LPGIQVKIV--DDDGNqlgvnqtGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKW 431
Cdd:cd05933 377 LPGCKTKIHnpDADGI-------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIIT 449
|
330 340 350
....*....|....*....|....*....|
gi 21356947 432 KGLQM---WPAEvEAVIDELPEVKRVCVIG 458
Cdd:cd05933 450 AGGENvppVPIE-DAVKKELPIISNAMLIG 478
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
196-520 |
1.76e-16 |
|
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: 81.85 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 196 SSGTTGMPKAVcisndILTQETVFVNGYDTIF------------ISaSLDWITGLWATIFS--TVNGCTRIISSKPFAAD 261
Cdd:cd05974 93 TSGTTSKPKLV-----EHTHRSYPVGHLSTMYwiglkpgdvhwnIS-SPGWAKHAWSCFFApwNAGATVFLFNYARFDAK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 262 YFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKlgSLTKLNFGGGRMTQATVERVKKlAPNGVLNSSYGMTEVGFIVFN 341
Cdd:cd05974 167 RVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV--KLREVVGAGEPLNPEVIEQVRR-AWGLTIRDGYGQTETTALVGN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 342 H--GHLKLTAAGNPLPGIQVKIVDDDGNQLgvnQTGEIIVHNGFS-----WNGYFADPEATKAMQdEEGWFHTGDMGYFD 414
Cdd:cd05974 244 SpgQPVKAGSMGRPLPGYRVALLDPDGAPA---TEGEVALDLGDTrpvglMKGYAGDPDKTAHAM-RGGYYRTGDIAMRD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 415 EDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNAT---LTAQQVIDHVAK 491
Cdd:cd05974 320 EDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEpspETALEIFRFSRE 399
|
330 340
....*....|....*....|....*....
gi 21356947 492 RLPDIQKQLRagVQFAdEIPQNHNGKVVR 520
Cdd:cd05974 400 RLAPYKRIRR--LEFA-ELPKTISGKIRR 425
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
54-524 |
2.12e-16 |
|
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: 82.09 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 54 VEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNttyiMPTAVACFFhGTPFQSA-----NPILEESTLKHLYNISKP 128
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFN----HFRHLEAYF-AVPGMGAvlhtaNPRLSPKEIAYILNHAED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 129 KIIFTDADhYDKLYSATSAFKPEIILTTGTKDGVLSIQDLLAPTKTEFfyQPT-PLKEgpSQTVAILTSSGTTGMPK--- 204
Cdd:cd05915 98 KVLLFDPN-LLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEE--ADPvRVPE--RAACGMAYTTGTTGLPKgvv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 -----------AVCISNDILTQET-VFVNgydTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVylvsKYSI 272
Cdd:cd05915 173 yshralvlhslAASLVDGTALSEKdVVLP---VVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFD----GEGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 273 T-YALIPPehCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLnSSYGMTEVgfivFNHGHLKL-TAA 350
Cdd:cd05915 246 TfTAGVPT--VWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIARFERMGVEVR-QGYGLTET----SPVVVQNFvKSH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 GNPLP---GIQVKIVDD-----------DGNQLGVNQTGEII----VHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGY 412
Cdd:cd05915 319 LESLSeeeKLTLKAKTGlpiplvrlrvaDEEGRPVPKDGKALgevqLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 413 FDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALvVREDNATLTAQQVIDHVAKR 492
Cdd:cd05915 399 WDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRGEKPTPEELNEHLLKA 477
|
490 500 510
....*....|....*....|....*....|..
gi 21356947 493 LPDIqKQLRAGVQFADEIPQNHNGKVVRRYAR 524
Cdd:cd05915 478 GFAK-WQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
319-529 |
2.24e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 81.58 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 319 KLAPngvlnsSYGMTEV-GFIV------FNHGHlklTAAGNPLPGIQVKIVDddgnqlgvNQTGEIIVHNGFSWNGYFad 391
Cdd:PRK07445 256 RLAP------TYGMTETaSQIAtlkpddFLAGN---NSSGQVLPHAQITIPA--------NQTGNITIQAQSLALGYY-- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 392 PEAtkamQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGAL 471
Cdd:PRK07445 317 PQI----LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAI 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356947 472 VVrEDNATLTAQQVIDHVAKRL--PDIQKQ-LRagvqfADEIPQNHNGKVVRRYARDLFVA 529
Cdd:PRK07445 393 YV-PKDPSISLEELKTAIKDQLspFKQPKHwIP-----VPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
347-527 |
2.45e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 81.68 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 347 LTAAGNPLPGIQVKIVDDDGNQL---GVNQtGEIIVHNGFSWNGYF---ADPEAtkamqdeEGWFHTGDMGYFDEDDYLY 420
Cdd:PRK07008 355 LEKQGRVIYGVDMKIVGDDGRELpwdGKAF-GDLQVRGPWVIDRYFrgdASPLV-------DGWFPTGDVATIDADGFMQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 421 MTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDH----VAK-RLPD 495
Cdd:PRK07008 427 ITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFyegkVAKwWIPD 506
|
170 180 190
....*....|....*....|....*....|..
gi 21356947 496 iqkqlraGVQFADEIPQNHNGKVVRRYARDLF 527
Cdd:PRK07008 507 -------DVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
131-531 |
5.59e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 80.80 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 131 IFTDADHYDKLYSATSAfkPEIILTTGtKDGVLSIQDLLAPTKTEFFYQPTPLKEgpsqtVAILT-SSGTTGMPK----- 204
Cdd:PRK10946 132 LFSDDDFLNTLVAEHSS--LRVVLLLN-DDGEHSLDDAINHPAEDFTATPSPADE-----VAFFQlSGGSTGTPKliprt 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 205 ------AVCISNDI--LTQETVFVNGYDTI--FISASLDWITGLWAtifstvnGCTRIISSKPFAADYFVyLVSKYSITY 274
Cdd:PRK10946 204 hndyyySVRRSVEIcgFTPQTRYLCALPAAhnYPMSSPGALGVFLA-------GGTVVLAPDPSATLCFP-LIEKHQVNV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 275 -ALIPPehCCSLLDCPTATP---EKLGSLTKLNFGGGRMTQATVERVKKLApNGVLNSSYGMTEvGFIvfNHGHLK---- 346
Cdd:PRK10946 276 tALVPP--AVSLWLQAIAEGgsrAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMAE-GLV--NYTRLDdsde 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 347 --LTAAGNPL-PGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTD 423
Cdd:PRK10946 350 riFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVG 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 424 RKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGA-LVVREDnatLTAQQVIDH-----VAK-RLPDi 496
Cdd:PRK10946 430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAfLVVKEP---LKAVQLRRFlreqgIAEfKLPD- 505
|
410 420 430
....*....|....*....|....*....|....*
gi 21356947 497 qkqlRagVQFADEIPQNHNGKVVRRYARDLFVALS 531
Cdd:PRK10946 506 ----R--VECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-520 |
6.28e-16 |
|
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: 80.20 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 190 TVAILTSSGTTGMPKAVCISNDIL-TQETVFVNGYDtiFISASLDWITGLWATIFSTVNGCTRII----SSKPFAAD--Y 262
Cdd:cd05910 87 PAAILFTSGSTGTPKGVVYRHGTFaAQIDALRQLYG--IRPGEVDLATFPLFALFGPALGLTSVIpdmdPTRPARADpqK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 263 FVYLVSKYSITYALIPPehccSLLDCPTATPE----KLGSLTKLNFGGGRMTQATVERVKKLAPNGV-LNSSYGMTE--- 334
Cdd:cd05910 165 LVGAIRQYGVSIVFGSP----ALLERVARYCAqhgiTLPSLRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATEalp 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 335 VGFI----VF-NHGHL----KLTAAGNPLPGIQVKIVD---------DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATK 396
Cdd:cd05910 241 VSSIgsreLLaTTTAAtsggAGTCVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 397 AMQ----DEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVydETQGDVPGALV 472
Cdd:cd05910 321 LAKiddnSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKPGCQLPVLC 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 21356947 473 V--REDNATLTAQ--QVIDHVAKRLPDIQKQLRagVQFADEIPQN--HNGKVVR 520
Cdd:cd05910 399 VepLPGTITPRARleQELRALAKDYPHTQRIGR--FLIHPSFPVDirHNAKIFR 450
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
49-417 |
8.03e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 80.31 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 49 SDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPF---QSANPILEE--STLKHLY 123
Cdd:PRK08180 63 ADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYapvSPAYSLVSQdfGKLRHVL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 124 NISKPKIIF-TDADHYDKLYSATSAFKPEIILTTGTKDG--VLSIQDLLAPTKT----EFFYQPTPlkegpsQTVA-ILT 195
Cdd:PRK08180 143 ELLTPGLVFaDDGAAFARALAAVVPADVEVVAVRGAVPGraATPFAALLATPPTaavdAAHAAVGP------DTIAkFLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 196 SSGTTGMPKAVcisndILTQETVFVN--------GYDTIFISASLDWITglWATIFSTV--------NGCTRIISS-KPF 258
Cdd:PRK08180 217 TSGSTGLPKAV-----INTHRMLCANqqmlaqtfPFLAEEPPVLVDWLP--WNHTFGGNhnlgivlyNGGTLYIDDgKPT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 259 AA--DYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEK----LGSLTKLNFGGGRMTQATVERVKKLAPNGV-----LN 327
Cdd:PRK08180 290 PGgfDETLRNLREISPTVYFNVPKGWEMLVPALERDAALrrrfFSRLKLLFYAGAALSQDVWDRLDRVAEATCgerirMM 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 328 SSYGMTEVG-FIVFNHGHLklTAAGN---PLPGIQVKIVDDDGNQlgvnqtgEIIVH--NGFSwnGYFADPEATKAMQDE 401
Cdd:PRK08180 370 TGLGMTETApSATFTTGPL--SRAGNiglPAPGCEVKLVPVGGKL-------EVRVKgpNVTP--GYWRAPELTAEAFDE 438
|
410
....*....|....*..
gi 21356947 402 EGWFHTGDMGYF-DEDD 417
Cdd:PRK08180 439 EGYYRSGDAVRFvDPAD 455
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
181-534 |
1.12e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.98 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 181 TPLKEGPSQTVAILTSSGTTGMPKAVCISNDILT------QETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIIS 254
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGALAnyvcviAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 255 SKP--FAADYFVYLVSKYSITYALIPPEHCCSLLDCPtaTPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGM 332
Cdd:PRK12467 729 PPDcaRDAEAFAALMADQGVTVLKIVPSHLQALLQAS--RVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGP 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 333 TEVGfIVFNHGHLKLTAA-------GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADP--EATKAMQDEEG 403
Cdd:PRK12467 807 TETT-VGVSTYELSDEERdfgnvpiGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPalTAERFVPDPFG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 -----WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVyDETQGDVPGALVVREDNA 478
Cdd:PRK12467 886 adggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAYLVPAAVA 964
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356947 479 TLTAQQVIDHVAKR-----LPDiqKQLRAGVQFADEIPQNHNGKVVRRyARDLFVALSKKN 534
Cdd:PRK12467 965 DGAEHQATRDELKAqlrqvLPD--YMVPAHLLLLDSLPLTPNGKLDRK-ALPKPDASAVQA 1022
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
330-458 |
1.41e-15 |
|
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: 79.57 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVF--NHGHLKLTAAGNPLPGIQVKIVD-DDGNQL--GVNQTGEIIV--HNGFSwnGYFADPEATKAMQDEE 402
Cdd:cd05927 306 YGQTECTAGATltLPGDTSVGHVGGPLPCAEVKLVDvPEMNYDakDPNPRGEVCIrgPNVFS--GYYKDPEKTAEALDED 383
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356947 403 GWFHTGDMGYFDEDDYLYMTDRKKEVLKW-KGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:cd05927 384 GWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
362-526 |
3.66e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 78.07 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 362 VDDDGNQLGvnqtgEIIVHNGFSWNGYFADPEATK-AMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAE 440
Cdd:PRK08162 381 VPADGETIG-----EIMFRGNIVMKGYLKNPKATEeAFAG--GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 441 VEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqKQLRAgVQFAdEIPQNHNGK--- 517
Cdd:PRK08162 454 VEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGF-KVPKA-VVFG-ELPKTSTGKiqk 530
|
170
....*....|
gi 21356947 518 -VVRRYARDL 526
Cdd:PRK08162 531 fVLREQAKSL 540
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
179-521 |
7.77e-15 |
|
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: 76.52 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 179 QPTPLKEGPSQTVAILTSSGTTGMPKAV-----CISNDILTQETVFVNGYDTI---FISASLD-WITGLWATIFStvnGC 249
Cdd:cd17652 84 RPALLLTTPDNLAYVIYTSGSTGRPKGVvvthrGLANLAAAQIAAFDVGPGSRvlqFASPSFDaSVWELLMALLA---GA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 250 T-------RIISSKPFAAdyfvyLVSKYSITYALIPPehccSLLDcpTATPEKLGSLTKLNFGGgrmTQATVERVKKLAP 322
Cdd:cd17652 161 TlvlapaeELLPGEPLAD-----LLREHRITHVTLPP----AALA--ALPPDDLPDLRTLVVAG---EACPAELVDRWAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 323 NGVLNSSYGMTEVGFIVFNHGHLKLTAA---GNPLPGIQVKIVDDDGNQLGVNQTGEI-IVHNGFSwNGYFADPEATKAM 398
Cdd:cd17652 227 GRRMINAYGPTETTVCATMAGPLPGGGVppiGRPVPGTRVYVLDARLRPVPPGVPGELyIAGAGLA-RGYLNRPGLTAER 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 399 -------QDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIgVYDETQGD---Vp 468
Cdd:cd17652 306 fvadpfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV-VRDDRPGDkrlV- 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21356947 469 gALVVREDNATLTAQQVIDHVAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd17652 384 -AYVVPAPGAAPTAAELRAHLAERLPGY--MVPAAFVVLDALPLTPNGKLDRR 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
187-521 |
8.92e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.08 E-value: 8.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISNDILT------QETVFVNGYDTIFISASLDWITGLWATIFSTVNGcTRIISSKP--- 257
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSnrlcwmQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG-ARLVVAAPgdh 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 258 FAADYFVYLVSKYSITYALIPPEHCCSLLdcPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGF 337
Cdd:PRK12316 733 RDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 338 IVFNHGHLKLTAA----GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT------KAMQDEEGWFHT 407
Cdd:PRK12316 811 DVTHWTCVEEGGDsvpiGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTaerfvpSPFVAGERMYRT 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 408 GDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVydetQGDVPGALVVREDNATLTAQQVID 487
Cdd:PRK12316 891 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESEGGDWREALKA 966
|
330 340 350
....*....|....*....|....*....|....
gi 21356947 488 HVAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:PRK12316 967 HLAASLPEY--MVPAQWLALERLPLTPNGKLDRK 998
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
345-520 |
1.01e-14 |
|
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: 76.76 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 345 LKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGyFDEDDYLYMTDR 424
Cdd:cd05908 311 LTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 425 KKEVLKWKGLQMWPAEVEAVIDELPEVK--RVCVIGVYDETQGDvpgalvvREDNATLTAQQVIDHVAKRLPDIQKQL-- 500
Cdd:cd05908 390 EKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTRN-------EEIFCFIEHRKSEDDFYPLGKKIKKHLnk 462
|
170 180
....*....|....*....|....*
gi 21356947 501 RAGVQFAD-----EIPQNHNGKVVR 520
Cdd:cd05908 463 RGGWQINEvlpirRIPKTTSGKVKR 487
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
54-494 |
1.38e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.42 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 54 VEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNttyiMPTAVACFFhGTPFQSA-----NPILEESTLKHLYNISKP 128
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPN----IPAMYEAHF-GVPMAGAvvncvNIRLNAPTIAFLLEHSKS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 129 KII------FTDADHYDKLYS--ATSAFKPEIILTTGTKD------------GVLSIQDLLAPTKTEFFYQPtPLKEGps 188
Cdd:PLN02479 119 EVVmvdqefFTLAEEALKILAekKKSSFKPPLLIVIGDPTcdpkslqyalgkGAIEYEKFLETGDPEFAWKP-PADEW-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 189 QTVAILTSSGTTGMPKAVCISND---ILTQETVFVNGYDtifISASLDWITGL---------WA-TIFSTVNGCTRIISS 255
Cdd:PLN02479 196 QSIALGYTSGTTASPKGVVLHHRgayLMALSNALIWGMN---EGAVYLWTLPMfhcngwcftWTlAALCGTNICLRQVTA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 256 KPfaadyfVY-LVSKYSITYALIPPEHCCSLLDCPTA-------------------TPEKLGSLTKLNFgggRMTQaTVE 315
Cdd:PLN02479 273 KA------IYsAIANYGVTHFCAAPVVLNTIVNAPKSetilplprvvhvmtagaapPPSVLFAMSEKGF---RVTH-TYG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 316 RVKKLAPNGV-----------------LNSSYGMTEVGFIVFNHGHLKLTAagnPLPGiqvkivddDGNQLGvnqtgEII 378
Cdd:PLN02479 343 LSETYGPSTVcawkpewdslppeeqarLNARQGVRYIGLEGLDVVDTKTMK---PVPA--------DGKTMG-----EIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 379 VHNGFSWNGYFADPEATKAMQdEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:PLN02479 407 MRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21356947 459 VYDETQGDVPGALVV------REDNATLtAQQVIDHVAKRLP 494
Cdd:PLN02479 486 RPDERWGESPCAFVTlkpgvdKSDEAAL-AEDIMKFCRERLP 526
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
330-521 |
2.42e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 75.07 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVFNHGHLKLTAAGNPLPGIQVKIVDDDgnqlgvNQTGEIIVHNGfswngyfadpeatkamqDEEgwFHTGD 409
Cdd:PRK08308 243 YGCSEAGCVSICPDMKSHLDLGNPLPHVSVSAGSDE------NAPEEIVVKMG-----------------DKE--IFTKD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 410 MGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDnaTLTAQQVIDHV 489
Cdd:PRK08308 298 LGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQLREWC 375
|
170 180 190
....*....|....*....|....*....|..
gi 21356947 490 AKRLPdiQKQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:PRK08308 376 IQHLA--PYQVPHEIESVTEIPKNANGKVSRK 405
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
52-494 |
3.85e-14 |
|
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: 75.02 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKS-RGLDHKDIIGISARNTtyimPTAVACFFH----GTPFQSANPILEESTLKHLYNIS 126
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNE----PAFLWIWLGlaklGCPVAFLNTNIRSKSLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 127 KPKIIFTDADHYDKLYSATSAFKPEII----LTTGTK-DGVLSIQDLLAPTKTEffyqPTPlkEGPSQTVAILT------ 195
Cdd:cd05938 78 GAKVLVVAPELQEAVEEVLPALRADGVsvwyLSHTSNtEGVISLLDKVDAASDE----PVP--ASLRAHVTIKSpalyiy 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 196 SSGTTGMPKAVCISNDILTQETVF-----VNGYDTIFISASLDWITGLWATIFSTVN-GCTRIISSKpFAADYFVYLVSK 269
Cdd:cd05938 152 TSGTTGLPKAARISHLRVLQCSGFlslcgVTADDVIYITLPLYHSSGFLLGIGGCIElGATCVLKPK-FSASQFWDDCRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 270 YSITYALIPPEHCCSLLDCPTaTPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVlNSSYGMTE--VGFIVFNHghlKL 347
Cdd:cd05938 231 HNVTVIQYIGELLRYLCNQPQ-SPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRI-REFYGSTEgnIGFFNYTG---KI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 348 TAAGN---------PLPGIQVKIV------DDDGNQLGV--NQTGEII--VHNGFSWNGYFADPEAT--KAMQD--EEG- 403
Cdd:cd05938 306 GAVGRvsylykllfPFELIKFDVEkeepvrDAQGFCIPVakGEPGLLVakITQQSPFLGYAGDKEQTekKLLRDvfKKGd 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 -WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVydetqgDVPG-------ALVVRE 475
Cdd:cd05938 386 vYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV------TVPGhegrigmAAVKLK 459
|
490
....*....|....*....
gi 21356947 476 DNATLTAQQVIDHVAKRLP 494
Cdd:cd05938 460 PGHEFDGKKLYQHVREYLP 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
186-521 |
6.06e-14 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 73.97 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 186 GPSQTVAILTSSGTTGMPKAVCISNDILTQ------ETVFV--NGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKP 257
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNlrtslsERYFGrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 258 FAADY--FVYLVSKYSITYAlippehccslldcpTATPE--------KLGSLTKLNFGGGRMTQATVERVKKLAPNGVLN 327
Cdd:cd17648 172 MRFDPdrFYAYINREKVTYL--------------SGTPSvlqqydlaRLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIIN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 328 SsYGMTEVGfiVFNHGHLKLT------AAGNPLPGIQVKIVDDDGNQLGVNQTGEI-IVHNGFSwNGYFADPEATK---- 396
Cdd:cd17648 238 A-YGPTETT--VTNHKRFFPGdqrfdkSLGRPVRNTKCYVLNDAMKRVPVGAVGELyLGGDGVA-RGYLNRPELTAerfl 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 397 ------AMQDEEG----WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGD 466
Cdd:cd17648 314 pnpfqtEQERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQ 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356947 467 VPGA--LV--VREDNATLTAQQVIDHVAKRLPDIQ--KQLragVQFADeIPQNHNGKV-VRR 521
Cdd:cd17648 394 SRIQkyLVgyYLPEPGHVPESDLLSFLRAKLPRYMvpARL---VRLEG-IPVTINGKLdVRA 451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
193-521 |
8.22e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.99 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVCISNDIL------TQETVFVNGYDTIFISASLDWITGLWATIFSTVNG-CTRIISSKPFAADYFVY 265
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLvnhlhaTGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGaSVVIRDDSLWDPERLYA 4778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 266 LVSKYSITYALIPPEHCCSLLDCPTATPEkLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGFIVFNHGHL 345
Cdd:PRK12316 4779 EIHEHRVTVLVFPPVYLQQLAEHAERDGE-PPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKAR 4857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 346 KLTAA-------GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAM-----QDEEG--WFHTGDMG 411
Cdd:PRK12316 4858 DGDACgaaympiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERfvpdpFGAPGgrLYRTGDLA 4937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 412 YFDED---DYLYMTDRKkevLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVyDETQGDVPGALVVREDNATLTA------ 482
Cdd:PRK12316 4938 RYRADgviDYLGRVDHQ---VKIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGYVVPQDPALADAdeaqae 5013
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21356947 483 --QQVIDHVAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:PRK12316 5014 lrDELKAALRERLPEY--MVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
53-521 |
1.39e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 53 GVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIF 132
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 133 TDADhydklysatsafkpeiiLTTGTKDGVlsiQDLLAPTKTEFFYQPTPLKEGPSQTVA-ILTSSGTTGMPKAVCISND 211
Cdd:PRK12316 3160 SQSH-----------------LRLPLAQGV---QVLDLDRGDENYAEANPAIRTMPENLAyVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 212 ILTQETVFVNGY------DTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSL 285
Cdd:PRK12316 3220 ALSNHLCWMQQAyglgvgDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQ 3299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 286 LDCPTATPEKLGSLTKLNFGGGRMTQatvERVKKLAPNGVLNSSYGMTEVGFIVFNHGHLKLTAA----GNPLPGIQVKI 361
Cdd:PRK12316 3300 AFLEEEDAHRCTSLKRIVCGGEALPA---DLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDavpiGRPIANRACYI 3376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 362 VDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT------KAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQ 435
Cdd:PRK12316 3377 LDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTaerfvpDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFR 3456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 436 MWPAEVEAVIDELPEVKRVCVIGVydetQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIqkQLRAGVQFADEIPQNHN 515
Cdd:PRK12316 3457 IELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPEDEAGDLREALKAHLKASLPEY--MVPAHLLFLERMPLTPN 3530
|
....*.
gi 21356947 516 GKVVRR 521
Cdd:PRK12316 3531 GKLDRK 3536
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-521 |
1.68e-13 |
|
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: 72.47 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVCISNDIL------TQETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKP--FAADYFV 264
Cdd:cd17644 111 VIYTSGSTGKPKGVMIEHQSLvnlshgLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEmrSSLEDFV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 265 YLVSKYSITYALIPPEHCCSLLDcpTATPEKLGSLTKLNF---GGGRMTQATVER-VKKLAPNGVLNSSYGMTE--VGFI 338
Cdd:cd17644 191 QYIQQWQLTVLSLPPAYWHLLVL--ELLLSTIDLPSSLRLvivGGEAVQPELVRQwQKNVGNFIQLINVYGPTEatIAAT 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 339 VFN-----HGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATK--------AMQDEEGWF 405
Cdd:cd17644 269 VCRltqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAekfishpfNSSESERLY 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 406 HTGDMGYFDED---DYLYMTDRKkevLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTA 482
Cdd:cd17644 349 KTGDLARYLPDgniEYLGRIDNQ---VKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPST 425
|
330 340 350
....*....|....*....|....*....|....*....
gi 21356947 483 QQVIDHVAKRLPDiqKQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd17644 426 VELRQFLKAKLPD--YMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
187-521 |
2.88e-13 |
|
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: 71.98 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCI-----SNDILT-QETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAA 260
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIehrgvVNLVEWaNKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 261 DY--FVYLVSKYSITYALIPPEHcCSLLDCPTATPEKlgSLTKLNFGGGRMTQATVERVKKLAPNGV-LNSSYGMTE--V 335
Cdd:cd17655 216 DGqaLTQYIRQNRITIIDLTPAH-LKLLDAADDSEGL--SLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTEttV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 336 GFIVFNHGHLKLTAA----GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKA--MQDE----EGWF 405
Cdd:cd17655 293 DASIYQYEPETDQQVsvpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEkfVDDPfvpgERMY 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 406 HTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNatLTAQQV 485
Cdd:cd17655 373 RTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LPVAQL 450
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21356947 486 IDHVAKRLPD-------IQkqlragvqfADEIPQNHNGKVVRR 521
Cdd:cd17655 451 REFLARELPDymipsyfIK---------LDEIPLTPNGKVDRK 484
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
55-521 |
3.08e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.07 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 55 EVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTD 134
Cdd:PRK12316 2028 HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQ 2107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 135 ADHYDKLysatsafkpeiILTTGtkdgvLSIQDLLAPTKTEFFYQPTPLKEGPSQTVA-ILTSSGTTGMPKAVCISNDIL 213
Cdd:PRK12316 2108 RHLLERL-----------PLPAG-----VARLPLDRDAEWADYPDTAPAVQLAGENLAyVIYTSGSTGLPKGVAVSHGAL 2171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 214 ------TQETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRII-SSKPFAADYFVYLVSKYSITYALIPP------- 279
Cdd:PRK12316 2172 vahcqaAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIrDDELWDPEQLYDEMERHGVTILDFPPvylqqla 2251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 280 EHCcSLLDCPTAtpeklgsLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTE--VGFIVFNHGHLKLTAA-----GN 352
Cdd:PRK12316 2252 EHA-ERDGRPPA-------VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEavVTPLLWKCRPQDPCGAayvpiGR 2323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 353 PLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADP--EATKAMQDE-----EGWFHTGDMGYFDEDDYLYMTDRK 425
Cdd:PRK12316 2324 ALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPglTAERFVPDPfsasgERLYRTGDLARYRADGVVEYLGRI 2403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 426 KEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVyDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDiqKQLRAGVQ 505
Cdd:PRK12316 2404 DHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPA--YMVPAHWV 2480
|
490
....*....|....*.
gi 21356947 506 FADEIPQNHNGKVVRR 521
Cdd:PRK12316 2481 VLERLPLNPNGKLDRK 2496
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
50-494 |
1.21e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 70.20 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 50 DSEGVEVTFGQALTWAIRIAQQLKSR-GLDHKDIIGISARNTTYIMPT--AVACFfhGTPFQSANPILEESTLKHLYNIS 126
Cdd:PRK05620 33 GAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVlfAVACM--GAVFNPLNKQLMNDQIVHIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 127 KPKIIFTDADHYDKL---------------YSATSAFKPEIILTTGTKdgVLSIQDLLAPTKTEFfyqptPLKEGPSQT- 190
Cdd:PRK05620 111 EDEVIVADPRLAEQLgeilkecpcvravvfIGPSDADSAAAHMPEGIK--VYSYEALLDGRSTVY-----DWPELDETTa 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 191 VAILTSSGTTGMPKAVCISNDILTQETVFVNGYDTIFISASLDWITGL-------WATIFST-VNGCTRIISSKPFAADY 262
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGESFLCCVpiyhvlsWGVPLAAfMSGTPLVFPGPDLSAPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 263 FVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATV----ERVkklapnGV-LNSSYGMTEVGF 337
Cdd:PRK05620 264 LAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIkaweERY------GVdVVHVWGMTETSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 338 I---------VFNHGHLKLTAAGNPLP-GIQVKIVDDdGNQLGVN--QTGEIIVHNGFSWNGYFADPEAT---------- 395
Cdd:PRK05620 338 VgtvarppsgVSGEARWAYRVSQGRFPaSLEYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPTEEgggaastfrg 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 396 KAMQD------EEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPG 469
Cdd:PRK05620 417 EDVEDandrftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPL 496
|
490 500
....*....|....*....|....*...
gi 21356947 470 ALVVREDN---ATLTAQQVIDHVAKRLP 494
Cdd:PRK05620 497 AVTVLAPGiepTRETAERLRDQLRDRLP 524
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
192-525 |
4.51e-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: 68.23 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 192 AILTSSGTTGMPKAVCISN-DILTQETVFVNGY-----DTIFISASLDWITG-LWATIFSTVNGCTRIISSKpFAADYF- 263
Cdd:cd05937 91 ILIYTSGTTGLPKAAAISWrRTLVTSNLLSHDLnlkngDRTYTCMPLYHGTAaFLGACNCLMSGGTLALSRK-FSASQFw 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 264 --VYLVSKYSITYAlipPEHCCSLLDCPTATPEKLGSLtKLNFGGGrMTQATVERVKKLAPNGVLNSSYGMTEVGFIVFN 341
Cdd:cd05937 170 kdVRDSGATIIQYV---GELCRYLLSTPPSPYDRDHKV-RVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEGVFALTN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 342 H--GHLKLTAAGNPLPGIQ---------VKIVDDDGN-----------QLGVNQTGEIIV----HNGFSWNGYFADPEAT 395
Cdd:cd05937 245 HnvGDFGAGAIGHHGLIRRwkfenqvvlVKMDPETDDpirdpktgfcvRAPVGEPGEMLGrvpfKNREAFQGYLHNEDAT 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 396 --KAMQD--EEG--WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGV----YDetqG 465
Cdd:cd05937 325 esKLVRDvfRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpgHD---G 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356947 466 DVPGALVVREDNAT----LTAQQVIDHVAKRLPDIQKQLRagVQFADEIPQNHNGKVVRRYARD 525
Cdd:cd05937 402 RAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLF--LRLTEEVATTDNHKQQKGVLRD 463
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
52-521 |
4.91e-12 |
|
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: 68.09 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 52 EGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKII 131
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 132 FTDADHYDKLysatsafkPEIILTTGtkdgVLSIQDLLAPTKTeffyQPTPLkegPSQTVAILTSSGTTGMPKAVCISND 211
Cdd:cd12116 89 LTDDALPDRL--------PAGLPVLL----LALAAAAAAPAAP----RTPVS---PDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 212 ILT------QETVFVNGYDTIF--------ISAsLDWITGLWAtifstvnGCTRIISSKPFAAD--YFVYLVSKYSITYA 275
Cdd:cd12116 150 NLVnflhsmRERLGLGPGDRLLavttyafdISL-LELLLPLLA-------GARVVIAPRETQRDpeALARLIEAHSITVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 276 LIPPEHCCSLLDcptATPEKLGSLTKLnFGGGRMTQATVERVkkLAPNGVLNSSYGMTE------VGFIVFNHGHLKLta 349
Cdd:cd12116 222 QATPATWRMLLD---AGWQGRAGLTAL-CGGEALPPDLAARL--LSRVGSLWNLYGPTEttiwstAARVTAAAGPIPI-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 350 aGNPLPGIQVKIVDDDGNQLGVNQTGEI-IVHNGFSwNGYFADPEATKAM-----QDEEG--WFHTGDMGYFDEDDYLYM 421
Cdd:cd12116 294 -GRPLANTQVYVLDAALRPVPPGVPGELyIGGDGVA-QGYLGRPALTAERfvpdpFAGPGsrLYRTGDLVRRRADGRLEY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 422 TDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVigVYDETQGDVP-GALVVREDNATLTAQQVIDHVAKRLPDiqKQL 500
Cdd:cd12116 372 LGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAV--VVREDGGDRRlVAYVVLKAGAAPDAAALRAHLRATLPA--YMV 447
|
490 500
....*....|....*....|.
gi 21356947 501 RAGVQFADEIPQNHNGKVVRR 521
Cdd:cd12116 448 PSAFVRLDALPLTANGKLDRK 468
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
305-430 |
1.08e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 67.31 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 305 GGGRMTQATVERVkklapNGVLN---SSYGMTE---VGFIVFNhGHLKLTAAGNPLPGIQVKIVDDDGNQlgvnQT---- 374
Cdd:PTZ00216 436 GGGPLSAATQEFV-----NVVFGmviQGWGLTEtvcCGGIQRT-GDLEPNAVGQLLKGVEMKLLDTEEYK----HTdtpe 505
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356947 375 --GEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLK 430
Cdd:PTZ00216 506 prGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAK 563
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
351-490 |
1.86e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 66.33 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 GNPLPGIQVKIVDDDGN-QLGVNQTGEIIVHNGFSWNGYFADPEAtkamqDEEGWFHTGDMGYFdEDDYLYMTDRKKEVL 429
Cdd:PRK05851 348 GNPIPGMEVRISPGDGAaGVAGREIGEIEIRGASMMSGYLGQAPI-----DPDDWFPTGDLGYL-VDGGLVVCGRAKELI 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 430 KWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVRE----DNATlTAQQVIDHVA 490
Cdd:PRK05851 422 TVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEfrgpDEAG-ARSEVVQRVA 485
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
324-444 |
2.42e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 66.28 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 324 GVLNSSYGMTEVGFIV-------FNHGHLkltaaGNPLPGIQVKIVD-DDGNQLGVNQT---GEIIVHNGFSWNGYFADP 392
Cdd:PLN02736 402 GRVLEGYGMTETSCVIsgmdegdNLSGHV-----GSPNPACEVKLVDvPEMNYTSEDQPyprGEICVRGPIIFKGYYKDE 476
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 21356947 393 EATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKW-KGLQMWPAEVEAV 444
Cdd:PLN02736 477 VQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 529
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
57-533 |
7.70e-11 |
|
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: 64.37 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 57 TFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHG--TPFQSANpiLEESTLKHLYNISKPKIIFTD 134
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGveTALINSN--LRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 135 adHYDKLYSATSAFKPeiilttgtkdgvlSIQDLLAPTKTEFFYqptplkegpsqtvailtSSGTTGMPKAVCISN---- 210
Cdd:cd05939 83 --LLDPLLTQSSTEPP-------------SQDDVNFRDKLFYIY-----------------TSGTTGLPKAAVIVHsryy 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 211 ---------------DILtqetvfvngYDTIFISASLDWITGLWATIfstVNGCTRIISSKpFAADYFVYLVSKYSITYA 275
Cdd:cd05939 131 riaagayyafgmrpeDVV---------YDCLPLYHSAGGIMGVGQAL---LHGSTVVIRKK-FSASNFWDDCVKYNCTIV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 276 LIPPEHCCSLLDCPTATPEKLGSLtKLNFGGGRMTQATVE-----RVKKLApngvlnSSYGMTEVGFIVFNHGHlKLTAA 350
Cdd:cd05939 198 QYIGEICRYLLAQPPSEEEQKHNV-RLAVGNGLRPQIWEQfvrrfGIPQIG------EFYGATEGNSSLVNIDN-HVGAC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 G-NPLPG-----IQVKIVDDDGNQL-----GV------NQTGE----IIVHNGFS-WNGYfADPEAT--KAMQD--EEG- 403
Cdd:cd05939 270 GfNSRILpsvypIRLIKVDEDTGELirdsdGLcipcqpGEPGLlvgkIIQNDPLRrFDGY-VNEGATnkKIARDvfKKGd 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 -WFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVydetqgDVPGalvvREDNATLTA 482
Cdd:cd05939 349 sAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV------EVPG----VEGRAGMAA 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 21356947 483 qqVIDHVAKRLPDiqkqlRAGVQFADEIPQnhngkvvrrYARDLFVALSKK 533
Cdd:cd05939 419 --IVDPERKVDLD-----RFSAVLAKSLPP---------YARPQFIRLLPE 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-521 |
8.52e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVCISNDILT------QETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAAD--YFV 264
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHAALAerlqwmQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDpqRIA 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 265 YLVSKYSITYALIPPEHCCSLLDCPTATpeKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGfIVFNHGH 344
Cdd:PRK05691 1358 ELVQQYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETA-INVTHWQ 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 345 LKL-----TAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAM-------QDEEGWFHTGDMGY 412
Cdd:PRK05691 1435 CQAedgerSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERfvpdplgEDGARLYRTGDRAR 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 413 FDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIgVYDETQGDVPGALVVREDNATLTAQQVIDHVAKR 492
Cdd:PRK05691 1515 WNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAE 1593
|
330 340 350
....*....|....*....|....*....|.
gi 21356947 493 LPD--IQKQLRAgvqfADEIPQNHNGKVVRR 521
Cdd:PRK05691 1594 LPEymVPAQLIR----LDQMPLGPSGKLDRR 1620
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
330-499 |
8.94e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 64.12 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVF---NHGHlklTAAGNPLPGIQVKIVDDdgnqlgvnqtgEIIVHNGFSWNGYFADPEATkAMQDEEGWFH 406
Cdd:PRK09029 271 YGLTEMASTVCakrADGL---AGVGSPLPGREVKLVDG-----------EIWLRGASLALGYWRQGQLV-PLVNDEGWFA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 407 TGDMGYFDEDdylymtdrkkevlKWK--------------GLQmwPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALV 472
Cdd:PRK09029 336 TRDRGEWQNG-------------ELTilgrldnlffsggeGIQ--PEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV 400
|
170 180 190
....*....|....*....|....*....|....*..
gi 21356947 473 VREDNATLT--AQQVIDHVAK--------RLPDIQKQ 499
Cdd:PRK09029 401 ESDSEAAVVnlAEWLQDKLARfqqpvayyLLPPELKN 437
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
51-521 |
1.07e-10 |
|
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: 63.90 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 51 SEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKI 130
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 131 IFTDADHYDKLysatsafkpeiiltTGTKDGVLSIQDLLAPTKTEffyQPTPLKEGPSQTVAILTSSGTTGMPKAV---- 206
Cdd:cd17651 96 VLTHPALAGEL--------------AVELVAVTLLDQPGAAAGAD---AEPDPALDADDLAYVIYTSGSTGRPKGVvmph 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 207 -CISNDILTQETVFVNGYDT---IFISASLDwiTGLWAtIFST--VNGCTRIISSK---PFAAdyFVYLVSKYSITYALI 277
Cdd:cd17651 159 rSLANLVAWQARASSLGPGArtlQFAGLGFD--VSVQE-IFSTlcAGATLVLPPEEvrtDPPA--LAAWLDEQRISRVFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 278 PPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMT-QATVERVKKLAPNGVLNSSYGMTEVGFI------VFNHGHLKLTAA 350
Cdd:cd17651 234 PTVALRALAEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVVtalslpGDPAAWPAPPPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGW------FHTGDMGYFDEDDYLYMTDR 424
Cdd:cd17651 314 GRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 425 KKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIgVYDETQGD---VpgALVVREDNATLTAQQVIDHVAKRLPDiqKQLR 501
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVL-AREDRPGEkrlV--AYVVGDPEAPVDAAELRAALATHLPE--YMVP 468
|
490 500
....*....|....*....|
gi 21356947 502 AGVQFADEIPQNHNGKVVRR 521
Cdd:cd17651 469 SAFVLLDALPLTPNGKLDRR 488
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
187-531 |
1.36e-10 |
|
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: 63.72 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISND-----ILTQETVF-VNGYDTIFISAS-------LDwitglwatIFST--VNGCTR 251
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRalstsALAHGRALgLTSESRVLQFASytfdvsiLE--------IFTTlaAGGCLC 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 252 IISSKPFAADyFVYLVSKYSITYALIPPehccS---LLDcptatPEKLGSLTKLNFGGGRMTQATVERvkkLAPNGVLNS 328
Cdd:cd05918 177 IPSEEDRLND-LAGFINRLRVTWAFLTP----SvarLLD-----PEDVPSLRTLVLGGEALTQSDVDT---WADRVRLIN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 329 SYGMTE-----VGFIVFNHGHLKLTaaGNPLPGIQVkIVD-DDGNQL-GVNQTGEIIV---HNGfswNGYFADPEATKA- 397
Cdd:cd05918 244 AYGPAEctiaaTVSPVVPSTDPRNI--GRPLGATCW-VVDpDNHDRLvPIGAVGELLIegpILA---RGYLNDPEKTAAa 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 398 --------MQDEEGW----FHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQG 465
Cdd:cd05918 318 fiedpawlKQEGSGRgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 466 DVPGALVV-----REDNATLTAQQVIDHVAKRLPDIQKQLRAGVQ-------------FADEIPQNHNGKVVRRYARDLF 527
Cdd:cd05918 398 SSSPQLVAfvvldGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRqrlpsymvpsvflPLSHLPLTASGKIDRRALRELA 477
|
....
gi 21356947 528 VALS 531
Cdd:cd05918 478 ESLS 481
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
346-521 |
9.19e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 61.12 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 346 KLTAAGNPLPGIQVKIVDD-DGNQLGVNQTGEIIVhngfswngyfADPEATKAMQ----DEEG-----WFH-------TG 408
Cdd:PRK10524 409 RLGSPGVPMYGYNVKLLNEvTGEPCGPNEKGVLVI----------EGPLPPGCMQtvwgDDDRfvktyWSLfgrqvysTF 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 409 DMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLT------- 481
Cdd:PRK10524 479 DWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearla 558
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21356947 482 -AQQVIDHVAKRLPDIQKQLRagVQFADEIPQNHNGKVVRR 521
Cdd:PRK10524 559 lEKEIMALVDSQLGAVARPAR--VWFVSALPKTRSGKLLRR 597
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
351-508 |
2.74e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 59.75 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 GNPLPGIQVKIVD-DDGNQLGVNQT---GEIIVhNGFSWN-GYFADPEATKAMQ--DEEG--WFHTGDMGYFDEDDYLYM 421
Cdd:PLN02387 475 GPPLPCCYVKLVSwEEGGYLISDKPmprGEIVI-GGPSVTlGYFKNQEKTDEVYkvDERGmrWFYTGDIGQFHPDGCLEI 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 422 TDRKKEVLKWK-GLQMWPAEVEAVIDELPEVKRV----------CVigvydetqgdvpgALVVrednatlTAQQVIDHVA 490
Cdd:PLN02387 554 IDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNImvhadpfhsyCV-------------ALVV-------PSQQALEKWA 613
|
170
....*....|....*...
gi 21356947 491 KrlpdiqkqlRAGVQFAD 508
Cdd:PLN02387 614 K---------KAGIDYSN 622
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
47-430 |
8.90e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 57.93 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 47 QISDSEG---VEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLY 123
Cdd:PLN02861 66 QVTDSKVgpyVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 124 NISKPKIIFTDADhydKLYSATSAFKPeiilTTGTKDGVLSIQDLLAPTKTE--------FFYQPTPL---------KEG 186
Cdd:PLN02861 146 NHAEVSIAFVQES---KISSILSCLPK----CSSNLKTIVSFGDVSSEQKEEaeelgvscFSWEEFSLmgsldcelpPKQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISN----------DILTQET------------------VFVNGYDTIFIS--AS----- 231
Cdd:PLN02861 219 KTDICTIMYTSGTTGEPKGVILTNraiiaevlstDHLLKVTdrvateedsyfsylplahVYDQVIETYCISkgASigfwq 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 232 ------LDWITGLWATIFSTV--------NGCTRIISSKPFAADYFVYLVSKYSITYAL--IPPEHCCSLLD--CPTATP 293
Cdd:PLN02861 299 gdirylMEDVQALKPTIFCGVprvydriyTGIMQKISSGGMLRKKLFDFAYNYKLGNLRkgLKQEEASPRLDrlVFDKIK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 294 EKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEV---GFIVFNHGHLKLTAAGNPLPGIQVKI--VDDDG-N 367
Cdd:PLN02861 379 EGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEScggCFTSIANVFSMVGTVGVPMTTIEARLesVPEMGyD 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356947 368 QLGVNQTGEIIVHNGFSWNGYFADPEATKAMQdEEGWFHTGDMGYFDEDDYLYMTDRKKEVLK 430
Cdd:PLN02861 459 ALSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFK 520
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
367-430 |
1.56e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 57.13 E-value: 1.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 367 NQLGVNQTGEIIVHNGFSWNGYFADPEATK-AMQDeeGWFHTGDMGYFDEDDYLYMTDRKKEVLK 430
Cdd:PLN02430 458 DPLGEPPRGEICVRGKCLFSGYYKNPELTEeVMKD--GWFHTGDIGEILPNGVLKIIDRKKNLIK 520
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
17-458 |
3.10e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 56.57 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 17 GIPqnNPFKPETSLGRIIFKNMRNWPKNVC----QISDSEG---VEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARN 89
Cdd:PLN02614 36 GFP--NPIEGMDSCWDVFRMSVEKYPNNPMlgrrEIVDGKPgkyVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGAN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 90 TTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKLYSaTSAFKPEIILTTGTKDGVLSIQD-- 167
Cdd:PLN02614 114 SPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFK-TCPNSTEYMKTVVSFGGVSREQKee 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 168 -----LLAPTKTEFF-------YQpTPLKEgPSQTVAILTSSGTTGMPKAVCISND------------------ILTQET 217
Cdd:PLN02614 193 aetfgLVIYAWDEFLklgegkqYD-LPIKK-KSDICTIMYTSGTTGDPKGVMISNEsivtliagvirllksanaALTVKD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 218 VFVNG------YDT------IFISASLDWITG-----------LWATIFSTV--------NGCTRIISSKPFAADYFVYL 266
Cdd:PLN02614 271 VYLSYlplahiFDRvieecfIQHGAAIGFWRGdvklliedlgeLKPTIFCAVprvldrvySGLQKKLSDGGFLKKFVFDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 267 VSKYSITYALIPPEHCCSLLDCP----TATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEV---GFIV 339
Cdd:PLN02614 351 AFSYKFGNMKKGQSHVEASPLCDklvfNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEScagTFVS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 340 FNHGHLKLTAAGNPLPGIQVK---IVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEeGWFHTGDMGYFDED 416
Cdd:PLN02614 431 LPDELDMLGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPN 509
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 21356947 417 DYLYMTDRKKEVLKW-KGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:PLN02614 510 GSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
187-521 |
4.15e-08 |
|
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: 55.55 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISNDILTQetvFVNGYDTIF------------ISASLDWITGLWATifSTVNGCTRIIS 254
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAH---AAHAWRREYeldsfpvrllqmASFSFDVFAGDFAR--SLLNGGTLVIC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 255 SKPFAAD-YFVY-LVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGG-GRMTQATVERVKKLAPNGVLNSSYG 331
Cdd:cd17650 167 PDEVKLDpAALYdLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSdGCKAQDFKTLAARFGQGMRIINSYG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 332 MTE--VGFIVFNHGHLKLTAAGN-----PLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDE--- 401
Cdd:cd17650 247 VTEatIDSTYYEEGRDPLGDSANvpigrPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEnpf 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 402 ---EGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREdnA 478
Cdd:cd17650 327 apgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA--A 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 21356947 479 TLTAQQVIDHVAKRLPD--IQKQLragVQFaDEIPQNHNGKVVRR 521
Cdd:cd17650 405 TLNTAELRAFLAKELPSymIPSYY---VQL-DALPLTPNGKVDRR 445
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
322-524 |
4.80e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.52 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 322 PNGVLNSSYGMTEVGFIVFN------------------HGHLKLTAAGNPLPGIQVK-----------IVDDD-GNQLGV 371
Cdd:PRK12476 347 PRTAFKPSYGIAEATLFVATiapdaepsvvyldreqlgAGRAVRVAADAPNAVAHVScgqvarsqwavIVDPDtGAELPD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 372 NQTGEIIVHNGFSWNGYFADPEATK-----AMQ-------------DEEGWFHTGDMG-YFDEDdyLYMTDRKKEVLKWK 432
Cdd:PRK12476 427 GEVGEIWLHGDNIGRGYWGRPEETErtfgaKLQsrlaegshadgaaDDGTWLRTGDLGvYLDGE--LYITGRIADLIVID 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 433 GLQMWPAEVEA-VIDELPEVKRVCVigvydeTQGDVPG----ALVVREDNATLTA----QQVID----HVAKR----LPD 495
Cdd:PRK12476 505 GRNHYPQDIEAtVAEASPMVRRGYV------TAFTVPAedneRLVIVAERAAGTSradpAPAIDairaAVSRRhglaVAD 578
|
250 260
....*....|....*....|....*....
gi 21356947 496 IqKQLRAGVqfadeIPQNHNGKVVRRYAR 524
Cdd:PRK12476 579 V-RLVPAGA-----IPRTTSGKLARRACR 601
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
185-430 |
7.13e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 55.21 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 185 EGPSQTVAILTSSGTTGMPKAVCISND--ILTQETVFvNGYDTIFISASLDWITGLWA------TIFSTVNGCTRIISSK 256
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHAnlLANQRACL-KFFSPKEDDVMMSFLPPFHAygfnscTLFPLLSGVPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 257 PFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVG 336
Cdd:PRK06334 259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 337 -FIVFN--HGHLKLTAAGNPLPGIQVKIVDDDGN-QLGVNQTGEIIVHNGFSWNGYF-ADPEATKAMQDEEGWFHTGDMG 411
Cdd:PRK06334 339 pVITINtvNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLG 418
|
250
....*....|....*....
gi 21356947 412 YFDEDDYLYMTDRKKEVLK 430
Cdd:PRK06334 419 YVDRHGELFLKGRLSRFVK 437
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
193-518 |
8.74e-08 |
|
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: 54.40 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAV-----CISNDILTQETVFVNGYDTIFISASLDWITGLWATIF-STVNGCTRII---SSKPFAADYF 263
Cdd:cd17654 123 VIHTSGTTGTPKIVavphkCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFlSLSSGATLLIvptSVKVLPSKLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 264 VYLVSKYSITYALIPPehccSLL------DCPTATPEKLGSLTKLNFGGGRMTQATVerVKKLAPNG----VLNsSYGMT 333
Cdd:cd17654 203 DILFKRHRITVLQATP----TLFrrfgsqSIKSTVLSATSSLRVLALGGEPFPSLVI--LSSWRGKGnrtrIFN-IYGIT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 334 EVG-FIVFNhgHLKLTAA----GNPLPGIQVKIVDDDGN-QLGVNQTGEIIvhngfswNGYFADPEATKAMQDeegWFHT 407
Cdd:cd17654 276 EVScWALAY--KVPEEDSpvqlGSPLLGTVIEVRDQNGSeGTGQVFLGGLN-------RVCILDDEVTVPKGT---MRAT 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 408 GDMGYFdEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIgVYDETQgdvPGALVVREDNATLTAQQVID 487
Cdd:cd17654 344 GDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-LSDQQR---LIAFIVGESSSSRIHKELQL 418
|
330 340 350
....*....|....*....|....*....|...
gi 21356947 488 HVAKR--LPDIQKQLragvqfaDEIPQNHNGKV 518
Cdd:cd17654 419 TLLSShaIPDTFVQI-------DKLPLTSHGKV 444
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
345-526 |
1.30e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 54.52 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 345 LKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNgfSWNGYF----ADPE--ATKAMQDEEGWFHTGDMGYFDEDDY 418
Cdd:PLN02654 451 QKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKK--SWPGAFrtlyGDHEryETTYFKPFAGYYFSGDGCSRDKDGY 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 419 LYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQqvidhVAKRL-PDIQ 497
Cdd:PLN02654 529 YWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE-----LRKSLiLTVR 603
|
170 180 190
....*....|....*....|....*....|....
gi 21356947 498 KQLRA-----GVQFADEIPQNHNGKVVRRYARDL 526
Cdd:PLN02654 604 NQIGAfaapdKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
224-511 |
1.52e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 54.34 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 224 DTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKY-----SITYALIPpehccSLLDCPTAT-----P 293
Cdd:PRK07868 647 DTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYgvtvvSYTWAMLR-----EVVDDPAFVlhgnhP 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 294 EKLgsltklnFGGGRMTQATVERV-KKLAPNGVLnSSYGMTEVGFIVFNHGHLKLTAAGNPLPGI-QVKIV--------- 362
Cdd:PRK07868 722 VRL-------FIGSGMPTGLWERVvEAFAPAHVV-EFFATTDGQAVLANVSGAKIGSKGRPLPGAgRVELAaydpehdli 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 363 --DDDG--NQLGVNQTGEIIVHNGFSwngyfADPEAT---KAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKW-KGl 434
Cdd:PRK07868 794 leDDRGfvRRAEVNEVGVLLARARGP-----IDPTASvkrGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTaRG- 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 435 qmwPAEVEAVIDELPEVKRVCVIGVYDETQGDVP---GALVVREDnATLTAQQVIDHVAKRLPDIQKQLragVQFADEIP 511
Cdd:PRK07868 868 ---PVYTEPVTDALGRIGGVDLAVTYGVEVGGRQlavAAVTLRPG-AAITAADLTEALASLPVGLGPDI---VHVVPEIP 940
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
49-519 |
1.10e-06 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 51.50 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 49 SDSEGVEVTFGQALTWAIRIAQQLKSRGldhkdiIGISARNTTYI--MPTAVACFFH----GTPFQSANPIL-EESTLKH 121
Cdd:cd05943 92 EDGERTEVTWAELRRRVARLAAALRALG------VKPGDRVAGYLpnIPEAVVAMLAtasiGAIWSSCSPDFgVPGVLDR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 122 LYNIsKPKIIFTDA---------DHYDK-------LYSATSAFKPEIILTTGTKDG-----VLSIQDLLAPTKT-EFFYQ 179
Cdd:cd05943 166 FGQI-EPKVLFAVDaytyngkrhDVREKvaelvkgLPSLLAVVVVPYTVAAGQPDLskiakALTLEDFLATGAAgELEFE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 180 PTPlkegPSQTVAILTSSGTTGMPKavCI---SNDILTQ---ETVFVNGY---DTIFISASLDW------ITGLW--ATI 242
Cdd:cd05943 245 PLP----FDHPLYILYSSGTTGLPK--CIvhgAGGTLLQhlkEHILHCDLrpgDRLFYYTTCGWmmwnwlVSGLAvgATI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 243 FsTVNGCtriisskPFAADYFVY--LVSKYSITY-----ALIppeHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVE 315
Cdd:cd05943 319 V-LYDGS-------PFYPDTNALwdLADEEGITVfgtsaKYL---DALEKAGLKPAETHDLSSLRTILSTGSPLKPESFD 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 316 RV-KKLAPNGVLNSSYGMTEVgfivfnhghLKLTAAGNPL----PG-IQ-------VKIVDDDGNQLgVNQTGEIIVHNG 382
Cdd:cd05943 388 YVyDHIKPDVLLASISGGTDI---------ISCFVGGNPLlpvyRGeIQcrglgmaVEAFDEEGKPV-WGEKGELVCTKP 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 383 FS------WNgyfaDPEATK---AMQDE-EG-WFHtGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEV 451
Cdd:cd05943 458 FPsmpvgfWN----DPDGSRyraAYFAKyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEV 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356947 452 KRVCVIGVYDEtQGDVPGAL-VVREDNATLTaqqviDHVAKRlpdIQKQLRAGVQ--------FA-DEIPQNHNGKVV 519
Cdd:cd05943 533 EDSLVVGQEWK-DGDERVILfVKLREGVELD-----DELRKR---IRSTIRSALSprhvpakiIAvPDIPRTLSGKKV 601
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
330-458 |
1.99e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 50.53 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVGFIVFNhGHLKltaagNPlPGIQVKIVDDDgnQLGVNQT------GEIIVHNGFSWNGYFADPEATKAMQDEEG 403
Cdd:cd17632 394 YGSTEAGAVILD-GVIV-----RP-PVLDYKLVDVP--ELGYFRTdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDG 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356947 404 WFHTGD-MGYFDEDDYLYMtDRKKEVLKW-KGLQMWPAEVEAVIDELPEVKRVCVIG 458
Cdd:cd17632 465 FYRTGDvMAELGPDRLVYV-DRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYG 520
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
305-530 |
2.42e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 50.33 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 305 GGGRMTQATVER-VKKLAPNG----VLNSSYGMTEVGFIV-------------FNH-----GHLKLTAAGNPLPGIQ--- 358
Cdd:PRK05850 296 GSERVHPATLKRfADRFAPFNlretAIRPSYGLAEATVYVatrepgqppesvrFDYeklsaGHAKRCETGGGTPLVSygs 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 359 -----VKIVDDDGN-QLGVNQTGEIIVHNGFSWNGYFADPEATK----AMQDE------EG-WFHTGDMGYFDEDDyLYM 421
Cdd:PRK05850 376 prsptVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETErtfgATLVDpspgtpEGpWLRTGDLGFISEGE-LFI 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 422 TDRKKEVLKWKGLQMWPAEVEAVIDELPEvKRVCVIGVYDETQGDvpgaLVV------REDnatlTAQQVIDhvakRLPD 495
Cdd:PRK05850 455 VGRIKDLLIVDGRNHYPDDIEATIQEITG-GRVAAISVPDDGTEK----LVAiielkkRGD----SDEEAMD----RLRT 521
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 21356947 496 IQKQLRA------GVQFAD-------EIPQNHNGKV-----VRRYARDLFVAL 530
Cdd:PRK05850 522 VKREVTSaiskshGLSVADlvlvapgSIPITTSGKIrraacVEQYRQDEFTRL 574
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
330-532 |
4.81e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 49.58 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 330 YGMTEVG-FIVFNHG-HLKLTAAGNPLPGIQVKIVDDDGnqlgVNQTGEIIVHNGFSWNGYFaDPEATKAMQD-EEGWFH 406
Cdd:PRK06814 939 YGVTETApVIALNTPmHNKAGTVGRLLPGIEYRLEPVPG----IDEGGRLFVRGPNVMLGYL-RAENPGVLEPpADGWYD 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 407 TGDMGYFDEDDYLYMTDRKKEVLKWKGlQMWP-AEVEAVIDEL-PEVKRVcVIGVYDETQGDvpgALVVREDNATLTAQQ 484
Cdd:PRK06814 1014 TGDIVTIDEEGFITIKGRAKRFAKIAG-EMISlAAVEELAAELwPDALHA-AVSIPDARKGE---RIILLTTASDATRAA 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21356947 485 VIDHVAKR-LPDIqkQLRAGVQFADEIPQNHNGKV----VRRYARDLFVALSK 532
Cdd:PRK06814 1089 FLAHAKAAgASEL--MVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPEA 1139
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
51-486 |
1.12e-05 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 48.11 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 51 SEGVEVTFGQALTWAIRIAQQLKSR-GLDHKDIIGISARNTTYIMPTAVACFFHG---TPFQsanPILEESTLKHLYNIS 126
Cdd:cd05905 10 KEATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGvvpIPIE---PPDISQQLGFLLGTC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 127 KPKIIFT-DADH----YDKLYSATSAFK------PEIILTTGTKDGvlsiqdlLAPTKTEFFYQPTPLKEgpsQTVAILT 195
Cdd:cd05905 87 KVRVALTvEACLkglpKKLLKSKTAAEIakkkgwPKILDFVKIPKS-------KRSKLKKWGPHPPTRDG---DTAYIEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 196 SSGTTGMPKAVCISN-DILTQ---ETVFVNGY--DTIFISASLDWITGLWATIFSTV-NG-CTRIISSKPFAADYFVYL- 266
Cdd:cd05905 157 SFSSDGSLSGVAVSHsSLLAHcraLKEACELYesRPLVTVLDFKSGLGLWHGCLLSVySGhHTILIPPELMKTNPLLWLq 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 267 -VSKYSITYALIPPEHCCSLLDCPTATPEKlGSLTKLNFGGGRM-------------TQATVERVKKLAPN--------- 323
Cdd:cd05905 237 tLSQYKVRDAYVKLRTLHWCLKDLSSTLAS-LKNRDVNLSSLRMcmvpcenrprissCDSFLKLFQTLGLSpravstefg 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 324 GVLNS-----SYGMTEVGFIVFN-----HG-----------HLKLTAAGNPLPGIQVKIVDDDG-NQLGVNQTGEIIVHN 381
Cdd:cd05905 316 TRVNPficwqGTSGPEPSRVYLDmralrHGvvrlderdkpnSLPLQDSGKVLPGAQVAIVNPETkGLCKDGEIGEIWVNS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 382 GFSWNGYFADPEATKAMQD------------EEGWFHTGDMGYF----------DEDDYLYMTDRKKEVLKWKGLQMWPA 439
Cdd:cd05905 396 PANASGYFLLDGETNDTFKvfpstrlstgitNNSYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEVRGLRHHPS 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21356947 440 EVEA-VIDELPEVKR----------VCVIGVYDETQGDVpGALVVREDNATLTAQQVI 486
Cdd:cd05905 476 DIEAtVMRVHPYRGRcavfsitglvVVVAEQPPGSEEEA-LDLVPLVLNAILEEHQVI 532
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
361-524 |
3.09e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 46.65 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 361 IVD-DDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAM-----------------QDEEGWFHTGDMG-YFDEDdyLYM 421
Cdd:PRK07769 404 IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATfqnilksrlseshaegaPDDALWVRTGDYGvYFDGE--LYI 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 422 TDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALV------VREDNATLTAQQVIdhVAKRLPD 495
Cdd:PRK07769 482 TGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVVFddshagLKFDPEDTSEQLVI--VAERAPG 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21356947 496 IQKQ--------------LRAGVQFAD-------EIPQNHNGKVVRRYAR 524
Cdd:PRK07769 560 AHKLdpqpiaddiraaiaVRHGVTVRDvllvpagSIPRTSSGKIARRACR 609
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
335-521 |
3.94e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.58 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 335 VGFIVFNHGHLKLTAAGNPLPgiqVKIVDD---DGNQLGvnqtgeiivhngfswNGYFADPEATKA------MQDEEGWF 405
Cdd:PRK10252 778 IGYPVWNTGLRILDARMRPVP---PGVAGDlylTGIQLA---------------QGYLGRPDLTASrfiadpFAPGERMY 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 406 HTGDMGYFDED---DYLymtDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRV----CVIGVYDETQGDVPG--ALVVRED 476
Cdd:PRK10252 840 RTGDVARWLDDgavEYL---GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthaCVINQAAATGGDARQlvGYLVSQS 916
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21356947 477 NATLTAQQVIDHVAKRLPDIQKQLrAGVQFaDEIPQNHNGKVVRR 521
Cdd:PRK10252 917 GLPLDTSALQAQLRERLPPHMVPV-VLLQL-DQLPLSANGKLDRK 959
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
193-521 |
4.11e-05 |
|
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: 46.31 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 193 ILTSSGTTGMPKAVCISNDILTQETVFVNGYDTI--------FISASLDWItglWATIFSTV-NGCTRIISSKPFAADY- 262
Cdd:cd17656 133 IIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNInfsdkvlqFATCSFDVC---YQEIFSTLlSGGTLYIIREETKRDVe 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 263 -FVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGR--MTQATVERVKKlaPNGVLNSSYGMTE---VG 336
Cdd:cd17656 210 qLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQlvITNEFKEMLHE--HNVHLHNHYGPSEthvVT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 337 FIVFNHG-HL-KLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEAT--KAMQD----EEGWFHTG 408
Cdd:cd17656 288 TYTINPEaEIpELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTaeKFFPDpfdpNERMYRTG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 409 DMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREdnATLTAQQVIDH 488
Cdd:cd17656 368 DLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELNISQLREY 445
|
330 340 350
....*....|....*....|....*....|...
gi 21356947 489 VAKRLPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd17656 446 LAKQLPEY--MIPSFFVPLDQLPLTPNGKVDRK 476
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
187-521 |
4.56e-05 |
|
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: 46.01 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 187 PSQTVAILTSSGTTGMPKAVCISNDILT------QETVFVNGYDTIFISASLDWITGLWaTIFST---------VNGCTR 251
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVnlcewhRPYFGVTPADKSLVYASFSFDASAW-EIFPHltagaalhvVPSERR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 252 IISSKpfAADYFvylvSKYSITYALIPPEHCCSLLDCPTAtpeklgSLTKLNFGGGRMTQAtVERVKKLAPNgvlnssYG 331
Cdd:cd17645 182 LDLDA--LNDYF----NQEGITISFLPTGAAEQFMQLDNQ------SLRVLLTGGDKLKKI-ERKGYKLVNN------YG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 332 MTEVGFIVFN------HGHLKLtaaGNPLPGIQVKIVDDDGNQLGVNQTGEI-IVHNGFSwNGYFADPEATKA------M 398
Cdd:cd17645 243 PTENTVVATSfeidkpYANIPI---GKPIDNTRVYILDEALQLQPIGVAGELcIAGEGLA-RGYLNRPELTAEkfivhpF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 399 QDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDetqGDVPGALVvrednA 478
Cdd:cd17645 319 VPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED---ADGRKYLV-----A 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 21356947 479 TLTAQQVIDHVAKR------LPDIqkQLRAGVQFADEIPQNHNGKVVRR 521
Cdd:cd17645 391 YVTAPEEIPHEELRewlkndLPDY--MIPTYFVHLKALPLTANGKVDRK 437
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
351-521 |
1.99e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 351 GNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAM-------QDEEGWFHTGDMGYFDEDDYLYMTD 423
Cdd:PRK05691 4043 GSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAfvphpfgAPGERLYRTGDLARRRSDGVLEYVG 4122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 424 RKKEVLKWKGLQMWPAEVEAVIDELPEVkRVCVIGVYDETQGDVpgaLVvrednATLTAQQVIDHVAKRLPDIQKQLRAG 503
Cdd:PRK05691 4123 RIDHQVKIRGYRIELGEIEARLHEQAEV-REAAVAVQEGVNGKH---LV-----GYLVPHQTVLAQGALLERIKQRLRAE 4193
|
170 180
....*....|....*....|....*..
gi 21356947 504 V---------QFADEIPQNHNGKVVRR 521
Cdd:PRK05691 4194 LpdymvplhwLWLDRLPLNANGKLDRK 4220
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
349-519 |
8.36e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 39.01 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 349 AAGNP-LP-----------GIQVKIVDDDGNQLgVNQTGEIIVHN-------GFsWNgyfadpeatkamqDEEG------ 403
Cdd:PRK03584 427 VGGNPlLPvyrgeiqcrglGMAVEAWDEDGRPV-VGEVGELVCTKpfpsmplGF-WN-------------DPDGsryrda 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356947 404 --------WFHtGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVyDETQGDVPGAL-VVR 474
Cdd:PRK03584 492 yfdtfpgvWRH-GDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQ-EWPDGDVRMPLfVVL 569
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21356947 475 EDNATLTaqqviDHVAKRlpdIQKQLRAG----------VQFADeIPQNHNGKVV 519
Cdd:PRK03584 570 AEGVTLD-----DALRAR---IRTTIRTNlsprhvpdkiIAVPD-IPRTLSGKKV 615
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
375-430 |
9.75e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 38.93 E-value: 9.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21356947 375 GEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLK 430
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| |
