|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-519 |
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: 604.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 46 CQICDVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSI 125
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 126 TKPTLIFCDGQEYDKVHKAT--VGWHPEILTLTDHVEGVQGIETLLDPT-TTEKIYQPEVLKEGGDQTVAILCSSGTTGL 202
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAkeLGPKDKIIVLDDKPDGVLSIEDLLSPTlGEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 203 PKAVCISNSILIQDSML--------ITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKaFTPEYFVGLVKKYKINY 274
Cdd:cd05911 161 PKGVCLSHRNLIANLSQvqtflygnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPK-FDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 275 AVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEVG-AITINIGISNVS-SAGR 352
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGgILTVNPDGDDKPgSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 353 PVPGIKIRIVDEDGKS-LGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKY 431
Cdd:cd05911 320 LLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 432 NGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQKQLRAGVQFTDKLP 511
Cdd:cd05911 400 KGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKV-ASYKQLRGGVVFVDEIP 478
|
....*...
gi 24653035 512 ANVNGKTM 519
Cdd:cd05911 479 KSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
52-534 |
2.65e-94 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 294.41 E-value: 2.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FcdgqeydkvhkatvgwhpeiltltdhvegvqgietlldptttekiyqpevlkeggdqTVAILCSSGTTGLPKAVCIS-- 209
Cdd:COG0318 101 V---------------------------------------------------------TALILYTSGTTGRPKGVMLThr 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 ----NSILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKINYAVLPPRHLSAL 285
Cdd:COG0318 124 nllaNAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 286 ITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNsGYGMTEVGAITI----NIGISNVSSAGRPVPGIKIRI 361
Cdd:COG0318 204 LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVE-GYGLTETSPVVTvnpeDPGERRPGSVGRPLPGVEVRI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 362 VDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR-MQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTE 440
Cdd:COG0318 283 VDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEaFRD--GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 441 IETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPAtQKQLRAgVQFTDKLPANVNGKTMR 520
Cdd:COG0318 361 VEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLAR-YKVPRR-VEFVDELPRTASGKIDR 438
|
490
....*....|....
gi 24653035 521 KTARDVFVALRVSG 534
Cdd:COG0318 439 RALRERYAAGALEA 452
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
189-517 |
8.37e-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: 266.07 E-value: 8.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 189 QTVAILCSSGTTGLPKAVCIS------NSILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKaFTPEY 262
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLShrnllaAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK-FDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 263 FVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNsGYGMTEVGAITINI 342
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVN-GYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 343 ----GISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPvETRRMQDFEGWFHTGDLGYFDEQNF 418
Cdd:cd04433 159 ppddDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 419 LYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQK 498
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERL-APYK 316
|
330
....*....|....*....
gi 24653035 499 QLRAgVQFTDKLPANVNGK 517
Cdd:cd04433 317 VPRR-VVFVDALPRTASGK 334
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
51-526 |
1.97e-73 |
|
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: 242.82 E-value: 1.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 51 VDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS-TYVMPLgVACLMNGTPFHSVNPVLDDATLTHVFSITKPT 129
Cdd:cd17642 40 HTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSlQFFLPV-IAGLFIGVGVAPTNDIYNERELDHSLNISKPT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFCDGQEYDKV----HKATVGWHPEILTLTDHVEGVQGIETL----LDPTTTEKIYQPEVLKEggDQTVA-ILCSSGTT 200
Cdd:cd17642 119 IVFCSKKGLQKVlnvqKKLKIIKTIIILDSKEDYKGYQCLYTFitqnLPPGFNEYDFKPPSFDR--DEQVAlIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 201 GLPKAVcisnsiliqdsMLITSQSVIYVGSCLDWITG---------LWAFVFSTVFGCT----------RIISNKAFTPE 261
Cdd:cd17642 197 GLPKGV-----------QLTHKNIVARFSHARDPIFGnqiipdtaiLTVIPFHHGFGMFttlgylicgfRVVLMYKFEEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 262 YFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE-VGAITI 340
Cdd:cd17642 266 LFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEtTSAILI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 341 -NIGISNVSSAGRPVPGIKIRIVDED-GKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNF 418
Cdd:cd17642 346 tPEGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGH 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 419 LYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQK 498
Cdd:cd17642 426 FFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQV-STAK 504
|
490 500
....*....|....*....|....*...
gi 24653035 499 QLRAGVQFTDKLPANVNGKTMRKTARDV 526
Cdd:cd17642 505 RLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
35-521 |
2.50e-73 |
|
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: 241.76 E-value: 2.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 35 FNNMKNWPKNVCQICDVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVL 114
Cdd:cd05904 12 FLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 115 DDATLTHVFSITKPTLIFCDGQEYDKVHKAtvgwHPEILTLTDHVEGVQGIETLLDPTTTEKIYQPEVLKeggDQTVAIL 194
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELAEKLASL----ALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQ---DDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 195 CSSGTTGLPKAVCISNSILIqdSMLitSQSVIYVGSCLDW------------ITGLWAFVFSTV-FGCTRIISNKAFTPE 261
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRNLI--AMV--AQFVAGEGSNSDSedvflcvlpmfhIYGLSSFALGLLrLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 262 yFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEVGAITIN 341
Cdd:cd05904 241 -LLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 342 I-----GISNVSSAGRPVPGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDE 415
Cdd:cd05904 320 CfapekDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 416 QNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpA 495
Cdd:cd05904 400 DGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQV-A 478
|
490 500
....*....|....*....|....*.
gi 24653035 496 TQKQLRAgVQFTDKLPANVNGKTMRK 521
Cdd:cd05904 479 PYKKVRK-VAFVDAIPKSPSGKILRK 503
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
42-517 |
7.85e-71 |
|
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: 232.89 E-value: 7.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 42 PKNVCQICDvdGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTH 121
Cdd:cd17631 9 PDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 122 VFSITKPTLIFcdgqeydkvhkatvgwhpeiltltdhvegvqgietlldptttekiyqpevlkeggDQTVAILCSSGTTG 201
Cdd:cd17631 87 ILADSGAKVLF-------------------------------------------------------DDLALLMYTSGTTG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 202 LPKAVCIS---------NSILIQDsmlITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKI 272
Cdd:cd17631 112 RPKGAMLThrnllwnavNALAALD---LGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 273 NYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQElcKTAMFNSGYGMTE-VGAITINIG---ISNVS 348
Cdd:cd17631 189 TSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA--RGVKFVQGYGMTEtSPGVTFLSPedhRRKLG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 349 SAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR-MQDfeGWFHTGDLGYFDEQNFLYIVDRKKE 427
Cdd:cd17631 267 SAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAaFRD--GWFHTGDLGRLDEDGYLYIVDRKKD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 428 ILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPA--TQKQlragVQ 505
Cdd:cd17631 345 MIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARykIPKS----VE 420
|
490
....*....|..
gi 24653035 506 FTDKLPANVNGK 517
Cdd:cd17631 421 FVDALPRNATGK 432
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
24-525 |
6.69e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 219.67 E-value: 6.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 24 YNYDTSVGKIIFNNMKNWPKNVcqICDVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMN 103
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKE--AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 104 GTPFHSVN----P-----VLDDAtlthvfsitKPTLIFCDGQ---EYDKVHKA--TVgwhPEILTLTD-----HVEGVQG 164
Cdd:PRK06187 80 GAVLHPINirlkPeeiayILNDA---------EDRVVLVDSEfvpLLAAILPQlpTV---RTVIVEGDgpaapLAPEVGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 165 IETLLDPTTTEKIyQPEVlkegGDQTVAILC-SSGTTGLPKAVCIS------NSILIQDSMLITSQSVIYVGSCLDWITG 237
Cdd:PRK06187 148 YEELLAAASDTFD-FPDI----DENDAAAMLyTSGTTGHPKGVVLShrnlflHSLAVCAWLKLSRDDVYLVIVPMFHVHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 238 LWAFVFSTVFGCTRIIsNKAFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRS 317
Cdd:PRK06187 223 WGLPYLALMAGAKQVI-PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 318 QELCKtAMFNSGYGMTEVG-AITIN-------IGISNVSSAGRPVPGIKIRIVDEDGKSL--GYNQVGEIYVHTGqaWN- 386
Cdd:PRK06187 302 KEKFG-IDLVQGYGMTETSpVVSVLppedqlpGQWTKRRSAGRPLPGVEARIVDDDGDELppDGGEVGEIIVRGP--WLm 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 387 -GYYGNPVETRR-MQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDERE 464
Cdd:PRK06187 379 qGYWNRPEATAEtIDG--GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKW 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653035 465 GDAAGALVVKSKGATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK06187 457 GERPVAVVVLKPGATLDAKELRAFLRGRL-AKFKLPKR-IAFVDELPRTSVGKILKRVLRE 515
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
52-431 |
7.38e-65 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 216.79 E-value: 7.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGQEYDKVHKATVGWHPEI-LTLTDHVEGVQGIETLLDPTTTEKIYQPEVLKEGGDQTVAILCSSGTTGLPKAVCIS- 209
Cdd:pfam00501 98 ITDDALKLEELLEALGKLEVVkLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTh 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 ----NSILIQDSMLITSQSV---IYVGSCLD--WITGLWAFVFSTVF-GCTRIISNK--AFTPEYFVGLVKKYKINYAVL 277
Cdd:pfam00501 178 rnlvANVLSIKRVRPRGFGLgpdDRVLSTLPlfHDFGLSLGLLGPLLaGATVVLPPGfpALDPAALLELIERYKVTVLYG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 278 PPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNsGYGMTEVGAITINIG-----ISNVSSAGR 352
Cdd:pfam00501 258 VPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVN-GYGLTETTGVVTTPLpldedLRSLGSVGR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 353 PVPGIKIRIVDED-GKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKY 431
Cdd:pfam00501 337 PLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
34-524 |
3.31e-56 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 196.74 E-value: 3.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 34 IFNNMKNWPKNVCQICDVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPV 113
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 114 LDDATLTHVFSITKPTLIFCDGQEYDKVHKATVGWHPEILTLTDHVEGVQGIETLLDPTTTEkiyQPEVlKEGGDQTVAI 193
Cdd:PLN02246 109 YTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENE---LPEV-EISPDDVVAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 194 LCSSGTTGLPKAVcisnsILIQDSmLITS--QSV-----------------------IYvgsCLDWI--TGLWAfvfstv 246
Cdd:PLN02246 185 PYSSGTTGLPKGV-----MLTHKG-LVTSvaQQVdgenpnlyfhsddvilcvlpmfhIY---SLNSVllCGLRV------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 247 fGCTRIISNKaFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGgsislATLQRsqELCKT--- 323
Cdd:PLN02246 250 -GAAILIMPK-FEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGA-----APLGK--ELEDAfra 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 324 ----AMFNSGYGMTEVG-AITINIGISN------VSSAGRPVPGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGN 391
Cdd:PLN02246 321 klpnAVLGQGYGMTEAGpVLAMCLAFAKepfpvkSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 392 PVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGAL 471
Cdd:PLN02246 401 PEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAF 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24653035 472 VVKSKGATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTAR 524
Cdd:PLN02246 481 VVRSNGSEITEDEIKQFVAKQV-VFYKRIHK-VFFVDSIPKAPSGKILRKDLR 531
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
52-521 |
5.09e-55 |
|
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: 192.01 E-value: 5.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:cd05936 21 MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDgqeydkvhkatvgwhpeiLTLTDHVEGvqgietlldPTTTEKIYQPEvlkegGDQTVAILCSSGTTGLPKAVcisns 211
Cdd:cd05936 101 IVA------------------VSFTDLLAA---------GAPLGERVALT-----PEDVAVLQYTSGTTGVPKGA----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 212 ILIQDSMLI-TSQSVIYVGSCLD----------------WITGLWAFVFstvFGCTRIISNKaFTPEYFVGLVKKYKINY 274
Cdd:cd05936 144 MLTHRNLVAnALQIKAWLEDLLEgddvvlaalplfhvfgLTVALLLPLA---LGATIVLIPR-FRPIGVLKEIRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 275 AVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQEL--CKTAmfnSGYGMTEVG-AITIN-IGISNVS-S 349
Cdd:cd05936 220 FPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELtgVPIV---EGYGLTETSpVVAVNpLDGPRKPgS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 350 AGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET-RRMQDfeGWFHTGDLGYFDEQNFLYIVDRKKEI 428
Cdd:cd05936 297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETaEAFVD--GWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 429 LKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPAtQKQLRAgVQFTD 508
Cdd:cd05936 375 IIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAG-YKVPRQ-VEFRD 452
|
490
....*....|...
gi 24653035 509 KLPANVNGKTMRK 521
Cdd:cd05936 453 ELPKSAVGKILRR 465
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
67-530 |
2.86e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 185.91 E-value: 2.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNS-TYVMpLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDGQEYDKVHKA- 144
Cdd:PRK08316 48 RVAAALLDLGLKKGDRVAALGHNSdAYAL-LWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 145 ------TVGWHPeILTLTDHVEGVQGIETLLDPTTTEkiyQPEVLKEGGDqTVAILCSSGTTGLPKAVCISNSILIQD-- 216
Cdd:PRK08316 127 allpvdTLILSL-VLGGREAPGGWLDFADWAEAGSVA---EPDVELADDD-LAQILYTSGTESLPKGAMLTHRALIAEyv 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 217 SMLIT---SQSVIYVGS-----C--LDWITGLWAFVfstvfGCTRIISNKAfTPEYFVGLVKKYKINYAVLPPRHLSALI 286
Cdd:PRK08316 202 SCIVAgdmSADDIPLHAlplyhCaqLDVFLGPYLYV-----GATNVILDAP-DPELILRTIEAERITSFFAPPTVWISLL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 287 TCPDAKPDALAPITHLNYGGGSISLATLQRSQE-LCKTAMFNSgYGMTEVGAITINIG----ISNVSSAGRPVPGIKIRI 361
Cdd:PRK08316 276 RHPDFDTRDLSSLRKGYYGASIMPVEVLKELRErLPGLRFYNC-YGQTEIAPLATVLGpeehLRRPGSAGRPVLNVETRV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 362 VDEDGKSLGYNQVGEIyVHTG-QAWNGYYGNPVETRR-MQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPT 439
Cdd:PRK08316 355 VDDDGNDVAPGEVGEI-VHRSpQLMLGYWDDPEKTAEaFRG--GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 440 EIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPA--TQKQlragVQFTDKLPANVNGK 517
Cdd:PRK08316 432 EVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGfkVPKR----VIFVDELPRNPSGK 507
|
490
....*....|...
gi 24653035 518 TMRKTARDVFVAL 530
Cdd:PRK08316 508 ILKRELRERYAGA 520
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
57-520 |
3.43e-51 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 182.37 E-value: 3.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 57 TFEQGLTWSIRIAQYLKKR-GLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDg 135
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 136 qeydkvhkatvgwhPEILTLTDHVEGVQGIETLLDPTTTEKIYQPEV--LKEGGDQTVAILC-SSGTTGLPKAvcisnSI 212
Cdd:PRK06839 108 --------------KTFQNMALSMQKVSYVQRVISITSLKEIEDRKIdnFVEKNESASFIICyTSGTTGKPKG-----AV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 213 LIQDSML-----------ITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKINYAVLPPRH 281
Cdd:PRK06839 169 LTQENMFwnalnntfaidLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 282 LSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQElcKTAMFNSGYGMTEVGAITINIGISN----VSSAGRPVPGI 357
Cdd:PRK06839 249 HQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID--RGFLFGQGFGMTETSPTVFMLSEEDarrkVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 358 KIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR-MQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHY 436
Cdd:PRK06839 327 DYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEEtIQD--GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 437 WPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQKQLRAGVqFTDKLPANVNG 516
Cdd:PRK06839 405 YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFL-AKYKIPKEIV-FLKELPKNATG 482
|
....
gi 24653035 517 KTMR 520
Cdd:PRK06839 483 KIQK 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
57-524 |
3.94e-51 |
|
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: 180.57 E-value: 3.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 57 TFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgq 136
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 137 eydkvhkatvgwhpeiltltdhvegvqgietlldptttekiyqpevlkeggdqTVAILCSSGTTGLPKAVCISNS----- 211
Cdd:cd05934 83 -----------------------------------------------------PASILYTSGTTGPPKGVVITHAnltfa 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 212 -ILIQDSMLITSQSVIYV--------GSCLDWITGLWAfvfstvfGCTRIISNKaFTPEYFVGLVKKYKINYAVLPPRHL 282
Cdd:cd05934 110 gYYSARRFGLGEDDVYLTvlplfhinAQAVSVLAALSV-------GATLVLLPR-FSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 283 SALITCPDAKPDALAPItHLNYGGGsislATLQRSQELCKTamFN----SGYGMTEVGAITIN-IGISNV-SSAGRPVPG 356
Cdd:cd05934 182 SYLLAQPPSPDDRAHRL-RAAYGAP----NPPELHEEFEER--FGvrllEGYGMTETIVGVIGpRDEPRRpGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 357 IKIRIVDEDGKSLGYNQVGEIYVHTGQAW---NGYYGNPVETR-RMQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYN 432
Cdd:cd05934 255 YEVRIVDDDGQELPAGEPGELVIRGLRGWgffKGYYNMPEATAeAMRN--GWFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 433 GLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPAtqKQLRAGVQFTDKLPA 512
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY--FKVPRYIRFVDDLPK 410
|
490
....*....|..
gi 24653035 513 NVNGKTMRKTAR 524
Cdd:cd05934 411 TPTEKVAKAQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
48-525 |
4.39e-50 |
|
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: 179.43 E-value: 4.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 48 ICDVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLGVAclMNGTPFHSVNPVLDDATLTHVFSI 125
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGleFVVAFLAAA--RAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 126 TKPTLIFCDGQEYDKVHKATVgwHPEILTLTDHVEGVQGIETL-------LDPTTTEKIYQPEVLkegGDQTVAILCSSG 198
Cdd:cd05926 85 LGSKLVLTPKGELGPASRAAS--KLGLAILELALDVGVLIRAPsaeslsnLLADKKNAKSEGVPL---PDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 199 TTGLPKAVCISNSIL------IQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKI 272
Cdd:cd05926 160 TTGRPKGVPLTHRNLaasatnITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 273 N-YAVLPPRHlSALITCPDAKP-DALAPITHLNYGGGSISLATLQRSQELCKTAMFNSgYGMTEVG-AIT---INIGISN 346
Cdd:cd05926 240 TwYTAVPTIH-QILLNRPEPNPeSPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEA-YGMTEAAhQMTsnpLPPGPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 347 VSSAGRPVpGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKK 426
Cdd:cd05926 318 PGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 427 EILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQKQLRAgVQF 506
Cdd:cd05926 397 ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL-AAFKVPKK-VYF 474
|
490
....*....|....*....
gi 24653035 507 TDKLPANVNGKTMRKTARD 525
Cdd:cd05926 475 VDELPKTATGKIQRRKVAE 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
187-517 |
1.46e-49 |
|
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: 176.42 E-value: 1.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 187 GDQTVAILCSSGTTGLPKAVCIS-NSILIQDSMLI-----TSQSVIYVGSCLDWITG-LWAFVFSTVFGcTRIISNKAFT 259
Cdd:cd05903 92 PDAVALLLFTSGTTGEPKGVMHShNTLSASIRQYAerlglGPGDVFLVASPMAHQTGfVYGFTLPLLLG-APVVLQDIWD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 260 PEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQElCKTAMFNSGYGMTEVGAIT 339
Cdd:cd05903 171 PDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAE-LLGAKVCSAYGSTECPGAV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 340 INIGISNVSSA----GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRmQDFEGWFHTGDLGYFDE 415
Cdd:cd05903 250 TSITPAPEDRRlytdGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-AAPEGWFRTGDLARLDE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 416 QNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPA 495
Cdd:cd05903 329 DGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVA 408
|
330 340
....*....|....*....|..
gi 24653035 496 TQKqLRAGVQFTDKLPANVNGK 517
Cdd:cd05903 409 KQY-WPERLVHVDDLPRTPSGK 429
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
69-525 |
2.96e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 177.39 E-value: 2.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 69 AQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgQEYDkvhkATVGW 148
Cdd:PRK06145 41 AGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVD-EEFD----AIVAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 149 HPEILTLTDHVEgvQGIETLLDPTTTekiyQPEVLKEGGDQTVAILCSSGTTGLPKAVCIS------NSI-------LIQ 215
Cdd:PRK06145 116 ETPKIVIDAAAQ--ADSRRLAQGGLE----IPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSygnlhwKSIdhvialgLTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 216 DSMLITSQSVIYVGSC-LDWITGLWafvfstVFGCTRIISNkaFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPD 294
Cdd:PRK06145 190 SERLLVVGPLYHVGAFdLPGIAVLW------VGGTLRIHRE--FDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 295 ALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEV--GAITINIG--ISNVSSAGRPVPGIKIRIVDEDGKSLG 370
Cdd:PRK06145 262 DLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETcsGDTLMEAGreIEKIGSTGRALAHVEIRIADGAGRWLP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 371 YNQVGEIYVHTGQAWNGYYGNPVETRRmQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQ 450
Cdd:PRK06145 342 PNMKGEICMRGPKVTKGYWKDPEKTAE-AFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPE 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653035 451 VQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPA--TQKQLRagvqFTDKLPANVNGKTMRKTARD 525
Cdd:PRK06145 421 VAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASfkVPRQLK----VRDELPRNPSGKVLKRVLRD 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
187-525 |
3.41e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 177.40 E-value: 3.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 187 GDQTVAILCSSGTTGLPKAVCISnsiliQDSMLITSQSViyvGSCLDWITG---LWAFVFSTVFGCT-----------RI 252
Cdd:PRK07656 165 PDDVADILFTSGTTGRPKGAMLT-----HRQLLSNAADW---AEYLGLTEGdryLAANPFFHVFGYKagvnaplmrgaTI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 253 ISNKAFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGM 332
Cdd:PRK07656 237 LPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 333 TEV-GAITIN-IGISNV---SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHT 407
Cdd:PRK07656 317 SEAsGVTTFNrLDDDRKtvaGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHT 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 408 GDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVE 487
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIA 476
|
330 340 350
....*....|....*....|....*....|....*...
gi 24653035 488 HVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK07656 477 YCREHL-AKYKVPRS-IEFLDELPKNATGKVLKRALRE 512
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
50-526 |
3.57e-49 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 178.38 E-value: 3.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 50 DVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLgvACLMNGTPFHSVNPVLDDATLTHVFSITK 127
Cdd:COG0365 34 DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIpeAVIAML--ACARIGAVHSPVFPGFGAEALADRIEDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 128 PTLIFCD--GQEYDKVH--KATVgwhPEILTLTDHVEGVQGIETLLDPTTTEKIYQPEVLKEGGDQTVA----------- 192
Cdd:COG0365 112 AKVLITAdgGLRGGKVIdlKEKV---DEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEFEpeptdaddplf 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVCISNS-ILIQDSML------ITSQSVIY----VGscldWITGLWAFVFST-VFGCTRII---SNKA 257
Cdd:COG0365 189 ILYTSGTTGKPKGVVHTHGgYLVHAATTakyvldLKPGDVFWctadIG----WATGHSYIVYGPlLNGATVVLyegRPDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 258 FTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDA--LAPITHLNYGGGSISLATLQRSQELCKTAMfNSGYGMTEV 335
Cdd:COG0365 265 PDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydLSSLRLLGSAGEPLNPEVWEWWYEAVGVPI-VDGWGQTET 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 336 GAITI-NIGISNV--SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVH---TGQAwNGYYGNPVETRR--MQDFEGWFHT 407
Cdd:COG0365 344 GGIFIsNLPGLPVkpGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKgpwPGMF-RGYWNDPERYREtyFGRFPGWYRT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 408 GDLGYFDEQNFLYIVDRKKEILKYNGlhYW--PTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---A 482
Cdd:COG0365 423 GDGARRDEDGYFWILGRSDDVINVSG--HRigTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelA 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24653035 483 KEIVEHVAKRLPAtQKQLRAgVQFTDKLPANVNGKTMRKTARDV 526
Cdd:COG0365 501 KELQAHVREELGP-YAYPRE-IEFVDELPKTRSGKIMRRLLRKI 542
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
48-521 |
6.91e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 177.04 E-value: 6.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 48 ICDVDGvTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNST-YVMPLgVACLMNGTPFHSVNPVLDDATLTHVFSIT 126
Cdd:PRK07788 68 LIDERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRgFVLAL-YAAGKVGARIILLNTGFSGPQLAEVAARE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 127 KPTLIFCDgQEYDKVHKATVGWHPEILTLTDHVE-------GVQGIETLLDPTTTEKIYQPEvlKEGGdqtvAILCSSGT 199
Cdd:PRK07788 146 GVKALVYD-DEFTDLLSALPPDLGRLRAWGGNPDddepsgsTDETLDDLIAGSSTAPLPKPP--KPGG----IVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 200 TGLPKAVCISN-SILIQDSMLIT-----SQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKaFTPEYFVGLVKKYKIN 273
Cdd:PRK07788 219 TGTPKGAPRPEpSPLAPLAGLLSrvpfrAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRR-FDPEATLEDIAKHKAT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 274 YAVLPPRHLSALItcpDAKPDALApithlNYGGGS---ISLATLQRSQELCKTAMFNSG------YGMTEVGAITI---- 340
Cdd:PRK07788 298 ALVVVPVMLSRIL---DLGPEVLA-----KYDTSSlkiIFVSGSALSPELATRALEAFGpvlynlYGSTEVAFATIatpe 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 341 NIGIsNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGnpveTRRMQDFEGWFHTGDLGYFDEQNFLY 420
Cdd:PRK07788 370 DLAE-APGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD----GRDKQIIDGLLSSGDVGYFDEDGLLF 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 421 IVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQKQL 500
Cdd:PRK07788 445 VDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNL-ARYKVP 523
|
490 500
....*....|....*....|.
gi 24653035 501 RAgVQFTDKLPANVNGKTMRK 521
Cdd:PRK07788 524 RD-VVFLDELPRNPTGKVLKR 543
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
27-525 |
1.01e-46 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 171.32 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 27 DTSVGKIIFNNMKNWPKNVCQICDVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKN-STY-VMPLGVacLMNG 104
Cdd:PLN02330 27 KLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNvAEYgIVALGI--MAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 105 TPFHSVNPVLDDATLTHVFSITKPTLIFCDGQEYDKVHKATVgwhPEILTLTDHVEGVQGIETLL-------DPTTTEKI 177
Cdd:PLN02330 105 GVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGL---PVIVLGEEKIEGAVNWKELLeaadragDTSDNEEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 178 YQPEVlkeggdqtVAILCSSGTTGLPKAVCISNSILIQDsmliTSQSVIYVGS-CLDWITGLWAFVFSTVFG----CTRI 252
Cdd:PLN02330 182 LQTDL--------CALPFSSGTTGISKGVMLTHRNLVAN----LCSSLFSVGPeMIGQVVTLGLIPFFHIYGitgiCCAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 253 ISNKA-------FTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLAT--LQRSQELCKT 323
Cdd:PLN02330 250 LRNKGkvvvmsrFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPelLTAFEAKFPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 324 AMFNSGYGMTEVGAITIN-------IGISNVSSAGRPVPGIKIRIVDED-GKSLGYNQVGEIYVHTGQAWNGYYGNPVET 395
Cdd:PLN02330 330 VQVQEAYGLTEHSCITLThgdpekgHGIAKKNSVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEET 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 396 RRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKS 475
Cdd:PLN02330 410 DRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVIN 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24653035 476 KGATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PLN02330 490 PKAKESEEDILNFVAANV-AHYKKVRV-VQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
52-524 |
3.75e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 160.92 E-value: 3.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYV-MPLGVACLMnGTPFHSVNP---------VLDDATLTh 121
Cdd:PRK06188 34 GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVlMAIGAAQLA-GLRRTALHPlgslddhayVLEDAGIS- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 122 vfsitkpTLIFCDG--QEYDKVHKATVGWHPEILTLTDhVEGVQGIETLLDPtttekiYQPEVLKEGGDQT--VAILCSS 197
Cdd:PRK06188 112 -------TLIVDPApfVERALALLARVPSLKHVLTLGP-VPDGVDLLAAAAK------FGPAPLVAAALPPdiAGLAYTG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 198 GTTGLPKAVcisnsiliqdsmLITSQSViyvGSCLDWITGLW-------------------AFVFSTVFGCTRIISNKAF 258
Cdd:PRK06188 178 GTTGKPKGV------------MGTHRSI---ATMAQIQLAEWewpadprflmctplshaggAFFLPTLLRGGTVIVLAKF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 259 TPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKtAMFNSGYGMTEVG-A 337
Cdd:PRK06188 243 DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFG-PIFAQYYGQTEAPmV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 338 ITINIGISNV-------SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMqdFE-GWFHTGD 409
Cdd:PRK06188 322 ITYLRKRDHDpddpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEA--FRdGWLHTGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 410 LGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHV 489
Cdd:PRK06188 400 VAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHV 479
|
490 500 510
....*....|....*....|....*....|....*..
gi 24653035 490 --AKRLPATQKQlragVQFTDKLPANVNGKTMRKTAR 524
Cdd:PRK06188 480 keRKGSVHAPKQ----VDFVDSLPLTALGKPDKKALR 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
196-521 |
4.82e-43 |
|
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: 158.80 E-value: 4.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKAVCISNSILIQDSMlitSQSVIYVGSCLDWITGLWAFVFST---------VFGCTRIISNKAFTPEYFVGL 266
Cdd:cd05935 92 TSGTTGLPKGCMHTHFSAAANAL---QSAVWTGLTPSDVILACLPLFHVTgfvgslntaVYVGGTYVLMARWDRETALEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 267 VKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELckTAM-FNSGYGMTEVGA-ITIN-IG 343
Cdd:cd05935 169 IEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKL--TGLrFVEGYGLTETMSqTHTNpPL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 344 ISNVSSAGRPVPGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRrmqdfEGW--------FHTGDLGYFD 414
Cdd:cd05935 247 RPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETE-----ESFieikgrrfFRTGDLGYMD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 415 EQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKG--ATISAKEIVEHVAKR 492
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQ 401
|
330 340
....*....|....*....|....*....
gi 24653035 493 LpATQKQLRAgVQFTDKLPANVNGKTMRK 521
Cdd:cd05935 402 M-AAYKYPRE-VEFVDELPRSASGKILWR 428
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
164-521 |
3.29e-42 |
|
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: 155.97 E-value: 3.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 164 GIETLL---DPTTTEKIYQPEVLKEGGDQTVAILCSSGTTGLPKAVCIS------NSILIQDSMLITSQSVIYVGSCLDW 234
Cdd:cd05912 50 GAEAVLlntRLTPNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTfgnhwwSAIGSALNLGLTEDDNWLCALPLFH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 235 ITGLWAFVFSTVFGCTRIISNKaFTPEYFVGLVKKYKINYAVLPPRHLSALIT-CPDAKPDALAPIThlnYGGGSISLAT 313
Cdd:cd05912 130 ISGLSILMRSVIYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQRLLEiLGEGYPNNLRCIL---LGGGPAPKPL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 314 LQRSQELcKTAMFNSgYGMTE----VGAITINIGISNVSSAGRPVPGIKIRIVDEDGKSlgyNQVGEIYVHTGQAWNGYY 389
Cdd:cd05912 206 LEQCKEK-GIPVYQS-YGMTEtcsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 390 GNPVETRrmQDFE-GWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAA 468
Cdd:cd05912 281 NRPDATE--ESFEnGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVP 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24653035 469 GALVVKSKgaTISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRK 521
Cdd:cd05912 359 VAFVVSER--PISEEELIAYCSEKL-AKYKVPKK-IYFVDELPRTASGKLLRH 407
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
188-525 |
3.52e-42 |
|
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: 156.34 E-value: 3.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVCISNSILIqdSMLITSQSVIYVG--------SCLDWITGLWAFVFST-VFGCTRIISN-KA 257
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPL--GHIPTAAYWLGLRpddihwniADPGWAKGAWSSFFGPwLLGATVFVYEgPR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 258 FTPEYFVGLVKKYKINYAVLPPRHLSALITcPDAKPDALAPITHLNYGGGSISLATLQRSQElcKTAM-FNSGYGMTEVG 336
Cdd:cd05972 159 FDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRA--ATGLpIRDGYGQTETG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 337 AItinigISNVS-------SAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTG--QAWNGYYGNPvetRRMQDF--EGWF 405
Cdd:cd05972 236 LT-----VGNFPdmpvkpgSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPppGLFLGYVGDP---EKTEASirGDYY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 406 HTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---A 482
Cdd:cd05972 308 LTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelA 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24653035 483 KEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd05972 388 EELQGHVKKVL-APYKYPRE-IEFVEELPKTISGKIRRVELRD 428
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
76-533 |
4.46e-41 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 155.77 E-value: 4.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 76 GLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCdgqEYDKVHKATVGWHPEILTL 155
Cdd:PLN02574 88 GVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT---SPENVEKLSPLGVPVIGVP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 156 TDHVEGVQGIEtllDPTTTEKIY-QPEVLKE---GGDQTVAILCSSGTTGLPKAVCISNSILIQDSMLI----------T 221
Cdd:PLN02574 165 ENYDFDSKRIE---FPKFYELIKeDFDFVPKpviKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeasqyeyP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 222 SQSVIYVGSC-LDWITGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKI-NYAVLPPRhLSALITcpDAKPDALAPI 299
Cdd:PLN02574 242 GSDNVYLAALpMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVtHFPVVPPI-LMALTK--KAKGVCGEVL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 300 THL---NYGGGSISLATLQRSQELCKTAMFNSGYGMTE---VGAITINI-GISNVSSAGRPVPGIKIRIVD-EDGKSLGY 371
Cdd:PLN02574 319 KSLkqvSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTEstaVGTRGFNTeKLSKYSSVGLLAPNMQAKVVDwSTGCLLPP 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 372 NQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQV 451
Cdd:PLN02574 399 GNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 452 QDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARDVFVALR 531
Cdd:PLN02574 479 IDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQV-APYKKVRK-VVFVQSIPKSPAGKILRRELKRSLTNSV 556
|
..
gi 24653035 532 VS 533
Cdd:PLN02574 557 SS 558
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
235-520 |
1.16e-40 |
|
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: 149.73 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 235 ITGLwaFVFSTVF--GCTRIISNKaFTPEYFVGLVKKYKINY-AVLPPRhLSALITCPDAKPDALAPITHLnygGGSISL 311
Cdd:cd17637 53 IAGL--NLALATFhaGGANVVMEK-FDPAEALELIEEEKVTLmGSFPPI-LSNLLDAAEKSGVDLSSLRHV---LGLDAP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 312 ATLQRSQELCKtAMFNSGYGMTEV-GAITINIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYG 390
Cdd:cd17637 126 ETIQRFEETTG-ATFWSLYGQTETsGLVTLSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 391 NPVETRrmQDF-EGWFHTGDLGYFDEQNFLYIVDRK--KEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDA 467
Cdd:cd17637 205 LPELTA--YTFrNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEG 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24653035 468 AGALVVKSKGATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMR 520
Cdd:cd17637 283 IKAVCVLKPGATLTADELIEFVGSRI-ARYKKPRY-VVFVEALPKTADGSIDR 333
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
67-531 |
2.79e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 152.27 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgqeyDKVHKATv 146
Cdd:PRK09088 34 RLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD----DAVAAGR- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 147 gwhPEILTLTDHVEGVQGietlLDPTTTEKIyqpevlkeGGDQTVAILCSSGTTGLPKAVCISNSILIQDSM------LI 220
Cdd:PRK09088 109 ---TDVEDLAAFIASADA----LEPADTPSI--------PPERVSLILFTSGTSGQPKGVMLSERNLQQTAHnfgvlgRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 221 TSQSVIYVGSCLDWITGLWAFVFSTVF-GCTRIISNkAFTPEYFVGLV--KKYKINYAVLPPRHLSALITCPDAKPDALA 297
Cdd:PRK09088 174 DAHSSFLCDAPMFHIIGLITSVRPVLAvGGSILVSN-GFEPKRTLGRLgdPALGITHYFCVPQMAQAFRAQPGFDAAALR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 298 PITHLnYGGGSISLATLQRSQeLCKTAMFNSGYGMTEVGAI---TINIGI--SNVSSAGRPVPGIKIRIVDEDGKSLGYN 372
Cdd:PRK09088 253 HLTAL-FTGGAPHAAEDILGW-LDDGIPMVDGFGMSEAGTVfgmSVDCDVirAKAGAAGIPTPTVQTRVVDDQGNDCPAG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 373 QVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQ 452
Cdd:PRK09088 331 VPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIR 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653035 453 DVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpaTQKQLRAGVQFTDKLPANVNGKTMRKTARDVFVALR 531
Cdd:PRK09088 411 ECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRL--AKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-517 |
7.47e-40 |
|
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: 147.81 E-value: 7.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVC------ISNSILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTV-FGCTRIISNKAFTP 260
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATlthhniVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLtHGATMVFPSPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 261 EYFVGLVKKYK--INYAVlpPRHLSALITCPDakpDALAPITHLNYG---GGSISLATLQRSQELCKTAMFNSGYGMTEV 335
Cdd:cd05917 82 LAVLEAIEKEKctALHGV--PTMFIAELEHPD---FDKFDLSSLRTGimaGAPCPPELMKRVIEVMNMKDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 336 GAITINIGI-----SNVSSAGRPVPGIKIRIVDEDGKS-LGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGD 409
Cdd:cd05917 157 SPVSTQTRTddsieKRVNTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 410 LGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHV 489
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYC 316
|
330 340
....*....|....*....|....*...
gi 24653035 490 AKRLpATQKQLRAgVQFTDKLPANVNGK 517
Cdd:cd05917 317 KGKI-AHYKVPRY-VFFVDEFPLTVSGK 342
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
67-520 |
1.10e-39 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 151.44 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIgiaaknsTYVMP-------LGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgqeyD 139
Cdd:PRK06087 61 RLANWLLAKGIEPGDRV-------AFQLPgwceftiIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP----T 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 140 KVHKATvgWHPEILTLTDHVEGVQGIeTLLD---PTTTEKIYQpEVLKEG----------GDQTVAILCSSGTTGLPKAV 206
Cdd:PRK06087 130 LFKQTR--PVDLILPLQNQLPQLQQI-VGVDklaPATSSLSLS-QIIADYeplttaitthGDELAAVLFTSGTEGLPKGV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 207 CIS-NSILIQD-----SMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKINYAVLPPR 280
Cdd:PRK06087 206 MLThNNILASEraycaRLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 281 HLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQE----LCktamfnSGYGMTE-VGAITINIGIS---NVSSAGR 352
Cdd:PRK06087 286 FIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQrgikLL------SVYGSTEsSPHAVVNLDDPlsrFMHTDGY 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 353 PVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYN 432
Cdd:PRK06087 360 AAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 433 GLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVV-KSKGATISAKEIVEHVA-KRLPATQKQLRagVQFTDKL 510
Cdd:PRK06087 440 GENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHSLTLEEVVAFFSrKRVAKYKYPEH--IVVIDKL 517
|
490
....*....|
gi 24653035 511 PANVNGKTMR 520
Cdd:PRK06087 518 PRTASGKIQK 527
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
67-524 |
1.20e-39 |
|
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: 149.90 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKD-VIGIAAKNSTYVmPLGVACLMNGTP----FHSVNPVLDDATLTHVFSITKPTLIFCDGQEYDKV 141
Cdd:cd05922 5 AAASALLEAGGVRGErVVLILPNRFTYI-ELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 142 HKATVGWHPEILTLTdhVEGVQGIETLLDPTTTEKiyqpevlkeggDQTVAILCSSGTTGLPKAV------CISNSILIQ 215
Cdd:cd05922 84 RDALPASPDPGTVLD--ADGIRAARASAPAHEVSH-----------EDLALLLYTSGSTGSPKLVrlshqnLLANARSIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 216 DSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKIN-YAVLPprHLSALITCPDAKPD 294
Cdd:cd05922 151 EYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATgLAGVP--STYAMLTRLGFDPA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 295 ALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEVGAITINIGISNV----SSAGRPVPGIKIRIVDEDGKSLG 370
Cdd:cd05922 229 KLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERIlekpGSIGLAIPGGEFEILDDDGTPTP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 371 YNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQ 450
Cdd:cd05922 309 PGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653035 451 VQDVCVVGiyDEREGDAAGALVVKSKgATISAKEIVEHVAKRLPATqkQLRAGVQFTDKLPANVNGKTMRKTAR 524
Cdd:cd05922 389 IIEAAAVG--LPDPLGEKLALFVTAP-DKIDPKDVLRSLAERLPPY--KVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
67-525 |
3.59e-39 |
|
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: 149.70 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNST--YVMPLGVACLmnGTPFHSVNP------------------VLDDATLTHVFSIT 126
Cdd:cd12119 37 RLANALRRLGVKPGDRVATLAWNTHrhLELYYAVPGM--GAVLHTINPrlfpeqiayiinhaedrvVFVDRDFLPLLEAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 127 KPTLifcdgqeyDKVHKATVGWHPEILTLtDHVEGVQGIETLLDPTTTEKIYqPEVlKEGgdqTVAILC-SSGTTGLPKA 205
Cdd:cd12119 115 APRL--------PTVEHVVVMTDDAAMPE-PAGVGVLAYEELLAAESPEYDW-PDF-DEN---TAAAICyTSGTTGNPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 206 VCISNSILIQDSMLITSQSVIYVGScLDWITGL--------WAFVFSTV-FGCTRIISNKAFTPEYFVGLVKKYKINYAV 276
Cdd:cd12119 181 VVYSHRSLVLHAMAALLTDGLGLSE-SDVVLPVvpmfhvnaWGLPYAAAmVGAKLVLPGPYLDPASLAELIEREGVTFAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 277 LPPRHLSALITCPDAKPDALAPITHLNYGGGSISLAtlqrsqeLCKTAM-----FNSGYGMTEVGAI-TINIGISNVS-- 348
Cdd:cd12119 260 GVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRS-------LIEAFEergvrVIHAWGMTETSPLgTVARPPSEHSnl 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 349 ----------SAGRPVPGIKIRIVDEDGKSL--GYNQVGEIYVHTgqAW--NGYYGNPVETRRMQDfEGWFHTGDLGYFD 414
Cdd:cd12119 333 sedeqlalraKQGRPVPGVELRIVDDDGRELpwDGKAVGELQVRG--PWvtKSYYKNDEESEALTE-DGWLRTGDVATID 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 415 EQNFLYIVDRKKEILKYNGlhYW--PTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKR 492
Cdd:cd12119 410 EDGYLTITDRSKDVIKSGG--EWisSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADK 487
|
490 500 510
....*....|....*....|....*....|....
gi 24653035 493 LPatqK-QLRAGVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd12119 488 VA---KwWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
301-525 |
4.87e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 149.82 E-value: 4.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 301 HLNYGGG-SISLATLQRSQELCKTAMFnSGYGMTE----VGAITINIGISNvSSAGRPVPGIKIRIVDEDGKSLGYNQVG 375
Cdd:PRK08974 328 KLSVGGGmAVQQAVAERWVKLTGQYLL-EGYGLTEcsplVSVNPYDLDYYS-GSIGLPVPSTEIKLVDDDGNEVPPGEPG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 376 EIYVHTGQAWNGYYGNPVETRRMQDfEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVC 455
Cdd:PRK08974 406 ELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVA 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653035 456 VVGIYDEREGDAAGALVVKsKGATISAKEIVEHVAKRLpaTQKQLRAGVQFTDKLP-ANVnGKTMRKTARD 525
Cdd:PRK08974 485 AVGVPSEVSGEAVKIFVVK-KDPSLTEEELITHCRRHL--TGYKVPKLVEFRDELPkSNV-GKILRRELRD 551
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-517 |
5.54e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 146.74 E-value: 5.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 55 TVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTH--------VFSIT 126
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFmlkhaeskVLVVP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 127 KptlIFcdgQEYDkvHKATV-GWHPEILTLtDHV-----EGVQGIETLL-DPTTTEKIYQPEVLKE---GGDQTVAILCS 196
Cdd:PRK13295 135 K---TF---RGFD--HAAMArRLRPELPAL-RHVvvvggDGADSFEALLiTPAWEQEPDAPAILARlrpGPDDVTQLIYT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 197 SGTTGLPKAV------CISNSILIQDSMLITSQSVIYVGSCLDWITG-LWAFVFSTVFGCTRIISNkAFTPEYFVGLVKK 269
Cdd:PRK13295 206 SGTTGEPKGVmhtantLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAVLQD-IWDPARAAELIRT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 270 YKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFnSGYGMTEVGAIT-INIGISN-- 346
Cdd:PRK13295 285 EGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIV-SAWGMTENGAVTlTKLDDPDer 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 347 -VSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRrmQDFEGWFHTGDLGYFDEQNFLYIVDRK 425
Cdd:PRK13295 364 aSTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISGRS 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 426 KEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVE-----HVAKR-LPAtqkq 499
Cdd:PRK13295 442 KDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEflkaqKVAKQyIPE---- 517
|
490
....*....|....*...
gi 24653035 500 lRAGVQftDKLPANVNGK 517
Cdd:PRK13295 518 -RLVVR--DALPRTPSGK 532
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
305-525 |
1.17e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 146.06 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 305 GGGSISLATLQRSQELCKTAMFnSGYGMTEVGAI-TIN-IGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTG 382
Cdd:PRK05677 334 GGMALQLATAERWKEVTGCAIC-EGYGMTETSPVvSVNpSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 383 QAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDE 462
Cdd:PRK05677 413 QVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDE 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653035 463 REGDAAGALVVKSKGATISAKEIVEHVAKRLPAtQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK05677 493 KSGEAIKVFVVVKPGETLTKEQVMEHMRANLTG-YKVPKA-VEFRDELPTTNVGKILRRELRD 553
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
196-525 |
1.44e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 145.79 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKAVCISNSILIQDsMLITSQSVIYVGSCLDW----ITGLWAF----------VFSTVFGCTRIISNKAFTPE 261
Cdd:PRK08751 216 TGGTTGVAKGAMLTHRNLVAN-MQQAHQWLAGTGKLEEGcevvITALPLYhifaltanglVFMKIGGCNHLISNPRDMPG 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 262 yFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSgYGMTEVG-AITI 340
Cdd:PRK08751 295 -FVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEA-YGLTETSpAACI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 341 N-IGISNVS-SAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNF 418
Cdd:PRK08751 373 NpLTLKEYNgSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGF 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 419 LYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKsKGATISAKEIVEHVAKRLPAtQK 498
Cdd:PRK08751 453 VYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVK-KDPALTAEDVKAHARANLTG-YK 530
|
330 340
....*....|....*....|....*..
gi 24653035 499 QLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK08751 531 QPRI-IEFRKELPKTNVGKILRRELRD 556
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
53-521 |
5.88e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 144.03 E-value: 5.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 53 GVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNST--YVMPLGVacLMNGTPFHSVNPVLDDATLTHVFSITKPTL 130
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPqfHIVFFGI--LKLGAVHVPVSPLFREHELSYELNDAGAEV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 131 IFCDGQEYDKV----------HKATVGWH---PEILTL---------TDHVEGVQGIETLLDPTTTEKIYQPEVLkeggD 188
Cdd:PRK06178 134 LLALDQLAPVVeqvraetslrHVIVTSLAdvlPAEPTLplpdslrapRLAAAGAIDLLPALRACTAPVPLPPPAL----D 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 189 QTVAILCSSGTTGLPKAvCISNsiliQDSMLITSQSVIYVGSCLD------------WITGL-WAFVFSTVFGCTRIISN 255
Cdd:PRK06178 210 ALAALNYTGGTTGMPKG-CEHT----QRDMVYTAAAAYAVAVVGGedsvflsflpefWIAGEnFGLLFPLFSGATLVLLA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 256 KaFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLnyggGSISL------ATLQRSQELCKTAMFNSG 329
Cdd:PRK06178 285 R-WDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQV----RVVSFvkklnpDYRQRWRALTGSVLAEAA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 330 YGMTEV-GAITINIGIS----NVSSA----GRPVPGIKIRIVDED-GKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQ 399
Cdd:PRK06178 360 WGMTEThTCDTFTAGFQdddfDLLSQpvfvGLPVPGTEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 400 DfEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGAT 479
Cdd:PRK06178 440 R-DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGAD 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24653035 480 ISAKEIVEHVAKRLpATQK--QLRagvqFTDKLPANVNGKtMRK 521
Cdd:PRK06178 519 LTAAALQAWCRENM-AVYKvpEIR----IVDALPMTATGK-VRK 556
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
67-521 |
1.10e-36 |
|
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: 141.05 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgqeydkvhkatv 146
Cdd:TIGR01923 11 HLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 147 gwhpEILTLtdhvEGVQGIEtlLDPTTTEKIYQPEVLKE-GGDQTVAILCSSGTTGLPKAVCIS------NSILIQDSML 219
Cdd:TIGR01923 79 ----SLLEE----KDFQADS--LDRIEAAGRYETSLSASfNMDQIATLMFTSGTTGKPKAVPHTfrnhyaSAVGSKENLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 220 ITSQSVIYVGSCLDWITGLwAFVFSTVFGCTRIISNKAFTPeyFVGLVKKYKINYAVLPPRHLSALItcpdakpDALAPI 299
Cdd:TIGR01923 149 FTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQLNRLL-------DEGGHN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 300 THLN---YGGGSISLATLQRSQELcKTAMFNsGYGMTEVGA--ITINIGISN-VSSAGRPVPGIKIRIVDEDGKslgynQ 373
Cdd:TIGR01923 219 ENLRkilLGGSAIPAPLIEEAQQY-GLPIYL-SYGMTETCSqvTTATPEMLHaRPDVGRPLAGREIKIKVDNKE-----G 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 374 VGEIYVHTGQAWNGYYGNPvETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQD 453
Cdd:TIGR01923 292 HGEIMVKGANLMKGYLYQG-ELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQE 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653035 454 VCVVGIYDEREGDAAGALVVKSKgaTISAKEIV----EHVAK-RLPATqkqlragVQFTDKLPANVNGKTMRK 521
Cdd:TIGR01923 371 AVVVPKPDAEWGQVPVAYIVSES--DISQAKLIayltEKLAKyKVPIA-------FEKLDELPYNASGKILRN 434
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-520 |
1.67e-36 |
|
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: 138.40 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVCISN--SILI------------QDSMLITSQSVIYVGSCLDWITGLwafvfstVFGCTrIISNKAF 258
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHrqTLRAaaawadcadlteDDRYLIINPFFHTFGYKAGIVACL-------LTGAT-VVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 259 TPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEVGAI 338
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 339 TINIGISNV----SSAGRPVPGIKIRIVDEdgkslgynqvGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFD 414
Cdd:cd17638 157 TMCRPGDDAetvaTTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 415 EQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLp 494
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL- 305
|
330 340
....*....|....*....|....*.
gi 24653035 495 ATQKQLRAgVQFTDKLPANVNGKTMR 520
Cdd:cd17638 306 ANYKVPRF-VRFLDELPRNASGKVMK 330
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
160-529 |
1.90e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 142.22 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 160 EGVQGIETLLDPTTTEkiyqPEVLKEGGDQTVAILCSSGTTGLPKAVCISNSILIQDSM-------LITSQSVIYVGSCL 232
Cdd:PRK07786 150 DSVLGYEDLLAEAGPA----HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMtclrtngADINSDVGFVGVPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 233 DWITGLWAFVFSTVFGCTRII-SNKAFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALApITHLNYGGGSISL 311
Cdd:PRK07786 226 FHIAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASD 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 312 ATLQRSQELCKTAMFNSGYGMTEVGAITINI----GISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNG 387
Cdd:PRK07786 305 TLLRQMAATFPEAQILAAFGQTEMSPVTCMLlgedAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSG 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 388 YYGNPVETrrMQDFEG-WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGD 466
Cdd:PRK07786 385 YWNNPEAT--AEAFAGgWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGE 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653035 467 AAGALV-VKSKGATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARDVFVA 529
Cdd:PRK07786 463 VPVAVAaVRNDDAALTLEDLAEFLTDRL-ARYKHPKA-LEIVDALPRNPAGKVLKTELRERYGA 524
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
188-521 |
5.96e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 140.10 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVcisnsilIQdsmliTSQSVIY--VGSCLD--------W--------ITGLWAFVFSTVFGC 249
Cdd:PRK03640 141 DEVATIMYTSGTTGKPKGV-------IQ-----TYGNHWWsaVGSALNlglteddcWlaavpifhISGLSILMRSVIYGM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 250 TRIISNKaFTPEYFVGLVKKYKINYAVLPPRHLSALitcpdakpdaLAPITHLNY---------GGGSISLATLQRSQEL 320
Cdd:PRK03640 209 RVVLVEK-FDAEKINKLLQTGGVTIISVVSTMLQRL----------LERLGEGTYpssfrcmllGGGPAPKPLLEQCKEK 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 321 cKTAMFNSgYGMTE----VGAITINIGISNVSSAGRPVPGIKIRIVDeDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETR 396
Cdd:PRK03640 278 -GIPVYQS-YGMTEtasqIVTLSPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 397 R-MQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVks 475
Cdd:PRK03640 355 EtFQD--GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV-- 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24653035 476 KGATISAKEIVEHVAKRLpATQKqLRAGVQFTDKLPANVNGKTMRK 521
Cdd:PRK03640 431 KSGEVTEEELRHFCEEKL-AKYK-VPKRFYFVEELPRNASGKLLRH 474
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
182-525 |
7.30e-36 |
|
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: 139.10 E-value: 7.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 182 VLKEGGDQTVAILCSSGTTGLPKAVCISNSILIQD--------SMLITSQSVIYVGSCLDWITGLWAFVF-STVFGCTrI 252
Cdd:cd05971 82 LVTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHlpgvqfpfNLFPRDGDLYWTPADWAWIGGLLDVLLpSLYFGVP-V 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 253 ISNKA--FTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMfNSGY 330
Cdd:cd05971 161 LAHRMtkFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEV-NEFY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 331 GMTEVGAITIN---IGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQ--AWNGYYGNPVETR-RMQDfeGW 404
Cdd:cd05971 240 GQTECNLVIGNcsaLFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEkKMAG--DW 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 405 FHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS--- 481
Cdd:cd05971 318 LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdal 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24653035 482 AKEIVEHVAKRLPATQKQlRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd05971 398 AREIQELVKTRLAAHEYP-RE-IEFVNELPRTATGKIRRRELRA 439
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
53-521 |
1.72e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 139.78 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 53 GVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIF 132
Cdd:PRK06710 47 GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 133 CDGQEYDKVHKATVGWHPEILTLTDHVEGVQGIETLLDP-------------TTTEKIYQPEVLKEGGDQTVAILC---- 195
Cdd:PRK06710 127 CLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPfvqkkqsnlvvkvSESETIHLWNSVEKEVNTGVEVPCdpen 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 -------SSGTTGLPKAVCISNSILIQDSMLitsqSVIYVGSCLDW---ITGLWAFVFstVFGCTRIIS-------NKAF 258
Cdd:PRK06710 207 dlallqyTGGTTGFPKGVMLTHKNLVSNTLM----GVQWLYNCKEGeevVLGVLPFFH--VYGMTAVMNlsimqgyKMVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 259 TPEYFVGLV----KKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLAtLQRSQELCKTAMFNSGYGMTE 334
Cdd:PRK06710 281 IPKFDMKMVfeaiKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVE-VQEKFETVTGGKLVEGYGLTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 VGAITInigiSNV-------SSAGRPVPGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR-MQDfeGWF 405
Cdd:PRK06710 360 SSPVTH----SNFlwekrvpGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAvLQD--GWL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 406 HTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEI 485
Cdd:PRK06710 434 HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEEL 513
|
490 500 510
....*....|....*....|....*....|....*.
gi 24653035 486 VEHVAKRLPATqkQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:PRK06710 514 NQFARKYLAAY--KVPKVYEFRDELPKTTVGKILRR 547
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
185-519 |
3.94e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 138.55 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 185 EGGDQTVAIL-CSSGTTGLPKAvCI-------SNSILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNK 256
Cdd:PRK08314 186 TAGPDDLAVLpYTSGTTGVPKG-CMhthrtvmANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 257 AFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAmFNSGYGMTEVG 336
Cdd:PRK08314 265 RWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLD-YVEGYGLTETM 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 337 AITInigiSNVSSA------GRPVPGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR-MQDFEG--WFH 406
Cdd:PRK08314 344 AQTH----SNPPDRpklqclGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEaFIEIDGkrFFR 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 407 TGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGA--TISAKE 484
Cdd:PRK08314 420 TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEE 499
|
330 340 350
....*....|....*....|....*....|....*
gi 24653035 485 IVEHvAKRLPATQKQLRAgVQFTDKLPANVNGKTM 519
Cdd:PRK08314 500 IIAW-AREHMAAYKYPRI-VEFVDSLPKSGSGKIL 532
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
52-525 |
4.51e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 137.73 E-value: 4.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGQEYDKVHKAT--VGWHPEILTLTD-HVEGVQGIETLLDPTTTekiYQPEVLKEGGDqtvaILCSSGTTGLPKAV-- 206
Cdd:PRK08276 88 IVSAALADTAAELAaeLPAGVPLLLVVAgPVPGFRSYEEALAAQPD---TPIADETAGAD----MLYSSGTTGRPKGIkr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 207 ----------CISNSILIQDSMLITSQSV------IYVGSCLDWITglwafvFSTVFGCTRIISNKaFTPEYFVGLVKKY 270
Cdd:PRK08276 161 plpgldpdeaPGMMLALLGFGMYGGPDSVylspapLYHTAPLRFGM------SALALGGTVVVMEK-FDAEEALALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 271 KINYAVLPPRHLSALITCPD---AKPD---------ALAPithlnygggsislatlqrsqelC----KTAMF-------N 327
Cdd:PRK08276 234 RVTHSQLVPTMFVRMLKLPEevrARYDvsslrvaihAAAP----------------------CpvevKRAMIdwwgpiiH 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 SGYGMTEVGAITInigISNVS------SAGRPVPGiKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDF 401
Cdd:PRK08276 292 EYYASSEGGGVTV---ITSEDwlahpgSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 402 EGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS 481
Cdd:PRK08276 368 HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24653035 482 ---AKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK08276 448 dalAAELIAWLRGRL-AHYKCPRS-IDFEDELPRTPTGKLYKRRLRD 492
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-473 |
5.55e-35 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 138.69 E-value: 5.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 19 KRNSIYNYDTSVGKIIFNNMKNWPKNVCQICDVDG--VTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS---TYV 93
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRpewVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 94 MplgVACLMNG---TPFHSVNP------VLDDAtlthvfsitKPTLIFCDGQE-YDKVHKA----------------TVG 147
Cdd:COG1022 82 D---LAILAAGavtVPIYPTSSaeevayILNDS---------GAKVLFVEDQEqLDKLLEVrdelpslrhivvldprGLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 148 WHPEILTLTDHVEgvQGiETLLDPTTTEkiyqpEVLKEGGDQTVAILC-SSGTTGLPKAVC------ISNSILIQDSMLI 220
Cdd:COG1022 150 DDPRLLSLDELLA--LG-REVADPAELE-----ARRAAVKPDDLATIIyTSGTTGRPKGVMlthrnlLSNARALLERLPL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 221 TSQSVIYvgSCL--DWITGLWAFVFSTVFGCT--------RIISN-KAFTPEYFV--------------------GLVKK 269
Cdd:COG1022 222 GPGDRTL--SFLplAHVFERTVSYYALAAGATvafaespdTLAEDlREVKPTFMLavprvwekvyagiqakaeeaGGLKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 270 ----------YKINYAVLPPRHLSALitcpDAKPDALA------PI-----THLNY---GGGSISlatlqrsQELCKtaM 325
Cdd:COG1022 300 klfrwalavgRRYARARLAGKSPSLL----LRLKHALAdklvfsKLrealgGRLRFavsGGAALG-------PELAR--F 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 326 FNS-------GYGMTEV-GAITIN------IGisnvsSAGRPVPGIKIRIvDEDGkslgynqvgEIYVHTGQAWNGYYGN 391
Cdd:COG1022 367 FRAlgipvleGYGLTETsPVITVNrpgdnrIG-----TVGPPLPGVEVKI-AEDG---------EILVRGPNVMKGYYKN 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 392 PVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYW-PTEIETVIAELSQVQDVCVVGiyDERegDAAGA 470
Cdd:COG1022 432 PEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVaPQPIENALKASPLIEQAVVVG--DGR--PFLAA 507
|
...
gi 24653035 471 LVV 473
Cdd:COG1022 508 LIV 510
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-520 |
5.86e-35 |
|
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: 134.31 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 190 TVAILCSSGTTGLPKAVCISNS-------ILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEY 262
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKtffavpdILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 263 FVGLVKKYKINYAVLPPRHLSALITcpdAKPDALAPITHLNY--GGGSISLATLQRSQELCKTAMFNSGYGMTEVGAIT- 339
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVS---ELKSANATVPSLRLigYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALc 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 340 --INIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQdFEGWFHTGDLGYFDEQN 417
Cdd:cd17635 160 lpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 418 FLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISA-KEIVEHVAKRLPat 496
Cdd:cd17635 239 FLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAiRALKHTIRRELE-- 316
|
330 340
....*....|....*....|....
gi 24653035 497 QKQLRAGVQFTDKLPANVNGKTMR 520
Cdd:cd17635 317 PYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
329-516 |
1.56e-34 |
|
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: 132.81 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEV-GAITIN-IGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNP-VETRRMQDfeGWF 405
Cdd:cd17636 142 GYGQTEVmGLATFAaLGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPeVNARRTRG--GWH 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 406 HTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEI 485
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAEL 299
|
170 180 190
....*....|....*....|....*....|.
gi 24653035 486 VEHVAKRLpATQKQLRAgVQFTDKLPANVNG 516
Cdd:cd17636 300 IEHCRARI-ASYKKPKS-VEFADALPRTAGG 328
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
185-505 |
1.90e-34 |
|
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: 135.03 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 185 EGGDQTVAILCSSGTTGLPKAVCIS------NSILIQDSMLITSQSVIYV----GSCLDWITGLWAFVfstVFGCT---- 250
Cdd:cd05907 84 EDPDDLATIIYTSGTTGRPKGVMLShrnilsNALALAERLPATEGDRHLSflplAHVFERRAGLYVPL---LAGARiyfa 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 251 ----RIISN-KAFTPEYFVG----LVKKYKINYAVLPPRHLSALItcpdakpdALAPITHLNY---GGGSISLATLQRSQ 318
Cdd:cd05907 161 ssaeTLLDDlSEVRPTVFLAvprvWEKVYAAIKVKAVPGLKRKLF--------DLAVGGRLRFaasGGAPLPAELLHFFR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 319 ELCKTAMfnSGYGMTEV-GAITINIGISNVS-SAGRPVPGIKIRIVDEdgkslgynqvGEIYVHTGQAWNGYYGNPVETR 396
Cdd:cd05907 233 ALGIPVY--EGYGLTETsAVVTLNPPGDNRIgTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 397 RMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYW-PTEIETVIAELSQVQDVCVVGiyDERegDAAGALVV-- 473
Cdd:cd05907 301 EALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNIsPEPIENALKASPLISQAVVIG--DGR--PFLVALIVpd 376
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24653035 474 --------KSKG-ATISAKEIVEHvakrlPATQKQLRAGVQ 505
Cdd:cd05907 377 pealeawaEEHGiAYTDVAELAAN-----PAVRAEIEAAVE 412
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
263-525 |
9.63e-34 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 134.76 E-value: 9.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 263 FVGLVKKYKINyaVLPPRH--LSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFnSGYGMTEVGAI-T 339
Cdd:PRK07059 293 FIKELKKYQVH--IFPAVNtlYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPIT-EGYGLSETSPVaT 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 340 INIGISNVSSA--GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQN 417
Cdd:PRK07059 370 CNPVDATEFSGtiGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 418 FLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKsKGATISAKEIVEHVAKRLpaTQ 497
Cdd:PRK07059 450 YTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVK-KDPALTEEDVKAFCKERL--TN 526
|
250 260
....*....|....*....|....*....
gi 24653035 498 KQLRAGVQFTDKLP-ANVnGKTMRKTARD 525
Cdd:PRK07059 527 YKRPKFVEFRTELPkTNV-GKILRRELRD 554
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
258-529 |
1.53e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 133.67 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 258 FTPEYFVGLVKKYKINYAVLPPRHLSALITCPD---AKPD--ALAPITHlnygGGSISLATLQRsqelcktAMF------ 326
Cdd:PRK12406 230 FDPEELLQLIERHRITHMHMVPTMFIRLLKLPEevrAKYDvsSLRHVIH----AAAPCPADVKR-------AMIewwgpv 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 327 -NSGYGMTEVGAITINIG---ISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFE 402
Cdd:PRK12406 299 iYEYYGSTESGAVTFATSedaLSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRG 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 403 GWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISA 482
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24653035 483 KEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARDVFVA 529
Cdd:PRK12406 459 ADIRAQLKARL-AGYKVPKH-IEIMAELPREDSGKIFKRRLRDPYWA 503
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
173-521 |
4.24e-33 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 132.50 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 173 TTEKIYQPEVLKE----GGDQTVAILCSSGTTGLPKAVcisnsiliqdsmLITSQSVIYVGSCLDWITGLW--------- 239
Cdd:PRK08008 154 TQLKAQQPATLCYapplSTDDTAEILFTSGTTSRPKGV------------VITHYNLRFAGYYSAWQCALRdddvyltvm 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 240 -AF-----------VFSTvfGCTRIISNKaFTPEYFVGLVKKYKINYAVLPP---RHLSALITCPDAKPDALAPIT-HLN 303
Cdd:PRK08008 222 pAFhidcqctaamaAFSA--GATFVLLEK-YSARAFWGQVCKYRATITECIPmmiRTLMVQPPSANDRQHCLREVMfYLN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 304 ygggsISLATLQRSQELCKTAMFNSgYGMTE--VGAITINIGIS-NVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVH 380
Cdd:PRK08008 299 -----LSDQEKDAFEERFGVRLLTS-YGMTEtiVGIIGDRPGDKrRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIK 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 381 --TGQA-WNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVV 457
Cdd:PRK08008 373 gvPGKTiFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653035 458 GIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQKqLRAGVQFTDKLPANVNGKTMRK 521
Cdd:PRK08008 453 GIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNM-AKFK-VPSYLEIRKDLPRNCSGKIIKK 514
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
193-525 |
1.61e-32 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 131.03 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVCIS--------NSILIQDSMLITSQSVIYVGSCLDWitGLWAFVFSTVFGCTrIISNKAFTPEYFV 264
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSgpggigtlKAILDRTPWRAEEPTVIVAPMFHAW--GFSQLVLAASLACT-IVTRRRFDPEATL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 265 GLVKKYKINYAVLPPRHLSALItcpDAKPDALAPithlnYGGGSISLATLQ----RSQELCKT------AMFNSgYGMTE 334
Cdd:PRK13382 278 DLIDRHRATGLAVVPVMFDRIM---DLPAEVRNR-----YSGRSLRFAAASgsrmRPDVVIAFmdqfgdVIYNN-YNATE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 VGAITINIGI---SNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYygNPVETRrmqDF-EGWFHTGDL 410
Cdd:PRK13382 349 AGMIATATPAdlrAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTK---DFhDGFMASGDV 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 411 GYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVA 490
Cdd:PRK13382 424 GYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVR 503
|
330 340 350
....*....|....*....|....*....|....*
gi 24653035 491 KRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK13382 504 DNL-ANYKVPRD-IVVLDELPRGATGKILRRELQA 536
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
173-524 |
5.42e-32 |
|
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: 128.00 E-value: 5.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 173 TTEKIYQPEVLKEGgdqtVAILCSSGTTGLPKAVCISNSILIQD------SMLITSQSVIYVGSCLDWITGLWAFVFSTV 246
Cdd:cd05969 78 TTEELYERTDPEDP----TLLHYTSGTTGTPKGVLHVHDAMIFYyftgkyVLDLHPDDIYWCTADPGWVTGTVYGIWAPW 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 247 F-GCTRIISNKAFTPEYFVGLVKKYKINYAVLPP---RHLSALITCPDAKPDaLAPITHLNYGGGSISLATLQRSQELCK 322
Cdd:cd05969 154 LnGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPtaiRMLMKEGDELARKYD-LSSLRFIHSVGEPLNPEAIRWGMEVFG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 323 TAmFNSGYGMTEVGAITINIGIS---NVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTG--QAWNGYYGNpvETRR 397
Cdd:cd05969 233 VP-IHDTWWQTETGSIMIANYPCmpiKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWND--EERY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 398 MQDF-EGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSK 476
Cdd:cd05969 310 KNSFiDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKE 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24653035 477 GATISAK---EIVEHVAKRLPATQKQLRagVQFTDKLPANVNGKTMRKTAR 524
Cdd:cd05969 390 GFEPSDElkeEIINFVRQKLGAHVAPRE--IEFVDNLPKTRSGKIMRRVLK 438
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
330-525 |
5.93e-32 |
|
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: 127.79 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 330 YGMTEVGAITIN--IGISNVSSAGRPVPGIKIRIVDED-GKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFH 406
Cdd:cd05941 244 YGMTEIGMALSNplDGERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 407 TGDLGYFDEQNFLYIVDRKK-EILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGA-TISAKE 484
Cdd:cd05941 324 TGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEE 403
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24653035 485 IVEHVAKRLPATqKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd05941 404 LKEWAKQRLAPY-KRPRR-LILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
52-521 |
6.37e-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: 6.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLGV-----ACLmngtPfhsVNPVLDDATLTHVFS 124
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSleMVVAILAVlkagaAYV----P---LDPSYPAERLAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 125 ITKPTLIfcdgqeydkvhkatvgwhpeiltLTDHvegvqgietlldptttekiyqpevlkeggDQTVAILCSSGTTGLPK 204
Cdd:cd05930 82 DSGAKLV-----------------------LTDP-----------------------------DDLAYVIYTSGSTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 205 AVCISNSILI------QDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRII--SNKAFTPEYFVGLVKKYKINYAV 276
Cdd:cd05930 110 GVMVEHRGLVnlllwmQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVlpEEVRKDPEALADLLAEEGITVLH 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 277 LPPRHLSALItcPDAKPDALAPITHLNYGGGSISLATLQRSQELC-KTAMFNsGYGMTEV------GAITINIGISNVSS 349
Cdd:cd05930 190 LTPSLLRLLL--QELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVN-LYGPTEAtvdatyYRVPPDDEEDGRVP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 350 AGRPVPGIKIRIVDEDGKSLGYNQVGEIYVH-TGQAwNGYYGNPVETRR---MQDFEGW---FHTGDLGYFDEQ-NFLYI 421
Cdd:cd05930 267 IGRPIPNTRVYVLDENLRPVPPGVPGELYIGgAGLA-RGYLNRPELTAErfvPNPFGPGermYRTGDLVRWLPDgNLEFL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 422 vDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPAtqkQLR 501
Cdd:cd05930 346 -GRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPD---YMV 421
|
490 500
....*....|....*....|.
gi 24653035 502 -AGVQFTDKLPANVNGKTMRK 521
Cdd:cd05930 422 pSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
56-530 |
1.09e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 128.74 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 56 VTFEQGLTWSI--------RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITK 127
Cdd:PRK12583 38 VVRHQALRYTWrqladavdRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 128 PTLIFC-DGQEYDKVHKATVGWHPEILTLTD---------HVEGVqgieTLLDPTTTEKIYQ-PEVLKEG---------- 186
Cdd:PRK12583 118 VRWVICaDAFKTSDYHAMLQELLPGLAEGQPgalacerlpELRGV----VSLAPAPPPGFLAwHELQARGetvsrealae 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 187 ------GDQTVAILCSSGTTGLPKAVCIS------NSILIQDSMLITSQSVIYVGSCLDWITGLwafVFSTV----FGCT 250
Cdd:PRK12583 194 rqasldRDDPINIQYTSGTTGFPKGATLShhnilnNGYFVAESLGLTEHDRLCVPVPLYHCFGM---VLANLgcmtVGAC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 251 RIISNKAFTPEYFVGLVKKYKIN--YAVlpPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNS 328
Cdd:PRK12583 271 LVYPNEAFDPLATLQAVEEERCTalYGV--PTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVGAITINIGISN-----VSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEG 403
Cdd:PRK12583 349 AYGMTETSPVSLQTTAADdlerrVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 404 WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAK 483
Cdd:PRK12583 429 WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24653035 484 EIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARDVFVAL 530
Cdd:PRK12583 509 ELREFCKARI-AHFKVPRY-FRFVDEFPMTVTGKVQKFRMREISIEE 553
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
164-520 |
1.50e-31 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 126.81 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 164 GIETLLDPTTTEKIY---QPEVLKEGGDQTVAILCSSGTTGLPKAVCIS--NSILIQDSML-----ITSQSVIYVGSCLD 233
Cdd:cd05919 64 VINPLLHPDDYAYIArdcEARLVVTSADDIAYLLYSSGTTGPPKGVMHAhrDPLLFADAMArealgLTPGDRVFSSAKMF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 234 WITGLWAFVFSTVF-GCTRIISNKAFTPEYFVGLVKKYK--INYAVlpPRHLSALITCPDAKPDALAPITHLNYGGGSIS 310
Cdd:cd05919 144 FGYGLGNSLWFPLAvGASAVLNPGWPTAERVLATLARFRptVLYGV--PTFYANLLDSCAGSPDALRSLRLCVSAGEALP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 311 LATLQRSQELCKTAMFNsGYGMTEVGAITIN--IGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGY 388
Cdd:cd05919 222 RGLGERWMEHFGGPILD-GIGATEVGHIFLSnrPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 389 YGNPvETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAA 468
Cdd:cd05919 301 WNNP-EKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRL 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24653035 469 GALVVKSKGATIS---AKEIVEHVAKRLPATQKQLRagVQFTDKLPANVNGKTMR 520
Cdd:cd05919 380 TAFVVLKSPAAPQeslARDIHRHLLERLSAHKVPRR--IAFVDELPRTATGKLQR 432
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
50-521 |
3.96e-31 |
|
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: 125.44 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 50 DVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPT 129
Cdd:cd05945 11 VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFCDGqeydkvhkatvgwhpeiltltdhvegvqgietlldptttekiyqpevlkeggDQTVAILCSSGTTGLPKAVCIS 209
Cdd:cd05945 91 LLIADG----------------------------------------------------DDNAYIIFTSGSTGRPKGVQIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 NSILI--------------QDSMLITSQ-----SVIYVGSCldWITGlwafvfstvfGCTRIISN--KAFTPEYFVGLvK 268
Cdd:cd05945 119 HDNLVsftnwmlsdfplgpGDVFLNQAPfsfdlSVMDLYPA--LASG----------ATLVPVPRdaTADPKQLFRFL-A 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 269 KYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE-VGAITIN------ 341
Cdd:cd05945 186 EHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEaTVAVTYIevtpev 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 342 IGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR---MQDFEGWFHTGDLGYFDEQNF 418
Cdd:cd05945 266 LDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVRLEADGL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 419 LYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS-AKEIVEHVAKRLPATQ 497
Cdd:cd05945 346 LFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGlTKAIKAELAERLPPYM 425
|
490 500
....*....|....*....|....
gi 24653035 498 KQLRAGVQftDKLPANVNGKTMRK 521
Cdd:cd05945 426 IPRRFVYL--DELPLNANGKIDRK 447
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
179-525 |
4.10e-31 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 125.95 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 179 QPEVLKEGGDQTVAILCSSGTTGLPK-------AVCISNSILIQDSMLI-TSQSVIYVGSCLDWITGLWAFVFSTVF-GC 249
Cdd:cd05929 116 SPETPIEDEAAGWKMLYSGGTTGRPKgikrglpGGPPDNDTLMAAALGFgPGADSVYLSPAPLYHAAPFRWSMTALFmGG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 250 TRIISNKaFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDA--LAPITHLNYGGGSISLATlqrsqelcKTAMFN 327
Cdd:cd05929 196 TLVLMEK-FDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAydLSSLKRVIHAAAPCPPWV--------KEQWID 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 SG-------YGMTEVGAITINIG---ISNVSSAGRPVPGiKIRIVDEDGKSLGYNQVGEIYVHTGQAWNgYYGNPVETRR 397
Cdd:cd05929 267 WGgpiiweyYGGTEGQGLTIINGeewLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 398 MQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKG 477
Cdd:cd05929 345 ARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPG 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24653035 478 A---TISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd05929 425 AdagTALAEELIAFLRDRL-SRYKCPRS-IEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
284-526 |
5.19e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 126.86 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 284 ALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFnSGYGMTEVG--AITINIG-ISNVSSAGRPVPGIKIR 360
Cdd:PRK12492 320 ALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIV-EGYGLTETSpvASTNPYGeLARLGTVGIPVPGTALK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 361 IVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTE 440
Cdd:PRK12492 399 VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 441 IETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGaTISAKEIVEHVAKRLpaTQKQLRAGVQFTDKLPANVNGKTMR 520
Cdd:PRK12492 479 IEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENF--TGYKVPKHIVLRDSLPMTPVGKILR 555
|
....*.
gi 24653035 521 KTARDV 526
Cdd:PRK12492 556 RELRDI 561
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
149-451 |
1.22e-30 |
|
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: 125.47 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 149 HPEILTLT--DHVEGVQG--IETLLDPTTTEKIYQPEvlkegGDQTVAILCSSGTTGLPKAVCISN-SIL------IQDS 217
Cdd:cd05906 129 VAEFAGLEtlSGLPGIRVlsIEELLDTAADHDLPQSR-----PDDLALLMLTSGSTGFPKAVPLTHrNILarsagkIQHN 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 218 MLiTSQSVIYVGSCLDWITGLWAF-VFSTVFGCTR-------IISNkaftPEYFVGLVKKYKINYAVLPPRHLS----AL 285
Cdd:cd05906 204 GL-TPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQvhvpteeILAD----PLRWLDLIDRYRVTITWAPNFAFAllndLL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 286 ITCPDAKPDaLAPITHLNYGGGSISLATLQRSQELCK-----TAMFNSGYGMTEVGA-ITIN--------IGISNVSSAG 351
Cdd:cd05906 279 EEIEDGTWD-LSSLRYLVNAGEAVVAKTIRRLLRLLEpyglpPDAIRPAFGMTETCSgVIYSrsfptydhSQALEFVSLG 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 352 RPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNfLYIVDRKKEILKY 431
Cdd:cd05906 358 RPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGN-LTITGRTKDTIIV 436
|
330 340
....*....|....*....|
gi 24653035 432 NGLHYWPTEIETVIAELSQV 451
Cdd:cd05906 437 NGVNYYSHEIEAAVEEVPGV 456
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
186-525 |
1.37e-30 |
|
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: 125.30 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 186 GGDQTVAILCSSGTTGLPKAVCISNSI-------------LIQDSMLITSQSVIYvGSCL------DWITGLWAFVFStv 246
Cdd:cd05970 183 CGEDILLVYFSSGTTGMPKMVEHDFTYplghivtakywqnVREGGLHLTVADTGW-GKAVwgkiygQWIAGAAVFVYD-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 247 fgctriisNKAFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDaLAPITHLNYGGGSISLATLQRSQELCKTAMF 326
Cdd:cd05970 260 --------YDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYD-LSSLRYCTTAGEALNPEVFNTFKEKTGIKLM 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 327 nSGYGMTEVgaiTINIGI-----SNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQA-----WNGYYGNPVETR 396
Cdd:cd05970 331 -EGFGQTET---TLTIATfpwmePKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGkpvglFGGYYKDAEKTA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 397 RMQdFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSK 476
Cdd:cd05970 407 EVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAK 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24653035 477 GATIS---AKEIVEHVaKRLPATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd05970 486 GYEPSeelKKELQDHV-KKVTAPYKYPRI-VEFVDELPKTISGKIRRVEIRE 535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
196-520 |
2.50e-30 |
|
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: 120.59 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKAVCISNSILI------QDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKaFTPEYFVGLVKK 269
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIesfvcnEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK-FNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 270 YKINYAVLPPRHLSALITcpdakpdALAPITHLNY---GGGSISLATLQRSQELCKTAMFNSGYGMTEVGAITINIGISN 346
Cdd:cd17633 87 YNATVIYLVPTMLQALAR-------TLEPESKIKSifsSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 347 --VSSAGRPVPGIKIRIVDEDGkslgyNQVGEIYVHTGQAWNGYYGNPVETRrmqdfEGWFHTGDLGYFDEQNFLYIVDR 424
Cdd:cd17633 160 rpPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 425 KKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVvksKGATISAKEIVEHVAKRLpaTQKQLRAGV 504
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRFLKQKL--SRYEIPKKI 304
|
330
....*....|....*.
gi 24653035 505 QFTDKLPANVNGKTMR 520
Cdd:cd17633 305 IFVDSLPYTSSGKIAR 320
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
196-525 |
1.78e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 121.69 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKAV---------CISNSI--LIQDSmliTSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTPEYFV 264
Cdd:PRK07470 171 TSGTTGRPKAAvlthgqmafVITNHLadLMPGT---TEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSERFDPAEVW 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 265 GLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRS-QELCKTAMfnSGYGMTEV-GAITI-- 340
Cdd:PRK07470 248 ALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRAlAKLGKVLV--QYFGLGEVtGNITVlp 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 341 ------------NIGisnvsSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMqdF-EGWFHT 407
Cdd:PRK07470 326 palhdaedgpdaRIG-----TCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKA--FrDGWFRT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 408 GDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVE 487
Cdd:PRK07470 399 GDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLA 478
|
330 340 350
....*....|....*....|....*....|....*...
gi 24653035 488 HVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK07470 479 WLDGKVA--RYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
57-525 |
8.57e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 119.86 E-value: 8.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 57 TFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDGQ 136
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 137 EYDKVHKATVGWHP-EILTLTDHVEGV---QGIETLLDPTTTEKIYQPEVlkEGGDqTVAILCSSGTTGLPKAVCISNS- 211
Cdd:PRK06155 128 LLAALEAADPGDLPlPAVWLLDAPASVsvpAGWSTAPLPPLDAPAPAAAV--QPGD-TAAILYTSGTTGPSKGVCCPHAq 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 212 -----ILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKaFTPEYFVGLVKKYKINYAVLpprhLSALI 286
Cdd:PRK06155 205 fywwgRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPR-FSASGFWPAVRRHGATVTYL----LGAMV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 287 TCPDAKPDALAPITH-LNYG-GGSISLATLQRSQELCKTAMFnSGYGMTEVGA-ITINIGISNVSSAGRPVPGIKIRIVD 363
Cdd:PRK06155 280 SILLSQPARESDRAHrVRVAlGPGVPAALHAAFRERFGVDLL-DGYGSTETNFvIAVTHGSQRPGSMGRLAPGFEARVVD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 364 EDGKSLGYNQVGEIYVHTGQAW---NGYYGNPVET-RRMQDFegWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPT 439
Cdd:PRK06155 359 EHDQELPDGEPGELLLRADEPFafaTGYFGMPEKTvEAWRNL--WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSF 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 440 EIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLP--ATQKQLRagvqFTDKLPANVNGK 517
Cdd:PRK06155 437 EVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAyfAVPRYVE----FVAALPKTENGK 512
|
....*...
gi 24653035 518 TMRKTARD 525
Cdd:PRK06155 513 VQKFVLRE 520
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
52-525 |
9.85e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 119.41 E-value: 9.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:PRK13391 21 TGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGQEYDKVHKATvgwhpeiltltDHVEGVQGIETLLDPTTTEKIYQ-PEVLKE-----GGDQT--VAILCSSGTTGLP 203
Cdd:PRK13391 101 ITSAAKLDVARALL-----------KQCPGVRHRLVLDGDGELEGFVGyAEAVAGlpatpIADESlgTDMLYSSGTTGRP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 204 KAVCISNSIL-IQDSMLITS---------QSVIYVGSCLDWITGLWAFVFSTV-FGCTRIISNKaFTPEYFVGLVKKYKI 272
Cdd:PRK13391 170 KGIKRPLPEQpPDTPLPLTAflqrlwgfrSDMVYLSPAPLYHSAPQRAVMLVIrLGGTVIVMEH-FDAEQYLALIEEYGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 273 NYAVLPPRHLSALITCPDAKPDalapithlnygggSISLATLQR---SQELC----KTAMFN-------SGYGMTE-VGA 337
Cdd:PRK13391 249 THTQLVPTMFSRMLKLPEEVRD-------------KYDLSSLEVaihAAAPCppqvKEQMIDwwgpiihEYYAATEgLGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 338 ITINIG--ISNVSSAGRPVPGiKIRIVDEDGKSLGYNQVGEIYVHTGQAWNgYYGNPVETRRMQDFEG-WFHTGDLGYFD 414
Cdd:PRK13391 316 TACDSEewLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 415 EQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---AKEIVEHVAK 491
Cdd:PRK13391 394 EDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQ 473
|
490 500 510
....*....|....*....|....*....|....
gi 24653035 492 RLpATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK13391 474 RL-SRQKCPRS-IDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
52-530 |
3.81e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 117.67 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:PRK07514 25 DGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGQEYDKVHK--ATVGwHPEILTLTDHVEGvqgieTLLDPTTTEKIYQPEVLKEGGDqTVAILCSSGTTGLPKA---- 205
Cdd:PRK07514 105 VCDPANFAWLSKiaAAAG-APHVETLDADGTG-----SLLEAAAAAPDDFETVPRGADD-LAAILYTSGTTGRSKGamls 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 206 --VCISNSILIQDSMLITSQSVI------------YVGSCLDWITG---LWAFVF-----------STVF-GC----TRI 252
Cdd:PRK07514 178 hgNLLSNALTLVDYWRFTPDDVLihalpifhthglFVATNVALLAGasmIFLPKFdpdavlalmprATVMmGVptfyTRL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 253 ISNKAFTPEyfvglvkkykinyAVLPPRhlsaLITCPDAkPdaLAPITHLNYG---GGSIslatLQRsqelcktamfnsg 329
Cdd:PRK07514 258 LQEPRLTRE-------------AAAHMR----LFISGSA-P--LLAETHREFQertGHAI----LER------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 330 YGMTEVGAITIN------IGisnvSSAGRPVPGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRrmQDF- 401
Cdd:PRK07514 301 YGMTETNMNTSNpydgerRA----GTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTA--EEFr 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 402 -EGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATI 480
Cdd:PRK07514 375 aDGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAL 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24653035 481 SAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARDVFVAL 530
Cdd:PRK07514 455 DEAAILAALKGRL-ARFKQPKR-VFFVDELPRNTMGKVQKNLLREQYADL 502
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
194-520 |
4.47e-28 |
|
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: 117.47 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 194 LCSSGTTGLPKAVCISNSILI-------QDSMLITSQSVIYVGSCLDWITGLW-AFVFSTVFGCTRIISNKAFTPEYFVG 265
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYwtaelyaRNVLGIREDDVCFSAAKLFFAYGLGnSLTFPLSVGATTVLMPERPTPAAVFK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 266 LVKKYK--INYAVlpPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNsGYGMTEVGaitiNIG 343
Cdd:cd05959 249 RIRRYRptVFFGV--PTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILD-GIGSTEML----HIF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 344 ISNV------SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMqdFEG-WFHTGDLGYFDEQ 416
Cdd:cd05959 322 LSNRpgrvryGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDT--FQGeWTRTGDKYVRDDD 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 417 NFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAK---EIVEHVAKRL 493
Cdd:cd05959 400 GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAleeELKEFVKDRL 479
|
330 340
....*....|....*....|....*..
gi 24653035 494 PAtQKQLRaGVQFTDKLPANVNGKTMR 520
Cdd:cd05959 480 AP-YKYPR-WIVFVDELPKTATGKIQR 504
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
41-521 |
1.10e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 116.63 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 41 WPKNVCqICDVDGvTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLT 120
Cdd:PRK13383 48 WPGRTA-IIDDDG-ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 121 HVFSITKPTLIFCDGQeydkvhkatvgwhpeiltLTDHVEGVQGIETLLDPTTT---EKIYQPEVLKEGGdqtvAILCSS 197
Cdd:PRK13383 126 AALRAHHISTVVADNE------------------FAERIAGADDAVAVIDPATAgaeESGGRPAVAAPGR----IVLLTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 198 GTTGLPKAV--------CISNSILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTrIISNKAFTPEYFVGLVKK 269
Cdd:PRK13383 184 GTTGKPKGVprapqlrsAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGT-VLTHRHFDAEAALAQASL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 270 YKINYAVLPPRHLSALITCPDaKPDALAPITHLNY---GGGSISLATLQRSQELCKTAMFNsGYGMTEVG--AITINIGI 344
Cdd:PRK13383 263 HRADAFTAVPVVLARILELPP-RVRARNPLPQLRVvmsSGDRLDPTLGQRFMDTYGDILYN-GYGSTEVGigALATPADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 345 SNV-SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRrmqdFEGWFHTGDLGYFDEQNFLYIVD 423
Cdd:PRK13383 341 RDApETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAV----VDGMTSTGDMGYLDNAGRLFIVG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 424 RKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLpATQKQLRaG 503
Cdd:PRK13383 417 REDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRV-SRFEQPR-D 494
|
490
....*....|....*...
gi 24653035 504 VQFTDKLPANVNGKTMRK 521
Cdd:PRK13383 495 INIVSSIPRNPTGKVLRK 512
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
98-521 |
1.11e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 115.86 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 98 VACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIF------CDGQEYDKVHKATVGWHPeiltltdhvegvqgietlldp 171
Cdd:PRK07787 63 VGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLgpapddPAGLPHVPVRLHARSWHR--------------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 172 tttekiyQPEVlkeGGDQTVAILCSSGTTGLPKAVCISNSIliqdsmlitsqsviyVGSCLDWITGLWAF---------- 241
Cdd:PRK07787 122 -------YPEP---DPDAPALIVYTSGTTGPPKGVVLSRRA---------------IAADLDALAEAWQWtaddvlvhgl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 242 ----VFSTVFGC-------TRIISNKAFTPE-YFVGLVKKYKINYAVlpPRHLSALITCPDAkPDALAPITHLNYGGGSI 309
Cdd:PRK07787 177 plfhVHGLVLGVlgplrigNRFVHTGRPTPEaYAQALSEGGTLYFGV--PTVWSRIAADPEA-ARALRGARLLVSGSAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 310 SLATLQRSQELCKTAMFNSgYGMTEVgAITINI---GISNVSSAGRPVPGIKIRIVDEDGKSLGYN--QVGEIYVHTGQA 384
Cdd:PRK07787 254 PVPVFDRLAALTGHRPVER-YGMTET-LITLSTradGERRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 385 WNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKK-EILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDER 463
Cdd:PRK07787 332 FDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDD 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24653035 464 EGDAAGALVVKSKGatISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRK 521
Cdd:PRK07787 412 LGQRIVAYVVGADD--VAADELIDFVAQQL-SVHKRPRE-VRFVDALPRNAMGKVLKK 465
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
46-522 |
1.46e-27 |
|
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: 115.68 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 46 CQICDVD-GVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFS 124
Cdd:cd05923 18 CAIADPArGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 125 ITKPTLIF-CDGQEydkVHKATVGWHPEILTLTDHVEgvQGIETLLDPTTTEKIYQPEvlkeggdQTVAILCSSGTTGLP 203
Cdd:cd05923 98 RGEMTAAViAVDAQ---VMDAIFQSGVRVLALSDLVG--LGEPESAGPLIEDPPREPE-------QPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 204 KAVCISNSILIQDSMLITSQSVIYVGS--------CLDWITGLWA-FVFSTVFGcTRIISNKAFTPEYFVGLVKKYKINY 274
Cdd:cd05923 166 KGAVIPQRAAESRVLFMSTQAGLRHGRhnvvlglmPLYHVIGFFAvLVAALALD-GTYVVVEEFDPADALKLIEQERVTS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 275 AVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQElCKTAMFNSGYGMTEVGAITINIGISNvSSAGRPV 354
Cdd:cd05923 245 LFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ-HLPGEKVNIYGTTEAMNSLYMRDART-GTEMRPG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 355 PGIKIRIVDEDGKS---LGYNQVGEIYV--HTGQAWNGYYGNPVETR-RMQDfeGWFHTGDLGYFDEQNFLYIVDRKKEI 428
Cdd:cd05923 323 FFSEVRIVRIGGSPdeaLANGEEGELIVaaAADAAFTGYLNQPEATAkKLQD--GWYRTGDVGYVDPSGDVRILGRVDDM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 429 LKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGaTISAKEIVEHVAKRLPATQKQLRAGVqFTD 508
Cdd:cd05923 401 IISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRASELADFKRPRRYF-FLD 478
|
490
....*....|....
gi 24653035 509 KLPANVNGKTMRKT 522
Cdd:cd05923 479 ELPKNAMNKVLRRQ 492
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
193-526 |
2.21e-27 |
|
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: 116.26 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVcisnsilIQDS-----MLITSQSVIY---------VGSCLDWITGLWAFVFSTVF-GCTRII--SN 255
Cdd:cd05967 235 ILYTSGTTGKPKGV-------VRDNgghavALNWSMRNIYgikpgdvwwAASDVGWVVGHSYIVYGPLLhGATTVLyeGK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 256 KAFTPE--YFVGLVKKYKINyavlpprhlsALITCPDA-------KPDA-------LAPITHLNYGGGSISLATLQRSQE 319
Cdd:cd05967 308 PVGTPDpgAFWRVIEKYQVN----------ALFTAPTAirairkeDPDGkyikkydLSSLRTLFLAGERLDPPTLEWAEN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 320 LCKTAMFNSgYGMTEVG-AITIN-IGISNVS----SAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVH----TGqAWNGYY 389
Cdd:cd05967 378 TLGVPVIDH-WWQTETGwPITANpVGLEPLPikagSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKlplpPG-CLLTLW 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 390 GNPVETRR--MQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGlHYWPT-EIETVIAELSQVQDVCVVGIYDEREGD 466
Cdd:cd05967 456 KNDERFKKlyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAG-HRLSTgEMEESVLSHPAVAECAVVGVRDELKGQ 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653035 467 AAGALVVKSKGATISA----KEIVEHVAKRL-P-ATQKQlragVQFTDKLPANVNGKTMRKTARDV 526
Cdd:cd05967 535 VPLGLVVLKEGVKITAeeleKELVALVREQIgPvAAFRL----VIFVKRLPKTRSGKILRRTLRKI 596
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
329-531 |
1.99e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 113.17 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVGAITINIGISNVSSAGR---PVPGIKIRIVDED--GKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMqdF-E 402
Cdd:PRK05605 367 GYGLTETSPIIVGNPMSDDRRPGYvgvPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKS--FlD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 403 GWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISA 482
Cdd:PRK05605 445 GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDP 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24653035 483 KEIVEHVAKRLPAtQKQLRAGVQFtDKLPANVNGKTMRKTARDVFVALR 531
Cdd:PRK05605 525 EGLRAYCREHLTR-YKVPRRFYHV-DELPRDQLGKVRRREVREELLEKL 571
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
183-525 |
8.04e-26 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 111.02 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 183 LKEGGDQTVAILCSSGTTGLPKAVCISNSILIQDSML-------ITSQSVIYVGSCLDWITGLWAFVFST-VFGCTRIIS 254
Cdd:cd05928 169 VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVngrywldLTASDIMWNTSDTGWIKSAWSSLFEPwIQGACVFVH 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 255 NKA-FTPEYFVGLVKKYKINYAVLPPRHLSALITcPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFnSGYGMT 333
Cdd:cd05928 249 HLPrFDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY-EGYGQT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 334 EVGAITINIGISNVS--SAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQA-----WNGYYGNPVETrrMQDFEGWFH 406
Cdd:cd05928 327 ETGLICANFKGMKIKpgSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIrpfglFSGYVDNPEKT--AATIRGDFY 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 407 -TGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVV-----KSKGATI 480
Cdd:cd05928 405 lTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqfLSHDPEQ 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24653035 481 SAKEIVEHVaKRLPATQKQLRAgVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd05928 485 LTKELQQHV-KSVTAPYKYPRK-VEFVQELPKTVTGKIQRNELRD 527
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
62-521 |
1.30e-25 |
|
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: 110.08 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 62 LTWS------IRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLGVAclMNGTPFHSVNPVLDDATLTHVFSITKPTLIFC 133
Cdd:cd12118 30 YTWRqtydrcRRLASALAALGISRGDTVAVLAPNTpaMYELHFGVP--MAGAVLNALNTRLDAEEIAFILRHSEAKVLFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 134 DGQ-EYDkvhkatvgwhpEILTltdhvEGvqgietllDPTttekiyqPEVLK-EGGDQTVAILCSSGTTGLPKAVCIS-- 209
Cdd:cd12118 108 DREfEYE-----------DLLA-----EG--------DPD-------FEWIPpADEWDPIALNYTSGTTGRPKGVVYHhr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 ----NSIliqdSMLITS---QSVIYVGS-----CLDWiTGLWAFvfsTVFGCTRIISNKaFTPEYFVGLVKKYKINYAVL 277
Cdd:cd12118 157 gaylNAL----ANILEWemkQHPVYLWTlpmfhCNGW-CFPWTV---AAVGGTNVCLRK-VDAKAIYDLIEKHKVTHFCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 278 PPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMfnSGYGMTEV-GAITINI-------------- 342
Cdd:cd12118 228 APTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVT--HVYGLTETyGPATVCAwkpewdelpteera 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 343 ------GISNVSSAG---------RPVPGikirivdeDGKSLgynqvGEIYVHTGQAWNGYYGNPVETRRMqdFE-GWFH 406
Cdd:cd12118 306 rlkarqGVRYVGLEEvdvldpetmKPVPR--------DGKTI-----GEIVFRGNIVMKGYLKNPEATAEA--FRgGWFH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 407 TGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIV 486
Cdd:cd12118 371 SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEII 450
|
490 500 510
....*....|....*....|....*....|....*..
gi 24653035 487 EHVAKRLPA--TQKQlragVQFTDkLPANVNGKtMRK 521
Cdd:cd12118 451 AFCREHLAGfmVPKT----VVFGE-LPKTSTGK-IQK 481
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
51-472 |
3.31e-25 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 109.50 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 51 VDGVtVTFEQGLTwsiriaqylkKRGLNHKDVIGIAAKNSTYVMP--LGVAClMNGTpfhsVNPV-----LDDATLThvF 123
Cdd:PLN02860 39 VDGV-LSLAAGLL----------RLGLRNGDVVAIAALNSDLYLEwlLAVAC-AGGI----VAPLnyrwsFEEAKSA--M 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 124 SITKPTLIFCDGQ---EYDKV---HKATVGWHpeILTLTDHVEGVQGIETLLdptTTEKIYQPEVLKEGGD-----QTVA 192
Cdd:PLN02860 101 LLVRPVMLVTDETcssWYEELqndRLPSLMWQ--VFLESPSSSVFIFLNSFL---TTEMLKQRALGTTELDyawapDDAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILC-SSGTTGLPKAVCISNSILIQDSMlitsQSVIYVGSCLD----------WITGLwafvfSTVFGCTRIISNKAFTPE 261
Cdd:PLN02860 176 LICfTSGTTGRPKGVTISHSALIVQSL----AKIAIVGYGEDdvylhtaplcHIGGL-----SSALAMLMVGACHVLLPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 262 YFVGLVkkykinYAVLPPRHLSALITCPDAKPDALAPI-------------THLNyGGGSISLATLQRSQELCKTAMFNS 328
Cdd:PLN02860 247 FDAKAA------LQAIKQHNVTSMITVPAMMADLISLTrksmtwkvfpsvrKILN-GGGSLSSRLLPDAKKLFPNAKLFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVGA----ITIN-------------IGISNVSSA--------GRPVPGIKIRIvDEDGKSlgynQVGEIYVHTGQ 383
Cdd:PLN02860 320 AYGMTEACSsltfMTLHdptlespkqtlqtVNQTKSSSVhqpqgvcvGKPAPHVELKI-GLDESS----RVGRILTRGPH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 384 AWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDER 463
Cdd:PLN02860 395 VMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSR 474
|
....*....
gi 24653035 464 EGDAAGALV 472
Cdd:PLN02860 475 LTEMVVACV 483
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
53-524 |
8.68e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 107.79 E-value: 8.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 53 GVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNpvlddatltHVFSITKPTLIF 132
Cdd:PRK13390 22 GEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAIN---------HHLTAPEADYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 133 CDGQEYDKVHKATV--------GWHPEILTLTDHVEGVQGIETLL---DPTTTEkiyQPevlkeggdQTVAILCSSGTTG 201
Cdd:PRK13390 93 GDSGARVLVASAALdglaakvgADLPLRLSFGGEIDGFGSFEAALagaGPRLTE---QP--------CGAVMLYSSGTTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 202 LPKA-----------------VCISNSIL-IQDSMLITSQSVIYVGSCLDWITGLWAFvfstvfGCTRIISnKAFTPEYF 263
Cdd:PRK13390 162 FPKGiqpdlpgrdvdapgdpiVAIARAFYdISESDIYYSSAPIYHAAPLRWCSMVHAL------GGTVVLA-KRFDAQAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 264 VGLVKKYKINYAVLPPRHLSALITCpDAKPDALAPIThlnygggsiSLATLQRSQELC----KTAMFN-------SGYGM 332
Cdd:PRK13390 235 LGHVERYRITVTQMVPTMFVRLLKL-DADVRTRYDVS---------SLRAVIHAAAPCpvdvKHAMIDwlgpivyEYYSS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 333 TEVGAIT-INIG--ISNVSSAGRPVPGiKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQD--FEGWFHT 407
Cdd:PRK13390 305 TEAHGMTfIDSPdwLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHpaHPFWTTV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 408 GDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---AKE 484
Cdd:PRK13390 384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSdelARE 463
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24653035 485 IVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTAR 524
Cdd:PRK13390 464 LIDYTRSRI-AHYKAPRS-VEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
328-523 |
1.09e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 107.59 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 SGYGMTEVGAITINIGISN-----VSSAGRPVPGIKIRIVDED-GKSLGYNQVGEI----YvHTGQawnGYYGNPVETRR 397
Cdd:PRK08315 346 IAYGMTETSPVSTQTRTDDplekrVTTVGRALPHLEVKIVDPEtGETVPRGEQGELctrgY-SVMK---GYWNDPEKTAE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 398 MQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKG 477
Cdd:PRK08315 422 AIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPG 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24653035 478 ATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKT----MRKTA 523
Cdd:PRK08315 502 ATLTEEDVRDFCRGKI-AHYKIPRY-IRFVDEFPMTVTGKIqkfkMREMM 549
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
186-531 |
1.18e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 108.12 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 186 GGDQTVAILCSSGTTGLPKAVC------ISNSILIQDSMLITSQSVI-------YVGSCLdwITGLWAF------VFSTV 246
Cdd:PRK07529 211 GPDDVAAYFHTGGTTGMPKLAQhthgneVANAWLGALLLGLGPGDTVfcglplfHVNALL--VTGLAPLargahvVLATP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 247 FGC--TRIISNkaftpeyFVGLVKKYKINYAVLPPRHLSALITCPDAKPDalapITHLNY---GGGSISLATLQRSQELC 321
Cdd:PRK07529 289 QGYrgPGVIAN-------FWKIVERYRINFLSGVPTVYAALLQVPVDGHD----ISSLRYalcGAAPLPVEVFRRFEAAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 322 KTAMFNsGYGMTE-VGAITINI--GISNVSSAGRPVPGIKIRIV--DEDGKSL---GYNQVGEIYVHTGQAWNGYygnpV 393
Cdd:PRK07529 358 GVRIVE-GYGLTEaTCVSSVNPpdGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIAGPNVFSGY----L 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 394 ETRRMQDF---EGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGA 470
Cdd:PRK07529 433 EAAHNKGLwleDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVA 512
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 471 LVVKSKGATISAKEIVEHVAKRLP---ATQKQLRagvqFTDKLPANVNGKTM-----RKTARDVFV-ALR 531
Cdd:PRK07529 513 YVQLKPGASATEAELLAFARDHIAeraAVPKHVR----ILDALPKTAVGKIFkpalrRDAIRRVLRaALR 578
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
197-527 |
1.42e-24 |
|
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: 104.34 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 197 SGTTGLPKAVCISNSILIQDSMliTSQSVIYVGSCLDWITGLWAFVFSTVFGCTR-IISNKAFT-PEYFVGLVKK---YK 271
Cdd:cd17630 9 SGSTGTPKAVVHTAANLLASAA--GLHSRLGFGGGDSWLLSLPLYHVGGLAILVRsLLAGAELVlLERNQALAEDlapPG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 272 INYAVLPPRHLSALITcPDAKPDALAPITHLNYGGGSISLATLQRSQEL---CKTamfnsGYGMTEVGAiTINIGISNV- 347
Cdd:cd17630 87 VTHVSLVPTQLQRLLD-SGQGPAALKSLRAVLLGGAPIPPELLERAADRgipLYT-----TYGMTETAS-QVATKRPDGf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 348 --SSAGRPVPGIKIRIVDEdgkslgynqvGEIYVHTGQAWNGYYGNPveTRRMQDFEGWFHTGDLGYFDEQNFLYIVDRK 425
Cdd:cd17630 160 grGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 426 KEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISakEIVEHVAKRLPATQ--KQLRag 503
Cdd:cd17630 228 DNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA--ELRAWLKDKLARFKlpKRIY-- 303
|
330 340
....*....|....*....|....
gi 24653035 504 vqFTDKLPANVNGKTMRKTARDVF 527
Cdd:cd17630 304 --PVPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
179-521 |
2.88e-24 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 105.47 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 179 QPEVLKEGGDQTVAILCSSGTTGLPKAVCISNSILIqdSMLITSQSVIYVGSCLDWIT-GLWAFVFST--VFGCTR---- 251
Cdd:cd17643 84 GPSLLLTDPDDLAYVIYTSGSTGRPKGVVVSHANVL--ALFAATQRWFGFNEDDVWTLfHSYAFDFSVweIWGALLhggr 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 252 --IISNK-AFTPEYFVGLVKKYKInyAVL--PPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQE---LCKT 323
Cdd:cd17643 162 lvVVPYEvARSPEDFARLLRDEGV--TVLnqTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGrfgLDRP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 324 AMFNsGYGMTEVgaiTI----------NIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPV 393
Cdd:cd17643 240 QLVN-MYGITET---TVhvtfrpldaaDLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 394 ET-------------RRMqdfegwFHTGDLG-YFDEQNFLYIvDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGI 459
Cdd:cd17643 316 LTaerfvanpfggpgSRM------YRTGDLArRLPDGELEYL-GRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVR 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653035 460 YDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPAtqKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd17643 389 EDEPGDTRLVAYVVADDGAAADIAELRALLKELLPD--YMVPARYVPLDALPLTVNGKLDRA 448
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
348-524 |
4.61e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 105.25 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 348 SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMqDFEGWFHTGDLGYFDEQNFLYIVDRKKE 427
Cdd:PRK07638 307 NSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGWMTVRDVGYEDEEGFIYIVGREKN 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 428 ILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVvksKGATiSAKEIVEHVAKRLPATQKQLRagVQFT 507
Cdd:PRK07638 386 MILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQQLKSFCLQRLSSFKIPKE--WHFV 459
|
170
....*....|....*..
gi 24653035 508 DKLPANVNGKTMRKTAR 524
Cdd:PRK07638 460 DEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
52-521 |
6.89e-24 |
|
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: 104.66 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:cd17646 20 EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGqeydkvhkATVGWHPEiltltDHVEGVQGIETLLDPTTTEkiyqPEVlKEGGDQTVAILCSSGTTGLPKAVC---- 207
Cdd:cd17646 100 LTTA--------DLAARLPA-----GGDVALLGDEALAAPPATP----PLV-PPRPDNLAYVIYTSGSTGRPKGVMvtha 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 208 -ISNSIL-IQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAF--TPEYFVGLVKKYKINYAVLPPRHLS 283
Cdd:cd17646 162 gIVNRLLwMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGhrDPAYLAALIREHGVTTCHFVPSMLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 284 ALITCPDakPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNsGYGMTEVgaiTINIGISNVSSA--------GRPVP 355
Cdd:cd17646 242 VFLAEPA--AGSCASLRRVFCSGEALPPELAARFLALPGAELHN-LYGPTEA---AIDVTHWPVRGPaetpsvpiGRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 356 GIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET------------RRMqdfegwFHTGDLGYFDEQNFLYIVD 423
Cdd:cd17646 316 NTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTaerfvpdpfgpgSRM------YRTGDLARWRPDGALEFLG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 424 RKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVgIYDEREGDA--AGALVVKSKGATISAKEIVEHVAKRLPATqkQLR 501
Cdd:cd17646 390 RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVV-ARAAPAGAArlVGYVVPAAGAAGPDTAALRAHLAERLPEY--MVP 466
|
490 500
....*....|....*....|
gi 24653035 502 AGVQFTDKLPANVNGKTMRK 521
Cdd:cd17646 467 AAFVVLDALPLTANGKLDRA 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-524 |
9.59e-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: 102.56 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 187 GDQTVAILCSSGTTGLPKAVC------ISNSILIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRII------- 253
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQhthsneVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVlagpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 254 SNKAFTPEyFVGLVKKYKINYAVLPPRHLSALITCPDAkpdalAPITHLNY---GGGSISLATLQRSQELCKTAMFnSGY 330
Cdd:cd05944 81 RNPGLFDN-FWKLVERYRITSLSTVPTVYAALLQVPVN-----ADISSLRFamsGAAPLPVELRARFEDATGLPVV-EGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 331 GMTE---VGAITINIGISNVSSAGRPVPGIKIRIVDEDG-----KSLGYNQVGEIYVhTGQAWNGYYGNPVETRRMQDFE 402
Cdd:cd05944 154 GLTEatcLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGvgrllRDCAPDEVGEICV-AGPGVFGGYLYTEGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 403 GWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISA 482
Cdd:cd05944 233 GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24653035 483 KEIVEHVAKRLP---ATQKQlragVQFTDKLPANVNGKTMRKTAR 524
Cdd:cd05944 313 EELLAWARDHVPeraAVPKH----IEVLEELPVTAVGKVFKPALR 353
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
182-473 |
2.09e-23 |
|
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: 103.21 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 182 VLKEGGDQTVAILCSSGTTGLPKAVCISN-SILIQdsmlITSQSVI---YVGSCLDWITGLW--------AFVFSTvfGC 249
Cdd:cd17640 82 VVENDSDDLATIIYTSGTTGNPKGVMLTHaNLLHQ----IRSLSDIvppQPGDRFLSILPIWhsyersaeYFIFAC--GC 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 250 TRIISnkafTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNY--------------GGGSISLaTLQ 315
Cdd:cd17640 156 SQAYT----SIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFlfflsggifkfgisGGGALPP-HVD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 316 RsqelcktaMFNS-------GYGMTEVGAI-TINIGISNV-SSAGRPVPGIKIRIVDEDGKS-LGYNQVGEIYVHTGQAW 385
Cdd:cd17640 231 T--------FFEAigievlnGYGLTETSPVvSARRLKCNVrGSVGRPLPGTEIKIVDPEGNVvLPPGEKGIVWVRGPQVM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 386 NGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKE-ILKYNGLHYWPTEIETVIAELSQVQDVCVVGiYDERe 464
Cdd:cd17640 303 KGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVVG-QDQK- 380
|
....*....
gi 24653035 465 gdAAGALVV 473
Cdd:cd17640 381 --RLGALIV 387
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
59-529 |
2.51e-23 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 103.47 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 59 EQGLTWS------IRIAQYLKKRGLnHKDVIGIAAKNST-YVMPLgVACLMNG---TPFHSVNPVLDDATLTHVFSITKP 128
Cdd:cd05931 22 EETLTYAeldrraRAIAARLQAVGK-PGDRVLLLAPPGLdFVAAF-LGCLYAGaiaVPLPPPTPGRHAERLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 129 TLIFCDGQEYDKVHkatvgwhpEILTLTDHVEGVQGIETLLDPTTTEKIYQPEVLKEGgdqTVAIL-CSSGTTGLPKAVC 207
Cdd:cd05931 100 RVVLTTAAALAAVR--------AFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPD---DIAYLqYTSGSTGTPKGVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 208 IS------NSILIQDSMLITSQSViyVGScldWI-----TGLWAFVFSTVF-GCTRIIsnkaFTPEYFVG-------LVK 268
Cdd:cd05931 169 VThrnllaNVRQIRRAYGLDPGDV--VVS---WLplyhdMGLIGGLLTPLYsGGPSVL----MSPAAFLRrplrwlrLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 269 KYKINYAVLPP---RHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQE------LCKTAMFnSGYGMTE----V 335
Cdd:cd05931 240 RYRATISAAPNfayDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEafapfgFRPEAFR-PSYGLAEatlfV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 336 GAITINIGISNVS------------------------SAGRPVPGIKIRIVDEDGKS-LGYNQVGEIYVHTGQAWNGYYG 390
Cdd:cd05931 319 SGGPPGTGPVVLRvdrdalagravavaaddpaarelvSCGRPLPDQEVRIVDPETGReLPDGEVGEIWVRGPSVASGYWG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 391 NPVETRRM------QDFEGWFHTGDLGYFDEQNfLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQD---VCVVGIYD 461
Cdd:cd05931 399 RPEATAETfgalaaTDEGGWLRTGDLGFLHDGE-LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653035 462 EREGDAAGALVVKSKGATISAKEIVEHVAKRL-------PATQKQLRAGvqftdKLPANVNGKTMRKTARDVFVA 529
Cdd:cd05931 478 DGEERLVVVAEVERGADPADLAAIAAAIRAAVarehgvaPADVVLVRPG-----SIPRTSSGKIQRRACRAAYLD 547
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
188-521 |
7.94e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 100.12 E-value: 7.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCS-SGTTGLPKAVCISNSILIQdSMLITSQsviYVGSCLDW--------ITGLWAFVFSTVFGCTRIISN--K 256
Cdd:PRK07824 34 DDDVALVVAtSGTTGTPKGAMLTAAALTA-SADATHD---RLGGPGQWllalpahhIAGLQVLVRSVIAGSEPVELDvsA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 257 AFTPEYFVGLVKKYKIN--YAVLPPRHLSALITCPDAKpDALAPITHLNYGGGSISLATLQRSQELCKTAMfnSGYGMTE 334
Cdd:PRK07824 110 GFDPTALPRAVAELGGGrrYTSLVPMQLAKALDDPAAT-AALAELDAVLVGGGPAPAPVLDAAAAAGINVV--RTYGMSE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 V-GAITINigisnvssaGRPVPGIKIRIVDedgkslGYNQVGEIYVHTGqawngyYGNPVETRRMQDfEGWFHTGDLGYF 413
Cdd:PRK07824 187 TsGGCVYD---------GVPLDGVRVRVED------GRIALGGPTLAKG------YRNPVDPDPFAE-PGWFRTDDLGAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 414 DEqNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRL 493
Cdd:PRK07824 245 DD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTL 323
|
330 340 350
....*....|....*....|....*....|
gi 24653035 494 PATQ--KQLRagvqFTDKLPANVNGKTMRK 521
Cdd:PRK07824 324 DRTAapRELH----VVDELPRRGIGKVDRR 349
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
67-522 |
9.57e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 101.62 E-value: 9.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKN--STYVMPLgvACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgqEYDKVHKA 144
Cdd:PRK05857 53 GLAADLRAQSVSRGSRVLVISDNgpETYLSVL--ACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVA--PGSKMASS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 145 TVgwhPEILTLTDHVEGVQGIETLLDPTTTEKIYQPEVLKEGGDQTVAILCSSGTTGLPKAVCISNSILIQDSMLITSQS 224
Cdd:PRK05857 129 AV---PEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 225 VIYVgsclDW--------------ITGLWAFVFSTVFGCTRIISNKAFTPeyFVGLVKKYKINYAVLPPRHLSALITCPD 290
Cdd:PRK05857 206 LNWV----TWvvgettysplpathIGGLWWILTCLMHGGLCVTGGENTTS--LLEILTTNAVATTCLVPTLLSKLVSELK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 291 AKPDALAPITHLNYGGgSISLATLQRSQELC--KTAMFnsgYGMTEVGAI-----TINIGISNVSSA--GRPVPGIKIRI 361
Cdd:PRK05857 280 SANATVPSLRLVGYGG-SRAIAADVRFIEATgvRTAQV---YGLSETGCTalclpTDDGSIVKIEAGavGRPYPGVDVYL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 362 VDEDG---------KSLGYnqvGEIYVHTGQAWNGYYGNPVETRRMQdFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYN 432
Cdd:PRK05857 356 AATDGigptapgagPSASF---GTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 433 GLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS-AKEIVEHVAKRLPATQKQLR--AGVQFTDK 509
Cdd:PRK05857 432 GVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESaARALKHTIAARFRRESEPMArpSTIVIVTD 511
|
490
....*....|...
gi 24653035 510 LPANVNGKTMRKT 522
Cdd:PRK05857 512 IPRTQSGKVMRAS 524
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
188-520 |
1.40e-22 |
|
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: 100.29 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVCISNSIL------IQDSMLITSQSVIYVGSCLDWITGLW-AFVFSTVFGCTRIISNKAFTP 260
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALaafgayLRDAVDLRPEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEGGFSV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 261 EYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEVGAITI 340
Cdd:cd05973 168 ESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 341 N----IGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQA---W-NGYYGNPVetrrmQDFEG-WFHTGDLG 411
Cdd:cd05973 248 NhhalEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSplmWfRGYQLPDT-----PAIDGgYYLTGDTV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 412 YFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---AKEIVEH 488
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLH 402
|
330 340 350
....*....|....*....|....*....|..
gi 24653035 489 VAKRLPAtQKQLRAgVQFTDKLPANVNGKTMR 520
Cdd:cd05973 403 VKKRLSA-HAYPRT-IHFVDELPKTPSGKIQR 432
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
60-504 |
2.09e-22 |
|
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: 100.62 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 60 QGLTWS------IRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFC 133
Cdd:cd05932 5 VEFTWGevadkaRRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 134 DGQEYDKVHKATVGWHPEILTLTDHVEG--VQGIETLLdpttteKIYQP--EVLKEGGDQTVAILCSSGTTGLPKAVCIS 209
Cdd:cd05932 85 GKLDDWKAMAPGVPEGLISISLPPPSAAncQYQWDDLI------AQHPPleERPTRFPEQLATLIYTSGTTGQPKGVMLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 ------------NSILI--QDSML-------ITSQSVIYVGScldWITG-LWAFVFSTVfgcTRIISNKAFTPEYFVG-- 265
Cdd:cd05932 159 fgsfawaaqagiEHIGTeeNDRMLsylplahVTERVFVEGGS---LYGGvLVAFAESLD---TFVEDVQRARPTLFFSvp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 266 -LVKKYKIN-YAVLPPRHLSALITCP---------DAKPDALAPITHLNYGGGSISLATLQ--RSQELcktaMFNSGYGM 332
Cdd:cd05932 233 rLWTKFQQGvQDKIPQQKLNLLLKIPvvnslvkrkVLKGLGLDQCRLAGCGSAPVPPALLEwyRSLGL----NILEAYGM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 333 TEVGAI-TINI-GISNVSSAGRPVPGIKIRIVDEdgkslgynqvGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDL 410
Cdd:cd05932 309 TENFAYsHLNYpGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 411 GYFDEQNFLYIVDRKKEILKYN-GLHYWPTEIETVIAELSQVQDVCVVGiyderEGDAAG-ALVVKSKGATISAKEIVEh 488
Cdd:cd05932 379 GELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG-----SGLPAPlALVVLSEEARLRADAFAR- 452
|
490
....*....|....*.
gi 24653035 489 vaKRLPATQKQLRAGV 504
Cdd:cd05932 453 --AELEASLRAHLARV 466
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
351-529 |
5.03e-22 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 99.69 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 351 GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPvETRRMQDFEGWFHTGDLGY-FDEQnfLYIVDRKKEIL 429
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYlLDGY--LYITGRAKDLI 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 430 KYNGLHYWPTEIETVIAELSQVQ--DVCVVGIydEREGDAAGALVVKSKGATISAKEIVEHVAKRLPATQKQLRAGVQFT 507
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEPELRsgDAAAFSI--AQENGEKIVLLVQCRISDEERRGQLIHALAALVRSEFGVEAAVELV 542
|
170 180
....*....|....*....|....
gi 24653035 508 --DKLPANVNGKTMRKTARDVFVA 529
Cdd:PRK09192 543 ppHSLPRTSSGKLSRAKAKKRYLS 566
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
329-451 |
6.44e-22 |
|
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: 98.67 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVGAITINIGISNV--SSAGRPVPGIKIRIVDEDGKSlgynQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFH 406
Cdd:cd05914 264 GYGMTETAPIISYSPPNRIrlGSAGKVIDGVEVRIDSPDPAT----GEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFH 339
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24653035 407 TGDLGYFDEQNFLYIVDRKKE-ILKYNGLHYWPTEIETVIAELSQV 451
Cdd:cd05914 340 TGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
188-524 |
9.49e-22 |
|
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: 97.93 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVC--ISNSILIQD----SMLITSQSVIYVGS---CLDWITGLWAFvFSTVFGCTRIISNKAf 258
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMhfHRDPLASADryavNVLRLREDDRFVGSpplAFTFGLGGVLL-FPFGVGASGVLLEEA- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 259 TPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNsGYGMTEVgai 338
Cdd:cd05958 175 TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIID-GIGSTEM--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 339 tINIGISN------VSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVhtgQAWNGYYGNPVETRRMQDFEGWFHTGDLGY 412
Cdd:cd05958 251 -FHIFISArpgdarPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV---RGPTGCRYLADKRQRTYVQGGWNITGDTYS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 413 FDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---AKEIVEHv 489
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlARELQDH- 405
|
330 340 350
....*....|....*....|....*....|....*
gi 24653035 490 AKRLPATQKQLRAgVQFTDKLPANVNGKTMRKTAR 524
Cdd:cd05958 406 AKAHIAPYKYPRA-IEFVTELPRTATGKLQRFALR 439
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
63-456 |
1.09e-21 |
|
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: 97.34 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 63 TWSIRIAQYLKKR-GLNHKDVIGIAAKNS--TYVMPLGVacLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDGQEYD 139
Cdd:TIGR01733 7 ERANRLARHLRAAgGVGPGDRVAVLLERSaeLVVAILAV--LKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 140 kvhkATVGWHPEILTLTDhVEGVQGIETLLDPTTTEKiyqpevlkEGGDQTVAILCSSGTTGLPKAVCISNSILIQdsmL 219
Cdd:TIGR01733 85 ----RLAGLVLPVILLDP-LELAALDDAPAPPPPDAP--------SGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN---L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 220 ITSQSVIYVGSCLDWITGLWAFVF----STVF------GCTRIISNKA--FTPEYFVGLVKKYKINYAVLPPRHLSALit 287
Cdd:TIGR01733 149 LAWLARRYGLDPDDRVLQFASLSFdasvEEIFgallagATLVVPPEDEerDDAALLAALIAEHPVTVLNLTPSLLALL-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 288 cPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE----VGAITINIGISNVSSA---GRPVPGIKIR 360
Cdd:TIGR01733 227 -AAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTEttvwSTATLVDPDDAPRESPvpiGRPLANTRLY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 361 IVDEDGKSLGYNQVGEIYVH-TGQAwNGYYGNPVETR--------RMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKY 431
Cdd:TIGR01733 306 VLDDDLRPVPVGVVGELYIGgPGVA-RGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI 384
|
410 420
....*....|....*....|....*
gi 24653035 432 NGLHYWPTEIETVIAELSQVQDVCV 456
Cdd:TIGR01733 385 RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
52-521 |
1.64e-21 |
|
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: 97.66 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLGVacLMNGTPFHSVNPVLDDATLTHVFSITKPT 129
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSpeLVVALLAV--LKAGAAYVPLDPELPAERLAFMLADAGAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFCDGqeydkvhkATVGWHPEILTLTDHVEGvqgietlLDPTTTEkiyqPEVLKEGGDQTVAILCSSGTTGLPKAVCIs 209
Cdd:cd12117 97 VLLTDR--------SLAGRAGGLEVAVVIDEA-------LDAGPAG----NPAVPVSPDDLAYVMYTSGSTGRPKGVAV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 nsiliqdsmliTSQSViyVGSCLDwiTGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKI----NYAVLPPRHLSAL 285
Cdd:cd12117 157 -----------THRGV--VRLVKN--TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLvlapKGTLLDPDALGAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 286 I----------TCP------DAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE--------------V 335
Cdd:cd12117 222 IaeegvtvlwlTAAlfnqlaDEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnttfttshvvteldE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 336 GAITINIGisnvssagRPVPGIKIRIVDEDGKSLGYNQVGEIYVH-TGQAwNGYYGNPVETRR------MQDFEGWFHTG 408
Cdd:cd12117 302 VAGSIPIG--------RPIANTRVYVLDEDGRPVPPGVPGELYVGgDGLA-LGYLNRPALTAErfvadpFGPGERLYRTG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 409 DLGYFDEQ-NFLYI--VDRKkeiLKYNGLHYWPTEIETVIAELSQVQDvCVVGIYDEREGDAA-GALVVksKGATISAKE 484
Cdd:cd12117 373 DLARWLPDgRLEFLgrIDDQ---VKIRGFRIELGEIEAALRAHPGVRE-AVVVVREDAGGDKRlVAYVV--AEGALDAAE 446
|
490 500 510
....*....|....*....|....*....|....*..
gi 24653035 485 IVEHVAKRLPATqkQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd12117 447 LRAFLRERLPAY--MVPAAFVVLDELPLTANGKVDRR 481
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
52-527 |
6.83e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.11 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGI-AAKNSTYVMPLgVACLMNGTPFHSVNPVLDDATLTHVFSITKPTL 130
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALrMGSNAEFVVAL-LAASRADLVVVPLDPALPIAEQRVRSQAAGARV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 131 IFCDGQEYDKVHKATVGWHPEILTLTDHVEGVQGIETL-LDPTT--TEKIYQPEVLkegGDQTVAILCSSGTTGLPKAV- 206
Cdd:PRK05852 119 VLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVhLDAATepTPATSTPEGL---RPDDAMIMFTGGTTGLPKMVp 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 207 ----CISNSI-LIQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRII--SNKAFTPEYFVGLVKKYKIN-YAVLP 278
Cdd:PRK05852 196 wthaNIASSVrAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLlpARGRFSAHTFWDDIKAVGATwYTAVP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 279 PRHlSALITCPDAKPDAL--APITHLNYGGGSISLATLQRSQELCKTAMFnSGYGMTEVgaiTINIGISNVSSAGR---P 353
Cdd:PRK05852 276 TIH-QILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEFAAPVV-CAFGMTEA---THQVTTTQIEGIGQtenP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 354 V---------PGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETrrMQDF-EGWFHTGDLGYFDEQNFLYIVD 423
Cdd:PRK05852 351 VvstglvgrsTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTIT--AANFtDGWLRTGDLGSLSAAGDLSIRG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 424 RKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPATqkQLRAG 503
Cdd:PRK05852 429 RIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAF--EIPAS 506
|
490 500
....*....|....*....|....
gi 24653035 504 VQFTDKLPANVNGKTMRKTARDVF 527
Cdd:PRK05852 507 FQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
57-532 |
9.83e-21 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 95.86 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 57 TFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgQ 136
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD-R 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 137 EYDKVHKATVGWHP-EILTLTDHVEGVQGIETLLDPTTTEKIYqpEVLKEGGDQTVAILCS----------------SGT 199
Cdd:PLN03102 120 SFEPLAREVLHLLSsEDSNLNLPVIFIHEIDFPKRPSSEELDY--ECLIQRGEPTPSLVARmfriqdehdpislnytSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 200 TGLPKAVCISNsiliQDSMLITSQSVI--YVGSCLDWITGL-------WAFVFSTVF-GCTRIISNKAFTPEYFVGlVKK 269
Cdd:PLN03102 198 TADPKGVVISH----RGAYLSTLSAIIgwEMGTCPVYLWTLpmfhcngWTFTWGTAArGGTSVCMRHVTAPEIYKN-IEM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 270 YKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMfnSGYGMTEVGA------------ 337
Cdd:PLN03102 273 HNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVM--HAYGLTEATGpvlfcewqdewn 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 338 ---------ITINIGISNVSSAGRPVPGIK-IRIVDEDGKSLGynqvgEIYVHTGQAWNGYYGNPVETrrMQDFE-GWFH 406
Cdd:PLN03102 351 rlpenqqmeLKARQGVSILGLADVDVKNKEtQESVPRDGKTMG-----EIVIKGSSIMKGYLKNPKAT--SEAFKhGWLN 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 407 TGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGAT------- 479
Cdd:PLN03102 424 TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvd 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24653035 480 ---ISAKEIVEHVAKRLPATQKQLRagVQFTDKLPANVNGKTMRKTARDVFVALRV 532
Cdd:PLN03102 504 klvTRERDLIEYCRENLPHFMCPRK--VVFLQELPKNGNGKILKPKLRDIAKGLVV 557
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
197-524 |
1.08e-20 |
|
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: 96.46 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 197 SGTTGLPKAVCIS-----NSIL-IQDSMLITSQSVIYvgscldWITGLwAFVFST--VF------GCTRIISNKAFT-PE 261
Cdd:COG1020 626 SGSTGRPKGVMVEhralvNLLAwMQRRYGLGPGDRVL------QFASL-SFDASVweIFgallsgATLVLAPPEARRdPA 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 262 YFVGLVKKYKINYAVLPPRHLSALItcpDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE--VGAIT 339
Cdd:COG1020 699 ALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTEttVDSTY 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 340 INIGISNVSSA----GRPVPGIKIRIVDEDGKSLGYNQVGEIYVH-TGQAwNGYYGNPVETRR-----MQDFEG--WFHT 407
Cdd:COG1020 776 YEVTPPDADGGsvpiGRPIANTRVYVLDAHLQPVPVGVPGELYIGgAGLA-RGYLNRPELTAErfvadPFGFPGarLYRT 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 408 GDLGYF------------DEQnflyivdrkkeiLKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKS 475
Cdd:COG1020 855 GDLARWlpdgnleflgraDDQ------------VKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPE 922
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24653035 476 KGATISAKEIVEHVAKRLPAtqkqLRAGVQFTDKLPANVNGKTMRKTAR 524
Cdd:COG1020 923 AGAAAAAALLRLALALLLPP----YMVPAAVVLLLPLPLTGNGKLDRLA 967
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
193-519 |
1.19e-20 |
|
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: 95.34 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVCISNS---ILIQDSML----ITSQSVIYVGSCLDWITG-LWAFVFSTVFGCTRIISNKAF---TPE 261
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGgylVYAATTMKyvfdYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLYEGVPnwpTPA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 262 YFVGLVKKYKINYAVLPPRHLSALITcpdAKPDALA--PITHLNYGGG--------SISLATLQRSQELCktAMFNSGYG 331
Cdd:cd17634 317 RMWQVVDKHGVNILYTAPTAIRALMA---AGDDAIEgtDRSSLRILGSvgepinpeAYEWYWKKIGKEKC--PVVDTWWQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 332 MTEVGAITINIGISNVSSAG---RPVPGIKIRIVDEDGKSLGYNQVGEIYVhtGQAWNG----YYGNPveTRRMQD---- 400
Cdd:cd17634 392 TETGGFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVI--TDPWPGqtrtLFGDH--ERFEQTyfst 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 401 FEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATI 480
Cdd:cd17634 468 FKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEP 547
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24653035 481 S---AKEIVEHVAKRL--PATQKQlragVQFTDKLPANVNGKTM 519
Cdd:cd17634 548 SpelYAELRNWVRKEIgpLATPDV----VHWVDSLPKTRSGKIM 587
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
186-525 |
1.91e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 94.75 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 186 GGDQTVAILCSSGTTGLPKAV-CISNSILIQDSML-----ITSQSVIYVGSCL--------DWITGLWAfvfstvfGCTR 251
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVrCTHRKVASAGVMLaqrfgLGPDDVCYVSMPLfhsnavmaGWAVALAA-------GASI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 252 IISNKaFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPItHLNYG--GGSISLATLQRSqelcktamFN-- 327
Cdd:PRK07867 223 ALRRK-FSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPL-RIVYGneGAPGDIARFARR--------FGcv 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 --SGYGMTEvGAITINIGISNVSSA-GRPVPGIKIR-----------IVDEDGKSLGYNQVGEIYVHTGQAW-NGYYGNP 392
Cdd:PRK07867 293 vvDGFGSTE-GGVAITRTPDTPPGAlGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVNTAGPGGfEGYYNDP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 393 -VETRRMQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGAL 471
Cdd:PRK07867 372 eADAERMRG--GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAA 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24653035 472 VVKSKGATISAKEIVEHVAKRLPATQKQLRAGVQFTDKLPANVNGKTMRKTARD 525
Cdd:PRK07867 450 LVLAPGAKFDPDAFAEFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
55-528 |
2.55e-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: 94.48 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 55 TVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIaaknstyVMP---------LGVACL-MNGTPFHSVNPVldDATLTHVFS 124
Cdd:cd05968 91 TLTYGELLYEVKRLANGLRALGVGKGDRVGI-------YLPmipeivpafLAVARIgGIVVPIFSGFGK--EAAATRLQD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 125 ITKPTLIFCDG-QEYDKV--HKATVGWHPEILTLTDHVEGVQGIETLLDPTTTEKIYQPEVL--------KEGGDQTVAI 193
Cdd:cd05968 162 AEAKALITADGfTRRGREvnLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKetagdgaeRTESEDPLMI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 194 LCSSGTTGLPK-AVCISNSILIQDSMLITSQSVIYVGSCLDWIT------GLWAFVFSTVFGCTRIISNKA---FTPEYF 263
Cdd:cd05968 242 IYTSGTTGKPKgTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTdlgwmmGPWLIFGGLILGATMVLYDGApdhPKADRL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 264 VGLVKKYKINYAVLPPRHLSALITCPDAkPDALAPITHLNYGGGSISLATLQRSQELCKTA------MFNSGyGMTEV-G 336
Cdd:cd05968 322 WRMVEDHEITHLGLSPTLIRALKPRGDA-PVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkgrnpIINYS-GGTEIsG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 337 AITINIGISNVSSAG--RPVPGIKIRIVDEDGKSLgYNQVGEIYVHTgqAW----NGYYGNP---VET--RRMQDFegWF 405
Cdd:cd05968 400 GILGNVLIKPIKPSSfnGPVPGMKADVLDESGKPA-RPEVGELVLLA--PWpgmtRGFWRDEdryLETywSRFDNV--WV 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 406 HtGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---A 482
Cdd:cd05968 475 H-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealA 553
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24653035 483 KEIVEHVAKRLpatQKQLRA-GVQFTDKLPANVNGKTMRKTARDVFV 528
Cdd:cd05968 554 EELMERVADEL---GKPLSPeRILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
305-458 |
2.99e-20 |
|
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: 93.82 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 305 GGGSISLATlqrsQELCKT--AMFNSGYGMTE-VGAITI-NIGISNVSSAGRPVPGIKIRIVD-EDGKSL---GYNQvGE 376
Cdd:cd17639 258 GGAPLSADT----QEFLNIvlCPVIQGYGLTEtCAGGTVqDPGDLETGRVGPPLPCCEIKLVDwEEGGYStdkPPPR-GE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 377 IYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTE-IETVIAELSQVQDVC 455
Cdd:cd17639 333 ILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEkLESIYRSNPLVNNIC 412
|
...
gi 24653035 456 VVG 458
Cdd:cd17639 413 VYA 415
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
67-527 |
3.58e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 93.91 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNG---TPFHSVNPVLD-----DATLTHVFSITKPTLIfcdgqey 138
Cdd:PRK07768 41 RIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGaslTMLHQPTPRTDlavwaEDTLRVIGMIGAKAVV------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 139 dkvhkatVG--WHPEILTLTDHVEGVQGIETLLDPTTTEKIyqpevlkEGGDQTVAIL-CSSGTTGLPKAVCISNSILIQ 215
Cdd:PRK07768 114 -------VGepFLAAAPVLEEKGIRVLTVADLLAADPIDPV-------ETGEDDLALMqLTSGSTGSPKAVQITHGNLYA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 216 --DSMLITSQSVIYVGSCLDWI-----TGLWAFVfsTV---FGCTRIISnkafTPEYFVG-------LVKKYKIN----- 273
Cdd:PRK07768 180 naEAMFVAAEFDVETDVMVSWLplfhdMGMVGFL--TVpmyFGAELVKV----TPMDFLRdpllwaeLISKYRGTmtaap 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 274 ---YAVLPPRHLSAlitcpdAKPDALaPITHLNY---GGGSISLATLQRSQE------LCKTAMFnSGYGMTE------- 334
Cdd:PRK07768 254 nfaYALLARRLRRQ------AKPGAF-DLSSLRFalnGAEPIDPADVEDLLDagarfgLRPEAIL-PAYGMAEatlavsf 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 --VG------------------AITINIG-ISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHtGQAWNGYYGNPV 393
Cdd:PRK07768 326 spCGaglvvdevdadllaalrrAVPATKGnTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELR-GESVTPGYLTMD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 394 ETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIY----DEREGdaaG 469
Cdd:PRK07768 405 GFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRldagHSREG---F 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653035 470 ALVVKSKGATISA--KEIVEHVAKRL-------PATQKQLRAGvqftdKLPANVNGKTMRKTARDVF 527
Cdd:PRK07768 482 AVAVESNAFEDPAevRRIRHQVAHEVvaevgvrPRNVVVLGPG-----SIPKTPSGKLRRANAAELV 543
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
181-492 |
5.50e-20 |
|
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: 92.94 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 181 EVLKEGGDQTVAILCSSGTTGLPKAVCISNSILIQDSMLITSQSVIYVG-SCLDWIT-----GLWAFVFSTVFGCTR--I 252
Cdd:cd05908 99 EVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKdRILSWMPlthdmGLIAFHLAPLIAGMNqyL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 253 ISNKAFT--PEYFVGLVKKYKINyavlpprhlsaLITCPD---------AKPDALAP--ITHLNY---GGGSISLatlqr 316
Cdd:cd05908 179 MPTRLFIrrPILWLKKASEHKAT-----------IVSSPNfgykyflktLKPEKANDwdLSSIRMilnGAEPIDY----- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 317 sqELC-------------KTAMFNSgYGMTE--VGA------------------ITINIGISNVS----------SAGRP 353
Cdd:cd05908 243 --ELChefldhmskyglkRNAILPV-YGLAEasVGAslpkaqspfktitlgrrhVTHGEPEPEVDkkdsecltfvEVGKP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 354 VPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGyFDEQNFLYIVDRKKEILKYNG 433
Cdd:cd05908 320 IDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDIIFVNG 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653035 434 LHYWPTEIETVIAELSQVQ--DVCVVGIYDER-EGDAAGALVVKSKGA---TISAKEIVEHVAKR 492
Cdd:cd05908 399 QNVYPHDIERIAEELEGVElgRVVACGVNNSNtRNEEIFCFIEHRKSEddfYPLGKKIKKHLNKR 463
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
56-524 |
6.76e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 93.56 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 56 VTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVL--DDATLTHvfSITKPTLIFC 133
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELhrDDHALAA--RNTEPALVVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 134 DGQEYDKVHKATVgwhpeiltltdhvegVQGIETLLDPTTTEKI-YQPEvlkeGGDQTVAILCSSGTTGLPKAVCISNS- 211
Cdd:PRK06060 109 SDALRDRFQPSRV---------------AEAAELMSEAARVAPGgYEPM----GGDALAYATYTSGTTGPPKAAIHRHAd 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 212 ------ILIQDSMLITSQSVIYVGSCLDWITGLWAFV-FSTVFGCTRIISNKAFTPEYFVGLVKKYK--INYAVlpPRHL 282
Cdd:PRK06060 170 pltfvdAMCRKALRLTPEDTGLCSARMYFAYGLGNSVwFPLATGGSAVINSAPVTPEAAAILSARFGpsVLYGV--PNFF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 283 SALITCpdAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEVGAITINIGISN--VSSAGRPVPGIKIR 360
Cdd:PRK06060 248 ARVIDS--CSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEwrLGTLGRVLPPYEIR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 361 IVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPvetRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTE 440
Cdd:PRK06060 326 VVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 441 IETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISaKEIVEHVAKRLPATQKQLRAGVQFT--DKLPANVNGKT 518
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATID-GSVMRDLHRGLLNRLSAFKVPHRFAvvDRLPRTPNGKL 481
|
....*.
gi 24653035 519 MRKTAR 524
Cdd:PRK06060 482 VRGALR 487
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
185-525 |
8.98e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 92.50 E-value: 8.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 185 EGGDQTVAILC--SSGTTGLPKAVCISNSILIQDSMLITSQSVIYVGSCLdwitgLWAFVFSTVFGCTR----------I 252
Cdd:PRK06164 176 RAADPDAGALLftTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVL-----LAALPFCGVFGFSTllgalaggapL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 253 ISNKAFTPEYFVGLVKKYKINYAVLPPRHLSALItcpDAKPDAlAPITHLNYGG-GSISLATLQRSQELCKTAMFNSG-Y 330
Cdd:PRK06164 251 VCEPVFDAARTARALRRHRVTHTFGNDEMLRRIL---DTAGER-ADFPSARLFGfASFAPALGELAALARARGVPLTGlY 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 331 GMTEVGAITINIGISNVSSA-----GRPV-PGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEG 403
Cdd:PRK06164 327 GSSEVQALVALQPATDPVSVrieggGRPAsPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 404 WFHTGDLGYF-DEQNFLYiVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIydEREGDA-AGALVVKSKGATIS 481
Cdd:PRK06164 407 YFRTGDLGYTrGDGQFVY-QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTvPVAFVIPTDGASPD 483
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24653035 482 AKEIVEHVAKRLPATqkQLRAGVQFTDKLPANVNG---KTMRKTARD 525
Cdd:PRK06164 484 EAGLMAACREALAGF--KVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
330-529 |
1.01e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 91.98 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 330 YGMTE----VGAITINIGISNVSSAGRPVPGIKIRIVDedgkslgyNQVGEIYVHTGQAWNGYYGNPVETRRMqdfegwF 405
Cdd:PRK07445 261 YGMTEtasqIATLKPDDFLAGNNSSGQVLPHAQITIPA--------NQTGNITIQAQSLALGYYPQILDSQGI------F 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 406 HTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGAtISAKEI 485
Cdd:PRK07445 327 ETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24653035 486 VEHVAKRLpATQKQLRAGVQFTDkLPANVNGKTMRKTARDVFVA 529
Cdd:PRK07445 406 KTAIKDQL-SPFKQPKHWIPVPQ-LPRNPQGKINRQQLQQIAVQ 447
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
193-461 |
1.31e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 92.50 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVCISNS-----ILIQDSMLITSQ--SVIYVGSCLDWITGLWAFVFSTVFGCTRIISNKAFTP----- 260
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGphlvgLKYYWRSIIEKDipTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKnkhie 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 261 EYFVGLVKKYKINYAVLPPRHLSALItcpdaKPDALAPITHLNY----------GGGSI--SLATLQRSQELCKTAmfnS 328
Cdd:PTZ00237 339 DDLWNTIEKHKVTHTLTLPKTIRYLI-----KTDPEATIIRSKYdlsnlkeiwcGGEVIeeSIPEYIENKLKIKSS---R 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVGAITI-NIGISNV--SSAGRPVPGIKIRIVDEDGKSLGYNQVGEI---------YVHTgqawngYYGNPVETR 396
Cdd:PTZ00237 411 GYGQTEIGITYLyCYGHINIpyNATGVPSIFIKPSILSEDGKELNVNEIGEVafklpmppsFATT------FYKNDEKFK 484
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653035 397 RM-QDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYD 461
Cdd:PTZ00237 485 QLfSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYD 550
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
197-521 |
1.91e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 91.50 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 197 SGTTGLPKAVcisnsILIQDSMLITSQSVIYVgscLD--------------WITGLWAFVFST-VFGCTRIISNKAFTPE 261
Cdd:PRK04319 214 SGSTGKPKGV-----LHVHNAMLQHYQTGKYV---LDlheddvywctadpgWVTGTSYGIFAPwLNGATNVIDGGRFSPE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 262 YFVGLVKKYKINYAVLPPRHLSALITCPD--AKPDALAPITH-------LNygggsislatlqrsQELCKTAM------F 326
Cdd:PRK04319 286 RWYRILEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDLSSLRHilsvgepLN--------------PEVVRWGMkvfglpI 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 327 NSGYGMTEVGAITInigiSNV-------SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGqaW----NGYYGNPVET 395
Cdd:PRK04319 352 HDNWWMTETGGIMI----ANYpamdikpGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKG--WpsmmRGIWNNPEKY 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 396 RRMqdFEG-WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVK 474
Cdd:PRK04319 426 ESY--FAGdWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAL 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24653035 475 SKGATIS---AKEIVEHVAKRLPAT--QKQlragVQFTDKLPANVNGKTMRK 521
Cdd:PRK04319 504 RPGYEPSeelKEEIRGFVKKGLGAHaaPRE----IEFKDKLPKTRSGKIMRR 551
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
50-488 |
2.00e-19 |
|
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: 91.24 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 50 DVDGVTVTFEQGLTWSIRIAQYLKKrGLNHKDVIGIAAKNSTYVMPLGVACLMNG-TP--------FHSVNPVLDDATLT 120
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGkVPvmlnytagLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 121 HVFS----ITKPTLIFCDGQEYDK--VH----KATVGWHPEILTltdhvegvqGIETLLDPTTTEKIYQpeVLKEGGDQT 190
Cdd:cd05909 81 TVLTskqfIEKLKLHHLFDVEYDAriVYledlRAKISKADKCKA---------FLAGKFPPKWLLRIFG--VAPVQPDDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 191 VAILCSSGTTGLPKAVCISNSILIQDSMLITSQ----------SVIYVGSCLDWITGLWAFV---FSTVFgctriisnkA 257
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLANVEQITAIfdpnpedvvfGALPFFHSFGLTGCLWLPLlsgIKVVF---------H 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 258 FTPEYF---VGLVKKYKINYAVLPPRHLSALITcpDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFnSGYGMTE 334
Cdd:cd05909 221 PNPLDYkkiPELIYDKKATILLGTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRIL-EGYGTTE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 VGA-ITINIGISN--VSSAGRPVPGIKIRIVDEDGKS-LGYNQVGEIYVHTGQAWNGYYGNPvETRRMQDFEGWFHTGDL 410
Cdd:cd05909 298 CSPvISVNTPQSPnkEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEP-ELTSFAFGDGWYDTGDI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653035 411 GYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQ-DVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEH 488
Cdd:cd05909 377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKN 455
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
55-417 |
2.06e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 91.86 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 55 TVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPV-----LDDATLTHVFSITKPT 129
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAyslvsQDFGKLRHVLELLTPG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFC-DGQEYDKVHKATVGWHPEILTLTDHVEG--VQGIETLLDPTTTEKIyQPEVLKEGGDQTVAILCSSGTTGLPKAV 206
Cdd:PRK08180 149 LVFAdDGAAFARALAAVVPADVEVVAVRGAVPGraATPFAALLATPPTAAV-DAAHAAVGPDTIAKFLFTSGSTGLPKAV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 207 -------CiSNSILIQDSM--LITSQSVIyvgscLDWITglWAFVFSTV--------FGCTRIISNKAFTPEYFVGLVKK 269
Cdd:PRK08180 228 inthrmlC-ANQQMLAQTFpfLAEEPPVL-----VDWLP--WNHTFGGNhnlgivlyNGGTLYIDDGKPTPGGFDETLRN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 270 YKinyAVLP------PRHLSALItcPDAKPDA------LAPITHLNYGGGSISLATLQRSQELCKTAM-----FNSGYGM 332
Cdd:PRK08180 300 LR---EISPtvyfnvPKGWEMLV--PALERDAalrrrfFSRLKLLFYAGAALSQDVWDRLDRVAEATCgerirMMTGLGM 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 333 TEVGAITINIGISNVSSA--GRPVPGIKIRIVDEDGKSlgynqvgEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDL 410
Cdd:PRK08180 375 TETAPSATFTTGPLSRAGniGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDA 447
|
....*...
gi 24653035 411 GYF-DEQN 417
Cdd:PRK08180 448 VRFvDPAD 455
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
55-499 |
2.83e-19 |
|
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: 90.95 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 55 TVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVL-----DDATLTHVFSITKPT 129
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqDLAKLKHLFELLKPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFC-DGQEYDKVHKATVGWHPEILTLTDHVEGVQGI--ETLLDPTTTEKIyqPEVLKEGGDQTVA-ILCSSGTTGLPKA 205
Cdd:cd05921 105 LVFAqDAAPFARALAAIFPLGTPLVVSRNAVAGRGAIsfAELAATPPTAAV--DAAFAAVGPDTVAkFLFTSGSTGLPKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 206 VcisnsILIQdSMLITSQSVIY---------VGSCLDWITglWAFVF--STVF------GCTRIISNKAFTPEYFVGLVK 268
Cdd:cd05921 183 V-----INTQ-RMLCANQAMLEqtypffgeePPVLVDWLP--WNHTFggNHNFnlvlynGGTLYIDDGKPMPGGFEETLR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 269 KYK----INYAVLPPRHlSALITCPDaKPDAL-----APITHLNYGGGSISLATLQRSQELC-KTA----MFNSGYGMTE 334
Cdd:cd05921 255 NLReispTVYFNVPAGW-EMLVAALE-KDEALrrrffKRLKLMFYAGAGLSQDVWDRLQALAvATVgeriPMMAGLGATE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 VG-AITINIGI-SNVSSAGRPVPGIKIRIVDEDGKSlgynqvgEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGY 412
Cdd:cd05921 333 TApTATFTHWPtERSGLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 413 F----DEQNFLYIVDRKKEILKYNG---LHYWPTEIETVIAELSQVQDVCVVGIyderEGDAAGALVV------------ 473
Cdd:cd05921 406 LadpdDPAKGLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVVAGE----DRAEVGALVFpdllacrrlvgl 481
|
490 500
....*....|....*....|....*...
gi 24653035 474 --KSKGATISAKEIVEHVAKRLPATQKQ 499
Cdd:cd05921 482 qeASDAEVLRHAKVRAAFRDRLAALNGE 509
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
29-491 |
5.88e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 90.75 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 29 SVGKIIFNNMKNWPKNVCqICDVDGVTVTFEQGLTWSIRIAQYLKkRGLNHKDVIGIAAKNSTYVMPLGVACLMNG-TPF 107
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLA-VADSTGGELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAGkVPV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 108 H--------SVNPVLDDATLTHVFSITKptliFCDGQEyDKVHKATVGWHPEILTLTDHVEGVQGIETL-------LDPT 172
Cdd:PRK08633 694 NlnytaseaALKSAIEQAQIKTVITSRK----FLEKLK-NKGFDLELPENVKVIYLEDLKAKISKVDKLtallaarLLPA 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 173 TT-EKIYQPEVLKeggDQTVAILCSSGTTGLPKAVCISN-SILI---QDSMLI--TSQSVIYvgSCLDW-----ITGLWA 240
Cdd:PRK08633 769 RLlKRLYGPTFKP---DDTATIIFSSGSEGEPKGVMLSHhNILSnieQISDVFnlRNDDVIL--SSLPFfhsfgLTVTLW 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 241 FVFSTVFGCtriISNKAFTPEYFVG-LVKKYKINYAVLPPRHLSALITCPDAKPDALAPIthlnygggSISLATLQRSQE 319
Cdd:PRK08633 844 LPLLEGIKV---VYHPDPTDALGIAkLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASL--------RLVVAGAEKLKP 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 320 LCKTAM---FN----SGYGMTEV-GAITINI------GI-----SNVSSAGRPVPGIKIRIVD-EDGKSLGYNQVGEIYV 379
Cdd:PRK08633 913 EVADAFeekFGirilEGYGATETsPVASVNLpdvlaaDFkrqtgSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILI 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 380 HTGQAWNGYYGNPVETR---RMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAEL--SQVQDV 454
Cdd:PRK08633 993 GGPQVMKGYLGDPEKTAeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVF 1072
|
490 500 510
....*....|....*....|....*....|....*..
gi 24653035 455 CVVGIYDEREGDaagALVVKSKGATISAKEIVEHVAK 491
Cdd:PRK08633 1073 AVTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKE 1106
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
52-524 |
1.29e-18 |
|
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: 88.55 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLGVacLMNGTPFHSVNPVLDDATLTHVFSITKPT 129
Cdd:cd17651 17 EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSaeLVVALLAI--LKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFcdGQEydkVHKATVGWHPEILTLTDHVEGVQGIETLLDPTTTekiyqpevlkegGDQTVAILCSSGTTGLPKAVCIS 209
Cdd:cd17651 95 LVL--THP---ALAGELAVELVAVTLLDQPGAAAGADAEPDPALD------------ADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 NSILIQdsmLITSQSVIYvGSCLDWITGLWA---F------VFSTVF--GCTRIISNKA-FTPEYFVGLVKKYKINYAVL 277
Cdd:cd17651 158 HRSLAN---LVAWQARAS-SLGPGARTLQFAglgFdvsvqeIFSTLCagATLVLPPEEVrTDPPALAAWLDEQRISRVFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 278 PPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRsqELCKTA----MFNSgYGMTE---VGAITINIGISN---V 347
Cdd:cd17651 234 PTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLR--EFCAGLpglrLHNH-YGPTEthvVTALSLPGDPAAwpaP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 348 SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNP------------VETRRMqdfegwFHTGDLGYFDE 415
Cdd:cd17651 311 PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPeltaerfvpdpfVPGARM------YRTGDLARWLP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 416 QNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVcVVGIYDEREGDAA-GALVVKSKGATISAKEIVEHVAKRLP 494
Cdd:cd17651 385 DGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREA-VVLAREDRPGEKRlVAYVVGDPEAPVDAAELRAALATHLP 463
|
490 500 510
....*....|....*....|....*....|
gi 24653035 495 AtqKQLRAGVQFTDKLPANVNGKTMRKTAR 524
Cdd:cd17651 464 E--YMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
52-523 |
2.30e-18 |
|
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: 87.71 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLGVacLMNGTPFHSVNPVLDDATLTHVFSITKPT 129
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGpeQVVAVLGI--LAAGAAYVPVDIDQPAARREAILADAGAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFCDGqeydkvhkatVGWHPEILTLTDHVEGVQGIETLLDPTTTEKiyQPevlkeggDQTVAILCSSGTTGLPKAVCIS 209
Cdd:cd12114 87 LVLTDG----------PDAQLDVAVFDVLILDLDALAAPAPPPPVDV--AP-------DDLAYVIFTSGSTGTPKGVMIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 210 -----NSIL-IQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRII--SNKAFTPEYFVGLVKKYKINYAVLPPRH 281
Cdd:cd12114 148 hraalNTILdINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpdEARRRDPAHWAELIERHGVTLWNSVPAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 282 LSALItcpDAKPDALAPITHLNY---GGGSISLATLQRSQELCKTAMFNSGYGMTEVGAITINIGISNVSSA------GR 352
Cdd:cd12114 228 LEMLL---DVLEAAQALLPSLRLvllSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDwrsipyGR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 353 PVPGIKIRIVDEDGKSLGYNQVGEIYVH-TGQAwNGYYGNPVETRR----MQDFEGWFHTGDLGYFDEQNFLYIVDRKKE 427
Cdd:cd12114 305 PLANQRYRVLDPRGRDCPDWVPGELWIGgRGVA-LGYLGDPELTAArfvtHPDGERLYRTGDLGRYRPDGTLEFLGRRDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 428 ILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPATQKQLRagVQFT 507
Cdd:cd12114 384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSR--VIAL 461
|
490
....*....|....*.
gi 24653035 508 DKLPANVNGKTMRKTA 523
Cdd:cd12114 462 EALPLTANGKVDRAAL 477
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
329-463 |
3.84e-18 |
|
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: 87.80 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEV-GAITINIGIS-NVSSAGRPVPGIKIRIVDEDGkslgyNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFH 406
Cdd:cd05933 350 LYGMSETsGPHTISNPQAyRLLSCGKALPGCKTKIHNPDA-----DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLH 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 407 TGDLGYFDEQNFLYIVDRKKEILKYNG---LHYWPTEiETVIAELSQVQDVCVVGiyDER 463
Cdd:cd05933 425 SGDLGKLDEDGFLYITGRIKELIITAGgenVPPVPIE-DAVKKELPIISNAMLIG--DKR 481
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
328-458 |
5.17e-18 |
|
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: 86.89 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 SGYGMTE-VGAITINI-GISNVSSAGRPVPGIKIRIVD--EDG-KSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFE 402
Cdd:cd05927 304 EGYGQTEcTAGATLTLpGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDED 383
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24653035 403 GWFHTGDLGYFDEQNFLYIVDRKKEILKY-NGLHYWPTEIETVIAELSQVQDVCVVG 458
Cdd:cd05927 384 GWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
182-521 |
9.86e-18 |
|
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: 85.88 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 182 VLKEGGDQTVAILCSSGTTGLPKAVCISNSILIQDSMLITSQSVIYVGSCL-------------DWITGLwafvfsTVFG 248
Cdd:cd17649 88 LLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRElqfasfnfdgaheQLLPPL------ICGA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 249 CTRIISNKAF-TPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHL-NYGGGSISLATLQRSQElCKTAMF 326
Cdd:cd17649 162 CVVLRPDELWaSADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLyIFGGEALSPELLRRWLK-APVRLF 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 327 NsGYGMTEvGAITI--------NIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET--R 396
Cdd:cd17649 241 N-AYGPTE-ATVTPlvwkceagAARAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTaeR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 397 RMQD-FEG----WFHTGDLG-YFDEQNFLYiVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIyDEREGDAAGA 470
Cdd:cd17649 319 FVPDpFGApgsrLYRTGDLArWRDDGVIEY-LGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVA 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24653035 471 LVVKSKGATISA--KEIVEHVAKRLPATqkQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd17649 397 YVVLRAAAAQPElrAQLRTALRASLPDY--MVPAHLVFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
52-521 |
1.27e-17 |
|
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: 85.42 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGQEYDKVHKATVGWHpeiLTLTDHVEGVQGIETLLDPtttekiyqpevlkeggDQTVAILCSSGTTGLPKAVCISNS 211
Cdd:cd12116 89 LTDDALPDRLPAGLPVLL---LALAAAAAAPAAPRTPVSP----------------DDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 212 ILI--------------QDSML-ITSqsVIYVGSCLDWITGLWAfvfstvfGCTRIISNK--AFTPEYFVGLVKKYKINY 274
Cdd:cd12116 150 NLVnflhsmrerlglgpGDRLLaVTT--YAFDISLLELLLPLLA-------GARVVIAPRetQRDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 275 AVLPPRHLSALItcpDAKPDALAPITHLnYGGGSIS--LAtlqrsQELCKTAM--FNSgYGMTEVgaiTINIGISNVSSA 350
Cdd:cd12116 221 MQATPATWRMLL---DAGWQGRAGLTAL-CGGEALPpdLA-----ARLLSRVGslWNL-YGPTET---TIWSTAARVTAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 351 ------GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET--RRMQDFEG-----WFHTGDLGYFDEQN 417
Cdd:cd12116 288 agpipiGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTaeRFVPDPFAgpgsrLYRTGDLVRRRADG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 418 FLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDvCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPATq 497
Cdd:cd12116 368 RLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQ-AAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAY- 445
|
490 500
....*....|....*....|....
gi 24653035 498 kQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd12116 446 -MVPSAFVRLDALPLTANGKLDRK 468
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
67-417 |
2.20e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 85.48 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVL-----DDATLTHVFSITKPTLIFC-DGQEYDK 140
Cdd:PRK12582 92 ALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshDHAKLKHLFDLVKPRVVFAqSGAPFAR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 141 VHKATVGWHPEILTLTDHVEGVQGI--ETLLDPTTTEKIYQpeVLKEGGDQTVA-ILCSSGTTGLPKAVcisnsILIQDS 217
Cdd:PRK12582 172 ALAALDLLDVTVVHVTGPGEGIASIafADLAATPPTAAVAA--AIAAITPDTVAkYLFTSGSTGMPKAV-----INTQRM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 218 MLITSQSVIYV---------GSCLDWI------TGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYkinYAVLP---- 278
Cdd:PRK12582 245 MCANIAMQEQLrprepdpppPVSLDWMpwnhtmGGNANFNGLLWGGGTLYIDDGKPLPGMFEETIRNL---REISPtvyg 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 279 --PRHLSALITCPDAKPDALAP----ITHLNYGGGSISLATLQRSQELCKTAM-----FNSGYGMTEVGAITINI--GIS 345
Cdd:PRK12582 322 nvPAGYAMLAEAMEKDDALRRSffknLRLMAYGGATLSDDLYERMQALAVRTTghripFYTGYGATETAPTTTGThwDTE 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653035 346 NVSSAGRPVPGIKIRIVDEDGKSlgynqvgEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYF-DEQN 417
Cdd:PRK12582 402 RVGLIGLPLPGVELKLAPVGDKY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFvDPDD 467
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
152-525 |
3.46e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 84.31 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 152 ILTLTDHVEGVQGIE----TLLD---PTTTEKIYQPEVLKE----GGDQTVAILCSSGTTGLPKAVCISNSILIQDSML- 219
Cdd:PRK13388 103 LVTDAEHRPLLDGLDlpgvRVLDvdtPAYAELVAAAGALTPhrevDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRAl 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 220 -----ITSQSVIYVGSCL---DWITGLWAFVFSTvfGCTRIISNKaFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDA 291
Cdd:PRK13388 183 terfgLTRDDVCYVSMPLfhsNAVMAGWAPAVAS--GAAVALPAK-FSASGFLDDVRRYGATYFNYVGKPLAYILATPER 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 292 KPDALAPITHlnyGGGSisLATLQRSQELCKT--AMFNSGYGMTEVGAITINIGISNVSSAGRPVPGIKI---------- 359
Cdd:PRK13388 260 PDDADNPLRV---AFGN--EASPRDIAEFSRRfgCQVEDGYGSSEGAVIVVREPGTPPGSIGRGAPGVAIynpetlteca 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 360 -RIVDEDGKSLGYNQ-VGEIYVHTGQA-WNGYYGNPVET-RRMQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLH 435
Cdd:PRK13388 335 vARFDAHGALLNADEaIGELVNTAGAGfFEGYYNNPEATaERMRH--GMYWSGDLAYRDADGWIYFAGRTADWMRVDGEN 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 436 YWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPATQKQLRAGVQFTDKLPANVN 515
Cdd:PRK13388 413 LSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIAADLPSTAT 492
|
410
....*....|
gi 24653035 516 GKTMRKTARD 525
Cdd:PRK13388 493 NKVLKRELIA 502
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
348-526 |
7.20e-17 |
|
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: 83.76 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 348 SSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHtgQAWNGY----YGNP---VETrRMQDFEGWFHTGDLGYFDEQNFLY 420
Cdd:cd05966 410 GSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK--RPWPGMartiYGDHeryEDT-YFSKFPGYYFTGDGARRDEDGYYW 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 421 IVDRKKEILKYNGlHYWPT-EIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---AKEIVEHVAKRL-P- 494
Cdd:cd05966 487 ITGRVDDVINVSG-HRLGTaEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIgPi 565
|
170 180 190
....*....|....*....|....*....|..
gi 24653035 495 ATQKQlragVQFTDKLPANVNGKTMRKTARDV 526
Cdd:cd05966 566 ATPDK----IQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
149-529 |
1.08e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.06 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 149 HPEILTLTDHVEGVQGI--ETLLDPTTTEKIYQPEVlKEGGDQTVAILCSSGTTGLPKAVCISNSIL------IQDSMLI 220
Cdd:PRK12467 616 QSHLLAQLPVPAGLRSLclDEPADLLCGYSGHNPEV-ALDPDNLAYVIYTSGSTGQPKGVAISHGALanyvcvIAERLQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 221 TSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNK--AFTPEYFVGLVKKYKINYAVLPPRHLSALitCPDAKPDALAP 298
Cdd:PRK12467 695 AADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcARDAEAFAALMADQGVTVLKIVPSHLQAL--LQASRVALPRP 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 299 ITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE--VGAITINIG----ISNVSSAGRPVPGIKIRIVDEDGKSLGYN 372
Cdd:PRK12467 773 QRALVCGGEALQVDLLARVRALGPGARLINHYGPTEttVGVSTYELSdeerDFGNVPIGQPLANLGLYILDHYLNPVPVG 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 373 QVGEIYVHTGQAWNGYYGNPVET--RRMQDFEG-----WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVI 445
Cdd:PRK12467 853 VVGELYIGGAGLARGYHRRPALTaeRFVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARL 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 446 AELSQVQDVCVVGIyderEGDAAGALV------VKSKGATISAK--EIVEHVAKRLPatQKQLRAGVQFTDKLPANVNGK 517
Cdd:PRK12467 933 LAQPGVREAVVLAQ----PGDAGLQLVaylvpaAVADGAEHQATrdELKAQLRQVLP--DYMVPAHLLLLDSLPLTPNGK 1006
|
410 420
....*....|....*....|
gi 24653035 518 TMRK--------TARDVFVA 529
Cdd:PRK12467 1007 LDRKalpkpdasAVQATFVA 1026
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
187-521 |
1.36e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 187 GDQTVAILCSSGTTGLPKAVCISNSILI-------QDSMLITSQSVIYVGS-CLDwiTGLWAFVFSTVFGCTRIIS--NK 256
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSnrlcwmqQAYGLGVGDTVLQKTPfSFD--VSVWEFFWPLMSGARLVVAapGD 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 257 AFTPEYFVGLVKKYKINYAVLPPRHLSALItcPDAKPDALAPITHLNYGGGSISLATLQR-SQELCKTAMFNSgYGMTEV 335
Cdd:PRK12316 732 HRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNL-YGPTEA 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 336 ------------GAITINIgisnvssaGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR------ 397
Cdd:PRK12316 809 aidvthwtcveeGGDSVPI--------GRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpsp 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 398 MQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIyderEGDAAGALVVKSKG 477
Cdd:PRK12316 881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESE 956
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24653035 478 ATISAKEIVEHVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:PRK12316 957 GGDWREALKAHLAASLP--EYMVPAQWLALERLPLTPNGKLDRK 998
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
347-492 |
2.03e-16 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 82.12 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 347 VSSAGRPV-PGIKIRIVDEDGKSLGYNQVGEIYV---HTgqaWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIV 422
Cdd:COG1021 352 LTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTrgpYT---IRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVE 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 423 DRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVkSKGATISAKEIVEHVAKR 492
Cdd:COG1021 429 GRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVV-PRGEPLTLAELRRFLRER 497
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
330-442 |
2.18e-16 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 82.09 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 330 YGMTEV-GAITIN-IGISNVSSAGRPVPGIKIRIvdedgkslgyNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHT 407
Cdd:cd17641 355 YGQTELaGAYTVHrDGDVDPDTVGVPFPGTEVRI----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHT 424
|
90 100 110
....*....|....*....|....*....|....*.
gi 24653035 408 GDLGYFDEQNFLYIVDRKKEILK-YNGLHYWPTEIE 442
Cdd:cd17641 425 GDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIE 460
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
440-517 |
9.63e-16 |
|
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: 72.19 E-value: 9.63e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653035 440 EIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPAtQKQLRAgVQFTDKLPANVNGK 517
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGP-YAVPKE-VVFVDELPKTRSGK 76
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
96-493 |
1.42e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 79.44 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 96 LGVACLmnGTPFHSVNPVLDDATLTHVFSITKPTLIFCDGQEYDKVhkatvgwhPEILTLTDHVEGVQGI---------- 165
Cdd:PRK05620 82 FAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQL--------GEILKECPCVRAVVFIgpsdadsaaa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 166 -----------ETLLDPTTTekIYQPEVLKEggdQTVAILC-SSGTTGLPKAVCISNSILIQDSM-LITSQSV------- 225
Cdd:PRK05620 152 hmpegikvysyEALLDGRST--VYDWPELDE---TTAAAICySTGTTGAPKGVVYSHRSLYLQSLsLRTTDSLavthges 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 226 ------IYvgSCLDWITGLWAFVFST--VF--------GCTRIISNKA-----FTPEYFVGLVkkykINYAVLPPRHLSa 284
Cdd:PRK05620 227 flccvpIY--HVLSWGVPLAAFMSGTplVFpgpdlsapTLAKIIATAMprvahGVPTLWIQLM----VHYLKNPPERMS- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 285 litcpdakpdalapITHLNYGGGSISLATLQRSQELCKTAMFNSgYGMTEVGAI-TINIGISNVS---------SAGRPV 354
Cdd:PRK05620 300 --------------LQEIYVGGSAVPPILIKAWEERYGVDVVHV-WGMTETSPVgTVARPPSGVSgearwayrvSQGRFP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 355 PGIKIRIVDeDGKSLG---YNQvGEIYVHTGQAWNGYYGNPVETR-------RMQDFE---------GWFHTGDLGYFDE 415
Cdd:PRK05620 365 ASLEYRIVN-DGQVMEstdRNE-GEIQVRGNWVTASYYHSPTEEGggaastfRGEDVEdandrftadGWLRTGDVGSVTR 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653035 416 QNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISAkEIVEHVAKRL 493
Cdd:PRK05620 443 DGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR-ETAERLRDQL 519
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
65-521 |
1.80e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.78 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 65 SIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGtpfHSVNPVlDDAT----LTHVFSITKPTLIFCdgqeydk 140
Cdd:PRK04813 37 SDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG---HAYIPV-DVSSpaerIEMIIEVAKPSLIIA------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 141 vhkaTVGWHPEILTLTdhvegVQGIETLLDPTTTEKIYQPEVLKEGgDQTVAILCSSGTTGLPKAVCIS-NSIL------ 213
Cdd:PRK04813 106 ----TEELPLEILGIP-----VITLDELKDIFATGNPYDFDHAVKG-DDNYYIIFTSGTTGKPKGVQIShDNLVsftnwm 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 214 IQDSMLITSQ------------SVIYVGSCLdwitglwafvfstVFGCTRIISNKAftpeyfvgLVKKYKINYAVLPPRH 281
Cdd:PRK04813 176 LEDFALPEGPqflnqapysfdlSVMDLYPTL-------------ASGGTLVALPKD--------MTANFKQLFETLPQLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 282 LSALITCP--------DAKPDA--LAPITHLNYGGGSISLATLQRSQELCKTAM-FNSgYGMTE-VGAIT-INIG---IS 345
Cdd:PRK04813 235 INVWVSTPsfadmcllDPSFNEehLPNLTHFLFCGEELPHKTAKKLLERFPSATiYNT-YGPTEaTVAVTsIEITdemLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 346 NVSS--AGRPVPGIKIRIVDEDGKSLGYNQVGEIYVhTGQAWN-GYYGNPVETRR-MQDFEGW--FHTGDLGYFDEQNFL 419
Cdd:PRK04813 314 QYKRlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGPSVSkGYLNNPEKTAEaFFTFDGQpaYHTGDAGYLEDGLLF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 420 YivdrKKEI---LKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKG-----ATISaKEIVEHVAK 491
Cdd:PRK04813 393 Y----QGRIdfqIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEdfereFELT-KAIKKELKE 467
|
490 500 510
....*....|....*....|....*....|...
gi 24653035 492 RLPA---TQKQLragvqFTDKLPANVNGKTMRK 521
Cdd:PRK04813 468 RLMEymiPRKFI-----YRDSLPLTPNGKIDRK 495
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
179-521 |
2.81e-15 |
|
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: 78.13 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 179 QPEVLKEGGDQTVAILCSSGTTGLPKAVCISNSiliqdsmlitsqsviYVGSCLDWItglwafvfSTVFGCTRIISNKAF 258
Cdd:cd12115 96 QARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHR---------------NAAAFLQWA--------AAAFSAEELAGVLAS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 259 TP--------EYFVGLVKKYKINYA--VLPPRHLSA-----LI-TCPDA-----KPDALAP-ITHLNYGGGSISLATLQR 316
Cdd:cd12115 153 TSicfdlsvfELFGPLATGGKVVLAdnVLALPDLPAaaevtLInTVPSAaaellRHDALPAsVRVVNLAGEPLPRDLVQR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 317 SQELCKTA-MFNSgYGMTEvgAIT------INIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYY 389
Cdd:cd12115 233 LYARLQVErVVNL-YGPSE--DTTystvapVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 390 GNPVET------------RRMqdfegwFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVV 457
Cdd:cd12115 310 GRPGLTaerflpdpfgpgARL------YRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVV 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653035 458 GIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPATqkQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd12115 384 AIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAY--MVPSRFVRLDALPLTPNGKIDRS 445
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
351-522 |
3.26e-15 |
|
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: 78.14 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 351 GRPV-PGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEIL 429
Cdd:cd05920 311 GRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQI 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 430 KYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVkSKGATISAKEIVEHVAKRLPATQKqLRAGVQFTDK 509
Cdd:cd05920 391 NRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVV-LRDPPPSAAQLRRFLRERGLAAYK-LPDRIEFVDS 468
|
170
....*....|...
gi 24653035 510 LPANVNGKTMRKT 522
Cdd:cd05920 469 LPLTAVGKIDKKA 481
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-524 |
3.32e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 77.04 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVCIS---------NSILIQDSMLITSQ-----------SVIYVGSCLDWITGLWAFVFSTVFGCTRI 252
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRqedifrmlmGGADFGTGEFTPSEdahkaaaaaagTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 253 ISNKAFTPEYFVGLVKKYKINY------AVLPPRhLSALitcPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMF 326
Cdd:cd05924 88 LPDDRFDPEEVWRTIEKHKVTSmtivgdAMARPL-IDAL---RDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 327 NSGYGMTEVGAI-TINIGISNVSSAGRPVPGIKIRIVDEDGKSL--GYNQVGEIyVHTGQAWNGYYGNP---VETRRMQD 400
Cdd:cd05924 164 VDAFGSSETGFTgSGHSAGSGPETGPFTRANPDTVVLDDDGRVVppGSGGVGWI-ARRGHIPLGYYGDEaktAETFPEVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 401 FEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATI 480
Cdd:cd05924 243 GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGV 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24653035 481 SAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTAR 524
Cdd:cd05924 323 DLEELREHCRTRI-ARYKLPKQ-VVFVDEIERSPAGKADYRWAK 364
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
187-521 |
3.92e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.05 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 187 GDQTVAILCSSGTTGLPKAVCISNSILiqdSMLITSQSVIYVGSCLDWITGLWAFVF-STVF---------GCTRIISNK 256
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGAL---ANHLCWIAEAYELDANDRVLLFMSFSFdGAQErflwtlicgGCLVVRDND 3312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 257 AFTPEYFVGLVKKYKINYAVLPPRHLSALITcpDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE-- 334
Cdd:PRK12467 3313 LWDPEELWQAIHAHRISIACFPPAYLQQFAE--DAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEav 3390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 VGAITINIGISNVSSA-----GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET--RRMQD-FEG--- 403
Cdd:PRK12467 3391 VTVTLWKCGGDAVCEApyapiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaeRFVADpFSGsgg 3470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 404 -WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIsA 482
Cdd:PRK12467 3471 rLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDW-R 3549
|
330 340 350
....*....|....*....|....*....|....*....
gi 24653035 483 KEIVEHVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:PRK12467 3550 ETLRDHLAASLP--DYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
186-525 |
4.17e-15 |
|
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: 77.35 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 186 GGDQTVAILCSSGTTGLPKAVCISNSILI------QDSMLIT-SQSVIYVGScldwiTGLWAF---VFSTV-FGCTRIIS 254
Cdd:cd17653 103 SPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyvsqpPARLDVGpGSRVAQVLS-----IAFDACigeIFSTLcNGGTLVLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 255 NkafTPEYFVGLVKKykINYAVLPPrhlSALITCPDAKPDALAPIThlnYGGGSISLATLQRSQElcKTAMFNsGYGMTE 334
Cdd:cd17653 178 D---PSDPFAHVART--VDALMSTP---SILSTLSPQDFPNLKTIF---LGGEAVPPSLLDRWSP--GRRLYN-AYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 --VGAITINIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR----MQDFEGW--FH 406
Cdd:cd17653 244 ctISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSrmYR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 407 TGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIE-TVIAELSQVQDVCVVGIydereGDAAGALVVKskgATISAKEI 485
Cdd:cd17653 324 TGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEeVVLQSQPEVTQAAAIVV-----NGRLVAFVTP---ETVDVDGL 395
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24653035 486 VEHVAKRLP--ATQKQLRAgvqfTDKLPANVNGKTMRKTARD 525
Cdd:cd17653 396 RSELAKHLPsyAVPDRIIA----LDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
196-517 |
6.87e-15 |
|
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: 77.06 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKAVCISNSILIQdsmLITSQSVIYVGSCLDW--ITGLWAFVF---------STVFGCTRIISNK--AFTPEY 262
Cdd:cd17648 102 TSGTTGKPKGVLVEHGSVVN---LRTSLSERYFGRDNGDeaVLFFSNYVFdffveqmtlALLNGQKLVVPPDemRFDPDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 263 FVGLVKKYKINYAVLPPRHLSALitcpdakpdALAPITHLN---YGGGSISLATLQRSQELCKTAMFNsGYGMTEVGAIT 339
Cdd:cd17648 179 FYAYINREKVTYLSGTPSVLQQY---------DLARLPHLKrvdAAGEEFTAPVFEKLRSRFAGLIIN-AYGPTETTVTN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 340 INIGISNVS----SAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET--------------RRMQDF 401
Cdd:cd17648 249 HKRFFPGDQrfdkSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTaerflpnpfqteqeRARGRN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 402 EGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGA--LV---VKSK 476
Cdd:cd17648 329 ARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkyLVgyyLPEP 408
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24653035 477 GaTISAKEIVEHVAKRLPATQ--KQLragVQFtDKLPANVNGK 517
Cdd:cd17648 409 G-HVPESDLLSFLRAKLPRYMvpARL---VRL-EGIPVTINGK 446
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
67-495 |
6.88e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.19 E-value: 6.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKN--STYVMPLGVAclMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDgQEYDKV--- 141
Cdd:PLN02479 57 RLASALAKRSIGPGSTVAVIAPNipAMYEAHFGVP--MAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVD-QEFFTLaee 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 142 ------HKATVGWHPEIL-TLTDHVEGVQGIETLLDPTTTEKiyqpEVLKEGGD------------QTVAILCSSGTTGL 202
Cdd:PLN02479 134 alkilaEKKKSSFKPPLLiVIGDPTCDPKSLQYALGKGAIEY----EKFLETGDpefawkppadewQSIALGYTSGTTAS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 203 PKAVCISNS---ILIQDSMLI--TSQSVIYV---------GSCLDWitGLWAFVFSTVfgCTRIISNKAFtpeyfVGLVK 268
Cdd:PLN02479 210 PKGVVLHHRgayLMALSNALIwgMNEGAVYLwtlpmfhcnGWCFTW--TLAALCGTNI--CLRQVTAKAI-----YSAIA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 269 KYKINYAVLPPRHLSALITCPdaKPDALAP---ITHLNYGGG----SISLATLQRSQELCKTAMFNSGYGMTEVGA---- 337
Cdd:PLN02479 281 NYGVTHFCAAPVVLNTIVNAP--KSETILPlprVVHVMTAGAapppSVLFAMSEKGFRVTHTYGLSETYGPSTVCAwkpe 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 338 -----------ITINIGISNVSSAGRPVPGIK-IRIVDEDGKSLGynqvgEIYVHTGQAWNGYYGNPVETRrmQDFE-GW 404
Cdd:PLN02479 359 wdslppeeqarLNARQGVRYIGLEGLDVVDTKtMKPVPADGKTMG-----EIVMRGNMVMKGYLKNPKANE--EAFAnGW 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 405 FHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS--- 481
Cdd:PLN02479 432 FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdea 511
|
490
....*....|....*.
gi 24653035 482 --AKEIVEHVAKRLPA 495
Cdd:PLN02479 512 alAEDIMKFCRERLPA 527
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
67-527 |
7.45e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 77.05 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVL------------DDATLthVFSITKPTLIfcd 134
Cdd:PRK07008 51 QLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLfpeqiayivnhaEDRYV--LFDLTFLPLV--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 135 gqeyDKVHKA--TV-GWhpeiLTLTDHVE------GVQGIETLLDPTTTEkiYQPEVLKEggdQTVAILC-SSGTTGLPK 204
Cdd:PRK07008 126 ----DALAPQcpNVkGW----VAMTDAAHlpagstPLLCYETLVGAQDGD--YDWPRFDE---NQASSLCyTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 205 AVCISN--SIL------IQDSMLITSQSVI-------YVGScldwitglWAFVFS-TVFGCTRIISNKAFTPEYFVGLVK 268
Cdd:PRK07008 193 GALYSHrsTVLhaygaaLPDAMGLSARDAVlpvvpmfHVNA--------WGLPYSaPLTGAKLVLPGPDLDGKSLYELIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 269 KYKINYAVLPPRHLSALITcpdakpdalapitHLNYGGgsISLATLQRS---QELCKTAMFNS-----------GYGMTE 334
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLLN-------------HMREAG--LRFSTLRRTvigGSACPPAMIRTfedeygvevihAWGMTE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 VGAITINIGISNVSSA-------------GRPVPGIKIRIVDEDGKSLGYNQV--GEIYVHTGQAWNGYYGNpvETRRMQ 399
Cdd:PRK07008 330 MSPLGTLCKLKWKHSQlpldeqrkllekqGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFRG--DASPLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 400 DfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIY----DEREGDAagalVVKS 475
Cdd:PRK07008 408 D--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAhpkwDERPLLV----VVKR 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24653035 476 KGATISAKEIVEH----VAKRlpatqkQLRAGVQFTDKLPANVNGKTMRKTARDVF 527
Cdd:PRK07008 482 PGAEVTREELLAFyegkVAKW------WIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
54-524 |
7.83e-15 |
|
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: 77.09 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 54 VTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFC 133
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 134 DgQEYDKVHKatvgwhpEILTLTDHVEGvqgietllDPTTTEKIYQPEVLKEGGDQT------------VAILCSSGTTG 201
Cdd:cd05915 103 D-PNLLPLVE-------AIRGELKTVQH--------FVVMDEKAPEGYLAYEEALGEeadpvrvperaaCGMAYTTGTTG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 202 LPKAVCISN--------SILIQDSMLITSQSViYVGSCLDWITGLWAFVFS-TVFG----CTRIISNKAFTpeyFVGLVK 268
Cdd:cd05915 167 LPKGVVYSHralvlhslAASLVDGTALSEKDV-VLPVVPMFHVNAWCLPYAaTLVGakqvLPGPRLDPASL---VELFDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 269 KYKINYAVLPPRhLSALITCPDAKPDALAPITHLNYGGGSISLATLQrsqeLCKTAMFN--SGYGMTEVGAITINI---- 342
Cdd:cd05915 243 EGVTFTAGVPTV-WLALADYLESTGHRLKTLRRLVVGGSAAPRSLIA----RFERMGVEvrQGYGLTETSPVVVQNfvks 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 343 -----------------GISNVSSAGRPVPGIKIRiVDEDGKSLGYnqvgeIYVHTGQAWNGYYGNPVETRRMQDFEGWF 405
Cdd:cd05915 318 hleslseeekltlkaktGLPIPLVRLRVADEEGRP-VPKDGKALGE-----VQLKGPWITGGYYGNEEATRSALTPDGFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 406 HTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALvVKSKGATISAKEI 485
Cdd:cd05915 392 RTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRGEKPTPEEL 470
|
490 500 510
....*....|....*....|....*....|....*....
gi 24653035 486 VEHVAKRLpATQKQLRAGVQFTDKLPANVNGKTMRKTAR 524
Cdd:cd05915 471 NEHLLKAG-FAKWQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-520 |
1.12e-14 |
|
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: 76.35 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVCISNSIL------IQDSMLITSQSViyvgsclDWITGLWAFVFSTVFGCTRIISNKAFT-- 259
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFaaqidaLRQLYGIRPGEV-------DLATFPLFALFGPALGLTSVIPDMDPTrp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 260 ----PEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQR-SQELCKTAMFNSGYGMTE 334
Cdd:cd05910 158 aradPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARlRKMLSDEAEILTPYGATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 335 VGAITInIGISNVSSA-------------GRPVPGIKIRIVD---------EDGKSLGYNQVGEIYVHTGQAWNGYYGNP 392
Cdd:cd05910 238 ALPVSS-IGSRELLATttaatsggagtcvGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 393 VETR--RMQDFEG--WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIydEREGDAA 468
Cdd:cd05910 317 VATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKPGCQL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24653035 469 GALVVKS-KGATISAKEIVEHV---AKRLPATQKQLRagVQFTDKLPANV--NGKTMR 520
Cdd:cd05910 395 PVLCVEPlPGTITPRARLEQELralAKDYPHTQRIGR--FLIHPSFPVDIrhNAKIFR 450
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
329-446 |
1.27e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 76.68 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVGAI--TINIGISNVSSAGRPVPGIKIRIVDEdgKSLGYNQV------GEIYVHTGQAWNGYYGNPVETRRMQD 400
Cdd:PLN02736 407 GYGMTETSCVisGMDEGDNLSGHVGSPNPACEVKLVDV--PEMNYTSEdqpyprGEICVRGPIIFKGYYKDEVQTREVID 484
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 24653035 401 FEGWFHTGDLGYFDEQNFLYIVDRKKEILKY-NGLHYWPTEIETVIA 446
Cdd:PLN02736 485 EDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYA 531
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
188-497 |
1.57e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.09 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVCISNSILIQDSMLITSQSVIYVGScldwiTGLWAF----VFSTVFGCTRIISNKAFT---- 259
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGE-----IDLPTFplfaLFGPALGMTSVIPDMDPTrpat 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 260 --PEYFVGLVKKYKINYAVLPPrhlsALItcpdakpDALApithlNYGGGS-ISLATLQR-----------SQELCkTAM 325
Cdd:PRK09274 249 vdPAKLFAAIERYGVTNLFGSP----ALL-------ERLG-----RYGEANgIKLPSLRRvisagapvpiaVIERF-RAM 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 326 FNSG------YGMTE------VGAITINIGISNVSSA------GRPVPGIKIRIVD---------EDGKSLGYNQVGEIY 378
Cdd:PRK09274 312 LPPDaeiltpYGATEalpissIESREILFATRAATDNgagicvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 379 VHTGQAWNGYYGNPVETR--RMQDFEG--WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDV 454
Cdd:PRK09274 392 VAGPMVTRSYYNRPEATRlaKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24653035 455 CVVGIydEREGDAAGALVV-KSKGATISAKEI---VEHVAKRLPATQ 497
Cdd:PRK09274 472 ALVGV--GVPGAQRPVLCVeLEPGVACSKSALyqeLRALAAAHPHTA 516
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
54-517 |
2.87e-14 |
|
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: 74.82 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 54 VTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS--TYVMPLgvACLMNGTPFHSVNPVLDDATLTHVFsitKPTLI 131
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGteSPVAIL--AILFLGAAYAPIDPASPEQRSLTVM---KKCHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGQEyDKVHKATVGWHPEiltltdhvegvqgietlldpTTTEKIYQPEVLkeggdqtVAILCSSGTTGLPKAV----- 206
Cdd:cd17654 90 SYLLQN-KELDNAPLSFTPE--------------------HRHFNIRTDECL-------AYVIHTSGTTGTPKIVavphk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 207 CISNSILIQDSMLITSQSVIYVGscldwiTGLWAFVFSTV-------FGCTRIISNKA-------FTPEYFvglvKKYKI 272
Cdd:cd17654 142 CILPNIQHFRSLFNITSEDILFL------TSPLTFDPSVVeiflslsSGATLLIVPTSvkvlpskLADILF----KRHRI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 273 NYAVLPP----RHLSALItcpdaKPDALAPITHLNYG--GGS---ISLATLQRSQELCKTAMFNSgYGMTEVGAITINIG 343
Cdd:cd17654 212 TVLQATPtlfrRFGSQSI-----KSTVLSATSSLRVLalGGEpfpSLVILSSWRGKGNRTRIFNI-YGITEVSCWALAYK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 344 ISNVSSA---GRPVPGIKIRIVDEDGKSlgynQVGEIYVhtGQAWNGYYGNPVETRRMQDfegWFHTGDLGYFdEQNFLY 420
Cdd:cd17654 286 VPEEDSPvqlGSPLLGTVIEVRDQNGSE----GTGQVFL--GGLNRVCILDDEVTVPKGT---MRATGDFVTV-KDGELF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 421 IVDRKKEILKYNGLHYWPTEIETVIAELSQVQDvCVVGIYDEREgdaagaLVVKSKGATISAKEIVEHVAKRLPATQKQL 500
Cdd:cd17654 356 FLGRKDSQIKRRGKRINLDLIQQVIESCLGVES-CAVTLSDQQR------LIAFIVGESSSSRIHKELQLTLLSSHAIPD 428
|
490
....*....|....*..
gi 24653035 501 RagVQFTDKLPANVNGK 517
Cdd:cd17654 429 T--FVQIDKLPLTSHGK 443
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
28-495 |
4.61e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 74.91 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 28 TSVGKIIFNNMKNWPKNVCQIcdVDGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS-TYVM------PLGVAC 100
Cdd:PRK08279 37 RSLGDVFEEAAARHPDRPALL--FEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRpEYLAawlglaKLGAVV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 101 LMngtpfhsVNPVLDDATLTHVFSITKPTLIFCDG---QEYDKVhKATVGWHPEILTLTD----HVEGVQGIETLL---- 169
Cdd:PRK08279 115 AL-------LNTQQRGAVLAHSLNLVDAKHLIVGEelvEAFEEA-RADLARPPRLWVAGGdtldDPEGYEDLAAAAagap 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 170 --DPTTTEKIYqpevlkeGGDQTVAILcSSGTTGLPKAVCISNSiliqdsmlitsqsviyvgsclDWITglWAFVFStvf 247
Cdd:PRK08279 187 ttNPASRSGVT-------AKDTAFYIY-TSGTTGLPKAAVMSHM---------------------RWLK--AMGGFG--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 248 GCTRIISNKAFtpeyfvglvkkykinYAVLPPRHLSALITCPDAkpdALApithlnyGGGSISL---------------- 311
Cdd:PRK08279 233 GLLRLTPDDVL---------------YCCLPLYHNTGGTVAWSS---VLA-------AGATLALrrkfsasrfwddvrry 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 312 -ATL-QRSQELCK----------------TAMFNSG---------------------YGMTEvGaitiNIGISNV----S 348
Cdd:PRK08279 288 rATAfQYIGELCRyllnqppkptdrdhrlRLMIGNGlrpdiwdefqqrfgiprilefYAASE-G----NVGFINVfnfdG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 349 SAGRpVPGIK---IRIV-----------DEDGKSL--GYNQVGEIYVHTGQAWN--GyYGNPVETRR--MQD-FE-G--W 404
Cdd:PRK08279 363 TVGR-VPLWLahpYAIVkydvdtgepvrDADGRCIkvKPGEVGLLIGRITDRGPfdG-YTDPEASEKkiLRDvFKkGdaW 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 405 FHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGI----YDEREGDAagALVVKSkGATI 480
Cdd:PRK08279 441 FNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVevpgTDGRAGMA--AIVLAD-GAEF 517
|
570
....*....|....*
gi 24653035 481 SAKEIVEHVAKRLPA 495
Cdd:PRK08279 518 DLAALAAHLYERLPA 532
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
196-521 |
4.62e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.92 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKavCISNS-------ILIQDSMLITSQSVIYVGSCLdwITGLWAFVFSTVFGCTR-----IISNKafTPEYF 263
Cdd:PRK08308 109 SSGTTGEPK--LIRRSwteidreIEAYNEALNCEQDETPIVACP--VTHSYGLICGVLAALTRgskpvIITNK--NPKFA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 264 VGLVKKYK--INYAVlpPRHLSALITCPDAK-------------PDALapithlnygggsisLATLQ-RSQELCKTamfn 327
Cdd:PRK08308 183 LNILRNTPqhILYAV--PLMLHILGRLLPGTfqfhavmtsgtplPEAW--------------FYKLReRTTYMMQQ---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 sgYGMTEVGAITINIGISNVSSAGRPVPGIKIRIvdedgkSLGYNQVGEIYVHTGQawngyygnpvetRRMqdfegwfHT 407
Cdd:PRK08308 243 --YGCSEAGCVSICPDMKSHLDLGNPLPHVSVSA------GSDENAPEEIVVKMGD------------KEI-------FT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 408 GDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKgaTISAKEIVE 487
Cdd:PRK08308 296 KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQLRE 373
|
330 340 350
....*....|....*....|....*....|....
gi 24653035 488 HVAKRLPATQKQLRagVQFTDKLPANVNGKTMRK 521
Cdd:PRK08308 374 WCIQHLAPYQVPHE--IESVTEIPKNANGKVSRK 405
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
196-524 |
5.48e-14 |
|
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: 74.14 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKAVCISnsiliQDSMLITSQSVIY-VG----------SCLDWITGLWAFVFS--TVFGCTRIISNKAFTPEY 262
Cdd:cd05974 93 TSGTTSKPKLVEHT-----HRSYPVGHLSTMYwIGlkpgdvhwniSSPGWAKHAWSCFFApwNAGATVFLFNYARFDAKR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 263 FVGLVKKYKINYAVLPPRHLSALITCPDAKPDAlaPITHLNYGGGSISLATLQRSQELCKTAMfNSGYGMTEVGAITINI 342
Cdd:cd05974 168 VLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV--KLREVVGAGEPLNPEVIEQVRRAWGLTI-RDGYGQTETTALVGNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 343 GISNV--SSAGRPVPGIKIRIVDEDGKSLgynQVGEIYVHTGQA-----WNGYYGNPVETRR-MQDfeGWFHTGDLGYFD 414
Cdd:cd05974 245 PGQPVkaGSMGRPLPGYRVALLDPDGAPA---TEGEVALDLGDTrpvglMKGYAGDPDKTAHaMRG--GYYRTGDIAMRD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 415 EQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---AKEIVEHVAK 491
Cdd:cd05974 320 EDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSpetALEIFRFSRE 399
|
330 340 350
....*....|....*....|....*....|...
gi 24653035 492 RLpATQKQLRAgVQFTDkLPANVNGKTMRKTAR 524
Cdd:cd05974 400 RL-APYKRIRR-LEFAE-LPKTISGKIRRVELR 429
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
67-521 |
6.83e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.99 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLThvFSITKPTLIFCDGQEYDKVhkatv 146
Cdd:PRK12316 3094 RLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLA--YMLEDSGAQLLLSQSHLRL----- 3166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 147 gwhpeiltltDHVEGVQGIetLLDPTTTEKIYQPEVLKEGGDQTVAILCSSGTTGLPKAVCISNSIL------IQDSMLI 220
Cdd:PRK12316 3167 ----------PLAQGVQVL--DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALsnhlcwMQQAYGL 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 221 TSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIISNK--AFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAP 298
Cdd:PRK12316 3235 GVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPedWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLK 3314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 299 ITHLnygGGSISLATLQrSQELCKTAMFNSgYGMTE----VGAITINIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQV 374
Cdd:PRK12316 3315 RIVC---GGEALPADLQ-QQVFAGLPLYNL-YGPTEatitVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGAL 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 375 GEIYVHTGQAWNGYYGNPVET--RRMQD----FEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAEL 448
Cdd:PRK12316 3390 GELYLGGEGLARGYHNRPGLTaeRFVPDpfvpGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH 3469
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653035 449 SQVQDVCVVGIyderEGDAAGALVVKSKGATISAKEIVEHVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:PRK12316 3470 PWVREAVVLAV----DGRQLVAYVVPEDEAGDLREALKAHLKASLP--EYMVPAHLLFLERMPLTPNGKLDRK 3536
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
324-458 |
1.37e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 73.31 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 324 AMFNSGYGMTE-VGAITINI--GISNVSSAGRPVPGIKIRI--VDEDG-KSLGYNQVGEIYVHTGQAWNGYYGNPVETRR 397
Cdd:PLN02430 409 AFVVQGYGLTEtLGPTTLGFpdEMCMLGTVGAPAVYNELRLeeVPEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEE 488
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653035 398 -MQDfeGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTE-IETVIAELSQVQDVCVVG 458
Cdd:PLN02430 489 vMKD--GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLENVYGQNPIVEDIWVYG 549
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
38-527 |
1.41e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 73.25 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 38 MKNWPKNVCQICD---------------VDG--VTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNST------Y-V 93
Cdd:PRK06018 5 MQDWPLLCHRIIDhaarihgnrevvtrsVEGpiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWrhleawYgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 94 MPLGVAClmngtpfHSVNPVLDDATLTHVFSITKPTLIFCDgqeydkvhkatVGWHPEILTLTDHVEGVQGIETLLD--- 170
Cdd:PRK06018 85 MGIGAIC-------HTVNPRLFPEQIAWIINHAEDRVVITD-----------LTFVPILEKIADKLPSVERYVVLTDaah 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 171 -PTTTEK---IYQPEVLKEGGD--------QTVAILC-SSGTTGLPKAVCISNSILIQDSMlITSQSVIYVGSCLDWI-- 235
Cdd:PRK06018 147 mPQTTLKnavAYEEWIAEADGDfawktfdeNTAAGMCyTSGTTGDPKGVLYSHRSNVLHAL-MANNGDALGTSAADTMlp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 236 ------TGLWAFVFSTVFGCTRIISNKAFTPEYFV-GLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGS 308
Cdd:PRK06018 226 vvplfhANSWGIAFSAPSMGTKLVMPGAKLDGASVyELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 309 ISLATLQRSQELCKTAMfnSGYGMTEVGAI----TINIGISNVS---------SAGRPVPGIKIRIVDEDGKSLGY--NQ 373
Cdd:PRK06018 306 MPRSMIKAFEDMGVEVR--HAWGMTEMSPLgtlaALKPPFSKLPgdarldvlqKQGYPPFGVEMKITDDAGKELPWdgKT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 374 VGEIYVHTGQAWNGYYGnpVETRRMQDfEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQD 453
Cdd:PRK06018 384 FGRLKVRGPAVAAAYYR--VDGEILDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAE 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653035 454 VCVVGIYDEREGDAAGALVVKSKGATISAKEIVEH----VAK-RLPATqkqlragVQFTDKLPANVNGKTMRKTARDVF 527
Cdd:PRK06018 461 AAVIGVYHPKWDERPLLIVQLKPGETATREEILKYmdgkIAKwWMPDD-------VAFVDAIPHTATGKILKTALREQF 532
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
55-500 |
1.41e-13 |
|
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: 72.77 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 55 TVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNS-TYVMP-LGVACLmnGTPFHSVNPVLDDATLTHVFSITKPTLIF 132
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRpEYVLLwLGLVKI--GAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 133 CDGQEYdkvhkatvgwhpeiltltdhvegvqgietlldptttekIYqpevlkeggdqtvailcSSGTTGLPKAVCISNS- 211
Cdd:cd05940 81 VDAALY--------------------------------------IY-----------------TSGTTGLPKAAIISHRr 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 212 -----ILIQDSMLITSQSVIYvgSCLDW---ITGLWAFVFSTVFGCTRIISNKaFTPEYFVGLVKKYK---INYAVLPPR 280
Cdd:cd05940 106 awrggAFFAGSGGALPSDVLY--TCLPLyhsTALIVGWSACLASGATLVIRKK-FSASNFWDDIRKYQatiFQYIGELCR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 281 HLSALITCPDAKPDALAPIthlnYGGG---SISLATLQRsqelcktamFNSG-----YGMTEVgaitiNIGISNVSS--- 349
Cdd:cd05940 183 YLLNQPPKPTERKHKVRMI----FGNGlrpDIWEEFKER---------FGVPriaefYAATEG-----NSGFINFFGkpg 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 350 -AGR-PVPGIK---IRIV-----------DEDG--KSLGYNQVGEIYVHTGQAWN--GYYGNPVETRRM-----QDFEGW 404
Cdd:cd05940 245 aIGRnPSLLRKvapLALVkydlesgepirDAEGrcIKVPRGEPGLLISRINPLEPfdGYTDPAATEKKIlrdvfKKGDAW 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 405 FHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDER-EGDAAGALVVKSKGATISAK 483
Cdd:cd05940 325 FNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGtDGRAGMAAIVLQPNEEFDLS 404
|
490
....*....|....*..
gi 24653035 484 EIVEHVAKRLPATQKQL 500
Cdd:cd05940 405 ALAAHLEKNLPGYARPL 421
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
351-490 |
2.37e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.49 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 351 GRPVPGIKIRIVDEDGKS-LGYNQVGEIYVHTGQAWNGYYGN-PVETrrmqdfEGWFHTGDLGYFDEQNfLYIVDRKKEI 428
Cdd:PRK05851 348 GNPIPGMEVRISPGDGAAgVAGREIGEIEIRGASMMSGYLGQaPIDP------DDWFPTGDLGYLVDGG-LVVCGRAKEL 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653035 429 LKYNGLHYWPTEIETVIAELSQVQDVCVVGIyDEREGDAAGALVVKS--KGATISA--KEIVEHVA 490
Cdd:PRK05851 421 ITVAGRNIFPTEIERVAAQVRGVREGAVVAV-GTGEGSARPGLVIAAefRGPDEAGarSEVVQRVA 485
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
67-531 |
1.04e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 67 RIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLIFCDGqeydkvhkatv 146
Cdd:PRK12316 2040 RLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR----------- 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 147 gwhpeilTLTDHVEGVQGIETL-LDPTTTEKIY---QPEVlKEGGDQTVAILCSSGTTGLPKAVCISNSILIqdsMLITS 222
Cdd:PRK12316 2109 -------HLLERLPLPAGVARLpLDRDAEWADYpdtAPAV-QLAGENLAYVIYTSGSTGLPKGVAVSHGALV---AHCQA 2177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 223 QSVIYVGSCLDWITGLWAFVF-STVFGCTRIISNKA---------FTPEYFVGLVKKYKINYAVLPPRHLSALITcpDAK 292
Cdd:PRK12316 2178 AGERYELSPADCELQFMSFSFdGAHEQWFHPLLNGArvlirddelWDPEQLYDEMERHGVTILDFPPVYLQQLAE--HAE 2255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 293 PDALAP-ITHLNYGGGSISLATLQRSQELCKT-AMFNsGYGMTEVgAITINI--------GISNVSSAGRPVPGIKIRIV 362
Cdd:PRK12316 2256 RDGRPPaVRVYCFGGEAVPAASLRLAWEALRPvYLFN-GYGPTEA-VVTPLLwkcrpqdpCGAAYVPIGRALGNRRAYIL 2333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 363 DEDGKSLGYNQVGEIYV-HTGQAwNGYYGNPVET--RRMQD-FEG----WFHTGDLGYFDEQNFLYIVDRKKEILKYNGL 434
Cdd:PRK12316 2334 DADLNLLAPGMAGELYLgGEGLA-RGYLNRPGLTaeRFVPDpFSAsgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGF 2412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 435 HYWPTEIETVIAELSQVQDVCVVGIyDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPAtqKQLRAGVQFTDKLPANV 514
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPA--YMVPAHWVVLERLPLNP 2489
|
490
....*....|....*..
gi 24653035 515 NGKTMRKTARDVFVALR 531
Cdd:PRK12316 2490 NGKLDRKALPKPDVSQL 2506
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
305-457 |
1.66e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 70.01 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 305 GGGSISLATlqrsQELCKT--AMFNSGYGMTE---VGAITInIGISNVSSAGRPVPGIKIRIVDEDGkslgynqvgeiYV 379
Cdd:PTZ00216 436 GGGPLSAAT----QEFVNVvfGMVIQGWGLTEtvcCGGIQR-TGDLEPNAVGQLLKGVEMKLLDTEE-----------YK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 380 HTGQA-------------WNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKyNGL-HYWPTE-IETV 444
Cdd:PTZ00216 500 HTDTPeprgeillrgpflFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAK-NCLgEYIALEaLEAL 578
|
170
....*....|....*
gi 24653035 445 IA--ELSQVQDVCVV 457
Cdd:PTZ00216 579 YGqnELVVPNGVCVL 593
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
332-526 |
2.26e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 69.40 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 332 MTEVGAITIN--IGISNV--SSAGRPVPGIKIRIVDEDGKSLGYNQVGeiYVHTGQAWNGY----YGNPvetRRMQD--- 400
Cdd:PRK00174 404 QTETGGIMITplPGATPLkpGSATRPLPGIQPAVVDEEGNPLEGGEGG--NLVIKDPWPGMmrtiYGDH---ERFVKtyf 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 401 --FEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGlHYWPT-EIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKG 477
Cdd:PRK00174 479 stFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSG-HRLGTaEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGG 557
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24653035 478 ATIS---AKEIVEHVAKRL-P-ATQKQlragVQFTDKLPANVNGKTMRKTARDV 526
Cdd:PRK00174 558 EEPSdelRKELRNWVRKEIgPiAKPDV----IQFAPGLPKTRSGKIMRRILRKI 607
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
53-495 |
2.51e-12 |
|
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: 69.24 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 53 GVTVTFEQGLTWSIRIAQYLKK-RGLNHKDVIGIAAKNS-TYV-MPLGVACLmnGTPFHSVNPVLDDATLTHVFSITKPT 129
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEpAFLwIWLGLAKL--GCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 130 LIFCDGQEYDKVHKATV-----GWHPEILTLTDHVEGVQGIETLLDPTTTEKIyqPEVLKEG--GDQTVAILCSSGTTGL 202
Cdd:cd05938 81 VLVVAPELQEAVEEVLPalradGVSVWYLSHTSNTEGVISLLDKVDAASDEPV--PASLRAHvtIKSPALYIYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 203 PKAVCISNSILIQDSML-----ITSQSVIYVGSCLDWITG-LWAFVFSTVFGCTRIISNKaFTPEYFVGLVKKYK---IN 273
Cdd:cd05938 159 PKAARISHLRVLQCSGFlslcgVTADDVIYITLPLYHSSGfLLGIGGCIELGATCVLKPK-FSASQFWDDCRKHNvtvIQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 274 YAVLPPRHLSALITCPDAKPDALapitHLNYGGG---SISLATLQRSQELCktamFNSGYGMTEVgaitiNIGISN---- 346
Cdd:cd05938 238 YIGELLRYLCNQPQSPNDRDHKV----RLAIGNGlraDVWREFLRRFGPIR----IREFYGSTEG-----NIGFFNytgk 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 347 VSSAGR---------PVPGIK--------IRivDEDGKSL--GYNQVGEIY--VHTGQAWNGYYGNPVET--RRMQD-FE 402
Cdd:cd05938 305 IGAVGRvsylykllfPFELIKfdvekeepVR--DAQGFCIpvAKGEPGLLVakITQQSPFLGYAGDKEQTekKLLRDvFK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 403 G---WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDE-REGDAAGALVVKSKGA 478
Cdd:cd05938 383 KgdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLKPGH 462
|
490
....*....|....*..
gi 24653035 479 TISAKEIVEHVAKRLPA 495
Cdd:cd05938 463 EFDGKKLYQHVREYLPA 479
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
193-526 |
2.69e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 69.14 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVC---------------------ISNSILIQDSMLITSQSVIYVGSCLDWITGLWAfVFSTVF--GC 249
Cdd:PRK07798 168 LLYTGGTTGMPKGVMwrqedifrvllggrdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWA-AFAALFsgQT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 250 TRIISNKAFTPEYFVGLVKKYKINyavlpprhlsaLITCP-DA--KP--DALAP--------ITHLNYGGGSISLATLQR 316
Cdd:PRK07798 247 VVLLPDVRFDADEVWRTIEREKVN-----------VITIVgDAmaRPllDALEArgpydlssLFAIASGGALFSPSVKEA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 317 SQELCKTAMFNSGYGMTEVGaitiNIGISNVSSAGRPVPGIKIRI------VDEDGKSL--GYNQVGEIyVHTGQAWNGY 388
Cdd:PRK07798 316 LLELLPNVVLTDSIGSSETG----FGGSGTVAKGAVHTGGPRFTIgprtvvLDEDGNPVepGSGEIGWI-ARRGHIPLGY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 389 YGNPVETRR-MQDFEG--WFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREG 465
Cdd:PRK07798 391 YKDPEKTAEtFPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWG 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653035 466 DAAGALVVKSKGATISAKEIVEHVAKRLpATQKQLRAgVQFTDKLPANVNGKTMRKTARDV 526
Cdd:PRK07798 471 QEVVAVVQLREGARPDLAELRAHCRSSL-AGYKVPRA-IWFVDEVQRSPAGKADYRWAKEQ 529
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
179-521 |
2.83e-12 |
|
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: 68.62 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 179 QPEVLKEGGDQTVAILCSSGTTGLPKAVCISNSILIQDSMLItsQSVIYVGSClDWITGLWAFVFST---------VFGC 249
Cdd:cd17644 97 QISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGL--IKEYGITSS-DRVLQFASIAFDVaaeeiyvtlLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 250 TRII-SNKAF-TPEYFVGLVKKYKINYAVLPPRHLSALITcpDAKPDALAPITHLN---YGGGSISLATLQRSQE-LCKT 323
Cdd:cd17644 174 TLVLrPEEMRsSLEDFVQYIQQWQLTVLSLPPAYWHLLVL--ELLLSTIDLPSSLRlviVGGEAVQPELVRQWQKnVGNF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 324 AMFNSGYGMTEVgaiTINIGISNVSS----------AGRPVPGIKIRIVDEDGKSLGYNQVGEIYV-HTGQAwNGYYGNP 392
Cdd:cd17644 252 IQLINVYGPTEA---TIAATVCRLTQlternitsvpIGRPIANTQVYILDENLQPVPVGVPGELHIgGVGLA-RGYLNRP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 393 VETRR--------MQDFEGWFHTGDLG-YFDEQNFLYIvDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDER 463
Cdd:cd17644 328 ELTAEkfishpfnSSESERLYKTGDLArYLPDGNIEYL-GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQP 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24653035 464 EGDAAGALVVKSKGATISAKEIVEHVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd17644 407 GNKRLVAYIVPHYEESPSTVELRQFLKAKLP--DYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
329-458 |
2.33e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 66.20 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVGA---ITINIGISNVSSAGRPVPGIKIR---IVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQdFE 402
Cdd:PLN02614 417 GYGLTESCAgtfVSLPDELDMLGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVL-ID 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24653035 403 GWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTE-IETVIAELSQVQDVCVVG 458
Cdd:PLN02614 496 GWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVEnIENIYGEVQAVDSVWVYG 552
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
345-495 |
2.73e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.73 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 345 SNVSSAGRPVPGIKIRIVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRM---QDFEGWFHTGDLGYFDEQNfLY 420
Cdd:PRK05691 367 SVLMSCGRSQPGHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLGFLRDGE-LF 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653035 421 IVDRKKEILKYNGLHYWPTEIETVIAElsqvqDVCVVgiydeREGDAAGALVVK--SKGATISAkEIVEHVAKRLPA 495
Cdd:PRK05691 446 VTGRLKDMLIVRGHNLYPQDIEKTVER-----EVEVV-----RKGRVAAFAVNHqgEEGIGIAA-EISRSVQKILPP 511
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
193-521 |
3.18e-11 |
|
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: 65.43 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCSSGTTGLPKAVCISNSILIQdsmLITS-QSVIYVGSCLDwiTGLWA-FVF---------STVFGCTRIISNKA--FT 259
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGVVN---LVEWaNKVIYQGEHLR--VALFAsISFdasvteifaSLLSGNTLYIVRKEtvLD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 260 PEYFVGLVKKYKINYAVLPPRHLSALitcPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTA--MFNSgYGMTE--V 335
Cdd:cd17655 217 GQALTQYIRQNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNptITNA-YGPTEttV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 336 GAITINIGISNVSSA----GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNP------------VETRRMq 399
Cdd:cd17655 293 DASIYQYEPETDQQVsvpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPeltaekfvddpfVPGERM- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 400 dfegwFHTGDLG-YFDEQNFLYIvDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGA 478
Cdd:cd17655 372 -----YRTGDLArWLPDGNIEFL-GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKEL 445
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24653035 479 TISakEIVEHVAKRL-----PATQKQLragvqftDKLPANVNGKTMRK 521
Cdd:cd17655 446 PVA--QLREFLARELpdymiPSYFIKL-------DEIPLTPNGKVDRK 484
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
189-494 |
4.23e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 65.35 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 189 QTVAILCSSGTTGLPKAV----------CISNsILIQDsMlitSQSVIYV---------GSCLDWITGLWAFVfsTVfgC 249
Cdd:PRK08162 183 DAIALNYTSGTTGNPKGVvyhhrgaylnALSN-ILAWG-M---PKHPVYLwtlpmfhcnGWCFPWTVAARAGT--NV--C 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 250 TRiisnkAFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQrsqelcktAMFNSG 329
Cdd:PRK08162 254 LR-----KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIA--------KMEEIG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 330 ------YGMTEV-GAITINI--------------------GISNVSSAG---------RPVPgikirivdEDGKSLGynq 373
Cdd:PRK08162 321 fdlthvYGLTETyGPATVCAwqpewdalplderaqlkarqGVRYPLQEGvtvldpdtmQPVP--------ADGETIG--- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 374 vgEIYVHTGQAWNGYYGNPVETRRMqdFE-GWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQ 452
Cdd:PRK08162 390 --EIMFRGNIVMKGYLKNPKATEEA--FAgGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVL 465
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24653035 453 DVCVVGIYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLP 494
Cdd:PRK08162 466 VAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLA 507
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-521 |
5.62e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTF-EQGLTW------SIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFS 124
Cdd:PRK12316 4566 DAVAVVFdEEKLTYaelnrrANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMME 4645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 125 ITKPTLIFcdgqeydkvhkaTVGWHPEILTLTDhvegvqGIETL-LDPTTTEKIY---QPEVlKEGGDQTVAILCSSGTT 200
Cdd:PRK12316 4646 DSGAALLL------------TQSHLLQRLPIPD------GLASLaLDRDEDWEGFpahDPAV-RLHPDNLAYVIYTSGST 4706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 201 GLPKAVCISNSILI--------------QDSMLITSqSVIYVGSCLDWITGLwafvfsTVFGCTRIISNKAFTPEYFVGL 266
Cdd:PRK12316 4707 GRPKGVAVSHGSLVnhlhatgeryeltpDDRVLQFM-SFSFDGSHEGLYHPL------INGASVVIRDDSLWDPERLYAE 4779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 267 VKKYKINYAVLPPRHLSALITCPDAKPDaLAPITHLNYGGGSISLATLQRS-QELCKTAMFNsGYGMTEVgAITI----- 340
Cdd:PRK12316 4780 IHEHRVTVLVFPPVYLQQLAEHAERDGE-PPSLRVYCFGGEAVAQASYDLAwRALKPVYLFN-GYGPTET-TVTVllwka 4856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 341 ---NIGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET--RRMQDFEG-----WFHTGDL 410
Cdd:PRK12316 4857 rdgDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTaeRFVPDPFGapggrLYRTGDL 4936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 411 GYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGiydeREGDAAGALV---VKSKGATISAKE--- 484
Cdd:PRK12316 4937 ARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA----QEGAVGKQLVgyvVPQDPALADADEaqa 5012
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24653035 485 -----IVEHVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:PRK12316 5013 elrdeLKAALRERLP--EYMVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
193-530 |
6.77e-11 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 64.49 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 193 ILCS-----------SGTTGLPKAVCISNSILiqdsmlitSQSVIYVGSCLDwITG----LW----AF------VFSTVF 247
Cdd:cd05918 100 VLTSspsdaayviftSGSTGKPKGVVIEHRAL--------STSALAHGRALG-LTSesrvLQfasyTFdvsileIFTTLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 248 --GCTRIISNKAfTPEYFVGLVKKYKINYAVLPPRhLSALItcpdaKPDALAPITHLNYGGGSISLATLQRSQElcKTAM 325
Cdd:cd05918 171 agGCLCIPSEED-RLNDLAGFINRLRVTWAFLTPS-VARLL-----DPEDVPSLRTLVLGGEALTQSDVDTWAD--RVRL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 326 FNsGYGMTE--VGAIT-INIGISNVSSAGRPVPGIkIRIVDEDGkslgYNQ------VGEIYVHTGQAWNGYYGNPVET- 395
Cdd:cd05918 242 IN-AYGPAEctIAATVsPVVPSTDPRNIGRPLGAT-CWVVDPDN----HDRlvpigaVGELLIEGPILARGYLNDPEKTa 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 396 ------------------RRMqdfegwFHTGDLGYFDEQNFLYIVDRKKEILKYNG----LHywptEIETVIAELSQVQD 453
Cdd:cd05918 316 aafiedpawlkqegsgrgRRL------YRTGDLVRYNPDGSLEYVGRKDTQVKIRGqrveLG----EIEHHLRQSLPGAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 454 VCVVGIYDEREGDAAGALVV-----KSKGATISAKEIVEHVAKRLPATQKQLRAGVQ-------------FTDKLPANVN 515
Cdd:cd05918 386 EVVVEVVKPKDGSSSPQLVAfvvldGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRqrlpsymvpsvflPLSHLPLTAS 465
|
410
....*....|....*
gi 24653035 516 GKTMRKTARDVFVAL 530
Cdd:cd05918 466 GKIDRRALRELAESL 480
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
349-524 |
7.59e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 64.76 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 349 SAGRPVPGIKIRIVDED-GKSLGYNQVGEIYVHTGQAWNGYYGNPVETR-----RMQ-------------DFEGWFHTGD 409
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETErtfgaKLQsrlaegshadgaaDDGTWLRTGD 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 410 LG-YFDEQnfLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATIS---AKEI 485
Cdd:PRK12476 483 LGvYLDGE--LYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSradPAPA 560
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24653035 486 VE----HVAKR---LPATQKQLRAGVqftdkLPANVNGKTMRKTAR 524
Cdd:PRK12476 561 IDairaAVSRRhglAVADVRLVPAGA-----IPRTTSGKLARRACR 601
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
328-493 |
1.30e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 63.35 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 SGYGMTEVgAITI----NIGISNVssaGRPVPGIKIRIVDED----GKSL--GYNQVGEIYVHTGQawngyygnpvetrr 397
Cdd:PRK09029 269 CGYGLTEM-ASTVcakrADGLAGV---GSPLPGREVKLVDGEiwlrGASLalGYWRQGQLVPLVND-------------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 398 mqdfEGWFHTGDLGYFDeQNFLYIVDRKKeilkyN-------GLHywPTEIETVIAELSQVQDVCVVGIYDEREGDAAGA 470
Cdd:PRK09029 331 ----EGWFATRDRGEWQ-NGELTILGRLD-----NlffsggeGIQ--PEEIERVINQHPLVQQVFVVPVADAEFGQRPVA 398
|
170 180
....*....|....*....|...
gi 24653035 471 LVVKSKGATISAkeIVEHVAKRL 493
Cdd:PRK09029 399 VVESDSEAAVVN--LAEWLQDKL 419
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
305-430 |
1.78e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 63.60 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 305 GGGSISLATlQRSQELCKTAMFNSGYGMTEV--GAITINIGISNVSSAGRPVPGIKIRIVD-EDGkslGYNQV------G 375
Cdd:PLN02387 428 GGAPLSGDT-QRFINICLGAPIGQGYGLTETcaGATFSEWDDTSVGRVGPPLPCCYVKLVSwEEG---GYLISdkpmprG 503
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24653035 376 EIYVHTGQAWNGYYGNPVETRRMQ--DFEG--WFHTGDLGYFDEQNFLYIVDRKKEILK 430
Cdd:PLN02387 504 EIVIGGPSVTLGYFKNQEKTDEVYkvDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVK 562
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
359-449 |
1.84e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 63.42 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 359 IRIVDED-GKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMqdFEG-------------WFHTGDLGYFDEQNfLYIVDR 424
Cdd:PRK05850 381 VRIVDPDtCIECPAGTVGEIWVHGDNVAAGYWQKPEETERT--FGAtlvdpspgtpegpWLRTGDLGFISEGE-LFIVGR 457
|
90 100
....*....|....*....|....*
gi 24653035 425 KKEILKYNGLHYWPTEIETVIAELS 449
Cdd:PRK05850 458 IKDLLIVDGRNHYPDDIEATIQEIT 482
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
329-458 |
8.38e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 61.40 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEV--GAITINIGI-SNVSSAGRPVPGIKIRIvdEDGKSLGYNQV-----GEIYVHTGQAWNGYYGNPVETRRMQd 400
Cdd:PLN02861 414 GYGLTEScgGCFTSIANVfSMVGTVGVPMTTIEARL--ESVPEMGYDALsdvprGEICLRGNTLFSGYHKRQDLTEEVL- 490
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24653035 401 FEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTE-IETVIAELSQVQDVCVVG 458
Cdd:PLN02861 491 IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVEnLENTYSRCPLIASIWVYG 549
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
182-464 |
9.95e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.99 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 182 VLKEGGDQTVAILCSSGTTGLPKAVCISNSILIQDSMlitsqsviyvgSCLDW---------ITGLWAF---------VF 243
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQR-----------ACLKFfspkeddvmMSFLPPFhaygfnsctLF 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 244 STVFGCTRIISNKAFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKT 323
Cdd:PRK06334 246 PLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 324 AMFNSGYGMTEVG-AITINIGIS--NVSSAGRPVPGIKIRIVDEDGK-SLGYNQVGEIYVHTGQAWNGYYGN-PVETRRM 398
Cdd:PRK06334 326 IQLRQGYGTTECSpVITINTVNSpkHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEdFGQGFVE 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653035 399 QDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAE---LSQVQD---VCVVGIYDERE 464
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHagpLVVCGLPGEKV 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
188-521 |
2.72e-09 |
|
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: 59.40 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 188 DQTVAILCSSGTTGLPKAVcisnsiliqdsmLITSQSVIYVGSCLDWITGLWAF-------------VF------STVFG 248
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGV------------MVEHRNVAHAAHAWRREYELDSFpvrllqmasfsfdVFagdfarSLLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 249 CTRII--SNKAFTPEYFVGLVKKYKINYAVLPP---RHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRsQELCKT 323
Cdd:cd17650 161 GTLVIcpDEVKLDPAALYDLILKSRITLMESTPaliRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAA-RFGQGM 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 324 AMFNSgYGMTEV--------GAITINIGISNVSsAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET 395
Cdd:cd17650 240 RIINS-YGVTEAtidstyyeEGRDPLGDSANVP-IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 396 R------RMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAG 469
Cdd:cd17650 318 AerfvenPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLC 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24653035 470 ALVVKSkgATISAKEIVEHVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd17650 398 AYVVAA--ATLNTAELRAFLAKELP--SYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
266-473 |
5.70e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 58.46 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 266 LVKKYKINYAVLPPRHLS---ALITCPDAKpDALAPITHLNYGGGSISLATLQR-SQEL-CKtamFNSGYGMTEvgaiti 340
Cdd:PRK10946 267 LIEKHQVNVTALVPPAVSlwlQAIAEGGSR-AQLASLKLLQVGGARLSETLARRiPAELgCQ---LQQVFGMAE------ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 341 niGISN-----------VSSAGRPV-PGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRMQDFEGWFHTG 408
Cdd:PRK10946 337 --GLVNytrlddsderiFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSG 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653035 409 DLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVV 473
Cdd:PRK10946 415 DLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLV 479
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-521 |
8.32e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNPVLDDATLTHVFSITKPTLI 131
Cdd:PRK05691 1153 DGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELL 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 132 FCDGQEYDKVHKAtvgwhpeiltltdhvEGVQGI--ETL-LD--PTttekiyQPEVLKEGGDQTVAILCSSGTTGLPKAV 206
Cdd:PRK05691 1233 LTQSHLLERLPQA---------------EGVSAIalDSLhLDswPS------QAPGLHLHGDNLAYVIYTSGSTGQPKGV 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 207 CISNSIL------IQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTRIIS--NKAFTPEYFVGLVKKYKINYAVLP 278
Cdd:PRK05691 1292 GNTHAALaerlqwMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAgpGEHRDPQRIAELVQQYGVTTLHFV 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 279 PRHLSALITCPDAKpdALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTEVgAITI-----NIGISNVSSAGRP 353
Cdd:PRK05691 1372 PPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET-AINVthwqcQAEDGERSPIGRP 1448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 354 VPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRM-------QDFEGWFHTGDLGYFDEQNFLYIVDRKK 426
Cdd:PRK05691 1449 LGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERfvpdplgEDGARLYRTGDRARWNADGALEYLGRLD 1528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 427 EILKYNGLHYWPTEIETVIAELSQVQDVCVVgiydEREGdAAGALVV----KSKGATISAKEIVEHVAKRLPA--TQKQL 500
Cdd:PRK05691 1529 QQVKLRGFRVEPEEIQARLLAQPGVAQAAVL----VREG-AAGAQLVgyytGEAGQEAEAERLKAALAAELPEymVPAQL 1603
|
490 500
....*....|....*....|.
gi 24653035 501 RAgvqfTDKLPANVNGKTMRK 521
Cdd:PRK05691 1604 IR----LDQMPLGPSGKLDRR 1620
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
178-521 |
9.70e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 58.13 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 178 YQPEVLKEGGDqTVAILCSSGTTGLPKAV-----CISNSIL-IQDSMLITSQSVIYVGSCLDWITGLWAFVFSTVFGCTR 251
Cdd:PRK10252 589 AAPLQLSQPHH-TAYIIFTSGSTGRPKGVmvgqtAIVNRLLwMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKL 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 252 IISNKAF--TPEYFVGLVKKYKINYAVLPPRHLSALITCPDAK--PDALAPITHLNYGGGSISLATLQRSQELCKTAMFN 327
Cdd:PRK10252 668 VMAEPEAhrDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFCSGEALPADLCREWQQLTGAPLHN 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 SgYGMTEvGAITINI------GISNVSSA----GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVET-- 395
Cdd:PRK10252 748 L-YGPTE-AAVDVSWypafgeELAAVRGSsvpiGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTas 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 396 RRMQD-F---EGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDV----CVVGIYDEREGDA 467
Cdd:PRK10252 826 RFIADpFapgERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthaCVINQAAATGGDA 905
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653035 468 AG--ALVVKSKGATISAKEIVEHVAKRLPA-----TQKQLragvqftDKLPANVNGKTMRK 521
Cdd:PRK10252 906 RQlvGYLVSQSGLPLDTSALQAQLRERLPPhmvpvVLLQL-------DQLPLSANGKLDRK 959
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
329-529 |
1.10e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.05 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVG-AITINIGISN-VSSAGRPVPGIKIRIVDEDGKSLGynqvGEIYVHTGQAWNGYY--GNP--VETRRmqdfE 402
Cdd:PRK06814 938 GYGVTETApVIALNTPMHNkAGTVGRLLPGIEYRLEPVPGIDEG----GRLFVRGPNVMLGYLraENPgvLEPPA----D 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 403 GWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDaagALVVKSKGATISA 482
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE---RIILLTTASDATR 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24653035 483 KEIVEHvAKRLPATQKQLRAGVQFTDKLPANVNGKT----MRKTARDVFVA 529
Cdd:PRK06814 1087 AAFLAH-AKAAGASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAK 1136
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
52-521 |
1.29e-08 |
|
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: 57.48 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 52 DGVTVTFE-QGLTW------SIRIAQYLKKRGLNHKDVIGIAAKNSTYVMPLGVACLMNGTPFHSVNP---------VLD 115
Cdd:cd17656 3 DAVAVVFEnQKLTYrelnerSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPeypeerriyIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 116 DATLTHVFSITKPTLIFcdGQEYDKVHkatvgwhpeiltltdhvegvqgietLLDPTTTEKIYQPEVLKEGGDQTVAILC 195
Cdd:cd17656 83 DSGVRVVLTQRHLKSKL--SFNKSTIL-------------------------LEDPSISQEDTSNIDYINNSDDLLYIIY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 196 SSGTTGLPKAVCISNSILIQ------DSMLI-TSQSVIYVGSCldwitglwAF------VFSTVF--GCTRIISNKA-FT 259
Cdd:cd17656 136 TSGTTGKPKGVQLEHKNMVNllhferEKTNInFSDKVLQFATC--------SFdvcyqeIFSTLLsgGTLYIIREETkRD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 260 PEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPITHLNYGGGSISLATLQRSQELCKTAMFNSGYGMTE---VG 336
Cdd:cd17656 208 VEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSEthvVT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 337 AITIN--IGISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR------MQDFEGWFHTG 408
Cdd:cd17656 288 TYTINpeAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEkffpdpFDPNERMYRTG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 409 DLG-YFDEQNFLYIvDRKKEILKYNGLHYWPTEIETVIAELSQVQDVcVVGIYDEREGDA-AGALVVKSKGATISakEIV 486
Cdd:cd17656 368 DLArYLPDGNIEFL-GRADHQVKIRGYRIELGEIEAQLLNHPGVSEA-VVLDKADDKGEKyLCAYFVMEQELNIS--QLR 443
|
490 500 510
....*....|....*....|....*....|....*
gi 24653035 487 EHVAKRLPatQKQLRAGVQFTDKLPANVNGKTMRK 521
Cdd:cd17656 444 EYLAKQLP--EYMIPSFFVPLDQLPLTPNGKVDRK 476
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
330-522 |
2.09e-08 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 56.88 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 330 YGMTEVG--AITINIGI----SNVSSAGRPVPGIKIRIVDE-DGKSLGYNQVGeIYVHTGQAWNGY----YGNpvETRRM 398
Cdd:PRK10524 387 YWQTETGwpILAIARGVedrpTRLGSPGVPMYGYNVKLLNEvTGEPCGPNEKG-VLVIEGPLPPGCmqtvWGD--DDRFV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 399 QDFegWFH-------TGDLGYFDEQNFLYIVDRKKEILKYNGlHYWPT-EIETVIAELSQVQDVCVVGIYDEREGDAAGA 470
Cdd:PRK10524 464 KTY--WSLfgrqvysTFDWGIRDADGYYFILGRTDDVINVAG-HRLGTrEIEESISSHPAVAEVAVVGVKDALKGQVAVA 540
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 471 LVVKSKGATIS--------AKEIVEHVAKRLPATQKQLRagVQFTDKLPANVNGKTMRKT 522
Cdd:PRK10524 541 FVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPAR--VWFVSALPKTRSGKLLRRA 598
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
352-525 |
8.11e-08 |
|
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: 54.75 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 352 RPVPGIKIRI-VDEDGKSLGynqvgEIYVHTGQAWNGYYGNPVET--RRMQD-FEG---WFHTGDLGYFDEQNFLYIVDR 424
Cdd:cd05937 285 DPKTGFCVRApVGEPGEMLG-----RVPFKNREAFQGYLHNEDATesKLVRDvFRKgdiYFRTGDLLRQDADGRWYFLDR 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 425 KKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGI----YDEREGDAAGALVVKSKG-ATISAKEIVEHVAKRLPATQKQ 499
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpgHDGRAGCAAITLEESSAVpTEFTKSLLASLARKNLPSYAVP 439
|
170 180
....*....|....*....|....*.
gi 24653035 500 LRagVQFTDKLPANVNGKTMRKTARD 525
Cdd:cd05937 440 LF--LRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
361-449 |
1.69e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 361 IVD-EDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRrmQDF-------------EG------WFHTGDLG-YFDEQnfL 419
Cdd:PRK07769 404 IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETA--ATFqnilksrlseshaEGapddalWVRTGDYGvYFDGE--L 479
|
90 100 110
....*....|....*....|....*....|
gi 24653035 420 YIVDRKKEILKYNGLHYWPTEIETVIAELS 449
Cdd:PRK07769 480 YITGRVKDLVIIDGRNHYPQDLEYTAQEAT 509
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
53-495 |
1.95e-07 |
|
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: 53.58 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 53 GVTVTFEQGLTWSIRIAQYLKKRGLNHKDVIGIAAKNST-YV-MPLGVACLMNGTPFhsVNPVLDDATLTHVFSITKPtl 130
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLeFVaLWLGLAKIGVETAL--INSNLRLESLLHCITVSKA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 131 ifcdgqeydkvhKATVgwhpeiltlTDHVegvqgieTLLDPTTTEKiyQPEVLKEGGDQTVAILCSSGTTGLPKAVCISN 210
Cdd:cd05939 77 ------------KALI---------FNLL-------DPLLTQSSTE--PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 211 S------ILIQDSMLITSQSVIY--------------VGSCLdwitglwafvfstVFGCTRIISNKaFTPEYFVGLVKKY 270
Cdd:cd05939 127 SryyriaAGAYYAFGMRPEDVVYdclplyhsaggimgVGQAL-------------LHGSTVVIRKK-FSASNFWDDCVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 271 K---INYAVLPPRHLSALITCPDAKPDALapitHLNYGGG---SISLATLQRSQeLCKTAMFnsgYGMTEVGAITINI-- 342
Cdd:cd05939 193 NctiVQYIGEICRYLLAQPPSEEEQKHNV----RLAVGNGlrpQIWEQFVRRFG-IPQIGEF---YGATEGNSSLVNIdn 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 343 ---GISNVSSAGRPVPGIKIRIVDEDGKSLGYNQVGE-IYVHTGQAwNGYYGNPVETRRMQDFEGW-------------- 404
Cdd:cd05939 265 hvgACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLcIPCQPGEP-GLLVGKIIQNDPLRRFDGYvnegatnkkiardv 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 405 -------FHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGI-YDEREGDAAGALVVKSK 476
Cdd:cd05939 344 fkkgdsaFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVeVPGVEGRAGMAAIVDPE 423
|
490
....*....|....*....
gi 24653035 477 GATISAKEIVEhVAKRLPA 495
Cdd:cd05939 424 RKVDLDRFSAV-LAKSLPP 441
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
307-430 |
3.38e-07 |
|
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: 52.84 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 307 GSISLAT-LQRSQELCKTAMFNSGYGMTEVGAITINIGISnvssagRPvPGIKIRIVDEdgKSLGYNQV------GEIYV 379
Cdd:cd17632 370 GSAPLSAeMKAFMESLLDLDLHDGYGSTEAGAVILDGVIV------RP-PVLDYKLVDV--PELGYFRTdrphprGELLV 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24653035 380 HTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILK 430
Cdd:cd17632 441 KTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLK 491
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
354-456 |
4.26e-07 |
|
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: 52.74 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 354 VPGIKIRIVDEDGKSL-GYNQVGEIYVHTGQAWNGYYGNPVET---------RRMQDFEG---WFHTGDLGYF------- 413
Cdd:cd05905 367 LPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFLLDGETndtfkvfpsTRLSTGITnnsYARTGLLGFLrptkctd 446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 24653035 414 ---DEQNFLYIVDRKKEILKYNGLHYWPTEIE-TVIAELSQVQDVCV 456
Cdd:cd05905 447 lnvEEHDLLFVVGSIDETLEVRGLRHHPSDIEaTVMRVHPYRGRCAV 493
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
328-522 |
9.67e-07 |
|
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: 51.40 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 328 SGYGMTE--VGAITINIGISNVS-SAGRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRR------M 398
Cdd:cd17645 239 NNYGPTEntVVATSFEIDKPYANiPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEkfivhpF 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 399 QDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDereGDAAGALVvkskgA 478
Cdd:cd17645 319 VPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED---ADGRKYLV-----A 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24653035 479 TISAKEIVEHVAKR-----------LPATQKQLragvqftDKLPANVNGKTMRKT 522
Cdd:cd17645 391 YVTAPEEIPHEELRewlkndlpdymIPTYFVHL-------KALPLTANGKVDRKA 438
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
349-526 |
6.48e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 49.13 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 349 SAGRPVPGIKIRIVDEDGKSLGYNQVGeiYVHTGQAWNG----YYGNP--VETRRMQDFEGWFHTGDLGYFDEQNFLYIV 422
Cdd:PLN02654 455 SATFPFFGVQPVIVDEKGKEIEGECSG--YLCVKKSWPGafrtLYGDHerYETTYFKPFAGYYFSGDGCSRDKDGYYWLT 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 423 DRKKEILKYNGLHYWPTEIETVIAELSQVQDVCVVGIYDEREGDAAGALVVKSKGATISA---KEIVEHVAKRLPATQKQ 499
Cdd:PLN02654 533 GRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEelrKSLILTVRNQIGAFAAP 612
|
170 180
....*....|....*....|....*..
gi 24653035 500 LRagVQFTDKLPANVNGKTMRKTARDV 526
Cdd:PLN02654 613 DK--IHWAPGLPKTRSGKIMRRILRKI 637
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
351-521 |
1.17e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 351 GRPVPGIKIRIVDEDGKSLGYNQVGEIYVHTGQAWNGYYGNPVETRRM---QDF----EGWFHTGDLGYFDEQNFLYIVD 423
Cdd:PRK05691 4043 GSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAfvpHPFgapgERLYRTGDLARRRSDGVLEYVG 4122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 424 RKKEILKYNGLHYWPTEIETVIAELSQVQDVcVVGIYDEREGDAAGALVVKSKGATiSAKEIVEHVAKRLPAT--QKQLR 501
Cdd:PRK05691 4123 RIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVPHQTVL-AQGALLERIKQRLRAElpDYMVP 4200
|
170 180
....*....|....*....|
gi 24653035 502 AGVQFTDKLPANVNGKTMRK 521
Cdd:PRK05691 4201 LHWLWLDRLPLNANGKLDRK 4220
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
329-433 |
2.14e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 43.93 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 329 GYGMTEVG-AITINIGIS-NVSSAGRPVPGIKIRIVD----EDGKSL---------GYNQVGEIYV-HTGQAWNGyygnp 392
Cdd:PRK08043 510 GYGVTECApVVSINVPMAaKPGTVGRILPGMDARLLSvpgiEQGGRLqlkgpnimnGYLRVEKPGVlEVPTAENA----- 584
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24653035 393 vetrRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNG 433
Cdd:PRK08043 585 ----RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
236-511 |
8.40e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 42.40 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 236 TGLWAFVFSTVFGCTRIISNKAFTPEYFVGLVKKYKINYAVLPPRHLSALITCPDAKPDALAPItHLNYGGGsISLATLQ 315
Cdd:PRK07868 659 SGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPV-RLFIGSG-MPTGLWE 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 316 RSQELCKTAMFNSGYGMTEVGAITINIGISNVSSAGRPVPGI-KIRIVD---EDGKSL----GYNQ---VGEIYVHTGQA 384
Cdd:PRK07868 737 RVVEAFAPAHVVEFFATTDGQAVLANVSGAKIGSKGRPLPGAgRVELAAydpEHDLILeddrGFVRraeVNEVGVLLARA 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 385 wngyyGNPVETRR------MQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYWPTEIETVIAELSQVqDVCVVG 458
Cdd:PRK07868 817 -----RGPIDPTAsvkrgvFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGV-DLAVTY 890
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24653035 459 IYDEREGDAAGALVVKSKGATISAKEIVEHVAKRLPATQKQLragVQFTDKLP 511
Cdd:PRK07868 891 GVEVGGRQLAVAAVTLRPGAAITAADLTEALASLPVGLGPDI---VHVVPEIP 940
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
305-443 |
5.89e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 39.32 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653035 305 GGGSISLatlQRSQELCK--TAMFNSGYGMTEV-GAITINIGIS-NVSSAGRPV-PGIKIRIVD-EDGKSLGYNQVGEIY 378
Cdd:PTZ00342 469 GGGKLSP---KIAEELSVllNVNYYQGYGLTETtGPIFVQHADDnNTESIGGPIsPNTKYKVRTwETYKATDTLPKGELL 545
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653035 379 VHTGQAWNGYYGNPVETRRMQDFEGWFHTGDLGYFDEQNFLYIVDRKKEILKYNGLHYwpteIET 443
Cdd:PTZ00342 546 IKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEY----IET 606
|
|
| |
