|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
5-630 |
0e+00 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 1031.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 5 PSIAGLSDIEALERVPLEQRDLPSSTYELLQRSARRHGQRIALSCLLHGSAAEEPLRISYAELFARVTQTANALHRLGLE 84
Cdd:PRK07529 2 PAFATLADIEAIEAVPLAARDLPASTYELLSRAAARHPDAPALSFLLDADPLDRPETWTYAELLADVTRTANLLHSLGVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 85 SHQAVSFLLPNLPQTHYVIWGGEAAGIVNAINPLLEPEHIAELIRASNTRVLVTLAPFPGTDLWQKVAGLRAQLPELYAI 164
Cdd:PRK07529 82 PGDVVAFLLPNLPETHFALWGGEAAGIANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEVLAALPELRTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 165 VVVDPANLLPAPQREALKAQRGPLPEGVLDFDTLIADCPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAM 244
Cdd:PRK07529 162 VEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 245 AEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGYRNPTLIQDFWKLVERYRVTSFSGVPTIYAA 324
Cdd:PRK07529 242 AWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGVIANFWKIVERYRINFLSGVPTVYAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 325 LLQVPSDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPYCQVKVAV 404
Cdd:PRK07529 322 LLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 405 LDGEGNYLRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQ 484
Cdd:PRK07529 402 LDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 485 MIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPERAAVPKDIWLIESMPVTAVGKTFK 564
Cdd:PRK07529 482 AIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKIFK 561
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 565 PALRLDAIRRVLEEESRRIAEDIR-VEVVADERHGQLAHLHVPalDERRQAALEELLGGYALNYRLH 630
Cdd:PRK07529 562 PALRRDAIRRVLRAALRDAGVEAEvVDVVEDGRRGLVAQVALR--GAEDREAVAAVLGRYAFPWEIS 626
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-574 |
0e+00 |
|
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: 642.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGY 294
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPsDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGT 374
Cdd:cd05944 81 RNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVP-VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 375 CGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGEGNYLRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGD 454
Cdd:cd05944 160 CLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 455 LGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHA 534
Cdd:cd05944 240 LGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15599055 535 SRHVPERAAVPKDIWLIESMPVTAVGKTFKPALRLDAIRR 574
Cdd:cd05944 320 RDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
31-578 |
1.46e-146 |
|
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: 432.31 E-value: 1.46e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG 110
Cdd:COG0318 2 ADLLRRAAARHPDRPALVF--------GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 -IVNAINPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkvaglraqlpelyaivvvdpanllpapqrealkaqrgplp 189
Cdd:COG0318 74 aVVVPLNPRLTAEELAYILEDSGARALVT--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 190 egvldfdtliadcpadrlesgraihpddvASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHV 269
Cdd:COG0318 103 -----------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 270 NGVMVTGLAPFHRGAQVLLagpQGYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPM 348
Cdd:COG0318 154 FGLTVGLLAPLLAGATLVL---LPRFDP---ERVLELIERERVTVLFGVPTMLARLLRHPEfARYDLSSLRLVVSGGAPL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 349 PVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPR-GGERRPGSIGLRLPYCQVKVavLDGEGnylRDAAPNEVGNLCLKG 427
Cdd:COG0318 228 PPELLERFEERFGVRIVEGYGLTETSPVVTVNPEdPGERRPGSVGRPLPGVEVRI--VDEDG---RELPPGEVGEIVVRG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 428 PTVFKGYLQQ-DRNRDIWIgDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPD 506
Cdd:COG0318 303 PNVMKGYWNDpEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPD 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599055 507 AKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALRLDAIRRVLEE 578
Cdd:COG0318 382 EKWGERVVAFVVLRPGAELDAEELRAFLRERLA-RYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
31-568 |
2.33e-138 |
|
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: 411.96 E-value: 2.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALSCLlhgsaaEEPLriSYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG 110
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFM------GRKL--TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 -IVNAINPLLEPEHIAELIRASNTRVLVTLAPFpgtdlwqkvaglraqlpelyaivvvdpanllpapqREALKAQRGPLP 189
Cdd:cd05936 74 aVVVPLNPLYTPRELEHILNDSGAKALIVAVSF-----------------------------------TDLLAAGAPLGE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 190 EgvldfdtliadcpadrlesgRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMG--LNADYGVDDVLLCGLPLF 267
Cdd:cd05936 119 R--------------------VALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKawLEDLLEGDDVVLAALPLF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 268 HVNGVMVTGLAPFHRGAQVLLAgpQGYRNPTLIqdfwKLVERYRVTSFSGVPTIYAALLQVPSD-GRDLSSLRFALCGAA 346
Cdd:cd05936 179 HVFGLTVALLLPLALGATIVLI--PRFRPIGVL----KEIRKHRVTIFPGVPTMYIALLNAPEFkKRDFSSLRLCISGGA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 347 PMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGEGNylrDAAPNEVGNLCLK 426
Cdd:cd05936 253 PLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLP--GTEVKIVDDDGE---ELPPGEVGELWVR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 427 GPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPD 506
Cdd:cd05936 328 GPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPD 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599055 507 AKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05936 408 PYSGEAVKAFVVLKEGASLTEEEIIAFCREQLA-GYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
217-561 |
3.78e-123 |
|
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: 367.77 E-value: 3.78e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 217 DVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQgyrn 296
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 297 ptlIQDFWKLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTE-GT 374
Cdd:cd04433 77 ---PEAALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTEtGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 375 CGTSCNPRGGERRPGSIGLRLPYCQVKVavLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGD 454
Cdd:cd04433 154 TVATGPPDDDARKPGSVGRPVPGVEVRI--VDPDGGEL---PPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 455 LGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHA 534
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHV 308
|
330 340
....*....|....*....|....*..
gi 15599055 535 SRHVPeRAAVPKDIWLIESMPVTAVGK 561
Cdd:cd04433 309 RERLA-PYKVPRRVVFVDALPRTASGK 334
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
32-568 |
1.10e-119 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 365.38 E-value: 1.10e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPqtHYVI--WGGEAA 109
Cdd:PRK07656 9 ELLARAARRFGDKEAY--------VFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSP--HWVIaaLGALKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 110 G-IVNAINPLLEPEHIAELIRASNTRVLVTLAPFPGTDlwqKVAGLRaqLPELYAIVVVDPAnllpapqrealkaQRGPL 188
Cdd:PRK07656 79 GaVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVD---YSATTR--LPALEHVVICETE-------------EDDPH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 189 PEGVLDFDTLIAdcPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFH 268
Cdd:PRK07656 141 TEKMKTFTDFLA--AGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 269 VNGVMVTGLAPFHRGAQVLlagPQGYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAP 347
Cdd:PRK07656 219 VFGYKAGVNAPLMRGATIL---PLPVFDP---DEVFRLIETERITVLPGPPTMYNSLLQHPDrSAEDLSSLRLAVTGAAS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 348 MPVELIRQFEARTGLK-VIEGYGLTEgTCGTSC-NPRGGERR--PGSIGLRLPYCQVKVAVLDGEgnylrDAAPNEVGNL 423
Cdd:PRK07656 293 MPVALLERFESELGVDiVLTGYGLSE-ASGVTTfNRLDDDRKtvAGTIGTAIAGVENKIVNELGE-----EVPVGEVGEL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 424 CLKGPTVFKGYLQQDRNRDIWI-GDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAV 502
Cdd:PRK07656 367 LVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599055 503 GKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVperaA---VPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK07656 447 GVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHL----AkykVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
25-568 |
2.06e-117 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 359.89 E-value: 2.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTYELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNlpQTHYVI- 103
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYF--------DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWN--SHEYLEa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 104 -WGGEAAGIV-NAINPLLEPEHIAELIRASNTRVLVTlapfpGTDLWQKVAGLRAQLPELYAIVVVDPAnllpapqreal 181
Cdd:PRK06187 73 yFAVPKIGAVlHPINIRLKPEEIAYILNDAEDRVVLV-----DSEFVPLLAAILPQLPTVRTVIVEGDG----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 182 kaQRGPLPEGVLDFDTLIADCPADRLEsgRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLL 261
Cdd:PRK06187 137 --PAAPLAPEVGEYEELLAAASDTFDF--PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 262 CGLPLFHVNGVMVtGLAPFHRGAQVLLAGpqgyR-NPTLIqdfWKLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLR 339
Cdd:PRK06187 213 VIVPMFHVHAWGL-PYLALMAGAKQVIPR----RfDPENL---LDLIETERVTFFFAVPTIWQMLLKAPrAYFVDFSSLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 340 FALCGAAPMPVELIRQFEARTGLKVIEGYGLTEgTCGT-SCNP-----RGGERRPGSIGLrlPYCQVKVAVLDGEGNYL- 412
Cdd:PRK06187 285 LVIYGGAALPPALLREFKEKFGIDLVQGYGMTE-TSPVvSVLPpedqlPGQWTKRRSAGR--PLPGVEARIVDDDGDELp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 413 RDaaPNEVGNLCLKGPTVFKGYL-QQDRNRDIWIGdGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALH 491
Cdd:PRK06187 362 PD--GGEVGEIIVRGPWLMQGYWnRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALY 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 492 RHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK06187 439 GHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLA-KFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
31-586 |
6.41e-109 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 339.40 E-value: 6.41e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALsclLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG 110
Cdd:COG0365 12 YNCLDRHAEGRGDKVAL---IWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 -IVNAINPLLEPEHIAELIRASNTRVLVT----LAPFPGTDLWQKVAGLRAQLPELYAIVVVDPANLLPAPqrealkaqr 185
Cdd:COG0365 89 aVHSPVFPGFGAEALADRIEDAEAKVLITadggLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPM--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 186 gplpEGVLDFDTLIA----DCPADRLESgraihpDDVASYFHTGGTTGTPKLAPHSH-----FNEVAMAEIMGLNADygv 256
Cdd:COG0365 160 ----EGDLDWDELLAaasaEFEPEPTDA------DDPLFILYTSGTTGKPKGVVHTHggylvHAATTAKYVLDLKPG--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 257 dDVLLCGLPLF----HVNGVmvtgLAPFHRGA-QVLLAGPQGYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQV--- 328
Cdd:COG0365 227 -DVFWCTADIGwatgHSYIV----YGPLLNGAtVVLYEGRPDFPDP---GRLWELIEKYGVTVFFTAPTAIRALMKAgde 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 329 PSDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGE 408
Cdd:COG0365 299 PLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVP--GYDVAVVDED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 409 GNylrDAAPNEVGNLCLKG--PTVFKGYLQQD-RNRDIWIG--DGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDP 483
Cdd:COG0365 377 GN---PVPPGEEGELVIKGpwPGMFRGYWNDPeRYRETYFGrfPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 484 QMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---ELLEHASRHVPERaAVPKDIWLIESMPVTAVG 560
Cdd:COG0365 454 AEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPY-AYPREIEFVDELPKTRSG 532
|
570 580
....*....|....*....|....*.
gi 15599055 561 KTfkpalrldaIRRVLeeesRRIAED 586
Cdd:COG0365 533 KI---------MRRLL----RKIAEG 545
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
34-564 |
1.29e-106 |
|
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: 328.80 E-value: 1.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 34 LQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVN 113
Cdd:cd17631 1 LRRRARRHPDRTALVF--------GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 114 A-INPLLEPEHIAELIRASNTRVLVtlapfpgtdlwqkvaglraqlpelyaivvvdpanllpapqrealkaqrgplpegv 192
Cdd:cd17631 73 VpLNFRLTPPEVAYILADSGAKVLF------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 193 ldfdtliadcpadrlesgraihpDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGV 272
Cdd:cd17631 98 -----------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 273 MVTGLAPFHRGA-QVLLAGPqgyrNPTLiqdFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPV 350
Cdd:cd17631 155 GVFTLPTLLRGGtVVILRKF----DPET---VLDLIERHRVTSFFLVPTMIQALLQHPRfATTDLSSLRAVIYGGAPMPE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 351 ELIRQFEARtGLKVIEGYGLTEGTCGTSCNPRGG-ERRPGSIGLRLPYCQVkvAVLDGEGnylRDAAPNEVGNLCLKGPT 429
Cdd:cd17631 228 RLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDhRRKLGSAGRPVFFVEV--RIVDPDG---REVPPGEVGEIVVRGPH 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 430 VFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKA 509
Cdd:cd17631 302 VMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKW 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 510 GELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFK 564
Cdd:cd17631 382 GEAVVAVVVPRPGAELDEDELIAHCRERLA-RYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
62-568 |
5.97e-101 |
|
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: 316.18 E-value: 5.97e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLA 140
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGaVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 PFPGTDLwqkvaglRAQLPELYAIV--VVDPANLLPAPQREALkaqrgplpeGVLDFDTLIAdcpadrlESGRAIHPDDV 218
Cdd:cd05926 95 GELGPAS-------RAASKLGLAILelALDVGVLIRAPSAESL---------SNLLADKKNA-------KSEGVPLPDDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 219 ASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLagPQGYRNPT 298
Cdd:cd05926 152 ALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL--PPRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 299 liqdFWKLVERYRVTSFSGVPTIYAALLQVP--SDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCG 376
Cdd:cd05926 230 ----FWPDVRDYNATWYTAVPTIHQILLNRPepNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 377 TSCNP-RGGERRPGSIGLrlPYcQVKVAVLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGD 454
Cdd:cd05926 306 MTSNPlPPGPRKPGSVGK--PV-GVEVRILDEDGEIL---PPGVVGEICLRGPNVTRGYLNNpEANAEAAFKDGWFRTGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 455 LGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHA 534
Cdd:cd05926 380 LGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFC 459
|
490 500 510
....*....|....*....|....*....|....*.
gi 15599055 535 SRHVperAA--VPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05926 460 RKHL---AAfkVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
34-477 |
9.01e-100 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 310.78 E-value: 9.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 34 LQRSARRHGQRIALSCllhgsaaEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQtHYVIWGG--EAAGI 111
Cdd:pfam00501 1 LERQAARTPDKTALEV-------GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPE-WVVAFLAclKAGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 112 VNAINPLLEPEHIAELIRASNTRVLVTLAPFpgtdLWQKVAGLRAQLPELYAIVVVDPAnllpapqrealkaqrGPLPEG 191
Cdd:pfam00501 73 YVPLNPRLPAEELAYILEDSGAKVLITDDAL----KLEELLEALGKLEVVKLVLVLDRD---------------PVLKEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 192 VLDFDtliADCPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADY----GVDDVLLCGLPLF 267
Cdd:pfam00501 134 PLPEE---AKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 268 HVNGVMVTGLAPFHRGAQVLLAGPqgyRNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGR-DLSSLRFALCGAA 346
Cdd:pfam00501 211 HDFGLSLGLLGPLLAGATVVLPPG---FPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRaLLSSLRLVLSGGA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 347 PMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGER--RPGSIGLRLPYCQVKVaVLDGEGNYLrdaAPNEVGNLC 424
Cdd:pfam00501 288 PLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrSLGSVGRPLPGTEVKI-VDDETGEPV---PPGEPGELC 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15599055 425 LKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRG 477
Cdd:pfam00501 364 VRGPGVMKGYLNDpELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
25-577 |
6.09e-95 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 303.07 E-value: 6.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTY-ELLQRSARRHGQRIALSCLLHgsaaeeplRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVI 103
Cdd:PRK05605 28 DYGDTTLvDLYDNAVARFGDRPALDFFGA--------TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 104 WGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVtlapfpgtdLWQKVAGLRAQLPE---LYAIVVVDPANLLPAPQRE 179
Cdd:PRK05605 100 YAVLRLGaVVVEHNPLYTAHELEHPFEDHGARVAI---------VWDKVAPTVERLRRttpLETIVSVNMIAAMPLLQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 180 ALK-------AQRGPL---PEGVLDFDTLIADCP--ADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAeI 247
Cdd:PRK05605 171 ALRlpipalrKARAALtgpAPGTVPWETLVDAAIggDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-A 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 248 MGLNADYGV---DDVLLCGLPLFHVNGV-MVTGLAPFHRGAQVLLAGPQgyrnPTLIQDFWKlveRYRVTSFSGVPTIYA 323
Cdd:PRK05605 250 QGKAWVPGLgdgPERVLAALPMFHAYGLtLCLTLAVSIGGELVLLPAPD----IDLILDAMK---KHPPTWLPGVPPLYE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 324 ALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPYCQVKV 402
Cdd:PRK05605 323 KIAEAAEeRGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 403 AvlDGEgNYLRDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIwIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNI 481
Cdd:PRK05605 403 V--DPE-DPDETMPDGEEGELLVRGPQVFKGYWNRpEETAKS-FLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 482 DPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVpERAAVPKDIWLIESMPVTAVGK 561
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHL-TRYKVPRRFYHVDELPRDQLGK 557
|
570
....*....|....*.
gi 15599055 562 TFKPALRLDAIRRVLE 577
Cdd:PRK05605 558 VRRREVREELLEKLGA 573
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
56-561 |
8.65e-92 |
|
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: 292.19 E-value: 8.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 56 AEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTR 134
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGgIFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 135 VLVTLApfpgtDLWQKVAGLRAQLPELYAIVVVDPANllpapqrealkaqRGPLPEGVLDFDTLIADCPADRLESGRAih 214
Cdd:cd05911 85 VIFTDP-----DGLEKVKEAAKELGPKDKIIVLDDKP-------------DGVLSIEDLLSPTLGEEDEDLPPPLKDG-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMG--LNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQ 292
Cdd:cd05911 145 KDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQtfLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 gyrnptlIQDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVI-EGYGL 370
Cdd:cd05911 225 -------SELFLDLIEKYKITFLYLVPPIAAALAKSPLlDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIkQGYGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 371 TEGTCGTSCNPrGGERRPGSIGLRLPYCQVKVavLDGEGNylRDAAPNEVGNLCLKGPTVFKGYLQ-QDRNRDIWIGDGW 449
Cdd:cd05911 298 TETGGILTVNP-DGDDKPGSVGRLLPNVEAKI--VDDDGK--DSLGPNEPGEICVRGPQVMKGYYNnPEATKETFDEDGW 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 450 FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEE 529
Cdd:cd05911 373 LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKE 452
|
490 500 510
....*....|....*....|....*....|..
gi 15599055 530 LLEHASRHVPERAAVPKDIWLIESMPVTAVGK 561
Cdd:cd05911 453 VKDYVAKKVASYKQLRGGVVFVDEIPKSASGK 484
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
33-568 |
7.38e-91 |
|
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: 290.69 E-value: 7.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 33 LLQRSARRHGQRIALSCllhgSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNlPQTHYVIWGGEAA--G 110
Cdd:cd12119 1 LLEHAARLHGDREIVSR----THEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWN-THRHLELYYAVPGmgA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 IVNAINPLLEPEHIAELIRASNTRVLvtlapFPGTDLWQKVAGLRAQLPELYAIVVVDPANLLPAPQrealkaqrgplPE 190
Cdd:cd12119 76 VLHTINPRLFPEQIAYIINHAEDRVV-----FVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPA-----------GV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 191 GVLDFDTLIADcpadrlESGRAIHPD----DVASYFHTGGTTGTPKLAPHSHFNEV--AMAEIMGLNADYGVDDVLLCGL 264
Cdd:cd12119 140 GVLAYEELLAA------ESPEYDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 265 PLFHVNGvmvTGL--APFHRGAQVLLAGPqgYRNP-TLIQdfwkLVERYRVTSFSGVPTIYAALLQ-VPSDGRDLSSLRF 340
Cdd:cd12119 214 PMFHVNA---WGLpyAAAMVGAKLVLPGP--YLDPaSLAE----LIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 341 ALCGAAPMPVELIRQFEARtGLKVIEGYGLTE-GTCGTSCNPRGGER-RPGSIGLRL------PYCQVKVAVLDGEGNYL 412
Cdd:cd12119 285 VVIGGSAVPRSLIEAFEER-GVRVIHAWGMTEtSPLGTVARPPSEHSnLSEDEQLALrakqgrPVPGVELRIVDDDGREL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 413 -RDaaPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALH 491
Cdd:cd12119 364 pWD--GKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIM 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 492 RHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd12119 442 AHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVA-KWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
24-538 |
2.89e-89 |
|
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: 286.05 E-value: 2.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 24 RDLPSSTYELLqrSARRHGQRIALSCLLHGSAaeeplrISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVI 103
Cdd:cd05904 3 TDLPLDSVSFL--FASAHPSRPALIDAATGRA------LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 104 WGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLAPfpgtdLWQKVAGLRAQlpelyaIVVVDpanllpapqrEALK 182
Cdd:cd05904 75 LAVLSLGaVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE-----LAEKLASLALP------VVLLD----------SAEF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 183 aqrGPLPEGVLDFDTLIADCPADRlesgraIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEI--MGLNADYGVDDVL 260
Cdd:cd05904 134 ---DSLSFSDLLFEADEAEPPVVV------IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSEDVF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 261 LCGLPLFHVNGVMVTGLAPFHRGAQVLLAgpQGYRnptlIQDFWKLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLR 339
Cdd:cd05904 205 LCVLPMFHIYGLSSFALGLLRLGATVVVM--PRFD----LEELLAAIERYKVTHLPVVPPIVLALVKSPiVDKYDLSSLR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 340 FALCGAAPMPVELIRQFEAR-TGLKVIEGYGLTEGTCGTS--CNPRGGERRPGSIGLRLPYCQVKVavLDGE-GNYLrda 415
Cdd:cd05904 279 QIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTESTGVVAmcFAPEKDRAKYGSVGRLVPNVEAKI--VDPEtGESL--- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 416 APNEVGNLCLKGPTVFKGYLQQDRNRDIWIG-DGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHP 494
Cdd:cd05904 354 PPNQTGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHP 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15599055 495 AVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHV 538
Cdd:cd05904 434 EILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQV 477
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
31-568 |
1.38e-85 |
|
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: 277.41 E-value: 1.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG 110
Cdd:COG1021 28 GDLLRRRAERHPDRIAVVD--------GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 I--VNAInP---LLEPEHIAELIRAsntRVLVTLAPFPGTDLWQKVAGLRAQLPELYAIVVVDPanllpapqrealkaqr 185
Cdd:COG1021 100 AipVFAL-PahrRAEISHFAEQSEA---VAYIIPDRHRGFDYRALARELQAEVPSLRHVLVVGD---------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 186 gplPEGVLDFDTLIADcPADRLEsgRAIHPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLNADygvdDVLL 261
Cdd:COG1021 160 ---AGEFTSLDALLAA-PADLSE--PRPDPDDVAFFQLSGGTTGLPKLIPRTHddylYSVRASAEICGLDAD----TVYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 262 CGLPLFHvN------GVmvtgLAPFHRGAQVLLAgpqgyRNPTlIQDFWKLVERYRVTSFSGVPTIYAALLQ-VPSDGRD 334
Cdd:COG1021 230 AALPAAH-NfplsspGV----LGVLYAGGTVVLA-----PDPS-PDTAFPLIERERVTVTALVPPLALLWLDaAERSRYD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 335 LSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGT-CGTSCN-PRggERRPGSIGLRL-PYCQVKVavLDGEGNy 411
Cdd:COG1021 299 LSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLvNYTRLDdPE--EVILTTQGRPIsPDDEVRI--VDEDGN- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 412 lrDAAPNEVGNLCLKGPTVFKGYLQQDR-NRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEAL 490
Cdd:COG1021 374 --PVPPGEVGELLTRGPYTIRGYYRAPEhNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 491 HRHPAVALAAAVGKPDAKAGELPVAYIQLKpGASASEEELLEH------ASRHVPERaavpkdIWLIESMPVTAVGKTFK 564
Cdd:COG1021 452 LAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFlrerglAAFKLPDR------LEFVDALPLTAVGKIDK 524
|
....
gi 15599055 565 PALR 568
Cdd:COG1021 525 KALR 528
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
58-568 |
1.80e-83 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 272.31 E-value: 1.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 58 EPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV-NAINPLLEPEHIAELIRASNTRVL 136
Cdd:PRK13295 52 APRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVlNPLMPIFRERELSFMLKHAESKVL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 137 VTLAPFPGTDLWQKVAGLRAQLPELYAIVVVDPanllpapqrealkaqrgplpEGVLDFDTLIADCP------ADRLESG 210
Cdd:PRK13295 132 VVPKTFRGFDHAAMARRLRPELPALRHVVVVGG--------------------DGADSFEALLITPAweqepdAPAILAR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 211 RAIHPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLnadyGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQV 286
Cdd:PRK13295 192 LRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAERLGL----GADDVILMASPMAHQTGFMYGLMMPVMLGATA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 287 LLagpqgyrnptliQDFW------KLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEAR 359
Cdd:PRK13295 268 VL------------QDIWdparaaELIRTEGVTFTMASTPFLTDLTRAVKeSGRPVSSLRTFLCAGAPIPGALVERARAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 360 TGLKVIEGYGLTEGTCGTSCNP-RGGERRPGSIGLRLPYCQVKVavLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQ- 437
Cdd:PRK13295 336 LGAKIVSAWGMTENGAVTLTKLdDPDERASTTDGCPLPGVEVRV--VDADGAPL---PAGQIGRLQVRGCSNFGGYLKRp 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 438 DRNRDIwiGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYI 517
Cdd:PRK13295 411 QLNGTD--ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 518 QLKPGASASEEELLEH------ASRHVPERAAVpkdiwlIESMPVTAVGKTFKPALR 568
Cdd:PRK13295 489 VPRPGQSLDFEEMVEFlkaqkvAKQYIPERLVV------RDALPRTPSGKIQKFRLR 539
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
32-575 |
1.49e-80 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 265.10 E-value: 1.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALSCLLHGsaaeepLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQ---THYVIwgGEA 108
Cdd:PRK12583 22 DAFDATVARFPDREALVVRHQA------LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEwllTQFAT--ARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 109 AGIVNAINPLLEPEHIAELIRASNTRVLVTLAPFPGTD-------------LWQKVAGLRAQLPELYAIVVVDPANllpa 175
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDyhamlqellpglaEGQPGALACERLPELRGVVSLAPAP---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 176 pqrealkaqrgplPEGVLDFDTLIAD----CPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLN 251
Cdd:PRK12583 170 -------------PPGFLAWHELQARgetvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAES 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 252 ADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLagPQGYRNP--TLiqdfwKLVERYRVTSFSGVPTIYAALLQVP 329
Cdd:PRK12583 237 LGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVY--PNEAFDPlaTL-----QAVEEERCTALYGVPTMFIAELDHP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 330 SDGR-DLSSLRFALCGAAPMPVELIRQFEARTGL-KVIEGYGLTEGTCGT--SCNPRGGERRPGSIGLRLPYCQVKVAVL 405
Cdd:PRK12583 310 QRGNfDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 406 DGEgnylrDAAPNEVGNLCLKGPTVFKGYLQQD-RNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQ 484
Cdd:PRK12583 390 DGA-----TVPRGEIGELCTRGYSVMKGYWNNPeATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 485 MIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFK 564
Cdd:PRK12583 465 EIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARI-AHFKVPRYFRFVDEFPMTVTGKVQK 543
|
570
....*....|.
gi 15599055 565 PALRLDAIRRV 575
Cdd:PRK12583 544 FRMREISIEEL 554
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
32-570 |
5.26e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 262.56 E-value: 5.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNlpQTHYVI-WGGEA-A 109
Cdd:PRK08316 15 DILRRSARRYPDKTALVF--------GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHN--SDAYALlWLACArA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 110 GIVN-AINPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkVAGLRAQLPELYAIVVVDPANLLP-APQREAlkaqrgp 187
Cdd:PRK08316 85 GAVHvPVNFMLTGEELAYILDHSGARAFLV------------DPALAPTAEAALALLPVDTLILSLvLGGREA------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 188 lPEGVLDFDTLIAdcPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHfnEVAMAEIMG--LNADYGVDDVLLCGLP 265
Cdd:PRK08316 146 -PGGWLDFADWAE--AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTH--RALIAEYVSciVAGDMSADDIPLHALP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 266 LFHVNGVMVTGLAPFHRGAQ-VLLAGPqgyrNPTLIQDfwkLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALC 343
Cdd:PRK08316 221 LYHCAQLDVFLGPYLYVGATnVILDAP----DPELILR---TIEAERITSFFAPPTVWISLLRHPDfDTRDLSSLRKGYY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 344 GAAPMPVELIRQFEAR-TGLKVIEGYGLTE-GTCGTSCNPRGGERRPGSIGLrlPYCQVKVAVLDGEGNylrDAAPNEVG 421
Cdd:PRK08316 294 GASIMPVEVLKELRERlPGLRFYNCYGQTEiAPLATVLGPEEHLRRPGSAGR--PVLNVETRVVDDDGN---DVAPGEVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 422 NLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAA 501
Cdd:PRK08316 369 EIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599055 502 VGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALRLD 570
Cdd:PRK08316 449 IGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLA-GFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
33-568 |
3.85e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 257.66 E-value: 3.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 33 LLQRSARRHGQRIALsclLHGSAaeeplRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV 112
Cdd:PRK07470 12 FLRQAARRFPDRIAL---VWGDR-----SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 113 NA-INPLLEPEHIAELIRASNTRVLVTLAPFPGtdlwqKVAGLRAQLPELYAIVVVDpanllpapqrealkaqrgpLPEG 191
Cdd:PRK07470 84 WVpTNFRQTPDEVAYLAEASGARAMICHADFPE-----HAAAVRAASPDLTHVVAIG-------------------GARA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 192 VLDFDTLIADCPADRLESGRAIHpDDVASYFHTGGTTGTPKLA--PHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHv 269
Cdd:PRK07470 140 GLDYEALVARHLGARVANAAVDH-DDPCWFFFTSGTTGRPKAAvlTHGQMAFVITNHLADLMPGTTEQDASLVVAPLSH- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 270 nGVMVTGLAPFHRGAQ-VLLAGPqgyrnPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAP 347
Cdd:PRK07470 218 -GAGIHQLCQVARGAAtVLLPSE-----RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAvDRYDHSSLRYVIYAGAP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 348 MPVELIRQFEARTGLKVIEGYGLTEGT-CGTSCNPR------GGERRPGSIGLrlPYCQVKVAVLDGEGNYLrdaAPNEV 420
Cdd:PRK07470 292 MYRADQKRALAKLGKVLVQYFGLGEVTgNITVLPPAlhdaedGPDARIGTCGF--ERTGMEVQIQDDEGREL---PPGET 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 421 GNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAA 500
Cdd:PRK07470 367 GEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVA 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599055 501 AVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK07470 447 VLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVA-RYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
61-568 |
2.70e-77 |
|
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: 252.98 E-value: 2.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLG-LESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVlvt 138
Cdd:cd05941 11 SITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGgVAVPLNPSYPLAELEYVITDSEPSL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 139 lapfpgtdlwqkvaglraqlpelyaivVVDPANLLpapqrealkaqrgplpegvldfdtliadcpadrlesgraihpddv 218
Cdd:cd05941 88 ---------------------------VLDPALIL--------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 219 asyfHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAG---PQGYr 295
Cdd:cd05941 96 ----YTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPkfdPKEV- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 296 nptliqdfWKLVERYRVTSFSGVPTIYAALLQVP---------SDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIE 366
Cdd:cd05941 171 --------AISRLMPSITVFMGVPTIYTRLLQYYeahftdpqfARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLE 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 367 GYGLTEGTCGTScNPRGGERRPGSIGLRLPycQVKVAVLDGEGNylRDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWI 445
Cdd:cd05941 243 RYGMTEIGMALS-NPLDGERRPGTVGMPLP--GVQARIVDEETG--EPLPRGEVGEIQVRGPSVFKEYWNKpEATKEEFT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 446 GDGWFNTGDLGRIDEDGYIWLTGRSKDLII-RGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGAS 524
Cdd:cd05941 318 DDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAA 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15599055 525 A-SEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05941 398 AlSLEELKEWAKQRLA-PYKRPRRLILVDELPRNAMGKVNKKELR 441
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
62-586 |
4.95e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 255.73 E-value: 4.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGE-AAGIVNAINPLLEPEHIAELIRASNTRVLVTLA 140
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLlAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 -PFPgtdlwqKVAGLRAQlPELYAIVVVDPANLLPAPQR---EALKAQRGPLPEGVLDFDTL-IADCPADRLESGRAIHP 215
Cdd:PRK06710 130 lVFP------RVTNVQSA-TKIEHVIVTRIADFLPFPKNllyPFVQKKQSNLVVKVSESETIhLWNSVEKEVNTGVEVPC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 D---DVASYFHTGGTTGTPKLAPHSHFNEVAMAeIMGLNADYGV---DDVLLCGLPLFHVNGVMvtglapfhrgAQVLLA 289
Cdd:PRK06710 203 DpenDLALLQYTGGTTGFPKGVMLTHKNLVSNT-LMGVQWLYNCkegEEVVLGVLPFFHVYGMT----------AVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 290 GPQGYRNpTLIQDF-----WKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGLK 363
Cdd:PRK06710 272 IMQGYKM-VLIPKFdmkmvFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 364 VIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDgEGNYLRdaaPNEVGNLCLKGPTVFKGYLQQDRNRDI 443
Cdd:PRK06710 351 LVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLE-TGEALP---PGEIGEIVVKGPQIMKGYWNKPEETAA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 444 WIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGA 523
Cdd:PRK06710 427 VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGT 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599055 524 SASEEELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTfkpalrldaIRRVLEEESRRIAED 586
Cdd:PRK06710 507 ECSEEELNQFARKYLAAY-KVPKVYEFRDELPKTTVGKI---------LRRVLIEEEKRKNED 559
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
25-561 |
4.23e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 252.96 E-value: 4.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSST-YELLQRSARRHGQRIALscLLHGSAaeeplrISYAELFARVTQTANALHR-LGLESHQAVSFLLPNLPQ---T 99
Cdd:PRK08314 6 TLPETSlFHNLEVSARRYPDKTAI--VFYGRA------ISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQfviA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 100 HYVIWGGEAagIVNAINPLLEPEHIAELIRASNTRVLVTlapfpGTDLWQKVAGLRAQLPeLYAIVVVDPANLLPAPQRE 179
Cdd:PRK08314 78 YYAILRANA--VVVPVNPMNREEELAHYVTDSGARVAIV-----GSELAPKVAPAVGNLR-LRHVIVAQYSDYLPAEPEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 180 ALKA---QRGPLPEGVLDFDTLIADCPADRLESG-RAIHPDDVASYFHTGGTTGTPKLAPHSHFNevAMAEIMG--LNAD 253
Cdd:PRK08314 150 AVPAwlrAEPPLQALAPGGVVAWKEALAAGLAPPpHTAGPDDLAVLPYTSGTTGVPKGCMHTHRT--VMANAVGsvLWSN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 254 YGVDDVLLCGLPLFHVNGvMVTGL-APFHRGAQVLLAgPQGYRNPTLiqdfwKLVERYRVTSFSGVPTIYAALLQVPS-D 331
Cdd:PRK08314 228 STPESVVLAVLPLFHVTG-MVHSMnAPIYAGATVVLM-PRWDREAAA-----RLIERYRVTHWTNIPTMVVDFLASPGlA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 332 GRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGgerRPGSIGLRLPYCQVKVAVLDGEGny 411
Cdd:PRK08314 301 ERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPD---RPKLQCLGIPTFGVDARVIDPET-- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 412 LRDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWI---GDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIE 487
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRpEATAEAFIeidGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599055 488 EALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASA--SEEELLEHASRHVperAA--VPKDIWLIESMPVTAVGK 561
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGktTEEEIIAWAREHM---AAykYPRIVEFVDSLPKSGSGK 530
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-568 |
1.50e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 250.67 E-value: 1.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 27 PSSTYELLQRSARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGG 106
Cdd:PRK06188 11 GATYGHLLVSALKRYPDRPAL--------VLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 107 EAAGIVN-AINPLLEPEHIAELIRASNTRVL-VTLAPFPgtdlwQKVAGLRAQLPELYAIVVVdpanllpapqrealkaq 184
Cdd:PRK06188 83 QLAGLRRtALHPLGSLDDHAYVLEDAGISTLiVDPAPFV-----ERALALLARVPSLKHVLTL----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 185 rGPLPEGVlDFDTLIADCPADRLESGRAihPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGL 264
Cdd:PRK06188 141 -GPVPDGV-DLLAAAAKFGPAPLVAAAL--PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 265 PLFHVNGVMVtgLAPFHRGAQVLLAgpQGYrNPtliQDFWKLVERYRVTSFSGVPT-IYAALLQVPSDGRDLSSLRFALC 343
Cdd:PRK06188 217 PLSHAGGAFF--LPTLLRGGTVIVL--AKF-DP---AEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYY 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 344 GAAPM-PVELIRQFEaRTGLKVIEGYGLTEG-----TCGTSCNPRGGERRPGSIGLRLPYCQVkvAVLDGEGnylRDAAP 417
Cdd:PRK06188 289 GASPMsPVRLAEAIE-RFGPIFAQYYGQTEApmvitYLRKRDHDPDDPKRLTSCGRPTPGLRV--ALLDEDG---REVAQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 418 NEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVA 497
Cdd:PRK06188 363 GEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVA 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599055 498 LAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEhasrHVPER---AAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK06188 443 QVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQA----HVKERkgsVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-568 |
2.95e-75 |
|
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: 244.49 E-value: 2.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPqGY 294
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSP-SF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RNPTLIQDfwklVERYRVTSFSGVPTIYAALLQVPSDGR-DLSSLRFALCGAAPMPVELIRQFEARTGLK-VIEGYGLTE 372
Cdd:cd05917 80 DPLAVLEA----IEKEKCTALHGVPTMFIAELEHPDFDKfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 GTCGTSCNPRGG--ERRPGSIGLRLPYcqVKVAVLDGEGNYLrdAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGW 449
Cdd:cd05917 156 TSPVSTQTRTDDsiEKRVNTVGRIMPH--TEAKIVDPEGGIV--PPVGVPGELCIRGYSVMKGYWNDpEKTAEAIDGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 450 FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEE 529
Cdd:cd05917 232 LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEED 311
|
330 340 350
....*....|....*....|....*....|....*....
gi 15599055 530 LLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05917 312 IKAYCKGKI-AHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
32-568 |
3.10e-75 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 250.88 E-value: 3.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALScllhgsAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQthYVIWGGEAAGI 111
Cdd:PRK08315 20 QLLDRTAARYPDREALV------YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPE--WVLTQFATAKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 112 ----VNaINPLLEPEHIAELIRASNTRVLVTLAPFPGTDLwqkVAGLRAQLPELYAivvvdpanllpaPQREALKAQRGP 187
Cdd:PRK08315 92 gailVT-INPAYRLSELEYALNQSGCKALIAADGFKDSDY---VAMLYELAPELAT------------CEPGQLQSARLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 188 -----------LPEGVLDFDTLIA---DCPADRLES-GRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNA 252
Cdd:PRK08315 156 elrrviflgdeKHPGMLNFDELLAlgrAVDDAELAArQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 253 DYGVDDVLLCGLPLFHVNGvMVTG-LAPFHRGAQVLLAGPqGYrNP--TLiqdfwKLVERYRVTSFSGVPTIYAALLQVP 329
Cdd:PRK08315 236 KLTEEDRLCIPVPLYHCFG-MVLGnLACVTHGATMVYPGE-GF-DPlaTL-----AAVEEERCTALYGVPTMFIAELDHP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 330 S-DGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIE-GYGLTE---GTCGTSCN-PRggERRPGSIGLRLPYCQVKVa 403
Cdd:PRK08315 308 DfARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTiAYGMTEtspVSTQTRTDdPL--EKRVTTVGRALPHLEVKI- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 404 vLDGEGNylRDAAPNEVGNLCLKGPTVFKGYL-QQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNID 482
Cdd:PRK08315 385 -VDPETG--ETVPRGEQGELCTRGYSVMKGYWnDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 483 PQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASrhvpERAA---VPKDIWLIESMPVTAV 559
Cdd:PRK08315 462 PREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCR----GKIAhykIPRYIRFVDEFPMTVT 537
|
....*....
gi 15599055 560 GKTFKPALR 568
Cdd:PRK08315 538 GKIQKFKMR 546
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
29-503 |
3.42e-75 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 251.94 E-value: 3.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 29 STYELLQRSARRHGQRIALSCLLHGSAAEeplrISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYV---IWG 105
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDGIWQS----LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIAdlaILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 106 geAAGIVNAINPLLEPEHIAELIRASNTRVLVTLapfpGTDLWQKVAGLRAQLPELYAIVVVDPANLLPAPqrealkaqr 185
Cdd:COG1022 88 --AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVE----DQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDP--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 186 gplpeGVLDFDTLIA-----DCPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMA----EIMGLNADygv 256
Cdd:COG1022 153 -----RLLSLDELLAlgrevADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNArallERLPLGPG--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 257 dDVLLCGLPLFHVNGVMVtGLAPFHRGAQVLLAGPQgyrnPTLIQDFwklvERYRVTSFSGVP----TIYAALLQ----- 327
Cdd:COG1022 225 -DRTLSFLPLAHVFERTV-SYYALAAGATVAFAESP----DTLAEDL----REVKPTFMLAVPrvweKVYAGIQAkaeea 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 328 --------------------VPSDGRDLSS------------------------LRFALCGAAPMPVELIRQFEArTGLK 363
Cdd:COG1022 295 gglkrklfrwalavgrryarARLAGKSPSLllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 364 VIEGYGLTEGTCGTSCNpRGGERRPGSIGLRLPYCQVKVAVlDGEgnylrdaapnevgnLCLKGPTVFKGYLQQDR-NRD 442
Cdd:COG1022 374 VLEGYGLTETSPVITVN-RPGDNRIGTVGPPLPGVEVKIAE-DGE--------------ILVRGPNVMKGYYKNPEaTAE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599055 443 IWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLII-RGGHNIDPQMIEEALHRHPAVALAAAVG 503
Cdd:COG1022 438 AFDADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
62-568 |
1.46e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 244.81 E-value: 1.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV-NAINPLLEPEHIAELIRASNTRVLVTla 140
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYyTPINWHLTAAEIAYIVDDSGAKVLIV-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 pfpgtdlwqkVAGLRAQLPELYAivvvdpanLLPAPQREaLKAQRGPLPeGVLDFDTLIADCPADRLesgraihPDDVAS 220
Cdd:PRK08276 90 ----------SAALADTAAELAA--------ELPAGVPL-LLVVAGPVP-GFRSYEEALAAQPDTPI-------ADETAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 221 Y--FHTGGTTGTPK----LAPHSHFNEVA--MAEIMGLNADYGVDDVLLCGLPLFHVngvmvtglAPFHRGAQVLLAGpq 292
Cdd:PRK08276 143 AdmLYSSGTTGRPKgikrPLPGLDPDEAPgmMLALLGFGMYGGPDSVYLSPAPLYHT--------APLRFGMSALALG-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 gyrNPTLIQDFW------KLVERYRVTSFSGVPTIYAALLQVPSDGR---DLSSLRFALCGAAPMPVELIRQFEARTGLK 363
Cdd:PRK08276 213 ---GTVVVMEKFdaeealALIERYRVTHSQLVPTMFVRMLKLPEEVRaryDVSSLRVAIHAAAPCPVEVKRAMIDWWGPI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 364 VIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLpycQVKVAVLDGEGNylrDAAPNEVGNLCLKGPTVFKGYLQ-QDRNRD 442
Cdd:PRK08276 290 IHEYYASSEGGGVTVITSEDWLAHPGSVGKAV---LGEVRILDEDGN---ELPPGEIGTVYFEMDGYPFEYHNdPEKTAA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 443 IWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPG 522
Cdd:PRK08276 364 ARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15599055 523 ASASEE---ELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK08276 444 ADAGDAlaaELIAWLRGRL-AHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
34-568 |
2.18e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 242.93 E-value: 2.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 34 LQRSARRHGQRIALsclLHGsaaeePLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLP---QTHYviwGGEAAG 110
Cdd:PRK08162 24 LERAAEVYPDRPAV---IHG-----DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPamvEAHF---GVPMAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 IV-NAINPLLEPEHIAELIRASNTRVLVTLAPFPGTdlwqkVAGLRAQLPELYAIVVVDpanllpapqreALKAQRGPLP 189
Cdd:PRK08162 93 AVlNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEV-----AREALALLPGPKPLVIDV-----------DDPEYPGGRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 190 EGVLDFDTLIAD--------CPADRLEsgrAIhpddvaSYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLL 261
Cdd:PRK08162 157 IGALDYEAFLASgdpdfawtLPADEWD---AI------ALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 262 CGLPLFHVNGV----MVTGLApfhrGAQVLLagpqgyR--NPTLIqdfWKLVERYRVTSFSGVPTIYAALLQVPSDGRDL 335
Cdd:PRK08162 228 WTLPMFHCNGWcfpwTVAARA----GTNVCL------RkvDPKLI---FDLIREHGVTHYCGAPIVLSALINAPAEWRAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 SS--LRFALCGAAPmPVELIRQFEARtGLKVIEGYGLTEgTCG--TSCNPRGG---------ERRPGSIGLRLPyCQVKV 402
Cdd:PRK08162 295 IDhpVHAMVAGAAP-PAAVIAKMEEI-GFDLTHVYGLTE-TYGpaTVCAWQPEwdalplderAQLKARQGVRYP-LQEGV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 403 AVLDGEGNYLRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNID 482
Cdd:PRK08162 371 TVLDPDTMQPVPADGETIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENIS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 483 PQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIEsMPVTAVGKT 562
Cdd:PRK08162 451 SIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLA-GFKVPKAVVFGE-LPKTSTGKI 528
|
....*.
gi 15599055 563 FKPALR 568
Cdd:PRK08162 529 QKFVLR 534
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
61-568 |
5.23e-72 |
|
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: 238.82 E-value: 5.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV-NAINPLLEPEHIAELIRASNTRVLVTL 139
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVtNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 140 APFPGTDlwqkvaglraqlpelyaivvvdpanllPAPQrealkaqrgplpegvldfdtliadcpadrlesgraihPDDVA 219
Cdd:cd05903 81 ERFRQFD---------------------------PAAM-------------------------------------PDAVA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 220 SYFHTGGTTGTPKLAPHSHFNevAMAEIMGLNADYGVD--DVLLCGLPLFHVNGVMVTGLAPFHRGAqvllagpqgyrnP 297
Cdd:cd05903 97 LLLFTSGTTGEPKGVMHSHNT--LSASIRQYAERLGLGpgDVFLVASPMAHQTGFVYGFTLPLLLGA------------P 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 298 TLIQDFW------KLVERYRVTSFSGVPTIYAALLQVPSD-GRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGL 370
Cdd:cd05903 163 VVLQDIWdpdkalALMREHGVTFMMGATPFLTDLLNAVEEaGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 371 TEgTCG--TSCNPRGGERRPGSIGLRLPYCQVKVavLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDG 448
Cdd:cd05903 243 TE-CPGavTSITPAPEDRRLYTDGRPLPGVEIKV--VDDTGATL---APGVEGELLSRGPSVFLGYLDRPDLTADAAPEG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 449 WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE 528
Cdd:cd05903 317 WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFD 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599055 529 ELLEHASRHVPERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05903 397 ELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
163-568 |
2.05e-71 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 239.01 E-value: 2.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 163 AIVVVDPANL---------LPAPQREALKAQR-GPLPEGVLDFDTLIADCPADrlesgraihPDDVASYFHTGGTTGTPK 232
Cdd:PRK07514 102 ALVVCDPANFawlskiaaaAGAPHVETLDADGtGSLLEAAAAAPDDFETVPRG---------ADDLAAILYTSGTTGRSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 233 LAPHSHFNEVAMAEIMglnADY---GVDDVLLCGLPLFHVNGVMV-TGLAPFHRGAQVLLAGpqgyRNPTLIQDFWKlve 308
Cdd:PRK07514 173 GAMLSHGNLLSNALTL---VDYwrfTPDDVLIHALPIFHTHGLFVaTNVALLAGASMIFLPK----FDPDAVLALMP--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 309 ryRVTSFSGVPTIYAALLQVPSDGRDL-SSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTScNPRGGERR 387
Cdd:PRK07514 243 --RATVMMGVPTFYTRLLQEPRLTREAaAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTS-NPYDGERR 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 388 PGSIGLRLPYCQVKVAVLDgEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWL 466
Cdd:PRK07514 320 AGTVGFPLPGVSLRVTDPE-TGAEL---PPGEIGMIEVKGPNVFKGYWRMpEKTAEEFRADGFFITGDLGKIDERGYVHI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 467 TGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPK 546
Cdd:PRK07514 396 VGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLA-RFKQPK 474
|
410 420
....*....|....*....|..
gi 15599055 547 DIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK07514 475 RVFFVDELPRNTMGKVQKNLLR 496
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
61-568 |
2.40e-71 |
|
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: 239.19 E-value: 2.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVN-AINPLLEPEHIAELIRASNTRVLVTL 139
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPvPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 140 ApfpgtDLWQKVA-GLRAQLPELYAIVVVDPAnllpapqrealkaqrGPLPeGVLDFDTLIADcPADRLESGrAIHPDDV 218
Cdd:cd05959 109 G-----ELAPVLAaALTKSEHTLVVLIVSGGA---------------GPEA-GALLLAELVAA-EAEQLKPA-ATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 219 ASYFHTGGTTGTPKLAPHSHFNEVAMAE-----IMGLNADygvdDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGpqG 293
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAElyarnVLGIRED----DVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMP--E 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 294 YRNPTLIQDFWklvERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTE 372
Cdd:cd05959 240 RPTPAAVFKRI---RRYRPTVFFGVPTLYAAMLAAPnLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 gTCGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGEgnylrDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGdGWFN 451
Cdd:cd05959 317 -MLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGG-----DVADGEPGELYVRGPSSATMYWNNrDKTRDTFQG-EWTR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 452 TGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASeEELL 531
Cdd:cd05959 390 TGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDS-EALE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599055 532 EHASRHVPERAA---VPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05959 469 EELKEFVKDRLApykYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
34-567 |
1.54e-70 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 236.68 E-value: 1.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 34 LQRSARRHGQRIALScllhgsAAEEPLriSYAELFARVTQTANAL-HRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV 112
Cdd:PRK06839 8 IEKRAYLHPDRIAII------TEEEEM--TYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 113 NA-INPLLEPEHIAELIRASNTRVLVTLAPFPGT-DLWQKVAGLRaqlpelYAIVVVDPAnllpapqrEALKAQRGPLPE 190
Cdd:PRK06839 80 AVpLNIRLTENELIFQLKDSGTTVLFVEKTFQNMaLSMQKVSYVQ------RVISITSLK--------EIEDRKIDNFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 191 GVLDFDTLIAdcpadrlesgraihpddvasyfHTGGTTGTPKLAphshfneVAMAEIMGLNA-------DYGVDDVLLCG 263
Cdd:PRK06839 146 KNESASFIIC----------------------YTSGTTGKPKGA-------VLTQENMFWNAlnntfaiDLTMHDRSIVL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 264 LPLFHVNGVMVTGLAPFHRGAQVLLAGPqgyRNPTliqDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFAL 342
Cdd:PRK06839 197 LPLFHIGGIGLFAFPTLFAGGVIIVPRK---FEPT---KALSMIEKHKVTVVMGVPTIHQALINCSKfETTNLQSVRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 343 CGAAPMPVELIRQFEARtGLKVIEGYGLTEgTCGT--SCNPRGGERRPGSIGLRLPYCQVKVavLDGEGNylrDAAPNEV 420
Cdd:PRK06839 271 NGGAPCPEELMREFIDR-GFLFGQGFGMTE-TSPTvfMLSEEDARRKVGSIGKPVLFCDYEL--IDENKN---KVEVGEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 421 GNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAA 500
Cdd:PRK06839 344 GELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVA 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 501 AVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:PRK06839 424 VVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLA-KYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-568 |
1.65e-70 |
|
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: 234.49 E-value: 1.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVNA-INPLLEPEHIAELIRASntrvlvtl 139
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVpINTALRGDELAYIIDHS-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 140 apfpgtdlwqkvaglRAQLpelyaiVVVDPANLLpapqrealkaqrgplpegvldfdtliadcpadrlesgraihpddva 219
Cdd:cd05934 75 ---------------GAQL------VVVDPASIL---------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 220 syfHTGGTTGTPK--LAPHSH--FNEVAMAEIMGLNADygvdDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGYR 295
Cdd:cd05934 88 ---YTSGTTGPPKgvVITHANltFAGYYSARRFGLGED----DVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSAS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 296 NptliqdFWKLVERYRVTSFSGVPTIYAALLQVPSDGRDlSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTC 375
Cdd:cd05934 161 R------FWSDVRRYGATVTNYLGAMLSYLLAQPPSPDD-RAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 376 GTScNPRGGERRPGSIGLRLPYCQVKVavLDGEGnylRDAAPNEVGNLCLK---GPTVFKGYLQQ-DRNRDIWIGdGWFN 451
Cdd:cd05934 234 GVI-GPRDEPRRPGSIGRPAPGYEVRI--VDDDG---QELPAGEPGELVIRglrGWGFFKGYYNMpEATAEAMRN-GWFH 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 452 TGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELL 531
Cdd:cd05934 307 TGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELF 386
|
490 500 510
....*....|....*....|....*....|....*..
gi 15599055 532 EHASRHVPERaAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05934 387 AFCEGQLAYF-KVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
33-568 |
1.47e-69 |
|
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: 233.73 E-value: 1.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 33 LLQRSARRHGQRIALsclLHGSaaeepLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV 112
Cdd:cd12118 9 FLERAAAVYPDRTSI---VYGD-----RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 113 -NAINPLLEPEHIAELIRASNTRVLVTLAPFPGTDLwqkvaglraqlpelyaivvvdpanllpapqrealkaqrgpLPEG 191
Cdd:cd12118 81 lNALNTRLDAEEIAFILRHSEAKVLFVDREFEYEDL----------------------------------------LAEG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 192 VLDFDTLiadCPADRlesgraihpDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNG 271
Cdd:cd12118 121 DPDFEWI---PPADE---------WDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 272 V----MVTGLApfhrGAQVLLagpqgyRN--PTLIqdfWKLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLRFALCG 344
Cdd:cd12118 189 WcfpwTVAAVG----GTNVCL------RKvdAKAI---YDLIEKHKVTHFCGAPTVLNMLANAPpSDARPLPHRVHVMTA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 345 AAPMPVELIRQFEaRTGLKVIEGYGLTEgTCG--TSC-----------------NPRGGERRPGSIGLRLPYCQVKVAV- 404
Cdd:cd12118 256 GAPPPAAVLAKME-ELGFDVTHVYGLTE-TYGpaTVCawkpewdelpteerarlKARQGVRYVGLEEVDVLDPETMKPVp 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 405 LDGEgnylrdaapnEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQ 484
Cdd:cd12118 334 RDGK----------TIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSV 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 485 MIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIEsMPVTAVGKTFK 564
Cdd:cd12118 404 EVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLA-GFMVPKTVVFGE-LPKTSTGKIQK 481
|
....
gi 15599055 565 PALR 568
Cdd:cd12118 482 FVLR 485
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
35-580 |
1.69e-69 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 235.41 E-value: 1.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 35 QRSARRHGQRIALSCLlHGSaaeeplRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVna 114
Cdd:PRK06087 30 QQTARAMPDKIAVVDN-HGA------SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 115 INPLLEPEHIAELIRASN---TRVLVTLAPFPGTDLWQKVAGLRAQLPELYAIVVVDpaNLLPAPQREALKaqrgplpEG 191
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNkcqAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVD--KLAPATSSLSLS-------QI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 192 VLDFDTLIADCPadrlesgraIHPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLNADygvdDVLLCGLPLF 267
Cdd:PRK06087 172 IADYEPLTTAIT---------THGDELAAVLFTSGTEGLPKGVMLTHnnilASERAYCARLNLTWQ----DVFMMPAPLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 268 HVNGVMVTGLAPFHRGAQVLLAgpQGYRNPTLIQdfwkLVERYRVTSFSG-VPTIYAALLQVPSDGRDLSSLRFALCGAA 346
Cdd:PRK06087 239 HATGFLHGVTAPFLIGARSVLL--DIFTPDACLA----LLEQQRCTCMLGaTPFIYDLLNLLEKQPADLSALRFFLCGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 347 PMPVELIRQFEARtGLKVIEGYGLTEGTCGTSCNP-RGGERRPGSIGLrlPYCQVKVAVLDGegnYLRDAAPNEVGNLCL 425
Cdd:PRK06087 313 TIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNLdDPLSRFMHTDGY--AAAGVEIKVVDE---ARKTLPPGCEGEEAS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 426 KGPTVFKGYLQQ----DRNRDiwiGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAA 501
Cdd:PRK06087 387 RGPNVFMGYLDEpeltARALD---EEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 502 VGKPDAKAGELPVAYIQLK-PGASASEEELLEHASR-HVPERaAVPKDIWLIESMPVTAVGKTFKPALRLDAIRRVLEEE 579
Cdd:PRK06087 464 VAMPDERLGERSCAYVVLKaPHHSLTLEEVVAFFSRkRVAKY-KYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQDV 542
|
.
gi 15599055 580 S 580
Cdd:PRK06087 543 C 543
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
61-561 |
6.30e-69 |
|
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: 230.44 E-value: 6.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQ---THYVIWggEAAGIVNAINPLLEPEHIAELIRASNTRVLV 137
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQyviAYFAIW--RANAVVVPINPMLKERELEYILNDSGAKVAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 138 TLApfpgtdlwqkvaglraqlpELyaivvvdpanllpapqrealkaqrgplpegvldfdtliadcpadrlesgraihpDD 217
Cdd:cd05935 79 VGS-------------------EL------------------------------------------------------DD 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 218 VASYFHTGGTTGTPKLAPHSHFNevAMAEIMGLNADYGVD--DVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPqgYR 295
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFS--AAANALQSAVWTGLTpsDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR--WD 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 296 NPTLIQdfwkLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGT 374
Cdd:cd05935 162 RETALE----LIEKYKVTFWTNIPTMLVDLLATPEfKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETM 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 375 CGTSCNPRGgerRPGSIGLRLPYCQVKVAVLDGEGnyLRDAAPNEVGNLCLKGPTVFKGYLQQDR-NRDIWIGDG---WF 450
Cdd:cd05935 238 SQTHTNPPL---RPKLQCLGIP*FGVDARVIDIET--GRELPPNEVGEIVVRGPQIFKGYWNRPEeTEESFIEIKgrrFF 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 451 NTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPG--ASASEE 528
Cdd:cd05935 313 RTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEE 392
|
490 500 510
....*....|....*....|....*....|...
gi 15599055 529 ELLEHASRHVPERaAVPKDIWLIESMPVTAVGK 561
Cdd:cd05935 393 DIIEWAREQMAAY-KYPREVEFVDELPRSASGK 424
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
150-568 |
8.92e-69 |
|
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: 229.92 E-value: 8.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 150 KVAGLRAQLPELYAIVV-VDPANLLPAPQREALKAQrgPLpegvldfdtliadcpADRLESGRA----IHPDDVASYFHT 224
Cdd:cd05972 27 RVAVLLPRVPELWAVILaVIKLGAVYVPLTTLLGPK--DI---------------EYRLEAAGAkaivTDAEDPALIYFT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 225 GGTTGTPKLAPHSHfnEVAMAEIMGLNADYGV--DDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLagpqgYRNPTLIQD 302
Cdd:cd05972 90 SGTTGLPKGVLHTH--SYPLGHIPTAAYWLGLrpDDIHWNIADPGWAKGAWSSFFGPWLLGATVFV-----YEGPRFDAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 303 FW-KLVERYRVTSFSGVPTIYAALLQVPSDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEgTCGTSCNP 381
Cdd:cd05972 163 RIlELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTE-TGLTVGNF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 382 RGGERRPGSIGLRLP-YcqvKVAVLDGEGNYLrdaAPNEVGNLCLKGPTV--FKGYLQQDRNRDIWIGDGWFNTGDLGRI 458
Cdd:cd05972 242 PDMPVKPGSMGRPTPgY---DVAIIDDDGREL---PPGEEGDIAIKLPPPglFLGYVGDPEKTEASIRGDYYLTGDRAYR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 459 DEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---ELLEHAS 535
Cdd:cd05972 316 DEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVK 395
|
410 420 430
....*....|....*....|....*....|...
gi 15599055 536 RHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05972 396 KVL-APYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
32-574 |
5.21e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 231.58 E-value: 5.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALSCLlhGSAaeeplrISYAELFARVTQTANAL-HRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG 110
Cdd:PRK05677 28 AVLKQSCQRFADKPAFSNL--GKT------LTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 -IVNAINPLLEPEHIAELIRASNTRVLVTLAPFpgTDLWQKVaglraqLPE--LYAIVVVDPANLLPAPQREALKAQRGP 187
Cdd:PRK05677 100 lIVVNTNPLYTAREMEHQFNDSGAKALVCLANM--AHLAEKV------LPKtgVKHVIVTEVADMLPPLKRLLINAVVKH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 188 LPEGVLDFDTLIADCPADRLESGR-------AIHPDDVASYFHTGGTTGTPKLAPHSHFNEVA-MAE---IMGLNADYGV 256
Cdd:PRK05677 172 VKKMVPAYHLPQAVKFNDALAKGAgqpvteaNPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnMLQcraLMGSNLNEGC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 257 DdVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGpqgyrNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQvPSDGR--D 334
Cdd:PRK05677 252 E-ILIAPLPLYHIYAFTFHCMAMMLIGNHNILIS-----NPRDLPAMVKELGKWKFSGFVGLNTLFVALCN-NEAFRklD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 335 LSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGeRRPGSIGLRLPYCQVKVavLDGEGNylrD 414
Cdd:PRK05677 325 FSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQA-IQVGTIGIPVPSTLCKV--IDDDGN---E 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 415 AAPNEVGNLCLKGPTVFKGYLQ-QDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRH 493
Cdd:PRK05677 399 LPLGEVGELCVKGPQVMKGYWQrPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 494 PAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKPALRLDAIR 573
Cdd:PRK05677 479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGY-KVPKAVEFRDELPTTNVGKILRRELRDEELK 557
|
.
gi 15599055 574 R 574
Cdd:PRK05677 558 K 558
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
63-561 |
6.98e-67 |
|
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: 225.02 E-value: 6.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 63 SYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVNA-INPLLEPEHIAELIRASNTRVLVTLAP 141
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAmLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 142 FPGTDLwQKVAglraqLPELYAivvvdpanllPAPQREALKAQrgplpegvldfdtliadcpadrlesgraIHPDDVASY 221
Cdd:TIGR01923 81 LEEKDF-QADS-----LDRIEA----------AGRYETSLSAS----------------------------FNMDQIATL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 222 FHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTgLAPFHRGAQVLLagpqgyrnPTLIQ 301
Cdd:TIGR01923 117 MFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSIL-FRWLIEGATLRI--------VDKFN 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 302 DFWKLVERYRVTSFSGVPTIYAALLQvpSDGRDLSsLRFALCGAAPMPVELIRqfEART-GLKVIEGYGLTEgTCGTSC- 379
Cdd:TIGR01923 188 QLLEMIANERVTHISLVPTQLNRLLD--EGGHNEN-LRKILLGGSAIPAPLIE--EAQQyGLPIYLSYGMTE-TCSQVTt 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 380 -NPRGGERRPGSiGLRLPYCQVKVAVLDGEGnylrdaapneVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRI 458
Cdd:TIGR01923 262 aTPEMLHARPDV-GRPLAGREIKIKVDNKEG----------HGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 459 DEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKpgASASEEELLEHASRHV 538
Cdd:TIGR01923 331 DGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKL 408
|
490 500
....*....|....*....|...
gi 15599055 539 pERAAVPKDIWLIESMPVTAVGK 561
Cdd:TIGR01923 409 -AKYKVPIAFEKLDELPYNASGK 430
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
216-568 |
8.40e-67 |
|
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: 224.15 E-value: 8.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 DDVASYFHTGGTTGTPKLAPHS---HFNE-VAMAEIMGLNADygvdDVLLCGLPLFHVNG--VMVTGLApfhRGAQVlla 289
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTfgnHWWSaIGSALNLGLTED----DNWLCALPLFHISGlsILMRSVI---YGMTV--- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 290 gpqgyrnpTLIQDF-----WKLVERYRVTSFSGVPTIYAALLQVPSDGRDlSSLRFALCGAAPMPVELIRQFEARtGLKV 364
Cdd:cd05912 147 --------YLVDKFdaeqvLHLINSGKVTIISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 365 IEGYGLTEgTCGTSC--NPRGGERRPGSIGLRLPYCQVKVAVLDGEgnylrdaaPNEVGNLCLKGPTVFKGYL-QQDRNR 441
Cdd:cd05912 217 YQSYGMTE-TCSQIVtlSPEDALNKIGSAGKPLFPVELKIEDDGQP--------PYEVGEILLKGPNVTKGYLnRPDATE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 442 DIwIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKp 521
Cdd:cd05912 288 ES-FENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE- 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15599055 522 gASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05912 366 -RPISEEELIAYCSEKLA-KYKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
41-564 |
2.58e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 221.84 E-value: 2.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 41 HGQRiALSCLLHGSAAEEPLR---------ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGI 111
Cdd:PRK06178 30 HGER-PLTEYLRAWARERPQRpaiifyghvITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 112 VNA-INPLLEPEHIAELIRASNTRVLVTLapfpgTDLWQKVAGLRAQLPeLYAIVVVDPANLLPA----PQREALKAQRg 186
Cdd:PRK06178 109 VHVpVSPLFREHELSYELNDAGAEVLLAL-----DQLAPVVEQVRAETS-LRHVIVTSLADVLPAeptlPLPDSLRAPR- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 187 PLPEGVLDFDTLIADCPADRLESGRAihPDDVASYFHTGGTTGTPKLAPHSHFNEV-AMAEIMGLNADYGVDDVLLCGLP 265
Cdd:PRK06178 182 LAAAGAIDLLPALRACTAPVPLPPPA--LDALAALNYTGGTTGMPKGCEHTQRDMVyTAAAAYAVAVVGGEDSVFLSFLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 266 LFHVNGVMVTGLAPFHRGAQ-VLLA--GPQGyrnptliqdFWKLVERYRVTSFSGVPTIYAALLQVPSDG-RDLSSLRFA 341
Cdd:PRK06178 260 EFWIAGENFGLLFPLFSGATlVLLArwDAVA---------FMAAVERYRVTRTVMLVDNAVELMDHPRFAeYDLSSLRQV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 342 LCGA--APMPVELIRQFEARTGLKVIEG-YGLTEG-TCGT-SCNPRGGE----RRPGSIGLRLPYCQVKVAvlDGEGNYL 412
Cdd:PRK06178 331 RVVSfvKKLNPDYRQRWRALTGSVLAEAaWGMTEThTCDTfTAGFQDDDfdllSQPVFVGLPVPGTEFKIC--DFETGEL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 413 RdaaP-NEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALH 491
Cdd:PRK06178 409 L---PlGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLG 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599055 492 RHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRH-----VPEraavpkdIWLIESMPVTAVGKTFK 564
Cdd:PRK06178 486 QHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENmavykVPE-------IRIVDALPMTATGKVRK 556
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
23-568 |
9.79e-64 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 219.47 E-value: 9.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 23 QRDLPSSTYeLLQRSARRHGQrialSCLLHGSAAEEplrISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYV 102
Cdd:PLN02246 20 PNHLPLHDY-CFERLSEFSDR----PCLIDGATGRV---YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 103 IWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLAPFPgtdlwQKVAGLRAQlpELYAIVVVDPAnllpapqreal 181
Cdd:PLN02246 92 FLGASRRGaVTTTANPFYTPAEIAKQAKASGAKLIITQSCYV-----DKLKGLAED--DGVTVVTIDDP----------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 182 kaqrgplPEGVLDFDTLIADCPADRLESgrAIHPDDVASYFHTGGTTGTPK---LAPHSHFNEVAMaEIMGLNAD--YGV 256
Cdd:PLN02246 154 -------PEGCLHFSELTQADENELPEV--EISPDDVVALPYSSGTTGLPKgvmLTHKGLVTSVAQ-QVDGENPNlyFHS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 257 DDVLLCGLPLFHV---NGVMVTGLapfHRGAQVLLAgpQGYRNPTLIQdfwkLVERYRVTSFSGVPTIYAALLQVPS-DG 332
Cdd:PLN02246 224 DDVILCVLPMFHIyslNSVLLCGL---RVGAAILIM--PKFEIGALLE----LIQRHKVTIAPFVPPIVLAIAKSPVvEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 333 RDLSSLRFALCGAAPMPVELIRQFEARTGLKVI-EGYGLTE-GTCGTSC-----NPRggERRPGSIGLRLPYCQVKVavL 405
Cdd:PLN02246 295 YDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEaGPVLAMClafakEPF--PVKSGSCGTVVRNAELKI--V 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 406 DGE-GNYLrdaAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIG-DGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDP 483
Cdd:PLN02246 371 DPEtGASL---PRNQPGEICIRGPQIMKGYLNDPEATANTIDkDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 484 QMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPERAAVpKDIWLIESMPVTAVGKTF 563
Cdd:PLN02246 448 AELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRI-HKVFFVDSIPKAPSGKIL 526
|
....*
gi 15599055 564 KPALR 568
Cdd:PLN02246 527 RKDLR 531
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
25-568 |
9.80e-64 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 219.89 E-value: 9.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTY----ELLQRSARRHGQRIALSCLlhGSAaeeplrISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTH 100
Cdd:PRK07059 16 EIDASQYpslaDLLEESFRQYADRPAFICM--GKA------ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 101 YVIWGGEAAG--IVNaINPLLEPEHIAELIRASNTRVLVTLAPFPGTdLWQKVA----------------GLRAQLPELy 162
Cdd:PRK07059 88 VAIAAVLRAGyvVVN-VNPLYTPRELEHQLKDSGAEAIVVLENFATT-VQQVLAktavkhvvvasmgdllGFKGHIVNF- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 163 aiVVVDPANLLPAPQrealkaqrgpLPeGVLDFDTLIADCPADRLESgRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEV 242
Cdd:PRK07059 165 --VVRRVKKMVPAWS----------LP-GHVRFNDALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 243 AMAEIMGL-----NADYGVDDVL--LCGLPLFHVNGVMVTGLAPFHRGAQVLLAGpqgyrNPTLIQDFWKLVERYRVTSF 315
Cdd:PRK07059 231 ANVLQMEAwlqpaFEKKPRPDQLnfVCALPLYHIFALTVCGLLGMRTGGRNILIP-----NPRDIPGFIKELKKYQVHIF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 316 SGVPTIYAALLQVPS-DGRDLSSLRFALCGAapMPVE--LIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIG 392
Cdd:PRK07059 306 PAVNTLYNALLNNPDfDKLDFSKLIVANGGG--MAVQrpVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 393 LRLPycQVKVAVLDGEGNylrDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSK 471
Cdd:PRK07059 384 LPLP--STEVSIRDDDGN---DLPLGEPGEICIRGPQVMAGYWNRpDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 472 DLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIqLKPGASASEEELLEHASRHVPERaAVPKDIWLI 551
Cdd:PRK07059 459 DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNY-KRPKFVEFR 536
|
570
....*....|....*..
gi 15599055 552 ESMPVTAVGKTFKPALR 568
Cdd:PRK07059 537 TELPKTNVGKILRRELR 553
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
81-586 |
1.29e-63 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 219.93 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 81 LGLESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLAPFPGTdLWQKVAGLRAQlp 159
Cdd:PRK08974 69 LGLKKGDRVALMMPNLLQYPIALFGILRAGmIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHT-LEKVVFKTPVK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 160 elyAIVVVDPANLLPAPQRE----ALKAQRGPLPEgvldFDTLIADCPADRLESGR-------AIHPDDVASYFHTGGTT 228
Cdd:PRK08974 146 ---HVILTRMGDQLSTAKGTlvnfVVKYIKRLVPK----YHLPDAISFRSALHKGRrmqyvkpELVPEDLAFLQYTGGTT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 229 GTPKLAPHSHFNEVAmaEIMGLNADYGV-----DDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAgpqgyRNPTLIQDF 303
Cdd:PRK08974 219 GVAKGAMLTHRNMLA--NLEQAKAAYGPllhpgKELVVTALPLYHIFALTVNCLLFIELGGQNLLI-----TNPRDIPGF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 304 WKLVERYRVTSFSGVPTIYAALLQVPSDGR-DLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPR 382
Cdd:PRK08974 292 VKELKKYPFTAITGVNTLFNALLNNEEFQElDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPY 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 383 GGERRPGSIGLRLPYCQVKVavLDGEGNylrDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDG 462
Cdd:PRK08974 372 DLDYYSGSIGLPVPSTEIKL--VDDDGN---EVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 463 YIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIqLKPGASASEEELLEHASRHVPERa 542
Cdd:PRK08974 447 FLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGY- 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15599055 543 AVPKDIWLIESMPVTAVGKTfkpalrldaIRRVLEEESRRIAED 586
Cdd:PRK08974 525 KVPKLVEFRDELPKSNVGKI---------LRRELRDEARAKVDN 559
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
62-570 |
6.58e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 217.34 E-value: 6.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLA 140
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGaIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 PFPGTdlwqkVAGLRAQLPELYAIVVVDpanllpapqrealkaqrGPLPEGVLDFDTLIAdcpadrlESGRAIHPDDV-- 218
Cdd:PRK07786 123 ALAPV-----ATAVRDIVPLLSTVVVAG-----------------GSSDDSVLGYEDLLA-------EAGPAHAPVDIpn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 219 ---ASYFHTGGTTGTPKLAPHSHFNEV--AMAEIMGLNADYGvDDVLLCGLPLFHVNGV--MVTGLApfhRGAQVLLAgP 291
Cdd:PRK07786 174 dspALIMYTSGTTGRPKGAVLTHANLTgqAMTCLRTNGADIN-SDVGFVGVPLFHIAGIgsMLPGLL---LGAPTVIY-P 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 292 QGYRNPTLIQDFWklvERYRVTSFSGVPTIYAALLQVP-SDGRDLSsLRFALCGAAPMPVELIRQF-EARTGLKVIEGYG 369
Cdd:PRK07786 249 LGAFDPGQLLDVL---EAEKVTGIFLVPAQWQAVCAEQqARPRDLA-LRVLSWGAAPASDTLLRQMaATFPEAQILAAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 370 LTEGTCGTsCNPRGGE--RRPGSIGLRLPYCQVKVavLDGEGNylrDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGD 447
Cdd:PRK07786 325 QTEMSPVT-CMLLGEDaiRKLGSVGKVIPTVAARV--VDENMN---DVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 448 GWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASE 527
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALT 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15599055 528 EELLEHASRHVPERAAVPKDIWLIESMPVTAVGKTFKPALRLD 570
Cdd:PRK07786 479 LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
150-568 |
1.08e-62 |
|
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: 214.29 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 150 KVAGLRAQLPELYAivvvdpaNLLPAPQreaLKAQRGPLpegvldFDTLIADCPADRLESGRA------------IHPDD 217
Cdd:cd05969 27 RVFVLSPRSPELYF-------SMLGIGK---IGAVICPL------FSAFGPEAIRDRLENSEAkvlitteelyerTDPED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 218 VASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGpqGYRNP 297
Cdd:cd05969 91 PTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE--GRFDA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 298 tliQDFWKLVERYRVTSFSGVPTIYAALLQV---PSDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGT 374
Cdd:cd05969 169 ---ESWYGIIERVKVTVWYTAPTAIRMLMKEgdeLARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 375 CGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGEGNYLRdaaPNEVGNLCLKG--PTVFKGYLQQDRNRDIWIGDGWFNT 452
Cdd:cd05969 246 SIMIANYPCMPIKPGSMGKPLP--GVKAAVVDENGNELP---PGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 453 GDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---E 529
Cdd:cd05969 321 GDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeE 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 15599055 530 LLEHASRHVPErAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05969 401 IINFVRQKLGA-HVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
62-562 |
1.10e-62 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 215.21 E-value: 1.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLA 140
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGaVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 PFPgtdlwqkvaglraqlPELYAIVVVDPANLLPAPQREAlkaqrgplpegvldfdTLIADcpadrlesgraIHPDDVAS 220
Cdd:PRK03640 108 DFE---------------AKLIPGISVKFAELMNGPKEEA----------------EIQEE-----------FDLDEVAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 221 YFHTGGTTGTPK---LAPHSHF-NEVAMAEIMGLNADygvdDVLLCGLPLFHVNG--VMVTGLApfhrgaqvllagpqgY 294
Cdd:PRK03640 146 IMYTSGTTGKPKgviQTYGNHWwSAVGSALNLGLTED----DCWLAAVPIFHISGlsILMRSVI---------------Y 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RNPTLIQDFW------KLVERYRVTSFSGVPTIYAALLQVPSDGRDLSSLRFALCGAAPMPVELIRQFEARtGLKVIEGY 368
Cdd:PRK03640 207 GMRVVLVEKFdaekinKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 369 GLTEgTCGTSC--NPRGGERRPGSIGLRLPYCQVKVAVlDGegnylRDAAPNEVGNLCLKGPTVFKGYL-QQDRNRDIwI 445
Cdd:PRK03640 286 GMTE-TASQIVtlSPEDALTKLGSAGKPLFPCELKIEK-DG-----VVVPPFEEGEIVVKGPNVTKGYLnREDATRET-F 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 446 GDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLkpGASA 525
Cdd:PRK03640 358 QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEV 435
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599055 526 SEEELLEHASrhvpERAA---VPKDIWLIESMPVTAVGKT 562
Cdd:PRK03640 436 TEEELRHFCE----EKLAkykVPKRFYFVEELPRNASGKL 471
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
31-576 |
1.74e-62 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 217.07 E-value: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARR-HGQRIALSCLlhgsAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAA 109
Cdd:PRK04319 46 YEAIDRHADGgRKDKVALRYL----DASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 110 GIVnaINPLLE---PEHIAELIRASNTRVLVTLApfpgtDLWQKVagLRAQLPELYAIVVVDpanllpapqrealkaQRG 186
Cdd:PRK04319 122 GAI--VGPLFEafmEEAVRDRLEDSEAKVLITTP-----ALLERK--PADDLPSLKHVLLVG---------------EDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 187 PLPEGVLDFDTLIADCPaDRLESgRAIHPDDVASYFHTGGTTGTPKLAPHSHfNEVAMAEIMGLNA-DYGVDDVLLC--- 262
Cdd:PRK04319 178 EEGPGTLDFNALMEQAS-DEFDI-EWTDREDGAILHYTSGSTGKPKGVLHVH-NAMLQHYQTGKYVlDLHEDDVYWCtad 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 263 -GlplfhvngvMVTG-----LAPFHRGAQVLLAGpqGYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQVPSD---GR 333
Cdd:PRK04319 255 pG---------WVTGtsygiFAPWLNGATNVIDG--GRFSP---ERWYRILEDYKVTVWYTAPTAIRMLMGAGDDlvkKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 334 DLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGEGNYLr 413
Cdd:PRK04319 321 DLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLP--GIEAAIVDDQGNEL- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 414 daAPNEVGNLCLKG--PTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALH 491
Cdd:PRK04319 398 --PPNRMGNLAIKKgwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 492 RHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---ELLEHASRHVPERAAvPKDIWLIESMPVTAVGKTfkpalr 568
Cdd:PRK04319 476 EHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAA-PREIEFKDKLPKTRSGKI------ 548
|
....*...
gi 15599055 569 ldaIRRVL 576
Cdd:PRK04319 549 ---MRRVL 553
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
214-579 |
1.66e-61 |
|
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: 211.30 E-value: 1.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPKLA--PHSHFNEVAMAEIMGLNADygVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGP 291
Cdd:cd05907 85 DPDDLATIIYTSGTTGRPKGVmlSHRNILSNALALAERLPAT--EGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 292 QgyrnPTLIQDFwklvERYRVTSFSGVPTIY------------AALLQVPSDGRDLSSLRFALCGAAPMPVELIRQFEAr 359
Cdd:cd05907 163 A----ETLLDDL----SEVRPTVFLAVPRVWekvyaaikvkavPGLKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRA- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 360 TGLKVIEGYGLTEgTCGTSCNPRGGERRPGSIGLRLPYCQVKVAvLDGEgnylrdaapnevgnLCLKGPTVFKGYLQQD- 438
Cdd:cd05907 234 LGIPVYEGYGLTE-TSAVVTLNPPGDNRIGTVGKPLPGVEVRIA-DDGE--------------ILVRGPNVMLGYYKNPe 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 439 RNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLII-RGGHNIDPQMIEEALHRHPAVALAAAVGkpDAKAGelPVAYI 517
Cdd:cd05907 298 ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG--DGRPF--LVALI 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599055 518 QLKPGASASEEELLEHASRHVPERAAVPKDIWLIESMpVTAVGKTFKPALRldaIRR--VLEEE 579
Cdd:cd05907 374 VPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAA-VEAANARLSRYEQ---IKKflLLPEP 433
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
33-568 |
7.10e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 211.87 E-value: 7.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 33 LLQRSARRHGQRIALSCLLHGSAAeeplRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV 112
Cdd:PRK07008 15 LIAHAARHAGDTEIVSRRVEGDIH----RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 113 -NAINPLLEPEHIAELIRASNTRVL---VTLAPFpgtdlwqkVAGLRAQLPELYAIVVVDPANLLPApqrealkaqrGPL 188
Cdd:PRK07008 91 cHTINPRLFPEQIAYIVNHAEDRYVlfdLTFLPL--------VDALAPQCPNVKGWVAMTDAAHLPA----------GST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 189 PegVLDFDTLIADCPAD----RLESGRAihpddvASYFHTGGTTGTPKLAPHSHFNEV------AMAEIMGLNADygvdD 258
Cdd:PRK07008 153 P--LLCYETLVGAQDGDydwpRFDENQA------SSLCYTSGTTGNPKGALYSHRSTVlhaygaALPDAMGLSAR----D 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 259 VLLCGLPLFHVNGVMVTGLAPFhRGAQVLLAGPQ--GyrnptliQDFWKLVERYRVTSFSGVPTIYAALLQ-VPSDGRDL 335
Cdd:PRK07008 221 AVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPGPDldG-------KSLYELIEAERVTFSAGVPTVWLGLLNhMREAGLRF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 SSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTE-GTCGTSCNPRGGE-RRPGSIGLRL------PYCQVKVAVLDG 407
Cdd:PRK07008 293 STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEmSPLGTLCKLKWKHsQLPLDEQRKLlekqgrVIYGVDMKIVGD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 408 EGNYLrdaaPNE---VGNLCLKGPTVFKGYLQQDRNRDIwigDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQ 484
Cdd:PRK07008 373 DGREL----PWDgkaFGDLQVRGPWVIDRYFRGDASPLV---DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 485 MIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFK 564
Cdd:PRK07008 446 DIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVA-KWWIPDDVVFVDAIPHTATGKLQK 524
|
....
gi 15599055 565 PALR 568
Cdd:PRK07008 525 LKLR 528
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
62-568 |
2.25e-60 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 210.89 E-value: 2.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQ-TANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG--IVNaINPLLEPEHIAELIRASNTRVLVT 138
Cdd:PRK08751 51 ITYREADQLVEQfAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGltVVN-VNPLYTPRELKHQLIDSGASVLVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 139 LAPFpGTDLWQKVAGLRAQlpelyAIVVVDPANLLPAPQRE----ALKAQRGPLPE----GVLDFDTLIADCPADRLeSG 210
Cdd:PRK08751 130 IDNF-GTTVQQVIADTPVK-----QVITTGLGDMLGFPKAAlvnfVVKYVKKLVPEyrinGAIRFREALALGRKHSM-PT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 211 RAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAE-----IMGLNADYGVDDVLLCGLPLFHVNGVMVTGLApFHR--G 283
Cdd:PRK08751 203 LQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqwLAGTGKLEEGCEVVITALPLYHIFALTANGLV-FMKigG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 284 AQVLLAgpqgyrNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGL 362
Cdd:PRK08751 282 CNHLIS------NPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 363 KVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQ-DRNR 441
Cdd:PRK08751 356 TLVEAYGLTETSPAACINPLTLKEYNGSIGLPIP--STDACIKDDAGTVL---AIGEIGELCIKGPQVMKGYWKRpEETA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 442 DIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELpVAYIQLKP 521
Cdd:PRK08751 431 KVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI-VKVVIVKK 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15599055 522 GASASEEELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK08751 510 DPALTAEDVKAHARANL-TGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
29-568 |
4.39e-60 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 210.45 E-value: 4.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 29 STYELLQRSARRHGQRIALSCLlhgsaaeePLRISYAEL------FARVTQtanalHRLGLESHQAVSFLLPNLPQTHYV 102
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAFSNL--------GVTLSYAELerhsaaFAAYLQ-----QHTDLVPGDRIAVQMPNVLQYPIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 103 IWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLAPFpgtdlwqkvaGLRAQlpELYAIVVVDpaNLLPAPQREAL 181
Cdd:PRK12492 92 VFGALRAGlIVVNTNPLYTAREMRHQFKDSGARALVYLNMF----------GKLVQ--EVLPDTGIE--YLIEAKMGDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 182 KAQRGPLPEGVLD----------FDTLIADCPADRLESGRAIHP-----DDVASYFHTGGTTGTPKLAPHSHFNEVA-MA 245
Cdd:PRK12492 158 PAAKGWLVNTVVDkvkkmvpayhLPQAVPFKQALRQGRGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVAnML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 246 EIMGLNADYGVD---------DVLLCGLPLFHVNG-------VMVTGlapfhrGAQVLLAgpqgyrNPTLIQDFWKLVER 309
Cdd:PRK12492 238 QVRACLSQLGPDgqplmkegqEVMIAPLPLYHIYAftancmcMMVSG------NHNVLIT------NPRDIPGFIKELGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 310 YRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRP 388
Cdd:PRK12492 306 WRFSALLGLNTLFVALMDHPGfKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 389 GSIGLRLPYCQVKVavLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWLT 467
Cdd:PRK12492 386 GTVGIPVPGTALKV--IDDDGNEL---PLGERGELCIKGPQVMKGYWQQpEATAEALDAEGWFKTGDIAVIDPDGFVRIV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 468 GRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGaSASEEELLEHASRHVPERaAVPKD 547
Cdd:PRK12492 461 DRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGY-KVPKH 538
|
570 580
....*....|....*....|.
gi 15599055 548 IWLIESMPVTAVGKTFKPALR 568
Cdd:PRK12492 539 IVLRDSLPMTPVGKILRRELR 559
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
194-568 |
5.99e-60 |
|
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: 206.56 E-value: 5.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 194 DFDTLIADC-PADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLP-LFHVNG 271
Cdd:cd05958 74 ELAYILDKArITVALCAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPpLAFTFG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 272 VMVTGLAPFHRGAQVLLAgPQgyRNPTLIQDfwkLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLRFALCGAAPMPV 350
Cdd:cd05958 154 LGGVLLFPFGVGASGVLL-EE--ATPDLLLS---AIARYKPTVLFTAPTAYRAMLAHPdAAGPDLSSLRKCVSAGEALPA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 351 ELIRQFEARTGLKVIEGYGLTEgTCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGEGNylrDAAPNEVGNLCLKGPTV 430
Cdd:cd05958 228 ALHRAWKEATGIPIIDGIGSTE-MFHIFISARPGDARPGATGKPVP--GYEAKVVDDEGN---PVPDGTIGRLAVRGPTG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 431 FKgYLQQDRNRDiWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAG 510
Cdd:cd05958 302 CR-YLADKRQRT-YVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRG 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599055 511 ELPVAYIQLKPGASASE---EELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05958 380 VVVKAFVVLRPGVIPGPvlaRELQDHAKAHIAPY-KYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
24-568 |
1.45e-59 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 208.45 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 24 RDLPSSTYELLQRSARRHGQRIALScllhgSAAEEPL-RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQtHYV 102
Cdd:PRK06018 6 QDWPLLCHRIIDHAARIHGNREVVT-----RSVEGPIvRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWR-HLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 103 IWGGeAAGI---VNAINPLLEPEHIAELIRASNTRVLVTLAPFpgTDLWQKVAGlraQLPELYAIVVVDPANLLPAPQRE 179
Cdd:PRK06018 80 AWYG-IMGIgaiCHTVNPRLFPEQIAWIINHAEDRVVITDLTF--VPILEKIAD---KLPSVERYVVLTDAAHMPQTTLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 180 ALKAqrgplpegvldFDTLIADCPADRleSGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVaMAEIMGLNAD---YGV 256
Cdd:PRK06018 154 NAVA-----------YEEWIAEADGDF--AWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNV-LHALMANNGDalgTSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 257 DDVLLCGLPLFHVNGVMVTGLAPfHRGAQVLLAGPQ--GyrnptliQDFWKLVERYRVTSFSGVPTIYAALLQ-VPSDGR 333
Cdd:PRK06018 220 ADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMPGAKldG-------ASVYELLDTEKVTFTAGVPTVWLMLLQyMEKEGL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 334 DLSSLRFALCGAAPMPVELIRQFEaRTGLKVIEGYGLTE----GTCGTScnPRGGERRPGSIGL-------RLPYcQVKV 402
Cdd:PRK06018 292 KLPHLKMVVCGGSAMPRSMIKAFE-DMGVEVRHAWGMTEmsplGTLAAL--KPPFSKLPGDARLdvlqkqgYPPF-GVEM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 403 AVLDGEGNYL-RDAapNEVGNLCLKGPTVFKGYLQQDRNrdIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNI 481
Cdd:PRK06018 368 KITDDAGKELpWDG--KTFGRLKVRGPAVAAAYYRVDGE--ILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 482 DPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGK 561
Cdd:PRK06018 444 SSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIA-KWWMPDDVAFVDAIPHTATGK 522
|
....*..
gi 15599055 562 TFKPALR 568
Cdd:PRK06018 523 ILKTALR 529
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
62-568 |
7.66e-58 |
|
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: 201.15 E-value: 7.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVNA-INPLLEPEHIAELIRASNTRVLVtla 140
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVvINPLLHPDDYAYIARDCEARLVV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 pfpgtdlwqkvaglraqlpelyaivvvdpanllpapqrealkaqrgplpegvldfdtliadcpadrlesgraIHPDDVAS 220
Cdd:cd05919 88 ------------------------------------------------------------------------TSADDIAY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 221 YFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNAdYGV--DDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAgpQGYRNPT 298
Cdd:cd05919 96 LLYSSGTTGPPKGVMHAHRDPLLFADAMAREA-LGLtpGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLN--PGWPTAE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 299 LIqdfWKLVERYRVTSFSGVPTIYAALLQVPSDGRD-LSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGT 377
Cdd:cd05919 173 RV---LATLARFRPTVLYGVPTFYANLLDSCAGSPDaLRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 378 SCNpRGGERRPGSIGLRLPYCQVKVavLDGEGNylrDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGR 457
Cdd:cd05919 250 LSN-RPGAWRLGSTGRPVPGYEIRL--VDEEGH---TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFC 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 458 IDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGaSASEEELLEHASRH 537
Cdd:cd05919 324 RDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSP-AAPQESLARDIHRH 402
|
490 500 510
....*....|....*....|....*....|....
gi 15599055 538 VPERAA---VPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05919 403 LLERLSahkVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
61-568 |
1.09e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 202.61 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIV-NAINPLLEPEHIAELIRASNTRVLVTl 139
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYyTCVNSHLTPAEAAYIVDDSGARALIT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 140 apfpGTDLWQKVAGLRAQLPELYAIVVVDPANLLPapqrealkaqrgplpeGVLDFDTLIADCPADRLesgraihPDDV- 218
Cdd:PRK13391 103 ----SAAKLDVARALLKQCPGVRHRLVLDGDGELE----------------GFVGYAEAVAGLPATPI-------ADESl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 219 -ASYFHTGGTTGTPK--LAPHSHFNEVAMAEIMG-LNADYGVDD--VLLCGLPLFHvngvmvtglapfhrgaqvllAGPQ 292
Cdd:PRK13391 156 gTDMLYSSGTTGRPKgiKRPLPEQPPDTPLPLTAfLQRLWGFRSdmVYLSPAPLYH--------------------SAPQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 GYRNPTL-------------IQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGR---DLSSLRFALCGAAPMPVELIRQF 356
Cdd:PRK13391 216 RAVMLVIrlggtvivmehfdAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRdkyDLSSLEVAIHAAAPCPPQVKEQM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 357 EARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLpycQVKVAVLDGEGnylRDAAPNEVGNLCLKGPTVFKgYLQ 436
Cdd:PRK13391 296 IDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAM---FGDLHILDDDG---AELPPGEPGTIWFEGGRPFE-YLN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 437 QD------RNRDiwigDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAG 510
Cdd:PRK13391 369 DPaktaeaRHPD----GTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLG 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599055 511 ELPVAYIQLKPGASASE---EELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK13391 445 EEVKAVVQPVDGVDPGPalaAELIAFCRQRL-SRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
38-568 |
4.95e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 197.98 E-value: 4.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 38 ARRHGQRIALSCllhGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYViWGGEA--AGIVNAI 115
Cdd:PRK08008 17 ADVYGHKTALIF---ESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFC-WFGLAkiGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 116 NPLLEPEHIAELIRASNTRVLVTLAPFPGtdLWQKVAGLRAQLPElyAIVVVDPANllpapqrealkaqrgPLPEGVLDF 195
Cdd:PRK08008 93 NARLLREESAWILQNSQASLLVTSAQFYP--MYRQIQQEDATPLR--HICLTRVAL---------------PADDGVSSF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 196 DTLIADCPADrLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFN----------EVAMAEimglnadygvDDVLLCGLP 265
Cdd:PRK08008 154 TQLKAQQPAT-LCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNlrfagyysawQCALRD----------DDVYLTVMP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 266 LFHVNGVMVTGLAPFHRGAQVLLAGPQGYRNptliqdFWKLVERYRVTSFSGVPTIYAAL-LQVPSDGRDLSSLR---FA 341
Cdd:PRK08008 223 AFHIDCQCTAAMAAFSAGATFVLLEKYSARA------FWGQVCKYRATITECIPMMIRTLmVQPPSANDRQHCLRevmFY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 342 LcgaaPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGlRLPYC-QVKVAVLDGegnylRDAAPNEV 420
Cdd:PRK08008 297 L----NLSDQEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIG-RPGFCyEAEIRDDHN-----RPLPAGEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 421 GNLCLKG---PTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAV 496
Cdd:PRK08008 367 GEICIKGvpgKTIFKEYYLDpKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKI 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599055 497 ALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK08008 447 QDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNM-AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
217-568 |
1.13e-55 |
|
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: 191.78 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 217 DVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVngvmvTGLAPFHRGaqvLLAGpqgyRN 296
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHV-----GGLAILVRS---LLAG----AE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 297 PTLIQDFWKLVER---YRVTSFSGVPTIYAALLQVPSDGRDLSSLRFALCGAAPMPVELIRQFEARtGLKVIEGYGLTEg 373
Cdd:cd17630 69 LVLLERNQALAEDlapPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTE- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 374 TCGTSCNPRGGERRPGSIGLRLPYCQVKVaVLDGEgnylrdaapnevgnLCLKGPTVFKGYLQQDRNRDIwIGDGWFNTG 453
Cdd:cd17630 147 TASQVATKRPDGFGRGGVGVLLPGRELRI-VEDGE--------------IWVGGASLAMGYLRGQLVPEF-NEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 454 DLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIqlKPGASASEEELLEH 533
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI--VGRGPADPAELRAW 288
|
330 340 350
....*....|....*....|....*....|....*
gi 15599055 534 ASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd17630 289 LKDKLA-RFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
217-564 |
1.24e-55 |
|
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: 191.95 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 217 DVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLlagPQGYRN 296
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVV---PVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 297 PTLIQdfwKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGLK-VIEGYGLTEGT 374
Cdd:cd17638 78 VDAIL---EAIERERITVLPGPPTLFQSLLDHPGrKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 375 CGTSCnprggerRPGSiglrlpyCQVKVAVLDGE---GNYLRDAAPNEVgnlCLKGPTVFKGYLQQDRNRDIWI-GDGWF 450
Cdd:cd17638 155 VATMC-------RPGD-------DAETVATTCGRacpGFEVRIADDGEV---LVRGYNVMQGYLDDPEATAEAIdADGWL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 451 NTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEEL 530
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDV 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 15599055 531 LEHASrhvpERAA---VPKDIWLIESMPVTAVGKTFK 564
Cdd:cd17638 298 IAWCR----ERLAnykVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
41-568 |
1.77e-55 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 197.76 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 41 HGQRIALSCLLHGSAAEEplrISYAELFARVTQTANALHR-LGLESHQAVSFLLPNlpQTHY-VIWGG--EAAGIVNAIN 116
Cdd:PLN02574 49 HHNHNGDTALIDSSTGFS---ISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPN--SVYFpVIFLAvlSLGGIVTTMN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 117 PLLEPEHIAELIRASNtrvlVTLApFPGTDLWQKVAGLRAQL---PELYAIVVVDPANllpAPQREALKAQRGPLPEGVl 193
Cdd:PLN02574 124 PSSSLGEIKKRVVDCS----VGLA-FTSPENVEKLSPLGVPVigvPENYDFDSKRIEF---PKFYELIKEDFDFVPKPV- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 194 dfdtliadcpadrlesgraIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIM-----GLNADYGVDDVLLCGLPLFH 268
Cdd:PLN02574 195 -------------------IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeaSQYEYPGSDNVYLAALPMFH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 269 VNGV--MVTGLAPFHRGAQVLLAGPQGyrnptliqDFWKLVERYRVTSFSGVPTIYAALLQV--PSDGRDLSSLRFALCG 344
Cdd:PLN02574 256 IYGLslFVVGLLSLGSTIVVMRRFDAS--------DMVKVIDRFKVTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 345 AAPMPVELIRQF-EARTGLKVIEGYGLTEGTC-GTSCNPRGGERRPGSIGLRLPYCQVKVAVLDgEGNYLrdaAPNEVGN 422
Cdd:PLN02574 328 AAPLSGKFIQDFvQTLPHVDFIQGYGMTESTAvGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWS-TGCLL---PPGNCGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 423 LCLKGPTVFKGYLQQDRNRDIWI-GDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAA 501
Cdd:PLN02574 404 LWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 502 VGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPERAAVPKDIwLIESMPVTAVGKTFKPALR 568
Cdd:PLN02574 484 TAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVV-FVQSIPKSPAGKILRRELK 549
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
32-567 |
3.39e-55 |
|
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: 194.85 E-value: 3.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGI 111
Cdd:cd05920 19 DLLARSAARHPDRIAVVD--------GDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 112 VnainPLLE-PEHiaeliRASNTRVLVTLApfpgtdlwqkvaglraqlpELYAIVVVDpanllpapqrealkaqRGPLPE 190
Cdd:cd05920 91 V----PVLAlPSH-----RRSELSAFCAHA-------------------EAVAYIVPD----------------RHAGFD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 191 GVLDFDTLIADCPadrlesgraihpdDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLNADygvdDVLLCGLPL 266
Cdd:cd05920 127 HRALARELAESIP-------------EVALFLLSGGTTGTPKLIPRTHndyaYNVRASAEVCGLDQD----TVYLAVLPA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 267 FHvnGVMVTG---LAPFHRGAQVLLAGPQgyrNPtliQDFWKLVERYRVTSFSGVPTIYAALLQ-VPSDGRDLSSLRFAL 342
Cdd:cd05920 190 AH--NFPLACpgvLGTLLAGGRVVLAPDP---SP---DAAFPLIEREGVTVTALVPALVSLWLDaAASRRADLSSLRLLQ 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 343 CGAAPMPVELIRQFEARTGLKVIEGYGLTEG-TCGTS--------CNPRGgerRPGSiglrlPYCQVKVAvlDGEGNylr 413
Cdd:cd05920 262 VGGARLSPALARRVPPVLGCTLQQVFGMAEGlLNYTRlddpdeviIHTQG---RPMS-----PDDEIRVV--DEEGN--- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 414 DAAPNEVGNLCLKGPTVFKGYLQ-QDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHR 492
Cdd:cd05920 329 PVPPGEEGELLTRGPYTIRGYYRaPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 493 HPAVALAAAVGKPDAKAGELPVAYIQLKPgASASEEELLEHASRHVPERAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd05920 409 HPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
215-562 |
9.24e-55 |
|
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: 194.09 E-value: 9.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLagpqgY 294
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF-----H 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPSDgRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGT 374
Cdd:cd05909 221 PNPLDYKKIPELIYDKKATILLGTPTFLRGYARAAHP-EDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 375 CGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGegnyLRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGD 454
Cdd:cd05909 300 PVISVNTPQSPNKEGTVGRPLPGMEVKIVSVET----HEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 455 LGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRH-PAVALAAAVGKPDAKAGElpvAYIQLKPGASASEEELLEH 533
Cdd:cd05909 376 IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDI 452
|
330 340
....*....|....*....|....*....
gi 15599055 534 ASRHVPERAAVPKDIWLIESMPVTAVGKT 562
Cdd:cd05909 453 LKNAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
214-570 |
2.37e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 192.51 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPKLAPHSHfNEVAmAEIMGLNADYG--VDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAG- 290
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKGVVLSR-RAIA-ADLDALAEAWQwtADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGr 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 291 --PQGYRNPTliqdfwklveRYRVTSFSGVPTIYAALLQVPSDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGY 368
Cdd:PRK07787 204 ptPEAYAQAL----------SEGGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 369 GLTEG--TCGTSCNprgGERRPGSIGLRLPycQVKVAVLDGEGNYLrDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWI 445
Cdd:PRK07787 274 GMTETliTLSTRAD---GERRPGWVGLPLA--GVETRLVDEDGGPV-PHDGETVGELQVRGPTLFDGYLNRpDATAAAFT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 446 GDGWFNTGDLGRIDEDGYIWLTGR-SKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQlkPGAS 524
Cdd:PRK07787 348 ADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADD 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15599055 525 ASEEELLEHASRH--VPERaavPKDIWLIESMPVTAVGKTFKPALRLD 570
Cdd:PRK07787 426 VAADELIDFVAQQlsVHKR---PREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-568 |
3.56e-54 |
|
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: 191.50 E-value: 3.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 69 ARVTQTANALHRLGLESHQAVSFLLPN----LPQTHYVIWGGEAAGIVNA-INPLLEPEHIaelirasntRVLVTLApfp 143
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNrftyIELSFAVAYAGGRLGLVFVpLNPTLKESVL---------RYLVADA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 144 gtdlwqkvaGLRaqlpelyaIVVVDPanllPAPQREALKAQRGPLPEGVLDFDTLIAdcpADRLESGRAIHPDDVASYFH 223
Cdd:cd05922 69 ---------GGR--------IVLADA----GAADRLRDALPASPDPGTVLDADGIRA---ARASAPAHEVSHEDLALLLY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 224 TGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTgLAPFHRGAQVLLAGpqGYRNPtliQDF 303
Cdd:cd05922 125 TSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVL-NTHLLRGATLVLTN--DGVLD---DAF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 304 WKLVERYRVTSFSGVPTIYAALLQVPSDGRDLSSLRFALCGAAPMPVELIRQF-EARTGLKVIEGYGLTEGTCG-TSCNP 381
Cdd:cd05922 199 WEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLrELLPGAQVYVMYGQTEATRRmTYLPP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 382 RGGERRPGSIGLRLPYCqvKVAVLDGEGNylrDAAPNEVGNLCLKGPTVFKGYLQQDRNR-DIWIGDGWFNTGDLGRIDE 460
Cdd:cd05922 279 ERILEKPGSIGLAIPGG--EFEILDDDGT---PTPPGEPGEIVHRGPNVMKGYWNDPPYRrKEGRGGGVLHTGDLARRDE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 461 DGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAkAGELPVAYIQLKPGASASEeellehASRHVPE 540
Cdd:cd05922 354 DGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDPKD------VLRSLAE 426
|
490 500 510
....*....|....*....|....*....|.
gi 15599055 541 R---AAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05922 427 RlppYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
61-568 |
5.32e-54 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 192.61 E-value: 5.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPN----LPQTHYVIWGGEAAGIVNAINpllEPEHIAELIRASNTRVL 136
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNdfafFEAAYAAMRLGAYAVPVNWHF---KPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 137 VTLApfpgtDLWqkvAGLRAQLPELYAIVVVD-PANLLpapQREALKAQRGPLPEGVLDFDTLIADCPAdrLESGRAIHP 215
Cdd:PRK12406 88 IAHA-----DLL---HGLASALPAGVTVLSVPtPPEIA---AAYRISPALLTPPAGAIDWEGWLAQQEP--YDGPPVPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 ddvASYFHTGGTTGTPKLAPHSHFN-EVAMAEIMGLNADYGV--DDVLLCGLPLFHvNGVMVTGLAPFHRGAQVLLagpQ 292
Cdd:PRK12406 155 ---QSMIYTSGTTGHPKGVRRAAPTpEQAAAAEQMRALIYGLkpGIRALLTGPLYH-SAPNAYGLRAGRLGGVLVL---Q 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 GYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGR---DLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYG 369
Cdd:PRK12406 228 PRFDP---EELLQLIERHRITHMHMVPTMFIRLLKLPEEVRakyDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 370 LTEGTCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGEGNYLrdaAPNEVGNLCLKGPTV--FKgYLQQDRNRDIWIGD 447
Cdd:PRK12406 305 STESGAVTFATSEDALSHPGTVGKAAP--GAELRFVDEDGRPL---PQGEIGEIYSRIAGNpdFT-YHNKPEKRAEIDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 448 GWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASE 527
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15599055 528 EELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK12406 459 ADIRAQLKARL-AGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
62-568 |
3.58e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 190.10 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVN-AINPLLEPEHIAELIRASNTRVLVTLA 140
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFlPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 PFpgtdlwQKVAGLRAQlpelyaIVVVDPAnllpapqrealkAQRgplpegvldfDTLIADCPADRLESGRAIHPDDVAS 220
Cdd:PRK06145 108 EF------DAIVALETP------KIVIDAA------------AQA----------DSRRLAQGGLEIPPQAAVAPTDLVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 221 YFHTGGTTGTPKLAPHS----HFNEVAMAEIMGLNADygvDDVLLCGlPLFHVNGVMVTGLAPFHRGAQVLLagpqgYRN 296
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSygnlHWKSIDHVIALGLTAS---ERLLVVG-PLYHVGAFDLPGIAVLWVGGTLRI-----HRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 297 --PtliQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGR-DLSSLRFALCGAAPMPVELIRQF-EARTGLKVIEGYGLTE 372
Cdd:PRK06145 225 fdP---EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRfDLDSLAWCIGGGEKTPESRIRDFtRVFTRARYIDAYGLTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 GTCGTSCNPRGGE-RRPGSIGLRLPYcqVKVAVLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFN 451
Cdd:PRK06145 302 TCSGDTLMEAGREiEKIGSTGRALAH--VEIRIADGAGRWL---PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 452 TGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELl 531
Cdd:PRK06145 377 SGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEAL- 455
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599055 532 ehaSRHVPERAA---VPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK06145 456 ---DRHCRQRLAsfkVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
223-561 |
7.55e-53 |
|
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: 184.40 E-value: 7.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 223 HTGGTTGTPKLAPHSHFNEVAMAeiMGLNADYGVD--DVLLCGLPLFHVNGvMVTGLAPFHRGAQVLLAG---PQgyrnp 297
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAAN--LQLIHAMGLTeaDVYLNMLPLFHIAG-LNLALATFHAGGANVVMEkfdPA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 298 tliqDFWKLVERYRVTSFSGVPTIYAALL-QVPSDGRDLSSLRFALCGAAPmpvELIRQFEARTGLKVIEGYGLTEGTCG 376
Cdd:cd17637 79 ----EALELIEEEKVTLMGSFPPILSNLLdAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 377 TSCNPrgGERRPGSIGLRLPYCQVKVAvlDGEGnylRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLG 456
Cdd:cd17637 152 VTLSP--YRERPGSAGRPGPLVRVRIV--DDND---RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 457 RIDEDGYIWLTGRS--KDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEha 534
Cdd:cd17637 225 RFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIE-- 302
|
330 340 350
....*....|....*....|....*....|
gi 15599055 535 srHVPERAA---VPKDIWLIESMPVTAVGK 561
Cdd:cd17637 303 --FVGSRIArykKPRYVVFVEALPKTADGS 330
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
31-568 |
7.31e-52 |
|
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: 187.32 E-value: 7.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALsclLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG 110
Cdd:cd05970 20 YDVVDAMAKEYPDKLAL---VWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 -IVNAINPLLEPEHIAELIRASNTRVLVTLApfpGTDLWQKVAGLRAQLPELYAIVVVDpanllpapqrealkaqrGPLP 189
Cdd:cd05970 97 aIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIEKAAPECPSKPKLVWVG-----------------DPVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 190 EGVLDFDTLIADCPAD--RLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHfnEVAMAEImgLNADYGvDDVLLCGLPLf 267
Cdd:cd05970 157 EGWIDFRKLIKNASPDfeRPTANSYPCGEDILLVYFSSGTTGMPKMVEHDF--TYPLGHI--VTAKYW-QNVREGGLHL- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 268 hvnGVMVTGLAPFHRG---AQvLLAGPQgyrnpTLIQDFWKL--------VERYRVTSFSGVPTIYAALLQVPSDGRDLS 336
Cdd:cd05970 231 ---TVADTGWGKAVWGkiyGQ-WIAGAA-----VFVYDYDKFdpkallekLSKYGVTTFCAPPTIYRFLIREDLSRYDLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 337 SLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPrGGERRPGSIGLRLPycQVKVAVLDGEGnylRDAA 416
Cdd:cd05970 302 SLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFP-WMEPKPGSMGKPAP--GYEIDLIDREG---RSCE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 417 PNEVGNLCL---KGPTV--FKGYLQ-QDRNRDIWiGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEAL 490
Cdd:cd05970 376 AGEEGEIVIrtsKGKPVglFGGYYKdAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 491 HRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---ELLEHASRhVPERAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd05970 455 IQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKK-VTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
.
gi 15599055 568 R 568
Cdd:cd05970 534 R 534
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
20-568 |
1.64e-51 |
|
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: 186.19 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 20 PLEQRDLPSSTYELLQRSARRHGqRIALScllhgsAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQT 99
Cdd:cd17642 10 PLEDGTAGEQLHKAMKRYASVPG-TIAFT------DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 100 HYVIWGGEAAGIVNAinPLLEPEHIAELIRA---SNTRVLvtlapFPGTDLWQKVAGLRAQLPELYAIVVVDPANLLPAP 176
Cdd:cd17642 83 FLPVIAGLFIGVGVA--PTNDIYNERELDHSlniSKPTIV-----FCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 177 QR-EALKAQRGPLPEGVLDFDTLIADcpadrlesgraiHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAE-----IMGL 250
Cdd:cd17642 156 QClYTFITQNLPPGFNEYDFKPPSFD------------RDEQVALIMNSSGSTGLPKGVQLTHKNIVARFShardpIFGN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 251 NADYGVddVLLCGLPLFHVNGvMVTGLAPFHRGAQVLLAgpqgyrnPTLIQD-FWKLVERYRVTSFSGVPTIYAALLQVP 329
Cdd:cd17642 224 QIIPDT--AILTVIPFHHGFG-MFTTLGYLICGFRVVLM-------YKFEEElFLRSLQDYKVQSALLVPTLFAFFAKST 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 330 -SDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVI-EGYGLTEGTCGTSCNPRGgERRPGSIGLRLPYCQVKVAVLDg 407
Cdd:cd17642 294 lVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEG-DDKPGAVGKVVPFFYAKVVDLD- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 408 EGNYLrdaAPNEVGNLCLKGPTVFKGYLQQDR-NRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMI 486
Cdd:cd17642 372 TGKTL---GPNERGELCVKGPMIMKGYVNNPEaTKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAEL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 487 EEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPERAAVPKDIWLIESMPVTAVGKTFKPA 566
Cdd:cd17642 449 ESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRK 528
|
..
gi 15599055 567 LR 568
Cdd:cd17642 529 IR 530
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
155-568 |
2.66e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 184.63 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 155 RAQLPELYAIVV-VDPANLLPAPQREALKAQrgplpegVLDFDTLIADCPADRLESGRAIHPDDVASYFHTGGTTGTPKL 233
Cdd:PRK09088 80 RLSASELDALLQdAEPRLLLGDDAVAAGRTD-------VEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 234 APHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGvMVTGLAP--FHRGAQVLLAGPQGYR------NPTLiqdfwk 305
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIG-LITSVRPvlAVGGSILVSNGFEPKRtlgrlgDPAL------ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 306 lveryRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARtGLKVIEGYGLTE-GTC-GTSCNPR 382
Cdd:PRK09088 226 -----GITHYFCVPQMAQAFRAQPGfDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEaGTVfGMSVDCD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 383 GGERRPGSIGLRLPYCQVKVavLDGEGNylrDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDED 461
Cdd:PRK09088 300 VIRAKAGAAGIPTPTVQTRV--VDDQGN---DCPAGVPGELLLRGPNLSPGYWRRpQATARAFTGDGWFRTGDIARRDAD 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 462 GYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeR 541
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLA-K 453
|
410 420
....*....|....*....|....*..
gi 15599055 542 AAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK09088 454 YKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
215-568 |
6.81e-51 |
|
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: 182.96 E-value: 6.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASY---FHTGGTTGTPK--LAPHSHFNEVAMAEIM-GLNADYGVDDVLLCGLPLFHVngvmvtglAPFHRGAQVLL 288
Cdd:cd05929 121 IEDEAAGwkmLYSGGTTGRPKgiKRGLPGGPPDNDTLMAaALGFGPGADSVYLSPAPLYHA--------APFRWSMTALF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 289 AGPqgyrnpTLI-------QDFWKLVERYRVTSFSGVPTIYAALLQVPSDGR---DLSSLRFALCGAAPMPVELIRQFEA 358
Cdd:cd05929 193 MGG------TLVlmekfdpEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRnayDLSSLKRVIHAAAPCPPWVKEQWID 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 359 RTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLpycQVKVAVLDGEGNylrDAAPNEVGNLCLKGP---TVFKGYL 435
Cdd:cd05929 267 WGGPIIWEYYGGTEGQGLTIINGEEWLTHPGSVGRAV---LGKVHILDEDGN---EVPPGEIGEVYFANGpgfEYTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 436 QQDRNRDiwiGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVA 515
Cdd:cd05929 341 KTAAARN---EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599055 516 YIQLKPGASASE---EELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05929 418 VVQPAPGADAGTalaEELIAFLRDRL-SRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
27-564 |
4.06e-50 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 183.54 E-value: 4.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 27 PSSTYEL---LQRSARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQThYVI 103
Cdd:PRK08279 33 PDSKRSLgdvFEEAAARHPDRPAL--------LFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEY-LAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 104 WGGEA--AGIVNAINPLLEPEHIAELIRASNTRVLVTlapfpGTDLWQKVAGLRAQLPELYAIVVVDPANLLPapqreal 181
Cdd:PRK08279 104 WLGLAklGAVVALLNTQQRGAVLAHSLNLVDAKHLIV-----GEELVEAFEEARADLARPPRLWVAGGDTLDD------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 182 kaqrgplPEGVLDFDTLIADCPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLL 261
Cdd:PRK08279 172 -------PEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 262 CGLPLFHVNGVMVtglAPfhrgAQVLLAGpqgyrnPTLI-------QDFWKLVERYRVTSFSGVPTIYAALLQVPSDGRD 334
Cdd:PRK08279 245 CCLPLYHNTGGTV---AW----SSVLAAG------ATLAlrrkfsaSRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 335 LS-SLRFAlCGAAPMPvELIRQFEARTGL-KVIEGYGLTEGTCGTsCNPRGgerRPGSIG-----LRLPYCQVKVAVLDG 407
Cdd:PRK08279 312 RDhRLRLM-IGNGLRP-DIWDEFQQRFGIpRILEFYAASEGNVGF-INVFN---FDGTVGrvplwLAHPYAIVKYDVDTG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 408 EgnYLRDA-------APNEVGnLCL-----KGPtvFKGYLQQDRN-----RDIWI-GDGWFNTGDLGRIDEDGYIWLTGR 469
Cdd:PRK08279 386 E--PVRDAdgrcikvKPGEVG-LLIgritdRGP--FDGYTDPEASekkilRDVFKkGDAWFNTGDLMRDDGFGHAQFVDR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 470 SKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKP----DAKAGelpVAYIQLKPGASASEEELLEHASRHVPeRAAVP 545
Cdd:PRK08279 461 LGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgtDGRAG---MAAIVLADGAEFDLAALAAHLYERLP-AYAVP 536
|
570
....*....|....*....
gi 15599055 546 KDIWLIESMPVTAvgkTFK 564
Cdd:PRK08279 537 LFVRLVPELETTG---TFK 552
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-561 |
1.11e-49 |
|
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: 182.01 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALscLLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQT----------- 99
Cdd:cd17634 56 ANALDRHLRENGDRTAI--IYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAavamlacarig 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 100 --HYVIWGGEAagivnainpllePEHIAELIRASNTRVLVTLAPF--PG--TDLWQKVA-GLRAQLPELYAIVVVDpanl 172
Cdd:cd17634 134 avHSVIFGGFA------------PEAVAGRIIDSSSRLLITADGGvrAGrsVPLKKNVDdALNPNVTSVEHVIVLK---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 173 lpapqREALKAQRGPLPEgvLDFDTLIADCPADrlESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFN-EVAMAEIMGLN 251
Cdd:cd17634 198 -----RTGSDIDWQEGRD--LWWRDLIAKASPE--HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 252 ADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAgpQGYRNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPSD 331
Cdd:cd17634 269 FDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLY--EGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 332 ---GRDLSSLRFALCGAAPMPVELIRQFEARTGLK---VIEGYGLTEgTCGTSCNPRggerrPGSIGLRL-----PYCQV 400
Cdd:cd17634 347 aieGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTE-TGGFMITPL-----PGAIELKAgsatrPVFGV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 401 KVAVLDGEGNylrDAAPNEVGNLCLKGP---TVFKGYLQQDRNRDIWIG--DGWFNTGDLGRIDEDGYIWLTGRSKDLII 475
Cdd:cd17634 421 QPAVVDNEGH---PQPGGTEGNLVITDPwpgQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVIN 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 476 RGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---ELLEHASRHVpERAAVPKDIWLIE 552
Cdd:cd17634 498 VAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEI-GPLATPDVVHWVD 576
|
....*....
gi 15599055 553 SMPVTAVGK 561
Cdd:cd17634 577 SLPKTRSGK 585
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
15-568 |
2.00e-48 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 177.64 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 15 ALERVPLEQRDLPSstyeLLQRSARRHGQRIALScllhgsAAEEplRISYAELFARVTQTANALHRLGLESHQAVSFLLP 94
Cdd:PRK06155 12 AVDPLPPSERTLPA----MLARQAERYPDRPLLV------FGGT--RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 95 NLPQTHYVIWG-GEAAGIVNAINPLLEPEHIAELIRASNTRVLVTLAPFpgTDLWQKVAGLRAQLPELYaIVVVDPANLL 173
Cdd:PRK06155 80 NRIEFLDVFLGcAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL--LAALEAADPGDLPLPAVW-LLDAPASVSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 174 PAPQREAlkaqrgPLPegvldfdtliadcPADRLESGRAIHPDDVASYFHTGGTTGTPK--LAPHSHFN--EVAMAEIMG 249
Cdd:PRK06155 157 PAGWSTA------PLP-------------PLDAPAPAAAVQPGDTAAILYTSGTTGPSKgvCCPHAQFYwwGRNSAEDLE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 250 LnadyGVDDVLLCGLPLFHVNGvmvtgLAPFhrgAQVLLAGPQGYRNPTL-IQDFWKLVERYRVTSFSGVPTIYAALLQV 328
Cdd:PRK06155 218 I----GADDVLYTTLPLFHTNA-----LNAF---FQALLAGATYVLEPRFsASGFWPAVRRHGATVTYLLGAMVSILLSQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 329 PSDGRD-LSSLRFALCGAapMPVELIRQFEARTGLKVIEGYGLTEGTcgTSCNPRGGERRPGSIGLRLPYCQVKVAvlDG 407
Cdd:PRK06155 286 PARESDrAHRVRVALGPG--VPAALHAAFRERFGVDLLDGYGSTETN--FVIAVTHGSQRPGSMGRLAPGFEARVV--DE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 408 EGNylrDAAPNEVGNLCLKG--PTVF-KGYLQQ-DRNRDIWiGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDP 483
Cdd:PRK06155 360 HDQ---ELPDGEPGELLLRAdePFAFaTGYFGMpEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISS 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 484 QMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTF 563
Cdd:PRK06155 436 FEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLA-YFAVPRYVEFVAALPKTENGKVQ 514
|
....*
gi 15599055 564 KPALR 568
Cdd:PRK06155 515 KFVLR 519
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
40-568 |
3.32e-48 |
|
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: 178.66 E-value: 3.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 40 RH-----GQRIALsclLHGSAAEEPLR-ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHY------------ 101
Cdd:cd05967 58 RHveagrGDQIAL---IYDSPVTGTERtYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIamlacarigaih 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 102 -VIWGGEAAgivnainpllepEHIAELIRASNTRVLVTlAPF---PGtdlwqKVAGLRAQLPELYAIVVVDPANLLpAPQ 177
Cdd:cd05967 135 sVVFGGFAA------------KELASRIDDAKPKLIVT-ASCgiePG-----KVVPYKPLLDKALELSGHKPHHVL-VLN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 178 REALKAQRGPlPEGVLDFDTLIADC-PAD--RLESGraiHPddvaSY-FHTGGTTGTPK-----LAPHSHFNEVAMAEIM 248
Cdd:cd05967 196 RPQVPADLTK-PGRDLDWSELLAKAePVDcvPVAAT---DP----LYiLYTSGTTGKPKgvvrdNGGHAVALNWSMRNIY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 249 GLNADygvdDVLLCGLPLFHVNGVMVTGLAPFHRGA-QVLLAGpqgyrNPTLIQD---FWKLVERYRVTSFSGVPTIYAA 324
Cdd:cd05967 268 GIKPG----DVWWAASDVGWVVGHSYIVYGPLLHGAtTVLYEG-----KPVGTPDpgaFWRVIEKYQVNALFTAPTAIRA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 325 LLQVPSDGR-----DLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGER---RPGSIGLRLP 396
Cdd:cd05967 339 IRKEDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPlpiKAGSPGKPVP 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 397 YCQVKVavLDGEGNYLrdaAPNEVGNLCLKGP----TVFKGYLQQDRNRDIWIGD--GWFNTGDLGRIDEDGYIWLTGRS 470
Cdd:cd05967 419 GYQVQV--LDEDGEPV---GPNELGNIVIKLPlppgCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRT 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 471 KDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPER---AAVPKD 547
Cdd:cd05967 494 DDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQigpVAAFRL 573
|
570 580
....*....|....*....|.
gi 15599055 548 IWLIESMPVTAVGKTFKPALR 568
Cdd:cd05967 574 VIFVKRLPKTRSGKILRRTLR 594
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
31-567 |
3.47e-48 |
|
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: 176.16 E-value: 3.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALScllhgsAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG 110
Cdd:cd05923 4 FEMLRRAASRAPDACAIA------DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 IVNA-INPLLEPEHIAELIRASntrvlvtlapfpgtdlwqkvaglraqlpELYAIVVVDPANLLPApqrealKAQRGPLP 189
Cdd:cd05923 78 AVPAlINPRLKAAELAELIERG----------------------------EMTAAVIAVDAQVMDA------IFQSGVRV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 190 EGVLDFDTLIADCPADRLESGRAIHPDDVASYFHTGGTTGTPKLA--PHSHFNE--VAMAEIMGLNadYGVDDVLLCGLP 265
Cdd:cd05923 124 LALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAviPQRAAESrvLFMSTQAGLR--HGRHNVVLGLMP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 266 LFHVNGVMVTGLAPfhrgaqvlLAGPQGYRNPTLI--QDFWKLVERYRVTSFSGVPTIYAALL-QVPSDGRDLSSLRFAL 342
Cdd:cd05923 202 LYHVIGFFAVLVAA--------LALDGTYVVVEEFdpADALKLIEQERVTSLFATPTHLDALAaAAEFAGLKLSSLRHVT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 343 CGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGT-SCNPRGGER-RPGSiglrlpYCQVKVAVLDGEGNYLrdAAPNEV 420
Cdd:cd05923 274 FAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLyMRDARTGTEmRPGF------FSEVRIVRIGGSPDEA--LANGEE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 421 GNLCLK--GPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVAL 498
Cdd:cd05923 346 GELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTE 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 499 AAAVGKPDAKAGELPVAYIQLKPGaSASEEEL------LEHASRHVPERAAVpkdiwlIESMPVTAVGKTFKPAL 567
Cdd:cd05923 426 VVVIGVADERWGQSVTACVVPREG-TLSADELdqfcraSELADFKRPRRYFF------LDELPKNAMNKVLRRQL 493
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
39-568 |
3.61e-48 |
|
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: 176.89 E-value: 3.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 39 RRHGQRIALSCL--LHGSAAEepLRISYAELFARVTQTANALHRL-GLESHQAVSFLLPNLPQTHYVIWGGEAAGIVnaI 115
Cdd:cd05928 19 EKAGKRPPNPALwwVNGKGDE--VKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 116 NP---LLEPEHIAELIRASNTRVLVTlapfpGTDLWQKVAGLRAQLPELYAivvvdpaNLLPAPQREalkaqrgplpEGV 192
Cdd:cd05928 95 IPgtiQLTAKDILYRLQASKAKCIVT-----SDELAPEVDSVASECPSLKT-------KLLVSEKSR----------DGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 193 LDFDTLIADCPADR--LESGraiHPDDVASYFhTGGTTGTPKLAPHSHfneVAMAEIMGLNADYGVD----DVLLCGLPL 266
Cdd:cd05928 153 LNFKELLNEASTEHhcVETG---SQEPMAIYF-TSGTTGSPKMAEHSH---SSLGLGLKVNGRYWLDltasDIMWNTSDT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 267 FHVNGVMVTGLAPFHRGAQVLLAGPQGYRNPTLIQDFWKlverYRVTSFSGVPTIYAALLQvpsdgRDLSSLRF-----A 341
Cdd:cd05928 226 GWIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSS----YPITTFCGAPTVYRMLVQ-----QDLSSYKFpslqhC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 342 LCGAAPMPVELIRQFEARTGLKVIEGYGLTEG--TCGtscNPRGGERRPGSIGLRLPYCQVKVavLDGEGNYLrdaAPNE 419
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETglICA---NFKGMKIKPGSMGKASPPYDVQI--IDDNGNVL---PPGT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 420 VGNLCLK-GPT----VFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHP 494
Cdd:cd05928 369 EGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHP 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599055 495 AVALAAAVGKPDAKAGELPVAYIQLKPG-ASASEEELLEHASRHVPERAA---VPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05928 449 AVVESAVVSSPDPIRGEVVKAFVVLAPQfLSHDPEQLTKELQQHVKSVTApykYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
62-568 |
1.50e-47 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 175.55 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLVTla 140
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGgVFSGANPTALESEIKKQAEAAGAKLIVT-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 pfpgTDL-WQKVAGLraqlpELYAIVVVDPANLLPAPQREALKAqrgplpegvldfdtliADCPADRLESgRAIHPDDVA 219
Cdd:PLN02330 134 ----NDTnYGKVKGL-----GLPVIVLGEEKIEGAVNWKELLEA----------------ADRAGDTSDN-EEILQTDLC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 220 SYFHTGGTTGTPKLAPHSHFNEVA--MAEIMGLNADYgVDDVLLCGL-PLFHVNGVMVTGLAPFHRGAQVLLAGPQGYRN 296
Cdd:PLN02330 188 ALPFSSGTTGISKGVMLTHRNLVAnlCSSLFSVGPEM-IGQVVTLGLiPFFHIYGITGICCATLRNKGKVVVMSRFELRT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 297 ptliqdFWKLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLRF--ALCGAAPMPVELIRQFEAR-TGLKVIEGYGLTE 372
Cdd:PLN02330 267 ------FLNALITQEVSFAPIVPPIILNLVKNPiVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 GTCGTSC--NPRGGE--RRPGSIGLRLPYCQVKVavLDGEGNylRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWI-GD 447
Cdd:PLN02330 341 HSCITLThgDPEKGHgiAKKNSVGFILPNLEVKF--IDPDTG--RSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 448 GWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASE 527
Cdd:PLN02330 417 GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15599055 528 EELLEHASRHVPERAAVpKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PLN02330 497 EDILNFVAANVAHYKKV-RVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
22-579 |
5.76e-47 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 174.44 E-value: 5.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 22 EQRDLPSSTYELLQRSARRHGQRialSCLLHGSAaeeplRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLP---Q 98
Cdd:PLN03102 8 EANNVPLTPITFLKRASECYPNR---TSIIYGKT-----RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPamyE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 99 THYVIwgGEAAGIVNAINPLLEPEHIAELIRASNTRVLVTLAPFpgTDLWQKVAGLRAQL---PELYAIVVvdpaNLLPA 175
Cdd:PLN03102 80 MHFAV--PMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSF--EPLAREVLHLLSSEdsnLNLPVIFI----HEIDF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 176 PQREALKAqrgplpegvLDFDTLIADCPADRLESGRA--IHPD-DVASYFHTGGTTGTPKLAPHSHFNEV--AMAEIMGL 250
Cdd:PLN03102 152 PKRPSSEE---------LDYECLIQRGEPTPSLVARMfrIQDEhDPISLNYTSGTTADPKGVVISHRGAYlsTLSAIIGW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 251 naDYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLL---AGPQGYRNptliqdfwklVERYRVTSFSGVPTIYAALLQ 327
Cdd:PLN03102 223 --EMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMrhvTAPEIYKN----------IEMHNVTHMCCVPTVFNILLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 328 VPS-DGRDLSSLRFALCGAAPMPVELIRQFEaRTGLKVIEGYGLTEGTCGT-SCN-----PRGGERRPGSIGLRLPYCQV 400
Cdd:PLN03102 291 GNSlDLSPRSGPVHVLTGGSPPPAALVKKVQ-RLGFQVMHAYGLTEATGPVlFCEwqdewNRLPENQQMELKARQGVSIL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 401 KVAVLDGEGNYLRDAAPNE---VGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRG 477
Cdd:PLN03102 370 GLADVDVKNKETQESVPRDgktMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 478 GHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGAS----------ASEEELLEHASRHVPErAAVPKD 547
Cdd:PLN03102 450 GENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPH-FMCPRK 528
|
570 580 590
....*....|....*....|....*....|..
gi 15599055 548 IWLIESMPVTAVGKTFKPALRLDAIRRVLEEE 579
Cdd:PLN03102 529 VVFLQELPKNGNGKILKPKLRDIAKGLVVEDE 560
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
61-567 |
5.96e-47 |
|
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: 171.56 E-value: 5.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPnlPQTHYVIwggeaA--GIVNA------INPLLEPEHIAELIRASN 132
Cdd:cd05930 12 SLTYAELDARANRLARYLRERGVGPGDLVAVLLE--RSLEMVV-----AilAVLKAgaayvpLDPSYPAERLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 133 TRVLVTlapfpgtdlwqkvaglraqlpelyaivvvdpanllpapqrealkaqrgplpegvldfdtliadcpadrlesgra 212
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 213 iHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTgLAPFHRGAQVLLAGPQ 292
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLVVLPEE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 GYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQVPSDgRDLSSLRFALCGAAPMPVELIRQF-EARTGLKVIEGYGLT 371
Cdd:cd05930 169 VRKDP---EALADLLAEEGITVLHLTPSLLRLLLQELEL-AALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 372 EGTCGTS---CNPRGGERRPGSIGLRLPycQVKVAVLDGEgnyLRDAAPNEVGNLCLKGPTVFKGYLQQDRN------RD 442
Cdd:cd05930 245 EATVDATyyrVPPDDEEDGRVPIGRPIP--NTRVYVLDEN---LRPVPPGVPGELYIGGAGLARGYLNRPELtaerfvPN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 443 IWIGDGW-FNTGDLGRIDEDGYIWLTGRSKDLI-IRGgHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLK 520
Cdd:cd05930 320 PFGPGERmYRTGDLVRWLPDGNLEFLGRIDDQVkIRG-YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPD 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15599055 521 PGASASEEELLEHASRHVPErAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd05930 399 EGGELDEEELRAHLAERLPD-YMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
25-568 |
1.22e-46 |
|
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: 172.85 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTYELLQRSARRHGQRIalscLLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIW 104
Cdd:cd05906 7 GAPRTLLELLLRAAERGPTKG----ITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 105 GGEAAGIVNAINPllepehIAELIRASNTRVlvtlapfpgtdlwQKVAGLRAQLPElyAIVVVDPANLlpapqrEALKAQ 184
Cdd:cd05906 83 ACVLAGFVPAPLT------VPPTYDEPNARL-------------RKLRHIWQLLGS--PVVLTDAELV------AEFAGL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 185 RGPLPEGVLDFDTLIADCPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGL 264
Cdd:cd05906 136 ETLSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 265 PLFHVNGVMVTGLAPFHRGA-QVLLAGPQGYRNPTLiqdFWKLVERYRVTsFSGVPTIYAALL-----QVPSDGRDLSSL 338
Cdd:cd05906 216 PLDHVGGLVELHLRAVYLGCqQVHVPTEEILADPLR---WLDLIDRYRVT-ITWAPNFAFALLndlleEIEDGTWDLSSL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 339 RFALCGAAPMPVELIRQFE---ARTGLK---VIEGYGLTEgTC-------GTSCNPRGGERRPGSIGLRLPYCQVKVAVL 405
Cdd:cd05906 292 RYLVNAGEAVVAKTIRRLLrllEPYGLPpdaIRPAFGMTE-TCsgviysrSFPTYDHSQALEFVSLGRPIPGVSMRIVDD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 406 DGEGNylrdaAPNEVGNLCLKGPTVFKGYLQQDR-NRDIWIGDGWFNTGDLGRIDeDGYIWLTGRSKDLIIRGGHNIDPQ 484
Cdd:cd05906 371 EGQLL-----PEGEVGRLQVRGPVVTKGYYNNPEaNAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 485 MIEEALHRHPAVA----LAAAVGKPDAKAGELPVAY---IQLKPGASASEEELLEHASR--HVPERAAVPKDiwlIESMP 555
Cdd:cd05906 445 EIEAAVEEVPGVEpsftAAFAVRDPGAETEELAIFFvpeYDLQDALSETLRAIRSVVSRevGVSPAYLIPLP---KEEIP 521
|
570
....*....|...
gi 15599055 556 VTAVGKTFKPALR 568
Cdd:cd05906 522 KTSLGKIQRSKLK 534
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
215-568 |
2.25e-45 |
|
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: 166.84 E-value: 2.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHfnEVAMAEIMGL----------------NADYGvddvllcglplfHVNGVMVTGLA 278
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGALHAH--RVLLGHLPGVqfpfnlfprdgdlywtPADWA------------WIGGLLDVLLP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 279 PFHRGAQVLLAGPQGYRNPTLIQdfwkLVERYRVTSFSGVPTIYAALLQVPSDGRDLS-SLRFALCGAAPMPVELIRQFE 357
Cdd:cd05971 153 SLYFGVPVLAHRMTKFDPKAALD----LMSRYGVTTAFLPPTALKMMRQQGEQLKHAQvKLRAIATGGESLGEELLGWAR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 358 ARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLrlPYCQVKVAVLDGEGNYLrdaAPNEVGNLCLK--GPTVFKGYL 435
Cdd:cd05971 229 EQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGK--PIPGHRVAIVDDNGTPL---PPGEVGEIAVElpDPVAFLGYW 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 436 QQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVA 515
Cdd:cd05971 304 NNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKA 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599055 516 YIQLKPGASASEE---ELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05971 384 FVVLNPGETPSDAlarEIQELVKTRLAAH-EYPREIEFVNELPRTATGKIRRRELR 438
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
30-588 |
3.71e-45 |
|
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: 169.66 E-value: 3.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 30 TYELLQRSARRHGQRIALscLLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQT---------- 99
Cdd:cd05966 55 SYNCLDRHLKERGDKVAI--IWEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELviamlacari 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 100 ---HYVIWGGEAAgivnainpllepEHIAELIRASNTRVLVTlapfpgTDlwqkvAGLR-AQLPELYAIVvvDPANLLPA 175
Cdd:cd05966 133 gavHSVVFAGFSA------------ESLADRINDAQCKLVIT------AD-----GGYRgGKVIPLKEIV--DEALEKCP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 176 PQREALKAQRGPLP----EGV-LDFDTLIAD----CPADRLESgraihpDDVASYFHTGGTTGTPKLAPHSHF-NEVAMA 245
Cdd:cd05966 188 SVEKVLVVKRTGGEvpmtEGRdLWWHDLMAKqspeCEPEWMDS------EDPLFILYTSGSTGKPKGVVHTTGgYLLYAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 246 EIMGLNADYGVDDVLLC----GlplfhvngvMVTG-----LAPFHRGA-QVLLAGPQGYRNPTLiqdFWKLVERYRVTSF 315
Cdd:cd05966 262 TTFKYVFDYHPDDIYWCtadiG---------WITGhsyivYGPLANGAtTVMFEGTPTYPDPGR---YWDIVEKHKVTIF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 316 SGVPTIYAALLQV---PSDGRDLSSLRfaLCGAA--PMPVELIRQFEARTGLK---VIEGYGLTEgTCGTSCNPRGG--E 385
Cdd:cd05966 330 YTAPTAIRALMKFgdeWVKKHDLSSLR--VLGSVgePINPEAWMWYYEVIGKErcpIVDTWWQTE-TGGIMITPLPGatP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 386 RRPGSIGLRLPycQVKVAVLDGEGNylrDAAPNEVGNLCLKGPtvFKGYLqqdrnRDIWiGD-------------GWFNT 452
Cdd:cd05966 407 LKPGSATRPFF--GIEPAILDEEGN---EVEGEVEGYLVIKRP--WPGMA-----RTIY-GDheryedtyfskfpGYYFT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 453 GDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---E 529
Cdd:cd05966 474 GDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkE 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 530 LLEHASRHV-PerAAVPKDIWLIESMPVTAVGKTfkpalrldaIRRVLeeesRRIAEDIR 588
Cdd:cd05966 554 LRKHVRKEIgP--IATPDKIQFVPGLPKTRSGKI---------MRRIL----RKIAAGEE 598
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
27-578 |
4.01e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 168.38 E-value: 4.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 27 PSSTYELLQRSARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNlpQTHYVIWGG 106
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVAL--------IDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPN--CIEWVVLFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 107 EAA---GIVNAINPLLEPEHIAELIRASNTRVLVTLAPFPGTDLWQKVAGL-RAQLPELYAIVVVDPAN-LLPAPQREAl 181
Cdd:PRK06164 79 ACArlgATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVpPDALPPLRAIAVVDDAAdATPAPAPGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 182 kaqrgplpeGVLDFDTliADCPADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLL 261
Cdd:PRK06164 158 ---------RVQLFAL--PDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 262 CGLPLFHVNGvMVTGLAPFHRGAQVLLAgPQGYRNPTLiqdfwKLVERYRVTSFSGVPTIYAALLQVPSDGRDLSSLR-F 340
Cdd:PRK06164 227 AALPFCGVFG-FSTLLGALAGGAPLVCE-PVFDAARTA-----RALRRHRVTHTFGNDEMLRRILDTAGERADFPSARlF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 341 ALCGAAPMPVELIRQFEAR----TGLkviegYGLTEGTCGTSCNPRG---GERRPGsiGLRLPYCQVKVAVLDGEGNYLr 413
Cdd:PRK06164 300 GFASFAPALGELAALARARgvplTGL-----YGSSEVQALVALQPATdpvSVRIEG--GGRPASPEARVRARDPQDGAL- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 414 dAAPNEVGNLCLKGPTVFKGYL-QQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHR 492
Cdd:PRK06164 372 -LPDGESGEIEIRAPSLMRGYLdNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 493 HPAVALAAAVGKpDAKAGELPVAYIQLKPGASASEEELLEHASRHVperAA--VPKDIWLIESMPVTAVG---KTFKPAL 567
Cdd:PRK06164 451 LPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREAL---AGfkVPARVQVVEAFPVTESAngaKIQKHRL 526
|
570
....*....|.
gi 15599055 568 RLDAIRRVLEE 578
Cdd:PRK06164 527 REMAQARLAAE 537
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
62-568 |
4.31e-45 |
|
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: 166.15 E-value: 4.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVNAinPLLE---PEHIAELIRASNTRVLVT 138
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ--PLFTafgPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 139 LApfpgtdlwqkvaglraqlpelyaivvvdpanllpapqrealkAQRgplpegvldfdtliadcpaDRLESGRAIHpddv 218
Cdd:cd05973 79 DA------------------------------------------ANR-------------------HKLDSDPFVM---- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 219 asyFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLagpqgYRNPT 298
Cdd:cd05973 94 ---MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTIL-----LEGGF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 299 LIQDFWKLVERYRVTSFSGVPTIYAALLQ--VPSDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTE-GTc 375
Cdd:cd05973 166 SVESTWRVIERLGVTNLAGSPTAYRLLMAagAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTElGM- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 376 gTSCNPRGGER--RPGSIGLRLPycQVKVAVLDGEGNylrDAAPNEVGNLCL---KGPTV-FKGYLQQDrnrDIWIGDGW 449
Cdd:cd05973 245 -VLANHHALEHpvHAGSAGRAMP--GWRVAVLDDDGD---ELGPGEPGRLAIdiaNSPLMwFRGYQLPD---TPAIDGGY 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 450 FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASeEE 529
Cdd:cd05973 316 YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGT-PA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15599055 530 LLEHASRHVPERA---AVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05973 395 LADELQLHVKKRLsahAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
32-567 |
9.38e-45 |
|
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: 166.30 E-value: 9.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGG-EAAG 110
Cdd:cd17646 2 ALVAEQAARTPDAPAV--------VDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVlKAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 IVNAINPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkVAGLRAQLPELYAIVVVDPANLlpapqrealkaqrgplpe 190
Cdd:cd17646 74 AYLPLDPGYPADRLAYMLADAGPAVVLT------------TADLAARLPAGGDVALLGDEAL------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 191 gvldfdtliADCPADRLEsgRAIHPDDVASYFHTGGTTGTPK--LAPHShfnevAMAE-IMGLNADYGV--DDVLLCGLP 265
Cdd:cd17646 124 ---------AAPPATPPL--VPPRPDNLAYVIYTSGSTGRPKgvMVTHA-----GIVNrLLWMQDEYPLgpGDRVLQKTP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 266 L-FHVNGVMVtgLAPFHRGAQVLLAGPQGYRNPTLIQDfwkLVERYRVTSFSGVPTIYAALLQVPSDGRdLSSLRFALCG 344
Cdd:cd17646 188 LsFDVSVWEL--FWPLVAGARLVVARPGGHRDPAYLAA---LIREHGVTTCHFVPSMLRVFLAEPAAGS-CASLRRVFCS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 345 AAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGegnYLRDAAPNEVGNLC 424
Cdd:cd17646 262 GEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDD---ALRPVPVGVPGELY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 425 LKGPTVFKGYLQQ-----DRNRDIWIGDG--WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVA 497
Cdd:cd17646 339 LGGVQLARGYLGRpaltaERFVPDPFGPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVT 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599055 498 LAAAVGKPDAKAGELPVAYIQLKPGASA-SEEELLEHASRHVPErAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd17646 419 HAVVVARAAPAGAARLVGYVVPAAGAAGpDTAALRAHLAERLPE-YMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
51-561 |
2.89e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 166.32 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 51 LHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLlpnlpqthyviwggeaAGivnainpllEPEHIAELIRA 130
Cdd:PRK07768 19 MVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVL----------------AG---------APVEIAPTAQG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 131 SNTR-VLVTLA--PFPGTDL--WQKVAGLRAQLPELYAIVVVDPANLLpAPQREALKAQrgplpegVLDFDTLIADCPAD 205
Cdd:PRK07768 74 LWMRgASLTMLhqPTPRTDLavWAEDTLRVIGMIGAKAVVVGEPFLAA-APVLEEKGIR-------VLTVADLLAADPID 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 206 RLESGraihPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVD-DVLLCGLPLFHVNGvMVTGLA-PFHRG 283
Cdd:PRK07768 146 PVETG----EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMG-MVGFLTvPMYFG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 284 AQVLLAGPQGYRNPTLIqdfW-KLVERYRVTSFSGVPTIYAA----LLQVPSDGR-DLSSLRFALCGAAPMPVELIRQF- 356
Cdd:PRK07768 221 AELVKVTPMDFLRDPLL---WaELISKYRGTMTAAPNFAYALlarrLRRQAKPGAfDLSSLRFALNGAEPIDPADVEDLl 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 357 --EARTGLK---VIEGYGLTEGTCGTSCNP-------------------------RGGERRPGSIGLRLPYCQVKVavLD 406
Cdd:PRK07768 298 daGARFGLRpeaILPAYGMAEATLAVSFSPcgaglvvdevdadllaalrravpatKGNTRRLATLGPPLPGLEVRV--VD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 407 GEGNYLrdaAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMI 486
Cdd:PRK07768 376 EDGQVL---PPRGVGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 487 EEALHRHPAV--ALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRH-VpeRAAV---PKDIWLIE--SMPVTA 558
Cdd:PRK07768 453 ERAAARVEGVrpGNAVAVRLDAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHeV--VAEVgvrPRNVVVLGpgSIPKTP 530
|
...
gi 15599055 559 VGK 561
Cdd:PRK07768 531 SGK 533
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
12-571 |
5.36e-44 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 165.79 E-value: 5.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 12 DIEALERVPLEQRDLpsSTYELLQRSARRHGQRIALsclLHGsaaeePLRISYAELFARVTQTANALHRLGLESHQAVSF 91
Cdd:PLN02479 6 DIDDLPKNAANYTAL--TPLWFLERAAVVHPTRKSV---VHG-----SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 92 LLPNLPQTHYVIWGGEAAG-IVNAINPLLEPEHIAELIRASNTRVLV------TLAPfPGTDLWQKVAGLRAQLPELyaI 164
Cdd:PLN02479 76 IAPNIPAMYEAHFGVPMAGaVVNCVNIRLNAPTIAFLLEHSKSEVVMvdqeffTLAE-EALKILAEKKKSSFKPPLL--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 165 VVVDPAnLLPAPQREALKaqrgplpEGVLDFDTLIADC--------PADRLESgraihpddvASYFHTGGTTGTPKLAPH 236
Cdd:PLN02479 153 VIGDPT-CDPKSLQYALG-------KGAIEYEKFLETGdpefawkpPADEWQS---------IALGYTSGTTASPKGVVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 237 SHFNEVAMAeiMGLNADYGVDD--VLLCGLPLFHVNGVMVTGLAPFHRGAQVLLagpqgyRNPTlIQDFWKLVERYRVTS 314
Cdd:PLN02479 216 HHRGAYLMA--LSNALIWGMNEgaVYLWTLPMFHCNGWCFTWTLAALCGTNICL------RQVT-AKAIYSAIANYGVTH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 315 FSGVPTIYAALLQVPSDGRDLSSLRFA---LCGAAPMPVELIRQFEarTGLKVIEGYGLTEgTCGTS--C---------- 379
Cdd:PLN02479 287 FCAAPVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPPSVLFAMSE--KGFRVTHTYGLSE-TYGPStvCawkpewdslp 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 380 -------NPRGGERRPGSIGLRlpycqvkvaVLDGEGNYLRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNT 452
Cdd:PLN02479 364 peeqarlNARQGVRYIGLEGLD---------VVDTKTMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHS 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 453 GDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELL- 531
Cdd:PLN02479 435 GDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALa 514
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 15599055 532 EHASRHVPERAA---VPKDIwLIESMPVTAVGKTFKPALRLDA 571
Cdd:PLN02479 515 EDIMKFCRERLPaywVPKSV-VFGPLPKTATGKIQKHVLRAKA 556
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-560 |
4.21e-42 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 159.67 E-value: 4.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTYELLQRSARRHGQRIALScllhgsAAEEPLRISYAELFARVTQTANALHRLGLeshqavsfllpnLPqthyviw 104
Cdd:PRK05852 13 DFGPRIADLVEVAATRLPEAPALV------VTADRIAISYRDLARLVDDLAGQLTRSGL------------LP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 105 gGEAAGIVNAINPllepEHIAELIRASNTR-VLVTLAP-FPGTDLWQKV--AGLRAQLPELYAIVVVDPANLLPAPQREA 180
Cdd:PRK05852 68 -GDRVALRMGSNA----EFVVALLAASRADlVVVPLDPaLPIAEQRVRSqaAGARVVLIDADGPHDRAEPTTRWWPLTVN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 181 LKAQRGPlPEGVLDFDTLIADCPADRLESGRAIHPDDVASYFhTGGTTGTPKLAPHSHFNevAMAEIMGLNADYGVD--D 258
Cdd:PRK05852 143 VGGDSGP-SGGTLSVHLDAATEPTPATSTPEGLRPDDAMIMF-TGGTTGLPKMVPWTHAN--IASSVRAIITGYRLSprD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 259 VLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGYRNPTliqdFWKLVERYRVTSFSGVPTIYAALLQVPSD---GRDL 335
Cdd:PRK05852 219 ATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHT----FWDDIKAVGATWYTAVPTIHQILLERAATepsGRKP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 SSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGT---CGTSCNPRGGERRPG-SIGL--RLPYCQVKVAVLDGEg 409
Cdd:PRK05852 295 AALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAThqvTTTQIEGIGQTENPVvSTGLvgRSTGAQIRIVGSDGL- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 410 nylrDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEA 489
Cdd:PRK05852 374 ----PLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599055 490 LHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASrhvpERAA---VPKDIWLIESMPVTAVG 560
Cdd:PRK05852 450 LASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCR----ERLAafeIPASFQEASGLPHTAKG 519
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
37-568 |
7.96e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 159.32 E-value: 7.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 37 SARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWggeAAGIVNA-- 114
Cdd:PRK07788 58 AARRAPDRAAL--------IDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALY---AAGKVGAri 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 115 --INPLLEPEHIAELIRASNTRVLVTLAPFpgTDLwqkVAGLRAQLPELYAIVVvDPANLlpapqrealkaqrGPLPEGV 192
Cdd:PRK07788 127 ilLNTGFSGPQLAEVAAREGVKALVYDDEF--TDL---LSALPPDLGRLRAWGG-NPDDD-------------EPSGSTD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 193 LDFDTLIAdcpadRLESGRAIHPDDVASY-FHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNG 271
Cdd:PRK07788 188 ETLDDLIA-----GSSTAPLPKPPKPGGIvILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 272 VMVTGLAPFHRGAQVLlagPQGYRNPTLIQDfwklVERYRVTSFSGVPTIYAALLQVPSDGR---DLSSLRFALCGAAPM 348
Cdd:PRK07788 263 WAHLTLAMALGSTVVL---RRRFDPEATLED----IAKHKATALVVVPVMLSRILDLGPEVLakyDTSSLKIIFVSGSAL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 349 PVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGlRLPYcQVKVAVLDGEGNYLrdaAPNEVGNLCLKGP 428
Cdd:PRK07788 336 SPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVG-RPPK-GVTVKILDENGNEV---PRGVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 429 TVFKGYlQQDRNRDIWigDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAK 508
Cdd:PRK07788 411 FPFEGY-TDGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEE 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599055 509 AGELPVAYIQLKPGASASEEEL----LEHASRHvperaAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK07788 488 FGQRLRAFVVKAPGAALDEDAIkdyvRDNLARY-----KVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
56-568 |
7.98e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 158.63 E-value: 7.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 56 AEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGI-VNAINPLLEPEHIAELIRASNTR 134
Cdd:PRK13390 19 AETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLyITAINHHLTAPEADYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 135 VLVTLAPFPGtdLWQKVAGlraqlpelyaivvvdpanllPAPQREALkaqrGPLPEGVLDFDTLIADCPADRLESGRAih 214
Cdd:PRK13390 99 VLVASAALDG--LAAKVGA--------------------DLPLRLSF----GGEIDGFGSFEAALAGAGPRLTEQPCG-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 pddvASYFHTGGTTGTPK-LAPHSHFNEV-----AMAEIMGLNADYGVDDVLLCGLPLFHVNGV----MVTGLapfhrGA 284
Cdd:PRK13390 151 ----AVMLYSSGTTGFPKgIQPDLPGRDVdapgdPIVAIARAFYDISESDIYYSSAPIYHAAPLrwcsMVHAL-----GG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 285 QVLLAgpqgyrNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGR---DLSSLRFALCGAAPMPVELIRQFEARTG 361
Cdd:PRK13390 222 TVVLA------KRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRtryDVSSLRAVIHAAAPCPVDVKHAMIDWLG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 362 LKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLpycQVKVAVLDGEGNylrDAAPNEVGNLclkgptvfkgYLQQDRNR 441
Cdd:PRK13390 296 PIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSV---LGDLHICDDDGN---ELPAGRIGTV----------YFERDRLP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 442 DIWIGDG-------------WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAK 508
Cdd:PRK13390 360 FRYLNDPektaaaqhpahpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPE 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599055 509 AGELPVAYIQLKPGASASEE---ELLEHASRHVPERAAvPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK13390 440 MGEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKA-PRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
61-568 |
9.63e-42 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 159.00 E-value: 9.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGI--VNA---------------INPLLepeh 123
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVapVNAlfshqrselnayasqIEPAL---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 124 iaeLIrASNTRVLvtlapFPGTDLWQKvagLRAQLPELYAIVVVDPAnllpapqrealkaqrgplpeGVLDFDTLIADCP 203
Cdd:PRK10946 124 ---LI-ADRQHAL-----FSDDDFLNT---LVAEHSSLRVVLLLNDD--------------------GEHSLDDAINHPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 204 ADRLESGRAihPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLNADygvdDVLLCGLPLFHvNGVMVT--GL 277
Cdd:PRK10946 172 EDFTATPSP--ADEVAFFQLSGGSTGTPKLIPRTHndyyYSVRRSVEICGFTPQ----TRYLCALPAAH-NYPMSSpgAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 278 APFHRGAQVLLAgpqgyRNPTLIQDFwKLVERYRVTSFSGVPTIYAALLQVPSDG---RDLSSLRFALCGAAPMPVELIR 354
Cdd:PRK10946 245 GVFLAGGTVVLA-----PDPSATLCF-PLIEKHQVNVTALVPPAVSLWLQAIAEGgsrAQLASLKLLQVGGARLSETLAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 355 QFEARTGLKVIEGYGLTEGTCGTSCNPRGGER------RPGSiglrlPYCQVKVAvlDGEGNYLrdaAPNEVGNLCLKGP 428
Cdd:PRK10946 319 RIPAELGCQLQQVFGMAEGLVNYTRLDDSDERifttqgRPMS-----PDDEVWVA--DADGNPL---PQGEVGRLMTRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 429 TVFKGYLQ-QDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDA 507
Cdd:PRK10946 389 YTFRGYYKsPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 508 KAGELPVAYIQLKPGASASE--EELLEH--ASRHVPERaavpkdIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK10946 469 LMGEKSCAFLVVKEPLKAVQlrRFLREQgiAEFKLPDR------VECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
224-568 |
3.39e-41 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 157.23 E-value: 3.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 224 TGGTTGTPKLAPHSHfnevamaeimglNADYGVDDVLLCGLPLFHVNGVMVTglAP-FHRG--AQVLLAGpqGYRNPTLI 300
Cdd:PRK13382 204 TSGTTGTPKGARRSG------------PGGIGTLKAILDRTPWRAEEPTVIV--APmFHAWgfSQLVLAA--SLACTIVT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 301 Q------DFWKLVERYRVTSFSGVPTIYAALLQVPSDGRD---LSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLT 371
Cdd:PRK13382 268 RrrfdpeATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNrysGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNAT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 372 EGTCGTSCNPRGGERRPGSIGLrlPYCQVKVAVLDGEGnylRDAAPNEVGNLCLKGPTVFKGYlQQDRNRDIwiGDGWFN 451
Cdd:PRK13382 348 EAGMIATATPADLRAAPDTAGR--PAEGTEIRILDQDF---REVPTGEVGTIFVRNDTQFDGY-TSGSTKDF--HDGFMA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 452 TGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELL 531
Cdd:PRK13382 420 SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLK 499
|
330 340 350
....*....|....*....|....*....|....*..
gi 15599055 532 EHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK13382 500 QHVRDNLA-NYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
36-561 |
2.60e-40 |
|
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: 155.09 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 36 RSARRHGQRIALSCLLHGSAAEEplRISYAELFARVTQTANALHRLGLEShQAVSFLLPnlPQTHYVI--WGGEAAGIVN 113
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREE--TLTYAELDRRARAIAARLQAVGKPG-DRVLLLAP--PGLDFVAafLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 114 AinPLLEPEHIAELIRASNtrVLVTLAPfpgtdlwqkvaglraqlpelyAIVVVDPAnLLPAPQREALKAQRGPLPeGVL 193
Cdd:cd05931 76 V--PLPPPTPGRHAERLAA--ILADAGP---------------------RVVLTTAA-ALAAVRAFAASRPAAGTP-RLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 194 DFDTLIADCPADrlESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVM 273
Cdd:cd05931 129 VVDLLPDTSAAD--WPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 274 VTGLAPFHRGAQVLLAGPQGY-RNPTLiqdfW-KLVERYRVTsFSGVPTIYAALLQ--VPSDGR---DLSSLRFALCGAA 346
Cdd:cd05931 207 GGLLTPLYSGGPSVLMSPAAFlRRPLR----WlRLISRYRAT-ISAAPNFAYDLCVrrVRDEDLeglDLSSWRVALNGAE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 347 PMPVELIRQFE---ARTGLK---VIEGYGLTEGTCGTSCNPRGGERR------------------PGSIGLRLPYC---- 398
Cdd:cd05931 282 PVRPATLRRFAeafAPFGFRpeaFRPSYGLAEATLFVSGGPPGTGPVvlrvdrdalagravavaaDDPAARELVSCgrpl 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 399 -QVKVAVLDGEGNylRDAAPNEVGNLCLKGPTVFKGYLQQD-------RNRDIWIGDGWFNTGDLGRIDeDGYIWLTGRS 470
Cdd:cd05931 362 pDQEVRIVDPETG--RELPDGEVGEIWVRGPSVASGYWGRPeataetfGALAATDEGGWLRTGDLGFLH-DGELYITGRL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 471 KDLIIRGGHNIDPQMIEEAL-HRHPAV--ALAAAVGKPDAKAGELpVAYIQLKPGASASEEELLEHASRH-VPERAAV-P 545
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATAeEAHPALrpGCVAAFSVPDDGEERL-VVVAEVERGADPADLAAIAAAIRAaVAREHGVaP 517
|
570
....*....|....*...
gi 15599055 546 KDIWLIE--SMPVTAVGK 561
Cdd:cd05931 518 ADVVLVRpgSIPRTSSGK 535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
224-561 |
8.92e-40 |
|
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: 148.32 E-value: 8.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 224 TGGTTGTPKLAPHSHFNEVAMAEI--MGLNADYgvDDVLLCGLPLFHvNGVMVTGLAPFHRGAQVLLagpQGYRNPtliQ 301
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCneDLFNISG--EDAILAPGPLSH-SLFLYGAISALYLGGTFIG---QRKFNP---K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 302 DFWKLVERYRVTSFSGVPTIYAALLQVpsdGRDLSSLRFALCGAAPMPVELIRQFEART-GLKVIEGYGLTEGTCGT-SC 379
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQALART---LEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITyNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 380 NprGGERRPGSIGLRLPYCQVkvavldgegnYLRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDiwigDGWFNTGDLGRID 459
Cdd:cd17633 156 N--QESRPPNSVGRPFPNVEI----------EIRNADGGEIGKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 460 EDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQlkpGASASEEELLEhASRHVP 539
Cdd:cd17633 220 EEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKR-FLKQKL 295
|
330 340
....*....|....*....|..
gi 15599055 540 ERAAVPKDIWLIESMPVTAVGK 561
Cdd:cd17633 296 SRYEIPKKIIFVDSLPYTSSGK 317
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
214-509 |
3.91e-39 |
|
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: 150.20 E-value: 3.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVngvmvtglapFHRGAQ--VLLAG- 290
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHS----------YERSAEyfIFACGc 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 291 PQGYRN-PTLIQDFwklvERYRVTSFSGVPTIYAALLQVPSDGRDLSS---------------LRFALCGAAPMPVELIR 354
Cdd:cd17640 156 SQAYTSiRTLKDDL----KRVKPHYIVSVPRLWESLYSGIQKQVSKSSpikqflflfflsggiFKFGISGGGALPPHVDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 355 QFEArTGLKVIEGYGLTEGTCGTSCNpRGGERRPGSIGLRLPYCQVKVAVLDGeGNYLRdaaPNEVGNLCLKGPTVFKGY 434
Cdd:cd17640 232 FFEA-IGIEVLNGYGLTETSPVVSAR-RLKCNVRGSVGRPLPGTEIKIVDPEG-NVVLP---PGEKGIVWVRGPQVMKGY 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 435 LQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLII-RGGHNIDPQMIEEALHRHPAVALAAAVGKpDAKA 509
Cdd:cd17640 306 YKNpEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQ-DQKR 381
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
217-561 |
9.74e-39 |
|
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: 145.87 E-value: 9.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 217 DVASYFHTGGTTGTPK---LAPHSHFNEVAMAEIMGLNadYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLlagpqg 293
Cdd:cd17635 2 DPLAVIFTSGTTGEPKavlLANKTFFAVPDILQKEGLN--WVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 294 YRNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPSDG-RDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTE 372
Cdd:cd17635 74 GGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSAnATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 GTCGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGEgnylrdAAPN-EVGNLCLKGPTVFKGYLQQ-DRNRDIWIgDGWF 450
Cdd:cd17635 154 TGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGI------AGPSaSFGTIWIKSPANMLGYWNNpERTAEVLI-DGWV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 451 NTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEEL 530
Cdd:cd17635 227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRA 306
|
330 340 350
....*....|....*....|....*....|.
gi 15599055 531 LEHASRHVPERAAVPKDIWLIESMPVTAVGK 561
Cdd:cd17635 307 LKHTIRRELEPYARPSTIVIVTDIPRTQSGK 337
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
223-546 |
1.04e-38 |
|
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: 145.52 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 223 HTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVnGVMVTGLAPFHRGAQVLL---AGPQGYRNptl 299
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFvrrVDAEEVLE--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 300 iqdfwkLVERYRVTS-FSGVPTIyAALLQVPSDGR-DLSSLRF--ALCGAAPMPVELIRQFEARTGlkvieGYGLTEGTc 375
Cdd:cd17636 83 ------LIEAERCTHaFLLPPTI-DQIVELNADGLyDLSSLRSspAAPEWNDMATVDTSPWGRKPG-----GYGQTEVM- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 376 GTSCNPRGGERRPGSIGLRLPYCQVKVavLDGEGnylRDAAPNEVGNLCLKGPTVFKGY-----LQQDRNRDiwigdGWF 450
Cdd:cd17636 150 GLATFAALGGGAIGGAGRPSPLVQVRI--LDEDG---REVPDGEVGEIVARGPTVMAGYwnrpeVNARRTRG-----GWH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 451 NTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEEL 530
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAEL 299
|
330 340
....*....|....*....|....*
gi 15599055 531 LEH-----AS----RHVPERAAVPK 546
Cdd:cd17636 300 IEHcrariASykkpKSVEFADALPR 324
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
63-578 |
1.11e-38 |
|
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: 149.54 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 63 SYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQ---THYVIWggeAAGIVNA-INPLLEPEHIAELIRASNTRVLvt 138
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEwfiTDLAIW---MAGHISVpLYPTLNPDTIRYVLEHSESKAL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 139 lapFPGT-DLWQKVA-GLRAQLPelyaivvvdpanLLPAPQREALKAQRGplpegvldFDTLIADCPadrLESGRAIH-P 215
Cdd:cd05932 83 ---FVGKlDDWKAMApGVPEGLI------------SISLPPPSAANCQYQ--------WDDLIAQHP---PLEERPTRfP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 DDVASYFHTGGTTGTPKLAPHShFNEVAMAEIMGLNA-DYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGy 294
Cdd:cd05932 137 EQLATLIYTSGTTGQPKGVMLT-FGSFAWAAQAGIEHiGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLD- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 rnpTLIQDfwklVERYRVTSFSGVPTIYAA----------------LLQVP----------SDGRDLSSLRFALCGAAPM 348
Cdd:cd05932 215 ---TFVED----VQRARPTLFFSVPRLWTKfqqgvqdkipqqklnlLLKIPvvnslvkrkvLKGLGLDQCRLAGCGSAPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 349 PVELIRQFEaRTGLKVIEGYGLTEgTCGTSCNPRGGERRPGSIGLRLPYCQVKVAvldgegnylrdaapnEVGNLCLKGP 428
Cdd:cd05932 288 PPALLEWYR-SLGLNILEAYGMTE-NFAYSHLNYPGRDKIGTVGNAGPGVEVRIS---------------EDGEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 429 TVFKGYLQQD-RNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLI-IRGGHNIDPQMIEEALHRHPAVALAAAVGK-- 504
Cdd:cd05932 351 ALMMGYYKDPeATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGSgl 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 505 PDAKAGELPVAYIQLKPGASASEE------ELLEHASRHVP--ERAA---VPKDIWLIESMPVTavgktfkPALRLDaiR 573
Cdd:cd05932 431 PAPLALVVLSEEARLRADAFARAEleaslrAHLARVNSTLDshEQLAgivVVKDPWSIDNGILT-------PTLKIK--R 501
|
....*
gi 15599055 574 RVLEE 578
Cdd:cd05932 502 NVLEK 506
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
63-501 |
1.53e-38 |
|
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: 147.03 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 63 SYAELFARVTQTANALH-RLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVN-AINPLLEPEHIAELIRASNTRVLVTLA 140
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYvPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 PFPGTDLWQkvaGLRAQLPELYAIVVVDPANLLPAPQREAlkaqrgplpegvldfdtliadcpadrlesgraiHPDDVAS 220
Cdd:TIGR01733 81 ALASRLAGL---VLPVILLDPLELAALDDAPAPPPPDAPS---------------------------------GPDDLAY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 221 YFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGYRNPTLI 300
Cdd:TIGR01733 125 VIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 301 QDfwkLVERYRVTSFSGVPTIYAALLqvPSDGRDLSSLRFALCGAAPMPVELIRQFEARTG-LKVIEGYGLTEGTCGTSC 379
Cdd:TIGR01733 205 AA---LIAEHPVTVLNLTPSLLALLA--AALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 380 N--PRGGERRPGSIGLRLPYCQVKVAVLDGEgnyLRDAAPNEVGNLCLKGPTVFKGYL-QQDRNR------DIWIGDG-- 448
Cdd:TIGR01733 280 TlvDPDDAPRESPVPIGRPLANTRLYVLDDD---LRPVPVGVVGELYIGGPGVARGYLnRPELTAerfvpdPFAGGDGar 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15599055 449 WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAA 501
Cdd:TIGR01733 357 LYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
75-568 |
4.74e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 148.25 E-value: 4.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 75 ANALHRLGLESHqaVSFLLPNLPQthYVIWGGEAA---GIVNAINPLLEPEHIAELIRASNTRVLVTlapfpGTDLWQKV 151
Cdd:PRK13388 43 LIALADPDRPLH--VGVLLGNTPE--MLFWLAAAAlggYVLVGLNTTRRGAALAADIRRADCQLLVT-----DAEHRPLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 152 AGLraQLPELYAIVVVDPAnllpapQREALKAqrgplpegvldfdtliadcpADRLESGRAIHPDDVASYFHTGGTTGTP 231
Cdd:PRK13388 114 DGL--DLPGVRVLDVDTPA------YAELVAA--------------------AGALTPHREVDAMDPFMLIFTSGTTGAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 232 KLAPHSH----FNEVAMAEIMGLNADygvdDVLLCGLPLFHVNGVMvTGLAP-FHRGAQVllAGPQGYRNPTLIQDfwkl 306
Cdd:PRK13388 166 KAVRCSHgrlaFAGRALTERFGLTRD----DVCYVSMPLFHSNAVM-AGWAPaVASGAAV--ALPAKFSASGFLDD---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 307 VERYRVTSFSGVPTIYAALLQVPS--DGRDlSSLRFALcG--AAPmpvELIRQFEARTGLKVIEGYGLTEGTCGTSCNPr 382
Cdd:PRK13388 235 VRRYGATYFNYVGKPLAYILATPErpDDAD-NPLRVAF-GneASP---RDIAEFSRRFGCQVEDGYGSSEGAVIVVREP- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 383 ggERRPGSIGLRLP---------YCQVKVAVLDGEGNYLR-DAAPNEVGNLclKGPTVFKGYLQQDRNRDIWIGDGWFNT 452
Cdd:PRK13388 309 --GTPPGSIGRGAPgvaiynpetLTECAVARFDAHGALLNaDEAIGELVNT--AGAGFFEGYYNNPEATAERMRHGMYWS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 453 GDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLE 532
Cdd:PRK13388 385 GDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAA 464
|
490 500 510
....*....|....*....|....*....|....*...
gi 15599055 533 --HASRHVPERAAvPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK13388 465 flAAQPDLGTKAW-PRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
58-573 |
4.23e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 145.21 E-value: 4.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 58 EPLRISYAELFARVTQTANALHRL---GLESHqaVSFLLPNLPQTHYVIWGGEAAGIVNA-INPLLEPEHIAELIRASNT 133
Cdd:PRK07867 25 EDSFTSWREHIRGSAARAAALRARldpTRPPH--VGVLLDNTPEFSLLLGAAALSGIVPVgLNPTRRGAALARDIAHADC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 134 RVLVTLAPFpgtdlwqkvAGLRAQLPELYAIVVVDPAnllpapqrealkaqrgplpegvlDFDTLIADCPADRLESGRAi 213
Cdd:PRK07867 103 QLVLTESAH---------AELLDGLDPGVRVINVDSP-----------------------AWADELAAHRDAEPPFRVA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLnadyGVDDVLLCGLPLFHVNGVMVtGLAP-FHRGAQVLL 288
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCTHrkvaSAGVMLAQRFGL----GPDDVCYVSMPLFHSNAVMA-GWAVaLAAGASIAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 289 agPQGYRNPTLIQDfwklVERYRVTSFSGVPTIYAALLQVPS--DGRDlSSLRFALcGAAPMPVElIRQFEARTGLKVIE 366
Cdd:PRK07867 225 --RRKFSASGFLPD----VRRYGATYANYVGKPLSYVLATPErpDDAD-NPLRIVY-GNEGAPGD-IARFARRFGCVVVD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 367 GYGLTEGTCGTSCNPRGgerRPGSIGLRLPYCQV---------KVAVLDGEGNYLRDAAPNEVGNLclKGPTVFKGYL-- 435
Cdd:PRK07867 296 GFGSTEGGVAITRTPDT---PPGALGPLPPGVAIvdpdtgtecPPAEDADGRLLNADEAIGELVNT--AGPGGFEGYYnd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 436 -QQDRNRdiwIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPV 514
Cdd:PRK07867 371 pEADAER---MRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVM 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599055 515 AYIQLKPGASASEEELLE--HASRHVPERaAVPKDIWLIESMPVTAVGKTFKPALRLDAIR 573
Cdd:PRK07867 448 AALVLAPGAKFDPDAFAEflAAQPDLGPK-QWPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
210-569 |
1.23e-36 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 146.99 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 210 GRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEV----AMAEIMGLNADygvdDVLLCGLPLFHVNGVMVTGLAPfhrgaq 285
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILsnieQISDVFNLRND----DVILSSLPFFHSFGLTVTLWLP------ 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 286 vLLAGPQG--YRNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELIRQFEARTGL 362
Cdd:PRK08633 846 -LLEGIKVvyHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKlHPLMFASLRLVVAGAEKLKPEVADAFEEKFGI 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 363 KVIEGYGLTEGTCGTSCNPRGGER---------RPGSIGLRLPycQVKVAVLDGEGnyLRDAAPNEVGNLCLKGPTVFKG 433
Cdd:PRK08633 925 RILEGYGATETSPVASVNLPDVLAadfkrqtgsKEGSVGMPLP--GVAVRIVDPET--FEELPPGEDGLILIGGPQVMKG 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 434 YLQQDRN-----RDIWiGDGWFNTGDLGRIDEDGYIWLTGR----SKdlIirGGHNIDPQMIEEALHrhpaVALA----- 499
Cdd:PRK08633 1001 YLGDPEKtaeviKDID-GIGWYVTGDKGHLDEDGFLTITDRysrfAK--I--GGEMVPLGAVEEELA----KALGgeevv 1071
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599055 500 -AAVGKPDAKAGElpvAYIQLKPGASASEEELLEHASRHVPERAAVPKDIWLIESMPVTAVGKT-FKPALRL 569
Cdd:PRK08633 1072 fAVTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLdLKGLKEL 1140
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
62-503 |
3.15e-36 |
|
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: 143.65 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGG-EAAGIVNAINPLLEPE---HIAELIRAS-----N 132
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAiFAGGIAVGIYTTNSPEacqYVAETSEANilvveN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 133 TRVLvtlapfpgtdlwQKVAGLRAQLPELYAIVVVdpanllpapqREALKAQRGPLP--EGVLDFDTLIADCPADRLESg 210
Cdd:cd05933 89 QKQL------------QKILQIQDKLPHLKAIIQY----------KEPLKEKEPNLYswDEFMELGRSIPDEQLDAIIS- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 211 rAIHPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQV 286
Cdd:cd05933 146 -SQKPNQCCTLIYTSGTTGMPKGVMLSHdnitWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 287 LLAGPQGYRNpTLIqdfwKLVERYRVTSFSGVPTIYAALLQ----VPSDGRDLS-------------------------- 336
Cdd:cd05933 225 YFAQPDALKG-TLV----KTLREVRPTAFMGVPRVWEKIQEkmkaVGAKSGTLKrkiaswakgvgletnlklmggespsp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 337 ----------------SLRFALC-----GAAPMPVELIrQFEARTGLKVIEGYGLTEGT-CGTSCNPrgGERRPGSIGLR 394
Cdd:cd05933 300 lfyrlakklvfkkvrkALGLDRCqkfftGAAPISRETL-EFFLSLNIPIMELYGMSETSgPHTISNP--QAYRLLSCGKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 395 LPYCQVKVAVLDGEGNylrdaapnevGNLCLKGPTVFKGYLQ-QDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDL 473
Cdd:cd05933 377 LPGCKTKIHNPDADGI----------GEICFWGRHVFMGYLNmEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKEL 446
|
490 500 510
....*....|....*....|....*....|..
gi 15599055 474 IIR-GGHNIDPQMIEEALH-RHPAVALAAAVG 503
Cdd:cd05933 447 IITaGGENVPPVPIEDAVKkELPIISNAMLIG 478
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
63-567 |
5.38e-36 |
|
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: 141.27 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 63 SYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGivnAINPLLEPEHIAELIRAsntrVLVTLAPf 142
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAG---AAYVPLDPDYPADRLRY----ILEDAEP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 143 pgtdlwqkvaglraqlpelyAIVVVDPAnlLPAPqrealkaqrgpLPEGVLDFDTLIADCPADRLESGRAIHPDDVASYF 222
Cdd:cd12116 86 --------------------ALVLTDDA--LPDR-----------LPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 223 HTGGTTGTPKLAPHSHFNEV----AMAEIMGLNADygvDDVLLCGLPLFHVNGVMVtgLAPFHRGAQVLLAGPQGYRNPt 298
Cdd:cd12116 133 YTSGSTGRPKGVVVSHRNLVnflhSMRERLGLGPG---DRLLAVTTYAFDISLLEL--LLPLLAGARVVIAPRETQRDP- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 299 liQDFWKLVERYRVTSFSGVPTIYAALLQvpSDGRDLSSLRfALCGAAPMPVELIRQFEARTGlKVIEGYGLTEGTCGTS 378
Cdd:cd12116 207 --EALARLIEAHSITVMQATPATWRMLLD--AGWQGRAGLT-ALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIWST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 379 CNPRGGERRPGSIGLRLPYCQVkvAVLDgegNYLRDAAPNEVGNLCLKGPTVFKGYLQQDR------NRDIWIGDG--WF 450
Cdd:cd12116 281 AARVTAAAGPIPIGRPLANTQV--YVLD---AALRPVPPGVPGELYIGGDGVAQGYLGRPAltaerfVPDPFAGPGsrLY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 451 NTGDLGRIDEDGYIWLTGRSKDLI-IRgGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELpVAYIQLKPGASASEEE 529
Cdd:cd12116 356 RTGDLVRRRADGRLEYLGRADGQVkIR-GHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAA 433
|
490 500 510
....*....|....*....|....*....|....*...
gi 15599055 530 LLEHASRHVPErAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd12116 434 LRAHLRATLPA-YMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
215-574 |
1.66e-35 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 141.09 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGlnadYGVDDVLLCGLPLFHVNGVMvTGLAPFHRGA-QVLLa 289
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHsaliVQSLAKIAIVG----YGEDDVYLHTAPLCHIGGLS-SALAMLMVGAcHVLL- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 290 gPQgYRNPTLIQdfwkLVERYRVTSFSGVPTIYAALLQV---PSDGRDLSSLRFALCGAAPMPVELI---RQFEARTglK 363
Cdd:PLN02860 245 -PK-FDAKAALQ----AIKQHNVTSMITVPAMMADLISLtrkSMTWKVFPSVRKILNGGGSLSSRLLpdaKKLFPNA--K 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 364 VIEGYGLTEG------------TCGTSCNPRGGERRPGS----------IGLRLPYCQVKVAvLDGegnylrdaaPNEVG 421
Cdd:PLN02860 317 LFSAYGMTEAcssltfmtlhdpTLESPKQTLQTVNQTKSssvhqpqgvcVGKPAPHVELKIG-LDE---------SSRVG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 422 NLCLKGPTVFKGYLQQ------DRNRDiwigdGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPA 495
Cdd:PLN02860 387 RILTRGPHVMLGYWGQnsetasVLSND-----GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 496 VALAAAVGKPDAKAGELPVAYIQLKPG--------------ASASEEELLEHASRHVPERAAVPKDIWLIES-MPVTAVG 560
Cdd:PLN02860 462 VASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKNLSRFKIPKLFVQWRKpFPLTTTG 541
|
410
....*....|....
gi 15599055 561 KtfkpaLRLDAIRR 574
Cdd:PLN02860 542 K-----IRRDEVRR 550
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
215-506 |
1.96e-35 |
|
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: 140.04 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVA-MAEIMG-LNADYGVDDVLLCGLPLFHVNGVMVTGLApFHRGAQVllagpq 292
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAgIAGLGDrVPELLGPDDRYLAYLPLAHIFELAAENVC-LYRGGTI------ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 GYRNP-TLIQDFWK-----LVErYRVTSFSGVPTIY-----AALLQVPSDG----------------------------- 332
Cdd:cd17639 160 GYGSPrTLTDKSKRgckgdLTE-FKPTLMVGVPAIWdtirkGVLAKLNPMGglkrtlfwtayqsklkalkegpgtpllde 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 333 ------RDL--SSLRFALCGAAPMPVELIRqFEARTGLKVIEGYGLTEgTCGTSCNPRGGERRPGSIGLRLPYCQVKVav 404
Cdd:cd17639 239 lvfkkvRAAlgGRLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTE-TCAGGTVQDPGDLETGRVGPPLPCCEIKL-- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 405 LD-GEGNYLRDAAPNEvGNLCLKGPTVFKGYL-QQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLI-IRGGHNI 481
Cdd:cd17639 315 VDwEEGGYSTDKPPPR-GEILIRGPNVFKGYYkNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYI 393
|
330 340
....*....|....*....|....*
gi 15599055 482 DPQMIEEALHRHPAVALAAAVGKPD 506
Cdd:cd17639 394 ALEKLESIYRSNPLVNNICVYADPD 418
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
38-567 |
3.61e-35 |
|
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: 138.53 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 38 ARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVsfllpnlpqthyVIWGGeaagivnainp 117
Cdd:cd05945 1 AAANPDRPAVVE--------GGRTLTYRELKERADALAAALASLGLDAGDPV------------VVYGH----------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 118 lLEPEHIAELIRASNtrvlvtlapfpgtdlwqkvAGLraqlpelyAIVVVDPANllPAPQREALKAQRGPlpegvldfDT 197
Cdd:cd05945 50 -KSPDAIAAFLAALK-------------------AGH--------AYVPLDASS--PAERIREILDAAKP--------AL 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 198 LIADcpadrlesgraihPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMglNADYGV--DDVLLCGLPL-FHVNgVMV 274
Cdd:cd05945 92 LIAD-------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM--LSDFPLgpGDVFLNQAPFsFDLS-VMD 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 275 TGLAPFHRGAQVLLagpqgyrNPTLIQDFWKLVER---YRVTSFSGVPTIYAALLQVPSDGRD-LSSLR-FALCGaAPMP 349
Cdd:cd05945 156 LYPALASGATLVPV-------PRDATADPKQLFRFlaeHGITVWVSTPSFAAMCLLSPTFTPEsLPSLRhFLFCG-EVLP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 350 VELIRQFEART-GLKVIEGYGLTEGTCGTSCN------PRGGERRPgsIGLRLPYCqvKVAVLDGEGnylRDAAPNEVGN 422
Cdd:cd05945 228 HKTARALQQRFpDARIYNTYGPTEATVAVTYIevtpevLDGYDRLP--IGYAKPGA--KLVILDEDG---RPVPPGEKGE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 423 LCLKGPTVFKGYL--QQDRNRDIWIGDG--WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVAL 498
Cdd:cd05945 301 LVISGPSVSKGYLnnPEKTAAAFFPDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKE 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 499 AAAVGKPDAKAGELPVAYIQLKPGASAS-EEELLEHASRHVPErAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd05945 381 AVVVPKYKGEKVTELIAFVVPKPGAEAGlTKAIKAELAERLPP-YMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
61-561 |
6.16e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 139.25 E-value: 6.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQthYVIwggEAAGIVNA------INPLLEPEHIAELIRASNTR 134
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIE--YVE---AMLGAFKAravpvnVNYRYVEDELRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 135 VLV---TLAPfpgtdlwqKVAGLRAQLPELYAIVVVDpanllpapqrealKAQRGPLPEGVLDFDTLIADCPADRLESGR 211
Cdd:PRK07798 103 ALVyerEFAP--------RVAEVLPRLPKLRTLVVVE-------------DGSGNDLLPGAVDYEDALAAGSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 212 AihPDDVasYF-HTGGTTGTPK--LAPHSHFNEVAMAEIMGLNADYGVDD-------------VLLCGLPLFHVNGvMVT 275
Cdd:PRK07798 162 S--PDDL--YLlYTGGTTGMPKgvMWRQEDIFRVLLGGRDFATGEPIEDEeelakraaagpgmRRFPAPPLMHGAG-QWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 276 GLAPFHRGAQVLLagpqgYRNPTL-IQDFWKLVERYRVTSFSGVPTIYAA-LLQ--VPSDGRDLSSLRFALCGAAPMPVE 351
Cdd:PRK07798 237 AFAALFSGQTVVL-----LPDVRFdADEVWRTIEREKVNVITIVGDAMARpLLDalEARGPYDLSSLFAIASGGALFSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 352 LIRQF-EARTGLKVIEGYGLTE-GTCGTSCNPRGGERRPGsiglrlPYCQVK--VAVLDGEGNYLRDAAPnEVGNLCLKG 427
Cdd:PRK07798 312 VKEALlELLPNVVLTDSIGSSEtGFGGSGTVAKGAVHTGG------PRFTIGprTVVLDEDGNPVEPGSG-EIGWIARRG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 428 PtVFKGYLQqD--------RNRDiwiGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALA 499
Cdd:PRK07798 385 H-IPLGYYK-DpektaetfPTID---GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599055 500 AAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVpERAAVPKDIWLIESMPVTAVGK 561
Cdd:PRK07798 460 LVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSL-AGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
25-567 |
1.22e-34 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 138.22 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTYELLQRSARRHGQRIALScLLHGSAAeeplrISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHY-VI 103
Cdd:PRK05857 11 QLPSTVLDRVFEQARQQPEAIALR-RCDGTSA-----LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLsVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 104 WGGEAAGIVNAINPLLEPEHIAELIRASNTrVLVTLAPFPGTDlwqkvaglRAQLPELYAIVVVDPANLLPAPQREALKA 183
Cdd:PRK05857 85 ACAKLGAIAVMADGNLPIAAIERFCQITDP-AAALVAPGSKMA--------SSAVPEALHSIPVIAVDIAAVTRESEHSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 184 QRgplpegvldfdtliaDCPADRLESGraihPDDVASYFHTGGTTGTPK--LAPHSHFneVAMAEIM---GLN-ADYGVD 257
Cdd:PRK05857 156 DA---------------ASLAGNADQG----SEDPLAMIFTSGTTGEPKavLLANRTF--FAVPDILqkeGLNwVTWVVG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 258 DVLLCGLPLFHVNGV--MVTGLApfhRGAQVLLAGPQGyrnPTLIQdfwkLVERYRVTSFSGVPTIYAALL-QVPSDGRD 334
Cdd:PRK05857 215 ETTYSPLPATHIGGLwwILTCLM---HGGLCVTGGENT---TSLLE----ILTTNAVATTCLVPTLLSKLVsELKSANAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 335 LSSLRFALCGAAPMPVELIRQFEArTGLKVIEGYGLTEGTCGTSCNPRGGER----RPGSIGLRLPYCQVKVAVLDGEGN 410
Cdd:PRK05857 285 VPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGCTALCLPTDDGSivkiEAGAVGRPYPGVDVYLAATDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 411 YLRDAAPN-EVGNLCLKGPTVFKGYLQQ-DRNRDIWIgDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEE 488
Cdd:PRK05857 364 TAPGAGPSaSFGTLWIKSPANMLGYWNNpERTAEVLI-DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 489 ALHRHPAVALAAAVGKPDAKAGEL----PVAYIQLKPGASASEEELLEHASRHVPERAAVPKDIWLIESMPVTAVGKTFK 564
Cdd:PRK05857 443 IAEGVSGVREAACYEIPDEEFGALvglaVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMR 522
|
...
gi 15599055 565 PAL 567
Cdd:PRK05857 523 ASL 525
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
27-568 |
1.32e-34 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 137.95 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 27 PSSTYELLQRSArrhgqrialscLLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGG 106
Cdd:cd05915 1 LERAAALFGRKE-----------VVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 107 EAAG-IVNAINPLLEPEHIAELIRASNTRVLVTLAPFpgTDLWQKVAGLRAQLPElyaivvvDPANLLPAPQREALKAQR 185
Cdd:cd05915 70 PGMGaVLHTANPRLSPKEIAYILNHAEDKVLLFDPNL--LPLVEAIRGELKTVQH-------FVVMDEKAPEGYLAYEEA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 186 GPlpegvlDFDTLIadcPADRLesgraihpDDVASYFhTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVD--DVLLCG 263
Cdd:cd05915 141 LG------EEADPV---RVPER--------AACGMAY-TTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSekDVVLPV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 264 LPLFHVNGVMVTGLAPFHRGAQVLLagpQGYRNPTLIQDFwklVERYRVTSFSGVPTIyaalLQVPSDGRDLSSLRF--- 340
Cdd:cd05915 203 VPMFHVNAWCLPYAATLVGAKQVLP---GPRLDPASLVEL---FDGEGVTFTAGVPTV----WLALADYLESTGHRLktl 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 341 -ALCGAAPMPVELIRQFEARTGLKVIEGYGLTE-GTCGTSC--NPRgGERRPGSIGLRLP------YCQVKVAVLD---- 406
Cdd:cd05915 273 rRLVVGGSAAPRSLIARFERMGVEVRQGYGLTEtSPVVVQNfvKSH-LESLSEEEKLTLKaktglpIPLVRLRVADeegr 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 407 ---GEGNYLRDAApnevgnlcLKGPTVFKGYLQ-QDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNID 482
Cdd:cd05915 352 pvpKDGKALGEVQ--------LKGPWITGGYYGnEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWIS 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 483 PQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPgASASEEELLEHASRHVPERAAVPKDIWLIESMPVTAVGKT 562
Cdd:cd05915 424 SVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG-EKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKF 502
|
....*.
gi 15599055 563 FKPALR 568
Cdd:cd05915 503 LKRALR 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
215-561 |
1.34e-34 |
|
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: 136.80 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGpqgy 294
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLD---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RNPTliqDFWKLVERYRVTSFSGVP-------------------TIYAALLQVPSDGRDLSSL-------------RFAL 342
Cdd:cd05914 164 KIPS---AKIIALAFAQVTPTLGVPvplviekifkmdiipkltlKKFKFKLAKKINNRKIRKLafkkvheafggniKEFV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 343 CGAAPMPVElIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRpGSIGLRLPYCQVKVAVLDGEgnylrdaapNEVGN 422
Cdd:cd05914 241 IGGAKINPD-VEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRL-GSAGKVIDGVEVRIDSPDPA---------TGEGE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 423 LCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRG-GHNIDPQMIEEALHRHPAVA--- 497
Cdd:cd05914 310 IIVRGPNVMKGYYKNpEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLesl 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 498 --------LAAAVGKPD---AKAGELPVAYIQLKpgasaseEELLEHASRHVPERAAVPKDIWLIESMPVTAVGK 561
Cdd:cd05914 390 vvvqekklVALAYIDPDfldVKALKQRNIIDAIK-------WEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGK 457
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
22-579 |
1.90e-34 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 140.49 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 22 EQRDLPSSTYELLQRSARRHGQRIAlscllhgsAAEEPLR--ISYAELFARvtqtANALHRL---GLESHQAVSFLLPNL 96
Cdd:PRK06814 625 ETSDYDRTLFEALIEAAKIHGFKKL--------AVEDPVNgpLTYRKLLTG----AFVLGRKlkkNTPPGENVGVMLPNA 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 97 PQTHYVIWGGEAAGIVNA-INPLLEPEHIAELIRASNTRVLVTLAPF-PGTDLWQKVAGLRAQLPELYAivvvdpanllp 174
Cdd:PRK06814 693 NGAAVTFFALQSAGRVPAmINFSAGIANILSACKAAQVKTVLTSRAFiEKARLGPLIEALEFGIRIIYL----------- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 175 apqrEALKAQRGPlpegVLDFDTLIADCPADRLESGRaiHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADY 254
Cdd:PRK06814 762 ----EDVRAQIGL----ADKIKGLLAGRFPLVYFCNR--DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDF 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 255 GVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLL-AGPQGYRN-PTLIQDfwklverYRVTSFSGVPTI---YAALlqvp 329
Cdd:PRK06814 832 SPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLyPSPLHYRIiPELIYD-------TNATILFGTDTFlngYARY---- 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 330 SDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCN-PRggERRPGSIGLRLPYCQVKVAVLDGe 408
Cdd:PRK06814 901 AHPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNtPM--HNKAGTVGRLLPGIEYRLEPVPG- 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 409 gnylrdaaPNEVGNLCLKGPTVFKGYLQQDRNRDIW-IGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIE 487
Cdd:PRK06814 978 --------IDEGGRLFVRGPNVMLGYLRAENPGVLEpPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE 1049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 488 EALHRHPAVALAAAVGKPDAKAGElpvAYIQLKPGASASEEELLEHASRH-VPErAAVPKDIWLIESMPVTAVGKTFKPA 566
Cdd:PRK06814 1050 ELAAELWPDALHAAVSIPDARKGE---RIILLTTASDATRAAFLAHAKAAgASE-LMVPAEIITIDEIPLLGTGKIDYVA 1125
|
570
....*....|...
gi 15599055 567 LRLDAIRRVLEEE 579
Cdd:PRK06814 1126 VTKLAEEAAAKPE 1138
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
62-568 |
2.43e-34 |
|
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: 138.39 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWG-GEAAGIVNAINPLLEPEHIAELIRASNTRVLVTLA 140
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAvARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 141 PFPG----TDLWQKVAGLRAQLPELYAIVVVdpanllpapqrEALKAQRGPLPEGVLDFDTLIADcPADRLESgraIHPD 216
Cdd:cd05968 172 GFTRrgreVNLKEEADKACAQCPTVEKVVVV-----------RHLGNDFTPAKGRDLSYDEEKET-AGDGAER---TESE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 217 DVASYFHTGGTTGTPKLAPHSHFN-EVAMAEIMGLNADYGVDDVLLCGLPLfhvnGVMVTGLAPF----HRGAQVLLAGP 291
Cdd:cd05968 237 DPLMIIYTSGTTGKPKGTVHVHAGfPLKAAQDMYFQFDLKPGDLLTWFTDL----GWMMGPWLIFggliLGATMVLYDGA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 292 QGYRNPTLIqdfWKLVERYRVTSFSGVPTIYAALL---QVPSDGRDLSSLRFALCGAAPMPVELIRQFEARTG---LKVI 365
Cdd:cd05968 313 PDHPKADRL---WRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGkgrNPII 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 366 EGYGLTEGTCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGEGNylrdAAPNEVGNLCLKGPTV--FKGYLQQD----- 438
Cdd:cd05968 390 NYSGGTEISGGILGNVLIKPIKPSSFNGPVP--GMKADVLDESGK----PARPEVGELVLLAPWPgmTRGFWRDEdryle 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 439 ----RNRDIWIgdgwfnTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPV 514
Cdd:cd05968 464 tywsRFDNVWV------HGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIV 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 515 AYIQLKPGASASE---EELLEHASRHVpERAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05968 538 CFVVLKPGVTPTEalaEELMERVADEL-GKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
25-568 |
3.55e-34 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 137.61 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTYELLQRSARRHGQRIALSclLHGSAAEEplrISYAELFARVTQTANALH-RLGLESHQAVSFLLPNLPQTHYVI 103
Cdd:PRK05620 7 DVPLSLTRILEYGSTVHGDTTVTT--WGGAEQEQ---TTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 104 WGGEAAGIV-NAINPLLEPEHIAELIRASNTRVLVT---LAPfpgtdlwqKVAGLRAQLPELYAIVVVDPaNLLPAPQRE 179
Cdd:PRK05620 82 FAVACMGAVfNPLNKQLMNDQIVHIINHAEDEVIVAdprLAE--------QLGEILKECPCVRAVVFIGP-SDADSAAAH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 180 ALKAQRGPLPEGVLDFDTLIADCPAdrlesgraIHPDDVASYFHTGGTTGTPKLAPHSHfnEVAMAEIMGLNA--DYGV- 256
Cdd:PRK05620 153 MPEGIKVYSYEALLDGRSTVYDWPE--------LDETTAAAICYSTGTTGAPKGVVYSH--RSLYLQSLSLRTtdSLAVt 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 257 -DDVLLCGLPLFHVNGVMVTgLAPFHRGAQVLLAGPQgYRNPTLIqdfwKLVERYRVTSFSGVPTIYAAL----LQVPSD 331
Cdd:PRK05620 223 hGESFLCCVPIYHVLSWGVP-LAAFMSGTPLVFPGPD-LSAPTLA----KIIATAMPRVAHGVPTLWIQLmvhyLKNPPE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 332 GRdlsSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTE-GTCGTSCNPRGG---ERRPG---SIGlRLPyCQVKVAV 404
Cdd:PRK05620 297 RM---SLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTEtSPVGTVARPPSGvsgEARWAyrvSQG-RFP-ASLEYRI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 405 LDgEGNYLRDAAPNEvGNLCLKGPTVFKGYLQQD-----------RNRDIWIG------DGWFNTGDLGRIDEDGYIWLT 467
Cdd:PRK05620 372 VN-DGQVMESTDRNE-GEIQVRGNWVTASYYHSPteegggaastfRGEDVEDAndrftaDGWLRTGDVGSVTRDGFLTIH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 468 GRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE--ELLEHASRHVPERAAVP 545
Cdd:PRK05620 450 DRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTREtaERLRDQLRDRLPNWMLP 529
|
570 580
....*....|....*....|...
gi 15599055 546 KDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK05620 530 EYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-605 |
1.03e-33 |
|
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: 138.07 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 23 QRDLPSST--YELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPnlPQTH 100
Cdd:COG1020 469 AAPYPADAtlHELFEAQAARTPDAVAVVF--------GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLE--RSLE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 101 YVIwggeaA--GIVNA------INPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkVAGLRAQLPELYAIVVVdpanl 172
Cdd:COG1020 539 MVV-----AllAVLKAgaayvpLDPAYPAERLAYMLEDAGARLVLT------------QSALAARLPELGVPVLA----- 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 173 lpapqrealkaqrgplpegvLDfDTLIADCPADRLESgrAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMaeIMGLNA 252
Cdd:COG1020 597 --------------------LD-ALALAAEPATNPPV--PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL--LAWMQR 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 253 DYGV--DDVLLcglplfhvngvMVTGLA----------PFHRGAQVLLAGPQGYRNPtliQDFWKLVERYRVTSFSGVPT 320
Cdd:COG1020 652 RYGLgpGDRVL-----------QFASLSfdasvweifgALLSGATLVLAPPEARRDP---AALAELLARHRVTVLNLTPS 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 321 IYAALLQVPSDgrDLSSLRFALCGAAPMPVELIRQFEART-GLKVIEGYGLTEGTCGTS---CNPRGGERRPGSIGLRLP 396
Cdd:COG1020 718 LLRALLDAAPE--ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTyyeVTPPDADGGSVPIGRPIA 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 397 YCQVkvAVLDGegnYLRDAAPNEVGNLCLKGPTVFKGYLQQD--------RNRDIWIGDGWFNTGDLGRIDEDGYIWLTG 468
Cdd:COG1020 796 NTRV--YVLDA---HLQPVPVGVPGELYIGGAGLARGYLNRPeltaerfvADPFGFPGARLYRTGDLARWLPDGNLEFLG 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 469 RSKDLI-IRGgHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPErAAVPKD 547
Cdd:COG1020 871 RADDQVkIRG-FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPP-YMVPAA 948
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599055 548 IWLIESMPVTAVGKTFKPALRLDAIRRVLEEESRRIAEDIRVEVVADERHGQLAHLHV 605
Cdd:COG1020 949 VVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDD 1006
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
61-586 |
2.24e-33 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 135.65 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQ-------------THYVIWGGeaagivnainplLEPEHIAEL 127
Cdd:PRK00174 98 KITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEaavamlacarigaVHSVVFGG------------FSAEALADR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 128 IRASNTRVLVTlapfpgTDlwqkvAGLRA--QLPeLYAIVvvDPANLLPAPQREALKAQR--GPLP--EGV-LDFDTLIA 200
Cdd:PRK00174 166 IIDAGAKLVIT------AD-----EGVRGgkPIP-LKANV--DEALANCPSVEKVIVVRRtgGDVDwvEGRdLWWHELVA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 201 ----DCPADRLEsgrAIHPddvasYF--HTGGTTGTPKLAPHS------HfneVAMAeiMGLNADYGVDDVLLC----Gl 264
Cdd:PRK00174 232 gasdECEPEPMD---AEDP-----LFilYTSGSTGKPKGVLHTtggylvY---AAMT--MKYVFDYKDGDVYWCtadvG- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 265 plfhvngvMVTG-----LAPFHRGA-QVLLAGPQGYRNPTliqDFWKLVERYRVTSFSGVPTIYAALLQVPSD---GRDL 335
Cdd:PRK00174 298 --------WVTGhsyivYGPLANGAtTLMFEGVPNYPDPG---RFWEVIDKHKVTIFYTAPTAIRALMKEGDEhpkKYDL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 SSLRfalcgaapmpveLIrqfeartglkviegyglteGTCGTSCNPR---------GGER-------------------- 386
Cdd:PRK00174 367 SSLR------------LL-------------------GSVGEPINPEawewyykvvGGERcpivdtwwqtetggimitpl 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 387 ------RPGSIGLRLPycQVKVAVLDGEGNylrDAAPNEVGNLCLKGPtvFKGYLqqdrnRDIWiGD------------- 447
Cdd:PRK00174 416 pgatplKPGSATRPLP--GIQPAVVDEEGN---PLEGGEGGNLVIKDP--WPGMM-----RTIY-GDherfvktyfstfk 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 448 GWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASE 527
Cdd:PRK00174 483 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD 562
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599055 528 E---ELLEHASRHV-PerAAVPKDIWLIESMPVTAVGKTfkpalrldaIRRVLeeesRRIAED 586
Cdd:PRK00174 563 ElrkELRNWVRKEIgP--IAKPDVIQFAPGLPKTRSGKI---------MRRIL----RKIAEG 610
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
198-568 |
2.63e-33 |
|
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: 132.69 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 198 LIADCPADRLESGRAI--------HPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLNADygvdDVllcglp 265
Cdd:cd05974 59 LTPDDLRDRVDRGGAVyaavdentHADDPMLLYFTSGTTSKPKLVEHTHrsypVGHLSTMYWIGLKPG----DV------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 266 lfHVNgVMVTG---------LAPFHRGAQVLLAGPQGYRNPTLIQdfwkLVERYRVTSFSGVPTIYAALLQvpsdgRDLS 336
Cdd:cd05974 129 --HWN-ISSPGwakhawscfFAPWNAGATVFLFNYARFDAKRVLA----ALVRYGVTTLCAPPTVWRMLIQ-----QDLA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 337 SLRFAL---CGAA-PMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPrGGERRPGSIGLRLPycQVKVAVLDGEGNyl 412
Cdd:cd05974 197 SFDVKLrevVGAGePLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSP-GQPVKAGSMGRPLP--GYRVALLDPDGA-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 413 rdaaPNEVGNLCL-----KGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIE 487
Cdd:cd05974 272 ----PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 488 EALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEhASRHVPERAAVPKDIWLIE--SMPVTAVGKTFKP 565
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALE-IFRFSRERLAPYKRIRRLEfaELPKTISGKIRRV 426
|
...
gi 15599055 566 ALR 568
Cdd:cd05974 427 ELR 429
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
44-568 |
3.63e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 133.37 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 44 RIALSCLLHGSAA-------EEPLRISYAELFARVTQTANALHRLGLEShQAVSFLLPNLPQTHYVIWGGEAAGIVNA-I 115
Cdd:PRK07638 2 GITKEYKKHASLQpnkiaikENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVpL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 116 NPLLEPEHIAELIRASNTRVLVT----LAPFPGTD----LWQKVAGL-RAQLPELYAIVvvdpaNLLPAPqrealkaqrg 186
Cdd:PRK07638 81 DIKWKQDELKERLAISNADMIVTerykLNDLPDEEgrviEIDEWKRMiEKYLPTYAPIE-----NVQNAP---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 187 plpegvldfdtliadcpadrlesgraihpddvasyFHTG---GTTGTPKLAPHSH------FNevAMAEIMGLNADygvD 257
Cdd:PRK07638 146 -----------------------------------FYMGftsGSTGKPKAFLRAQqswlhsFD--CNVHDFHMKRE---D 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 258 DVLLCGlPLFHvngvmvtglAPFHRGA-QVLLAGPQGYRNPTLI-QDFWKLVERYRVTSFSGVPTIYAALLQVpsDGRDL 335
Cdd:PRK07638 186 SVLIAG-TLVH---------SLFLYGAiSTLYVGQTVHLMRKFIpNQVLDKLETENISVMYTVPTMLESLYKE--NRVIE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 SSLRFALCGA---APMPVELIRQFEArtgLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGEgnyl 412
Cdd:PRK07638 254 NKMKIISSGAkweAEAKEKIKNIFPY---AKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGE---- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 413 rDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHR 492
Cdd:PRK07638 327 -EVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHE 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599055 493 HPAVALAAAVGKPDAKAGELPVAYIQlkpgASASEEELlehaSRHVPERAA---VPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK07638 406 HPAVDEIVVIGVPDSYWGEKPVAIIK----GSATKQQL----KSFCLQRLSsfkIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
32-567 |
3.76e-33 |
|
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: 133.10 E-value: 3.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWG-GEAAG 110
Cdd:cd12117 1 ELFEEQAARTPDAVAVVY--------GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAvLKAGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 IVNAINPLLEPEHIAELIRASNTRVLVTLAPFPGtdlwqkvaglraQLPELYAIVVVDpanllpapqrEALKAQRGPLPE 190
Cdd:cd12117 73 AYVPLDPELPAERLAFMLADAGAKVLLTDRSLAG------------RAGGLEVAVVID----------EALDAGPAGNPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 191 GVLDfdtliadcpadrlesgraihPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAeimgLNADY---GVDDVLLCGLPL- 266
Cdd:cd12117 131 VPVS--------------------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV----KNTNYvtlGPDDRVLQTSPLa 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 267 -----FHVNGVMVTglapfhrGAQVLLAGPQGYRNPTLIQDFwklVERYRVTsfsgVPTIYAALLQ--VPSDGRDLSSLR 339
Cdd:cd12117 187 fdastFEIWGALLN-------GARLVLAPKGTLLDPDALGAL---IAEEGVT----VLWLTAALFNqlADEDPECFAGLR 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 340 FALCGAAPMPVELIRQF-EARTGLKVIEGYGLTEGT-CGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGegnYLRDAAP 417
Cdd:cd12117 253 ELLTGGEVVSPPHVRRVlAACPGLRLVNGYGPTENTtFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDE---DGRPVPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 418 NEVGNLCLKGPTVFKGYLqqdrNR----------DIWIGDG-WFNTGDLGRIDEDGYIWLTGRSKDLI-IRgGHNIDPQM 485
Cdd:cd12117 330 GVPGELYVGGDGLALGYL----NRpaltaerfvaDPFGPGErLYRTGDLARWLPDGRLEFLGRIDDQVkIR-GFRIELGE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 486 IEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASAseEELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKP 565
Cdd:cd12117 405 IEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA--AELRAFLRERLPAY-MVPAAFVVLDELPLTANGKVDRR 481
|
..
gi 15599055 566 AL 567
Cdd:cd12117 482 AL 483
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
215-567 |
1.68e-32 |
|
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: 130.51 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLcglpLFHvngvmvtGLA----------PFHRGA 284
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFH-------SYAfdfsvweiwgALLHGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 285 QVLLAGPQGYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLRFALCGAAPMPVELIRQFEARTGL- 362
Cdd:cd17643 161 RLVVVPYEVARSP---EDFARLLRDEGVTVLNQTPSAFYQLVEAAdRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLd 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 363 --KVIEGYGLTEGTCGTSCNPRGGERRPGS----IGLRLPYCQVkvAVLDgegNYLRDAAPNEVGNLCLKGPTVFKGYLQ 436
Cdd:cd17643 238 rpQLVNMYGITETTVHVTFRPLDAADLPAAaaspIGRPLPGLRV--YVLD---ADGRPVPPGVVGELYVSGAGVARGYLG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 437 QDR--------NRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLI-IRGgHNIDPQMIEEALHRHPAVALAAAVGKPDA 507
Cdd:cd17643 313 RPEltaerfvaNPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVkIRG-FRIELGEIEAALATHPSVRDAAVIVREDE 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 508 KAGELPVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd17643 392 PGDTRLVAYVVADDGAAADIAELRALLKELLP-DYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
176-618 |
1.35e-31 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 130.54 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 176 PQRE---ALKAQRGPL-----PEGVLDFDTLIADcpADRLE-SGRAIHPDDVASY-FHTGGTTGTPKLAPHSHFNEVAMA 245
Cdd:PRK06060 97 AARNtepALVVTSDALrdrfqPSRVAEAAELMSE--AARVApGGYEPMGGDALAYaTYTSGTTGPPKAAIHRHADPLTFV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 246 EIMGLNA-DYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAG-PQGYRNPTLiqdfwkLVERYRVTSFSGVPTIYA 323
Cdd:PRK06060 175 DAMCRKAlRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSaPVTPEAAAI------LSARFGPSVLYGVPNFFA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 324 ALLQVPSdGRDLSSLRFALCGAAPMPVELI-RQFEARTGLKVIEGYGLTEgTCGTSCNPRGGERRPGSIGLRLPYCQVKV 402
Cdd:PRK06060 249 RVIDSCS-PDSFRSLRCVVSAGEALELGLAeRLMEFFGGIPILDGIGSTE-VGQTFVSNRVDEWRLGTLGRVLPPYEIRV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 403 AVLDGEGnylrdAAPNEVGNLCLKGPTVFKGYLqqDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNID 482
Cdd:PRK06060 327 VAPDGTT-----AGPGVEGDLWVRGPAIAKGYW--NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVD 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 483 PQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYiqLKPGASAS-EEELLEHASRHVPERAA---VPKDIWLIESMPVTA 558
Cdd:PRK06060 400 PREVERLIIEDEAVAEAAVVAVRESTGASTLQAF--LVATSGATiDGSVMRDLHRGLLNRLSafkVPHRFAVVDRLPRTP 477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599055 559 VGKTFKPALRLDAIRRVLEE----ESRRIAEDIRVEVVADERHGQLAHLHVPALDERRQAALEE 618
Cdd:PRK06060 478 NGKLVRGALRKQSPTKPIWElsltEPGSGVRAQRDDLSASNMTIAGGNDGGATLRERLVALRQE 541
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
36-568 |
1.52e-31 |
|
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: 128.62 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 36 RSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVNA- 114
Cdd:cd17651 3 RQAARTPDAPALVA--------EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 115 INPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkvaglraqlpelyaivvvdpanllpapQREALKAQRGPLPEGVLD 194
Cdd:cd17651 75 LDPAYPAERLAFMLADAGPVLVLT--------------------------------------HPALAGELAVELVAVTLL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 195 FDTLIADCPADRLEsgRAIHPDDVASYFHTGGTTGTPK--LAPHSHFN--------------EVAMAEIMGLNADYGVDD 258
Cdd:cd17651 117 DQPGAAAGADAEPD--PALDADDLAYVIYTSGSTGRPKgvVMPHRSLAnlvawqarasslgpGARTLQFAGLGFDVSVQE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 259 VL--LCGlplfhvngvmvtglapfhrGAQVLLAGPQGYRNPTliqDFWKLVERYRVT-SFSGVPTIYAALLQVPSDGRDL 335
Cdd:cd17651 195 IFstLCA-------------------GATLVLPPEEVRTDPP---ALAAWLDEQRISrVFLPTVALRALAEHGRPLGVRL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 SSLRFALCGAAPMPV-ELIRQFEAR-TGLKVIEGYGLTEG---TCGTSCNPRGGERRPGSIGLRLPycQVKVAVLDGegn 410
Cdd:cd17651 253 AALRYLLTGGEQLVLtEDLREFCAGlPGLRLHNHYGPTEThvvTALSLPGDPAAWPAPPPIGRPID--NTRVYVLDA--- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 411 YLRDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGW------FNTGDLGRIDEDGYIWLTGRSKDLI-IRgGHNID 482
Cdd:cd17651 328 ALRPVPPGVPGELYIGGAGLARGYLNRpELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVkIR-GFRIE 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 483 PQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPErAAVPKDIWLIESMPVTAVGKT 562
Cdd:cd17651 407 LGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPE-YMVPSAFVLLDALPLTPNGKL 485
|
....*.
gi 15599055 563 FKPALR 568
Cdd:cd17651 486 DRRALP 491
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
215-497 |
9.27e-31 |
|
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: 126.95 E-value: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEV----AMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLApFHRGAQVllag 290
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVsnvaGVFKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHGAKI---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 291 pqGY---RNPTLIQDFWKLveryRVTSFSGVP----TIYAALLQVPSDG----------------RDLSS---------- 337
Cdd:cd05927 188 --GFysgDIRLLLDDIKAL----KPTVFPGVPrvlnRIYDKIFNKVQAKgplkrklfnfalnyklAELRSgvvraspfwd 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 338 --------------LRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNpRGGERRPGSIGLRLPYCQVKVA 403
Cdd:cd05927 262 klvfnkikqalggnVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLT-LPGDTSVGHVGGPLPCAEVKLV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 404 VLDgEGNYLRDAAPNEvGNLCLKGPTVFKGYLQ-QDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLI-IRGGHNI 481
Cdd:cd05927 341 DVP-EMNYDAKDPNPR-GEVCIRGPNVFSGYYKdPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYV 418
|
330
....*....|....*.
gi 15599055 482 DPQMIEEALHRHPAVA 497
Cdd:cd05927 419 APEKIENIYARSPFVA 434
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
156-497 |
2.64e-30 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 126.37 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 156 AQLPELYAIVVV--DPANLLPAPQREALKaqrgplpegVLDFDTLIADCPADrLESGRAIHPDDVASYFHTGGTTGTPKL 233
Cdd:PLN02736 169 SEIPSVRLIVVVggADEPLPSLPSGTGVE---------IVTYSKLLAQGRSS-PQPFRPPKPEDVATICYTSGTTGTPKG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 234 APHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFH----VNGVMVTglapfHRGAQVLLAgpQGyRNPTLIQDFWKLver 309
Cdd:PLN02736 239 VVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyerVNQIVML-----HYGVAVGFY--QG-DNLKLMDDLAAL--- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 310 yRVTSFSGVP--------------------------TIYAALLQVPSDGRDLSSL-----------------RFALCGAA 346
Cdd:PLN02736 308 -RPTIFCSVPrlynriydgitnavkesgglkerlfnAAYNAKKQALENGKNPSPMwdrlvfnkikaklggrvRFMSSGAS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 347 PMPVELIRQFEARTGLKVIEGYGLTEGTCGTScNPRGGERRPGSIGLRLPYCQVKVAVLDgEGNYLRDAAPNEVGNLCLK 426
Cdd:PLN02736 387 PLSPDVMEFLRICFGGRVLEGYGMTETSCVIS-GMDEGDNLSGHVGSPNPACEVKLVDVP-EMNYTSEDQPYPRGEICVR 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 427 GPTVFKGYLQ-QDRNRDIWIGDGWFNTGDLGridedgyIWLTGRSKDLIIRG--------GHNIDPQMIEEALHRHPAVA 497
Cdd:PLN02736 465 GPIIFKGYYKdEVQTREVIDEDGWLHTGDIG-------LWLPGGRLKIIDRKknifklaqGEYIAPEKIENVYAKCKFVA 537
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
215-562 |
6.12e-30 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 125.59 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLL-AGPQG 293
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLyPSPLH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 294 YR-NPTLIQDfwklverYRVTSFSGVPTI---YAALlqvpSDGRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYG 369
Cdd:PRK08043 444 YRiVPELVYD-------RNCTVLFGTSTFlgnYARF----ANPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 370 LTEGTCGTSCN-PRGGerRPGSIGLRLPYCQVKVAVLDG--EGnylrdaapnevGNLCLKGPTVFKGYLQ---------- 436
Cdd:PRK08043 513 VTECAPVVSINvPMAA--KPGTVGRILPGMDARLLSVPGieQG-----------GRLQLKGPNIMNGYLRvekpgvlevp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 437 QDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGElpvAY 516
Cdd:PRK08043 580 TAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---AL 656
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15599055 517 IQLKPGASASEEELLEHASRH-VPErAAVPKDIWLIESMPVTAVGKT 562
Cdd:PRK08043 657 VLFTTDSELTREKLQQYAREHgVPE-LAVPRDIRYLKQLPLLGSGKP 702
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
61-567 |
3.61e-29 |
|
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: 121.22 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVNA-INPLLEPEHIAELIRASNTRVLVTL 139
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVpVDIDQPAARREAILADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 140 APFPgtdlwqkvaglraqlpelyaiVVVDPANLLPAPQREALKAQRGPLPegvldfdtliadcpadrlesgRAIHPDDVA 219
Cdd:cd12114 92 GPDA---------------------QLDVAVFDVLILDLDALAAPAPPPP---------------------VDVAPDDLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 220 SYFHTGGTTGTPKLAPHSHfnEVAMAEIMGLNADYGV--DDVLLC------GLPLFHVNGVMVTGlapfhrgAQVLLAGP 291
Cdd:cd12114 130 YVIFTSGSTGTPKGVMISH--RAALNTILDINRRFAVgpDDRVLAlsslsfDLSVYDIFGALSAG-------ATLVLPDE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 292 QGYRNPtliqDFW-KLVERYRVTSFSGVPTIYAALLQV-PSDGRDLSSLRFALCGAAPMPVELIRQFEART-GLKVIEGY 368
Cdd:cd12114 201 ARRRDP----AHWaELIERHGVTLWNSVPALLEMLLDVlEAAQALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 369 GLTEGTCGTSCNPRG-GERRPGSIGLRLPYCQVKVAVLDGEGnylRDAAPNEVGNLCLKGPTVFKGYLQ-----QDRNRD 442
Cdd:cd12114 277 GATEASIWSIYHPIDeVPPDWRSIPYGRPLANQRYRVLDPRG---RDCPDWVPGELWIGGRGVALGYLGdpeltAARFVT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 443 IWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPG 522
Cdd:cd12114 354 HPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDG 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15599055 523 ASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd12114 434 TPIAPDALRAFLAQTLP-AYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-561 |
1.83e-28 |
|
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: 117.10 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 223 HTGGTTGTPKLAPHSH--------------FNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGvMVTGLAPFHRGAQVLL 288
Cdd:cd05924 10 YTGGTTGMPKGVMWRQedifrmlmggadfgTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTG-SWTAFGGLLGGQTVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 289 AGPQgyRNPtliQDFWKLVERYRVTSFSGVPTIYAA-LLQVPSDGR--DLSSLRFALCGAAPMPVELIRQF-EARTGLKV 364
Cdd:cd05924 89 PDDR--FDP---EEVWRTIEKHKVTSMTIVGDAMARpLIDALRDAGpyDLSSLFAISSGGALLSPEVKQGLlELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 365 IEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPycqvKVAVLDGEGNYLRDAAPnEVGNLCLKGpTVFKGYLQQDRN---- 440
Cdd:cd05924 164 VDAFGSSETGFTGSGHSAGSGPETGPFTRANP----DTVVLDDDGRVVPPGSG-GVGWIARRG-HIPLGYYGDEAKtaet 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 441 -RDIwigDG--WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYI 517
Cdd:cd05924 238 fPEV---DGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15599055 518 QLKPGASASEEELLEHASRHVpERAAVPKDIWLIESMPVTAVGK 561
Cdd:cd05924 315 QLREGAGVDLEELREHCRTRI-ARYKLPKQVVFVDEIERSPAGK 357
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
61-564 |
2.47e-28 |
|
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: 119.32 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHR-LGLESHQAVSFLLPNLPQthYV-IWGGEA-AGIVNA-INPLLEPEHIAELIRASNTRVL 136
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPA--FLwIWLGLAkLGCPVAfLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 137 VTlapfpGTDLwqkVAGLRAQLPELYAIVVvdpanllpapqrEALKAQRGPLPEGVLDFDTLIADCPADRL-ESGRA-IH 214
Cdd:cd05938 83 VV-----APEL---QEAVEEVLPALRADGV------------SVWYLSHTSNTEGVISLLDKVDAASDEPVpASLRAhVT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLnadYGV--DDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAgpq 292
Cdd:cd05938 143 IKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSL---CGVtaDDVIYITLPLYHSSGFLLGIGGCIELGATCVLK--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 gyRNPTLIQdFWKLVERYRVTSFSGVPTIYAALLQVP-SDGRDLSSLRFALcGAAPMPvELIRQFEARTG-LKVIEGYGL 370
Cdd:cd05938 217 --PKFSASQ-FWDDCRKHNVTVIQYIGELLRYLCNQPqSPNDRDHKVRLAI-GNGLRA-DVWREFLRRFGpIRIREFYGS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 371 TEGTCGTsCNPRGgerRPGSIG-------LRLPYCQVKVAVLDGEGnyLRDA-------APNEVGNLCLK--GPTVFKGY 434
Cdd:cd05938 292 TEGNIGF-FNYTG---KIGAVGrvsylykLLFPFELIKFDVEKEEP--VRDAqgfcipvAKGEPGLLVAKitQQSPFLGY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 435 L------QQDRNRDI-WIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKP-- 505
Cdd:cd05938 366 AgdkeqtEKKLLRDVfKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTvp 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599055 506 --DAKAGelpVAYIQLKPGASASEEELLEHASRHVPERAAvPKDIWLIESMPVTAvgkTFK 564
Cdd:cd05938 446 ghEGRIG---MAAVKLKPGHEFDGKKLYQHVREYLPAYAR-PRFLRIQDSLEITG---TFK 499
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
204-568 |
2.84e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 116.30 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 204 ADRLESGRAIHpDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEimGLNADYGVDDVLLCGLPLFHVNGVMV------TGL 277
Cdd:PRK07824 24 RDALRVGEPID-DDVALVVATSGTTGTPKGAMLTAAALTASAD--ATHDRLGGPGQWLLALPAHHIAGLQVlvrsviAGS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 278 APfhrgaqVLLAGPQGYRNPTLIQDFWKLVERYRVTSFsgVPTIYAALLQVPSDGRDLSSLRFALCGAAPMPVELIRQFE 357
Cdd:PRK07824 101 EP------VELDVSAGFDPTALPRAVAELGGGRRYTSL--VPMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 358 ArTGLKVIEGYGLTEgTCGtSCNPRGgerRPgsiglrLPYCQVKVavldgegnylrdaapnEVGNLCLKGPTVFKGYlqq 437
Cdd:PRK07824 173 A-AGINVVRTYGMSE-TSG-GCVYDG---VP------LDGVRVRV----------------EDGRIALGGPTLAKGY--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 438 dRN---RDIWIGDGWFNTGDLGRIDeDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPV 514
Cdd:PRK07824 222 -RNpvdPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15599055 515 AYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:PRK07824 300 AAVVGDGGPAPTLEALRAHVARTLD-RTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
217-564 |
5.43e-28 |
|
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: 117.45 E-value: 5.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 217 DVASYFHTGGTTGTPKLAPHSHFNEVAMAEI---MGLNADygvDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLagpqg 293
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFfagSGGALP---SDVLYTCLPLYHSTALIVGWSACLASGATLVI----- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 294 yRNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPS--DGRDlSSLRfALCGAAPMPvELIRQFEARTGL-KVIEGYGL 370
Cdd:cd05940 154 -RKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPkpTERK-HKVR-MIFGNGLRP-DIWEEFKERFGVpRIAEFYAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 371 TEGTCGtSCNPrggERRPGSIGlRLPYCQVKVAVL-----DGE-GNYLRDA-------APNEVGNLCLK--GPTVFKGYL 435
Cdd:cd05940 230 TEGNSG-FINF---FGKPGAIG-RNPSLLRKVAPLalvkyDLEsGEPIRDAegrcikvPRGEPGLLISRinPLEPFDGYT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 436 -----QQDRNRDIWI-GDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKP---- 505
Cdd:cd05940 305 dpaatEKKILRDVFKkGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgt 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599055 506 DAKAGelpVAYIQLKPGASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAvgkTFK 564
Cdd:cd05940 385 DGRAG---MAAIVLQPNEEFDLSALAAHLEKNLP-GYARPLFLRLQPEMEITG---TFK 436
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
38-535 |
7.00e-28 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 117.28 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 38 ARRHGQRIALSclLHGSaaeeplRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAG-IVNAIN 116
Cdd:PRK09029 13 AQVRPQAIALR--LNDE------VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGaRVLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 117 PLLEPEHIAELIRASNTRVLVTLAPFPgtdlwqkvaglraqlpelyAIVVVDPANLLPAPQREALkaqrgplpegvldfd 196
Cdd:PRK09029 85 PQLPQPLLEELLPSLTLDFALVLEGEN-------------------TFSALTSLHLQLVEGAHAV--------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 197 tliadcpadrlesgrAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEimGLNA--DYGVDDVLLCGLPLFHVngvmv 274
Cdd:PRK09029 131 ---------------AWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAE--GVLSlmPFTAQDSWLLSLPLFHV----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 275 TGLAPFHR----GAQVLLAGPQgyrnptliqDFWKLVERyrVTSFSGVPTIYAALLQvpSDGRDLSSLRFALCGAApMPV 350
Cdd:PRK09029 189 SGQGIVWRwlyaGATLVVRDKQ---------PLEQALAG--CTHASLVPTQLWRLLD--NRSEPLSLKAVLLGGAA-IPV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 351 ELIRQFEARtGLKVIEGYGLTEgTCGTSCNPRGgERRPGsIGLRLPYCQVKVAvlDGEgnylrdaapnevgnLCLKGPTV 430
Cdd:PRK09029 255 ELTEQAEQQ-GIRCWCGYGLTE-MASTVCAKRA-DGLAG-VGSPLPGREVKLV--DGE--------------IWLRGASL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 431 FKGYLQQDRNRDIWIGDGWFNTGDLGRIDeDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAG 510
Cdd:PRK09029 315 ALGYWRQGQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFG 393
|
490 500
....*....|....*....|....*
gi 15599055 511 ELPVAYIQLKpgASASEEELLEHAS 535
Cdd:PRK09029 394 QRPVAVVESD--SEAAVVNLAEWLQ 416
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
34-556 |
1.56e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 117.31 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 34 LQRSARRHGQRIALSCLlHGSAAEEPLR---ISYAELFARVTQTANALHRLGLES-HQAVSFLLPNLPQTHYVIwggeA- 108
Cdd:PRK09274 12 LPRAAQERPDQLAVAVP-GGRGADGKLAydeLSFAELDARSDAIAHGLNAAGIGRgMRAVLMVTPSLEFFALTF----Al 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 109 --AGIVnainP-LLEP----EHIAELIRASNTRVLVTLApfpgtdlwqkvaglRAQL---------PELYAIVVVDPANL 172
Cdd:PRK09274 87 fkAGAV----PvLVDPgmgiKNLKQCLAEAQPDAFIGIP--------------KAHLarrlfgwgkPSVRRLVTVGGRLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 173 LPAPQREALKAQRGPLPegvldFDtlIADCPadrlesgraihPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEImgLNA 252
Cdd:PRK09274 149 WGGTTLATLLRDGAAAP-----FP--MADLA-----------PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA--LRE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 253 DYGV--DDVLLCGLPLFHVNGVM--VTGLAP---FHRGAQVllagpqgyrNPTLIqdfWKLVERYRVTSFSGVPTIYAAL 325
Cdd:PRK09274 209 DYGIepGEIDLPTFPLFALFGPAlgMTSVIPdmdPTRPATV---------DPAKL---FAAIERYGVTNLFGSPALLERL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 326 LQV-PSDGRDLSSLRFALCGAAPMPVELIRQFEA--RTGLKVIEGYGLTE------------------------GTCgts 378
Cdd:PRK09274 277 GRYgEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEalpissiesreilfatraatdngaGIC--- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 379 cnprggerrpgsIGLRLPYCQVKV-AVLDGEGNYLRDA---APNEVGNLCLKGPTVFKGYL---QQDRNRDIWIGDG--W 449
Cdd:PRK09274 354 ------------VGRPVDGVEVRIiAISDAPIPEWDDAlrlATGEIGEIVVAGPMVTRSYYnrpEATRLAKIPDGQGdvW 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 450 FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPdAKAGELPVAYIQLKPGASAS--- 526
Cdd:PRK09274 422 HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG-VPGAQRPVLCVELEPGVACSksa 500
|
570 580 590
....*....|....*....|....*....|.
gi 15599055 527 -EEELLEHASRHvpERAAVPKDIWLIESMPV 556
Cdd:PRK09274 501 lYQELRALAAAH--PHTAGIERFLIHPSFPV 529
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
214-567 |
2.43e-27 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 115.04 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPK--LAPHSHFNEVAMAEIMGLNADYGvDDVLLCGLPLFhvNGVMVTGLAPFHRGAQVLLAgP 291
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKgvVVTHRGLANLAAAQIAAFDVGPG-SRVLQFASPSF--DASVWELLMALLAGATLVLA-P 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 292 QGYRNPTliQDFWKLVERYRVTSFSGVPtiyAALLQVPSDgrDLSSLRFALCGAAPMPVELIRQFEarTGLKVIEGYGLT 371
Cdd:cd17652 167 AEELLPG--EPLADLLREHRITHVTLPP---AALAALPPD--DLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 372 EGT-CGTSCNPRGGERRPgSIGLrlPYCQVKVAVLDgegNYLRDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGW 449
Cdd:cd17652 238 ETTvCATMAGPLPGGGVP-PIGR--PVPGTRVYVLD---ARLRPVPPGVPGELYIAGAGLARGYLNRpGLTAERFVADPF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 450 -------FNTGDLGRIDEDGYIWLTGRSKDLI-IRGgHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKP 521
Cdd:cd17652 312 gapgsrmYRTGDLARWRADGQLEFLGRADDQVkIRG-FRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15599055 522 GASASEEELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd17652 391 GAAPTAAELRAHLAERLPGY-MVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
310-567 |
1.46e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 113.94 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 310 YRVTSFSGVPTIYAALLQVPSDGR---DLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGER 386
Cdd:PRK13383 263 HRADAFTAVPVVLARILELPPRVRarnPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 387 RPGSIGLRLPYCQVKVavLDGEGnylRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIwigDGWFNTGDLGRIDEDGYIWL 466
Cdd:PRK13383 343 APETVGKPVAGCPVRI--LDRNN---RPVGPRVTGRIFVGGELAGTRYTDGGGKAVV---DGMTSTGDMGYLDNAGRLFI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 467 TGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVpERAAVPK 546
Cdd:PRK13383 415 VGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRV-SRFEQPR 493
|
250 260
....*....|....*....|.
gi 15599055 547 DIWLIESMPVTAVGKTFKPAL 567
Cdd:PRK13383 494 DINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
201-568 |
9.55e-26 |
|
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: 110.54 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 201 DCPADRL-----ESGRAI----HPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPlFHVNG 271
Cdd:cd17649 70 EYPAERLrymleDSGAGLllthHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFAS-FNFDG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 272 VMVTGLAPFHRGAQVLLAGPQGYRNPtliQDFWKLVERYRVTSFSgVPTIY----AALLQVPSDGRDLSsLRFALCGAAP 347
Cdd:cd17649 149 AHEQLLPPLICGACVVLRPDELWASA---DELAEMVRELGVTVLD-LPPAYlqqlAEEADRTGDGRPPS-LRLYIFGGEA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 348 MPVELIRQFeARTGLKVIEGYGLTEGT-CGTSCNPRGGERRPGS---IGLRLPycQVKVAVLDGEgnyLRDAAPNEVGNL 423
Cdd:cd17649 224 LSPELLRRW-LKAPVRLFNAYGPTEATvTPLVWKCEAGAARAGAsmpIGRPLG--GRSAYILDAD---LNPVPVGVTGEL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 424 CLKGPTVFKGYLQQ-----DR---NRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPA 495
Cdd:cd17649 298 YIGGEGLARGYLGRpeltaERfvpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599055 496 VALAAAVGKPDAKAGELpVAYiqLKPGASASEEELLEHASRHVPER---AAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd17649 378 VREAAVVALDGAGGKQL-VAY--VVLRAAAAQPELRAQLRTALRASlpdYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-567 |
1.26e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.51 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 2 NPSPSIAGLSDIEALERVPL----EQRD----LPSSTYELLQRSARRHGQRIALSCllhgsaAEEplRISYAELFARVTQ 73
Cdd:PRK12316 477 NPQARVDELPMLDAEERGQLvegwNATAaeypLQRGVHRLFEEQVERTPEAPALAF------GEE--TLDYAELNRRANR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 74 TANALHRLGLESHQAVSFLLPNLPQTHYVIWGG-EAAGIVNAINPLLEPEHIAELIRASNTRVLVTLapfpgtdlwqkva 152
Cdd:PRK12316 549 LAHALIERGVGPDVLVGVAMERSIEMVVALLAIlKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ------------- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 153 glRAQLPELyaivvvdpanllpapqrealkaqrgPLPEGVldfDTLIADCPADRLES------GRAIHPDDVASYFHTGG 226
Cdd:PRK12316 616 --SHLGRKL-------------------------PLAAGV---QVLDLDRPAAWLEGyseenpGTELNPENLAYVIYTSG 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 227 TTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPL-FHVNGVMVTGlaPFHRGAQVLLAGPQGYRNPtliQDFWK 305
Cdd:PRK12316 666 STGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFW--PLMSGARLVVAAPGDHRDP---AKLVE 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 306 LVERYRVTSFSGVPTIYAALLQVPSDGrDLSSLRFALCGAAPMPVELIRQFEAR---TGLkvIEGYGLTEGTCGTSCNPR 382
Cdd:PRK12316 741 LINREGVDTLHFVPSMLQAFLQDEDVA-SCTSLRRIVCSGEALPADAQEQVFAKlpqAGL--YNLYGPTEAAIDVTHWTC 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 383 GGERRpGSIGLRLPYCQVKVAVLDGEGNylrdAAPNEV-GNLCLKGPTVFKGYLQQ-----DRNRDIWIGDG--WFNTGD 454
Cdd:PRK12316 818 VEEGG-DSVPIGRPIANLACYILDANLE----PVPVGVlGELYLAGRGLARGYHGRpgltaERFVPSPFVAGerMYRTGD 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 455 LGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVgkpdAKAGELPVAYIQLKPGASASEEELLEHA 534
Cdd:PRK12316 893 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVLESEGGDWREALKAHL 968
|
570 580 590
....*....|....*....|....*....|...
gi 15599055 535 SRHVPERaAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:PRK12316 969 AASLPEY-MVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
224-568 |
2.74e-25 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 109.31 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 224 TGGTTGTPKLAPHSHfnEVAMAEIMGLNADYGVDDV-LLCGLPLFHVNGVM------VTG----LAPFHR--GAQVLLAG 290
Cdd:PRK07445 128 TGGSSGQIRFAIHTW--ETLTASVQGFQRYFQLQQVnSFCVLPLYHVSGLMqfmrsfLTGgklvILPYKRlkSGQELPPN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 291 PQgyrnptliqDFWklveryrvtsFSGVPTIYAALLQVPSdgRDLSSLRFALCGAAPMPVELIRQfeART-GLKVIEGYG 369
Cdd:PRK07445 206 PS---------DFF----------LSLVPTQLQRLLQLRP--QWLAQFRTILLGGAPAWPSLLEQ--ARQlQLRLAPTYG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 370 LTEgTCGTSCNPRGGERRPGSIGLR--LPYCQVKVAvldgegnylrdaaPNEVGNLCLKGPTVFKGYLQQdrnrdIWIGD 447
Cdd:PRK07445 263 MTE-TASQIATLKPDDFLAGNNSSGqvLPHAQITIP-------------ANQTGNITIQAQSLALGYYPQ-----ILDSQ 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 448 GWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGaSASE 527
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISL 402
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15599055 528 EELLEHASRHVpERAAVPKDiWL-IESMPVTAVGKTFKPALR 568
Cdd:PRK07445 403 EELKTAIKDQL-SPFKQPKH-WIpVPQLPRNPQGKINRQQLQ 442
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-573 |
3.97e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.79 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTYELLQRSARRHGQRIALSCllhgsaAEEplRISYAELFARVTQTANALHRLGLESHQAVSFllpNLPQTHYVIW 104
Cdd:PRK12467 1571 PLARLVHQLIEDQAAATPEAVALVF------GEQ--ELTYGELNRRANRLAHRLIALGVGPEVLVGI---AVERSLEMVV 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 105 G----GEAAGIVNAINPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkvaglraqlpelyaivvvdpanllpapQREA 180
Cdd:PRK12467 1640 GllaiLKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT--------------------------------------QSHL 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 181 LkaQRGPLPEGVldfDTLIADCPADRLES------GRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADY 254
Cdd:PRK12467 1682 Q--ARLPLPDGL---RSLVLDQEDDWLEGysdsnpAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQL 1756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 255 GVDDVLLCGLPlFHVNGVMVTGLAPFHRGAQVLLAGPQGYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGRD 334
Cdd:PRK12467 1757 SAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAPPGAHRDP---EQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEH 1832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 335 LSSLRFALCGAAPMPVELIRQFEARTG-LKVIEGYGLTEG-------TCgTSCNPRGGERRPgsIGlrLPYCQVKVAVLD 406
Cdd:PRK12467 1833 PLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETavdvthwTC-RRKDLEGRDSVP--IG--QPIANLSTYILD 1907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 407 gegNYLRDAAPNEVGNLCLKGPTVFKGYLQQ-----DR---NRDIWIGDGWFNTGDLGRIDEDGYIWLTGR-SKDLIIRg 477
Cdd:PRK12467 1908 ---ASLNPVPIGVAGELYLGGVGLARGYLNRpaltaERfvaDPFGTVGSRLYRTGDLARYRADGVIEYLGRiDHQVKIR- 1983
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 478 GHNIDPQMIEEALHRHPAVALAAAVGKpDAKAGELPVAYI--------QLKPGASASEEELLEHASRHVPERaAVPKDIW 549
Cdd:PRK12467 1984 GFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVvptdpglvDDDEAQVALRAILKNHLKASLPEY-MVPAHLV 2061
|
570 580
....*....|....*....|....*
gi 15599055 550 LIESMPVTAVGKTFKPAL-RLDAIR 573
Cdd:PRK12467 2062 FLARMPLTPNGKLDRKALpAPDASE 2086
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
62-504 |
1.07e-24 |
|
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: 108.66 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 62 ISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQthyVIWGGEAAGIVNAIN-PLLE---PEHIAELIRASNTRVLV 137
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPE---WVWAELAAQAIGALSlGIYQdsmAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 138 TlapfpgTDLWQ--KVAGLRAQLPELYAIVVVDPANLLpapqrealKAQRGPLpegvLDFDTLIADCPA-DRLESG---- 210
Cdd:cd17641 89 A------EDEEQvdKLLEIADRIPSVRYVIYCDPRGMR--------KYDDPRL----ISFEDVVALGRAlDRRDPGlyer 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 211 --RAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMaEIMGLNADY-GVDDVLLCGLPL-------FHVNGVMVTG---- 276
Cdd:cd17641 151 evAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGH-CAAYLAADPlGPGDEYVSVLPLpwigeqmYSVGQALVCGfivn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 277 ---------------------LAP------------------------FHRGAQVLL-AGPQGYRNPTLiqDFWklverY 310
Cdd:cd17641 230 fpeepetmmedlreigptfvlLPPrvwegiaadvrarmmdatpfkrfmFELGMKLGLrALDRGKRGRPV--SLW-----L 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 311 RVTSFSGVPTIYAALlqvpsdgRD---LSSLRFALCGAAPMPVELIRQFEArTGLKVIEGYGLTEgTCGTSCNPRGGERR 387
Cdd:cd17641 303 RLASWLADALLFRPL-------RDrlgFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRDGDVD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 388 PGSIGLRLPYCQVKVAvldgegnylrdaapnEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGRIDEDGYIWL 466
Cdd:cd17641 374 PDTVGVPFPGTEVRID---------------EVGEILVRSPGVFVGYYKNpEATAEDFDEDGWLHTGDAGYFKENGHLVV 438
|
490 500 510
....*....|....*....|....*....|....*....
gi 15599055 467 TGRSKDL-IIRGGHNIDPQMIEEALHRHPAVALAAAVGK 504
Cdd:cd17641 439 IDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
38-578 |
1.88e-24 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 108.11 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 38 ARRHGQR--IALScllhgSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQT-------------HYV 102
Cdd:PRK10524 64 AKRPEQLalIAVS-----TETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAafamlacarigaiHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 103 IWGGEAAGivnainpllepeHIAELIRASNTRVLVTL-------APFPGTDLWQKVAGLRAQLPElyAIVVVDpANLLPA 175
Cdd:PRK10524 139 VFGGFASH------------SLAARIDDAKPVLIVSAdagsrggKVVPYKPLLDEAIALAQHKPR--HVLLVD-RGLAPM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 176 PQREALKAQRGPLPEGVLDfdtliADCPADRLESGraiHPddvaSY-FHTGGTTGTPK-----LAPHShfneVAMAEIMG 249
Cdd:PRK10524 204 ARVAGRDVDYATLRAQHLG-----ARVPVEWLESN---EP----SYiLYTSGTTGKPKgvqrdTGGYA----VALATSMD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 250 LNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRG-AQVLLAGPQGYRNPTLiqdFWKLVERYRVTSFSGVPTIYAALLQV 328
Cdd:PRK10524 268 TIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGmATIMYEGLPTRPDAGI---WWRIVEKYKVNRMFSAPTAIRVLKKQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 329 PSD---GRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRP---GSIGLrlPYCQVKV 402
Cdd:PRK10524 345 DPAllrKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPILAIARGVEDRPtrlGSPGV--PMYGYNV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 403 AVLD---GEgnylrDAAPNEVGNLCLKGPTVfKGYLQ---QDRNRDI---W--IGDGWFNTGDLGRIDEDGYIWLTGRSK 471
Cdd:PRK10524 423 KLLNevtGE-----PCGPNEKGVLVIEGPLP-PGCMQtvwGDDDRFVktyWslFGRQVYSTFDWGIRDADGYYFILGRTD 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 472 DLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEEL---LEHASRHVPERA----AV 544
Cdd:PRK10524 497 DVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQlgavAR 576
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 15599055 545 PKDIWLIESMPVTAVGKTFKPALR-------------------LDAIRRVLEE 578
Cdd:PRK10524 577 PARVWFVSALPKTRSGKLLRRAIQaiaegrdpgdlttiedpaaLQQIRQALEE 629
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
31-567 |
6.51e-24 |
|
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: 105.09 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 31 YELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNlpqthyviwggeaag 110
Cdd:cd12115 2 HDLVEAQAARTPDAIALVC--------GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLER--------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 ivnainpllepehiaelirasntrvlvtlapfpGTDLwqkVAGLRAQLPELYAIVVVDPANllpapqrealkaqrgplpe 190
Cdd:cd12115 59 ---------------------------------TPDL---VVALLAVLKAGAAYVPLDPAY------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 191 gvldfdtliadcPADR----LESGRAIH----PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGlnADYGVDD---V 259
Cdd:cd12115 84 ------------PPERlrfiLEDAQARLvltdPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAA--AAFSAEElagV 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 260 L----LC-GLPLFHVngvmvtgLAPFHRGAQVLLAGPqgyrnptlIQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGRD 334
Cdd:cd12115 150 LastsICfDLSVFEL-------FGPLATGGKVVLADN--------VLALPDLPAAAEVTLINTVPSAAAELLRHDALPAS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 335 LSSLRFAlcgAAPMPVELIRQFEARTGLKVIEG-YGLTEGTC-GTSCN-PRGGERRPgSIGLRLPYCQVKVavLDGEGNY 411
Cdd:cd12115 215 VRVVNLA---GEPLPRDLVQRLYARLQVERVVNlYGPSEDTTySTVAPvPPGASGEV-SIGRPLANTQAYV--LDRALQP 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 412 LrdaAPNEVGNLCLKGPTVFKGYLQQ-----DRNRDIWIGDG--WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQ 484
Cdd:cd12115 289 V---PLGVPGELYIGGAGVARGYLGRpgltaERFLPDPFGPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELG 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 485 MIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPErAAVPKDIWLIESMPVTAVGKTFK 564
Cdd:cd12115 366 EIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPA-YMVPSRFVRLDALPLTPNGKIDR 444
|
...
gi 15599055 565 PAL 567
Cdd:cd12115 445 SAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
200-567 |
7.94e-24 |
|
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: 104.86 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 200 ADCPADRLE-----SGRAI---HPDDVASYFHTGGTTGTPK--LAPHSHFNEVAMAeimgLNADYGVDDvllcglplFHV 269
Cdd:cd17650 69 PDYPAERLQymledSGAKLlltQPEDLAYVIYTSGTTGKPKgvMVEHRNVAHAAHA----WRREYELDS--------FPV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 270 NGVMVTGLA---PFHRGAQVLLAG------PQGYR-NPTLIqdfWKLVERYRVTSFSGVPTIYAALLQ-VPSDGRDLSSL 338
Cdd:cd17650 137 RLLQMASFSfdvFAGDFARSLLNGgtlvicPDEVKlDPAAL---YDLILKSRITLMESTPALIRPVMAyVYRNGLDLSAM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 339 RFALCGA----APMPVELIRQFEARTglKVIEGYGLTEGTCGTSCNPRGGERRPGS----IGLRLPycQVKVAVLDgegN 410
Cdd:cd17650 214 RLLIVGSdgckAQDFKTLAARFGQGM--RIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLP--NTAMYVLD---E 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 411 YLRDAAPNEVGNLCLKGPTVFKGY-----LQQDRNRDIWIGDG--WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDP 483
Cdd:cd17650 287 RLQPQPVGVAGELYIGGAGVARGYlnrpeLTAERFVENPFAPGerMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIEL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 484 QMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQlkPGASASEEELLEHASRHVPErAAVPKDIWLIESMPVTAVGKTF 563
Cdd:cd17650 367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELRAFLAKELPS-YMIPSYYVQLDALPLTPNGKVD 443
|
....
gi 15599055 564 KPAL 567
Cdd:cd17650 444 RRAL 447
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
64-561 |
1.05e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 105.47 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 64 YAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVNAinPLLEPehiaelirasntrvlvtlAPFP 143
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV--PLPLP------------------MGFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 144 GTDLWqkVAGLRAQLPELYAIVVVDPANLLPAPQrEALKAQRGPLPEGVLDFDTL-IADCPADRlesgraIHPDDVASYF 222
Cdd:PRK09192 112 GRESY--IAQLRGMLASAQPAAIITPDELLPWVN-EATHGNPLLHVLSHAWFKALpEADVALPR------PTPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 223 HTGGTTGTPK------------LAPHSHfnevamaeiMGLNADYGvdDVLLCGLPLFHVNGVMVTGLAPFhrGAQV---L 287
Cdd:PRK09192 183 YSSGSTRFPRgviithralmanLRAISH---------DGLKVRPG--DRCVSWLPFYHDMGLVGFLLTPV--ATQLsvdY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 288 LAGPQGYRNPTLiqdfW-KLVERYRVT-SFSgvPTIYAALLQVPSDGR-----DLSSLRFALCGAAPMPVELIRQFEAR- 359
Cdd:PRK09192 250 LPTRDFARRPLQ----WlDLISRNRGTiSYS--PPFGYELCARRVNSKdlaelDLSCWRVAGIGADMIRPDVLHQFAEAf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 360 --TGLK---VIEGYGLTEGTCGTSCNPRGGERRPGSIGL-RLPYCQVKVAVLDGEGNY----------------LRDAAP 417
Cdd:PRK09192 324 apAGFDdkaFMPSYGLAEATLAVSFSPLGSGIVVEEVDRdRLEYQGKAVAPGAETRRVrtfvncgkalpgheieIRNEAG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 418 NE-----VGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIdEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHR 492
Cdd:PRK09192 404 MPlpervVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQ 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599055 493 HPAV-ALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPERAAVPKDIWLI--ESMPVTAVGK 561
Cdd:PRK09192 483 EPELrSGDAAAFSIAQENGEKIVLLVQCRISDEERRGQLIHALAALVRSEFGVEAAVELVppHSLPRTSSGK 554
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-569 |
1.37e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 106.79 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 25 DLPSSTYELLQRSARRHGQRIALSCLlhGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVsFLLPNLPQTHYVIW 104
Cdd:PRK05691 6 ELPLTLVQALQRRAAQTPDRLALRFL--ADDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 105 GGEAAGIVNAinPLLEPE--------HIAELIRASNTRVLVTLAPFPGTdLWQKVAGLRAQLPELYAIVVVDPAnllpap 176
Cdd:PRK05691 83 GCLYAGVIAV--PAYPPEsarrhhqeRLLSIIADAEPRLLLTVADLRDS-LLQMEELAAANAPELLCVDTLDPA------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 177 qrealkaqrgplpegvldfdtliadcPADRLEsGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIM--GLNADY 254
Cdd:PRK05691 154 --------------------------LAEAWQ-EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIrhGFGIDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 255 GVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGYRNPTLiqDFWKLVERYRVTSFSGVPTIYAALLQVPSD--- 331
Cdd:PRK05691 207 NPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYFLERPL--RWLEAISEYGGTISGGPDFAYRLCSERVSEsal 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 332 -GRDLSSLRFALCGAAPMPVELIRQFEAR------TGLKVIEGYGLTEGTCGTSCNPRG-----------------GERR 387
Cdd:PRK05691 285 eRLDLSRWRVAYSGSEPIRQDSLERFAEKfaacgfDPDSFFASYGLAEATLFVSGGRRGqgipaleldaealarnrAEPG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 388 PGSIGLRLPYCQVKVAVLDGEGNYLRDAAPNEVGNLCLKGPTVFKGYLQQDR-------NRDiwiGDGWFNTGDLGRIdE 460
Cdd:PRK05691 365 TGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEasaktfvEHD---GRTWLRTGDLGFL-R 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 461 DGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVA----LAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASR 536
Cdd:PRK05691 441 DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkgrVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQ 520
|
570 580 590
....*....|....*....|....*....|....*.
gi 15599055 537 HVPER-AAVPKDIWLIE--SMPVTAVGKTFKPALRL 569
Cdd:PRK05691 521 AVAEAcQEAPSVVLLLNpgALPKTSSGKLQRSACRL 556
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
216-473 |
2.42e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 105.06 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 DDVASYFHTGGTTGTPKLAPHSHFNevAMAEIMGLN-------ADYGVDDVLLCGLPLFHVN--GVMVTGLApfhRGAQV 286
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGS--LTAGILALEdrlndliGPPEEDETYCSYLPLAHIMefGVTNIFLA---RGALI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 287 llagpqGYRNP-TLIQDFWK----LVErYRVTSFSGVPTI--------------------------YAALLQVPSDGRDL 335
Cdd:PTZ00216 339 ------GFGSPrTLTDTFARphgdLTE-FRPVFLIGVPRIfdtikkaveaklppvgslkrrvfdhaYQSRLRALKEGKDT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 ----------------SSLRFALCGAAPMpvelirqfEART--------GLkVIEGYGLTEgtcgTSCN---PRGGERRP 388
Cdd:PTZ00216 412 pywnekvfsapravlgGRVRAMLSGGGPL--------SAATqefvnvvfGM-VIQGWGLTE----TVCCggiQRTGDLEP 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 389 GSIGLRLPYCQVKVavLDGEGnYLRDAAPNEVGNLCLKGPTVFKGYLQQDR-NRDIWIGDGWFNTGDLGRIDEDGYIWLT 467
Cdd:PTZ00216 479 NAVGQLLKGVEMKL--LDTEE-YKHTDTPEPRGEILLRGPFLFKGYYKQEElTREVLDEDGWFHTGDVGSIAANGTLRII 555
|
....*.
gi 15599055 468 GRSKDL 473
Cdd:PTZ00216 556 GRVKAL 561
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
216-537 |
3.38e-23 |
|
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: 102.92 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 DDVASYFHTGGTTGTPKLAPHSHFNEVAmaEIMGLNADYGV--DDVLLCGLPLFHVNGVM--VTGLAP---FHRGAQVll 288
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAA--QIDALRQLYGIrpGEVDLATFPLFALFGPAlgLTSVIPdmdPTRPARA-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 289 agpqgyrNPTLIQDFwklVERYRVTSFSGVPTIYAALLQV-PSDGRDLSSLRFALCGAAPMPVELIRQFEA--RTGLKVI 365
Cdd:cd05910 161 -------DPQKLVGA---IRQYGVSIVFGSPALLERVARYcAQHGITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 366 EGYGLTEGTCGTSCNPRG--GERRPGS-------IGLRLPYCQVKVAVLDGEGNYLRDAA----PNEVGNLCLKGPTVFK 432
Cdd:cd05910 231 TPYGATEALPVSSIGSREllATTTAATsggagtcVGRPIPGVRVRIIEIDDEPIAEWDDTlelpRGEIGEITVTGPTVTP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 433 GYL---QQDRNRDIWIGDG--WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVG--KP 505
Cdd:cd05910 311 TYVnrpVATALAKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGvgKP 390
|
330 340 350
....*....|....*....|....*....|....*.
gi 15599055 506 dakAGELPVAYIQLKPG----ASASEEELLEHASRH 537
Cdd:cd05910 391 ---GCQLPVLCVEPLPGtitpRARLEQELRALAKDY 423
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
135-571 |
3.72e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.42 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 135 VLVTLAPFPGTDLwqkVAGLRAQLPELYAIVVVDP-------ANLLPAPQREALKAQ---RGPLPEGVLDFDTLIADCPA 204
Cdd:PRK12316 3108 VLVGVAVERSLEM---VVGLLAILKAGGAYVPLDPeypeerlAYMLEDSGAQLLLSQshlRLPLAQGVQVLDLDRGDENY 3184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 205 DRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLcGLPLFHVNGVMVTGLAPFHRGA 284
Cdd:PRK12316 3185 AEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVL-QFTTFSFDVFVEELFWPLMSGA 3263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 285 QVLLAGPQGYRNPTLIQDfwkLVERYRVTSFSGVPTIYAALLQVPsDGRDLSSLRFALCGAAPMPVELIRQFEArtGLKV 364
Cdd:PRK12316 3264 RVVLAGPEDWRDPALLVE---LINSEGVDVLHAYPSMLQAFLEEE-DAHRCTSLKRIVCGGEALPADLQQQVFA--GLPL 3337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 365 IEGYGLTEGTCgTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGEGNYLRDAApneVGNLCLKGPTVFKGYLQQDR----- 439
Cdd:PRK12316 3338 YNLYGPTEATI-TVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGA---LGELYLGGEGLARGYHNRPGltaer 3413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 440 --NRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVgkpdAKAGELPVAYI 517
Cdd:PRK12316 3414 fvPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYV 3489
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 518 QLKPGASASEEELLEHASRHVPERAaVPKDIWLIESMPVTAVGKTFKPAL-RLDA 571
Cdd:PRK12316 3490 VPEDEAGDLREALKAHLKASLPEYM-VPAHLLFLERMPLTPNGKLDRKALpRPDA 3543
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
11-567 |
1.08e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 103.59 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 11 SDIEALERVPLEQRDLPSSTY-ELLQRSARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLESHQAV 89
Cdd:PRK10252 440 GEYAQLAQVNATAVEIPETTLsALVAQQAAKTPDAPAL--------ADARYQFSYREMREQVVALANLLRERGVKPGDSV 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 90 SFLLPNLPQTHYVIWGGEAAGIVN-AINPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkVAGLRAQLPELYAIVVVD 168
Cdd:PRK10252 512 AVALPRSVFLTLALHAIVEAGAAWlPLDTGYPDDRLKMMLEDARPSLLIT------------TADQLPRFADVPDLTSLC 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 169 PANLLPAPQREALkaqrgplpegvldfdtliadcpadrlesgRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIM 248
Cdd:PRK10252 580 YNAPLAPQGAAPL-----------------------------QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 249 glNADYGV--DDVLLCGLPL-FHVNgvMVTGLAPFHRGAQVLLAGPQGYRNPTLIQDFwklVERYRVTSFSGVPTIYAAL 325
Cdd:PRK10252 631 --QNHYPLtaDDVVLQKTPCsFDVS--VWEFFWPFIAGAKLVMAEPEAHRDPLAMQQF---FAEYGVTTTHFVPSMLAAF 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 326 LQVPSD---GRDLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGE----RRPGSIGLRLPYC 398
Cdd:PRK10252 704 VASLTPegaRQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEelaaVRGSSVPIGYPVW 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 399 QVKVAVLDGEgnyLRDAAPNEVGNLCLKGPTVFKGYL-QQDRNRDIWIGDGW------FNTGDLGRIDEDGYIWLTGRSK 471
Cdd:PRK10252 784 NTGLRILDAR---MRPVPPGVAGDLYLTGIQLAQGYLgRPDLTASRFIADPFapgermYRTGDVARWLDDGAVEYLGRSD 860
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 472 DLI-IRgGHNIDPQMIEEALHRHP----AVALAAAVGKPDAKAGELP--VAYIQLKPGASASEEELLEHASRHVPErAAV 544
Cdd:PRK10252 861 DQLkIR-GQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARqlVGYLVSQSGLPLDTSALQAQLRERLPP-HMV 938
|
570 580
....*....|....*....|...
gi 15599055 545 PKDIWLIESMPVTAVGKTFKPAL 567
Cdd:PRK10252 939 PVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
42-577 |
2.42e-22 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 101.90 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 42 GQRIALscLLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQ-------------THYVIWGGEA 108
Cdd:PLN02654 103 GDKIAI--YWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMElpiamlacarigaVHSVVFAGFS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 109 AgivnainpllepEHIAELIRASNTRVLVT-------LAPFPGTDLWQkvAGLRAQLPELYAIVVVDPANLLPAPQREAL 181
Cdd:PLN02654 181 A------------ESLAQRIVDCKPKVVITcnavkrgPKTINLKDIVD--AALDESAKNGVSVGICLTYENQLAMKREDT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 182 KAQRGP---LPEGVLDFDTliaDCPADRLESgraihpDDVASYFHTGGTTGTPKLAPHSHFN-EVAMAEIMGLNADYGVD 257
Cdd:PLN02654 247 KWQEGRdvwWQDVVPNYPT---KCEVEWVDA------EDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 258 DVLLCGLPLFHVNGVMVTGLAPFHRGAQVLL-AGPQGYRNPTLIqdfWKLVERYRVTSFSGVPTIYAALLQvpsDGRDL- 335
Cdd:PLN02654 318 DVYWCTADCGWITGHSYVTYGPMLNGATVLVfEGAPNYPDSGRC---WDIVDKYKVTIFYTAPTLVRSLMR---DGDEYv 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 -----SSLRFALCGAAPMPVELIRQFEARTG---LKVIEGYGLTEgTCGTSCNPRGG--ERRPGSIglRLPYCQVKVAVL 405
Cdd:PLN02654 392 trhsrKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTE-TGGFMITPLPGawPQKPGSA--TFPFFGVQPVIV 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 406 DGEGNYLRDAAPnevGNLCLKG--PTVFKG-YLQQDRNRDIWIG--DGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHN 480
Cdd:PLN02654 469 DEKGKEIEGECS---GYLCVKKswPGAFRTlYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHR 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 481 IDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE---ELLEHASRHVPERAAvPKDIWLIESMPVT 557
Cdd:PLN02654 546 IGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEElrkSLILTVRNQIGAFAA-PDKIHWAPGLPKT 624
|
570 580
....*....|....*....|
gi 15599055 558 AVGKTFKPALRLDAIRRVLE 577
Cdd:PLN02654 625 RSGKIMRRILRKIASRQLDE 644
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-567 |
4.90e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 101.78 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 8 AGLSDIEALERVPLE--QRDLPsstyELLQRSARRHGQRIALscllhgsaAEEPLRISYAELFARVTQTANALHRLGLES 85
Cdd:PRK05691 1113 AERAQLAQWGQAPCApaQAWLP----ELLNEQARQTPERIAL--------VWDGGSLDYAELHAQANRLAHYLRDKGVGP 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 86 HQAVSFLLPNLPQTHYVIWG-GEAAGIVNAINPLLEPEHIAELIRASNTRVLVTLAPFPGtdlwqkvaglraqlpelyai 164
Cdd:PRK05691 1181 DVCVAIAAERSPQLLVGLLAiLKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLE-------------------- 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 165 vvvdpanllpapqrealkaqRGPLPEGV--LDFDTLIADCPADRlESGRAIHPDDVASYFHTGGTTGTPKLAPHSHfneV 242
Cdd:PRK05691 1241 --------------------RLPQAEGVsaIALDSLHLDSWPSQ-APGLHLHGDNLAYVIYTSGSTGQPKGVGNTH---A 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 243 AMAE-IMGLNADYGVD--DVLLCGLPL-FHVNgvMVTGLAPFHRGAQVLLAGPQGYRNPTLIQdfwKLVERYRVTSFSGV 318
Cdd:PRK05691 1297 ALAErLQWMQATYALDdsDVLMQKAPIsFDVS--VWECFWPLITGCRLVLAGPGEHRDPQRIA---ELVQQYGVTTLHFV 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 319 PTIYAALLQVPsDGRDLSSLRFALCGAAPMPVELI-RQFEARTGLKVIEGYGLTEGTCGTS---CNPRGGERRPgsIGlr 394
Cdd:PRK05691 1372 PPLLQLFIDEP-LAAACTSLRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTETAINVThwqCQAEDGERSP--IG-- 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 395 LPYCQVKVAVLDGEgnyLRDAAPNEVGNLCLKGPTVFKGYLQQ-----DR---NRDIWIGDGWFNTGDLGRIDEDGYIWL 466
Cdd:PRK05691 1447 RPLGNVLCRVLDAE---LNLLPPGVAGELCIGGAGLARGYLGRpaltaERfvpDPLGEDGARLYRTGDRARWNADGALEY 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 467 TGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELpVAYIQLKPGASASEEELLEHASRHVPERaAVPK 546
Cdd:PRK05691 1524 LGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQL-VGYYTGEAGQEAEAERLKAALAAELPEY-MVPA 1601
|
570 580
....*....|....*....|.
gi 15599055 547 DIWLIESMPVTAVGKTFKPAL 567
Cdd:PRK05691 1602 QLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
184-571 |
1.05e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.80 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 184 QRGPLPEGV----LDFDTLIADCPADrlESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDV 259
Cdd:PRK12316 4660 QRLPIPDGLaslaLDRDEDWEGFPAH--DPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDR 4737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 260 LLCGLPlFHVNGVMVTGLAPFHRGAQVLLAGPQGYRNPTLIQdfwkLVERYRVTSFSGVPTIYAALLQVPSDGRDLSSLR 339
Cdd:PRK12316 4738 VLQFMS-FSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYA----EIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 340 FALCGAAPMPVELIRQ-FEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGS----IGLRLPycQVKVAVLDGEGNYLrd 414
Cdd:PRK12316 4813 VYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAaympIGTPLG--NRSGYVLDGQLNPL-- 4888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 415 aAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGW-------FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMI 486
Cdd:PRK12316 4889 -PVGVAGELYLGGEGVARGYLERpALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEI 4967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 487 EEALHRHPAVALAAAVGKPDAKAGELpVAYI-----QLKPGASASEE---ELLEHASRHVPERaAVPKDIWLIESMPVTA 558
Cdd:PRK12316 4968 EARLREHPAVREAVVIAQEGAVGKQL-VGYVvpqdpALADADEAQAElrdELKAALRERLPEY-MVPAHLVFLARMPLTP 5045
|
410
....*....|....
gi 15599055 559 VGKTFKPAL-RLDA 571
Cdd:PRK12316 5046 NGKLDRKALpQPDA 5059
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
224-578 |
2.12e-21 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 97.91 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 224 TGGTTGTPKLAPHSHfnEVAMAEIMGLNADYGVD---DVLLCGLPLFHVNGvMVTGLAPFHRGAQVLLAgpqgyrnPTli 300
Cdd:PRK05851 160 TAGSTGTPRTAILSP--GAVLSNLRGLNARVGLDaatDVGCSWLPLYHDMG-LAFLLTAALAGAPLWLA-------PT-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 301 qdfwklveryrvTSFSGVPTIY--------AALLQVPS-------------DGRDLSSLRFALCGAAPMPVELIRQFE-- 357
Cdd:PRK05851 228 ------------TAFSASPFRWlswlsdsrATLTAAPNfaynligkyarrvSDVDLGALRVALNGGEPVDCDGFERFAta 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 358 -ARTGLK---VIEGYGLTEGTCGTSCnPRGGE---------------RRPGSIGLRLPYCQVKVAVLDGEgnylRDAAPN 418
Cdd:PRK05851 296 mAPFGFDagaAAPSYGLAESTCAVTV-PVPGIglrvdevttddgsgaRRHAVLGNPIPGMEVRISPGDGA----AGVAGR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 419 EVGNLCLKGPTVFKGYLQQDRNRdiwiGDGWFNTGDLGRIDEDGYIwLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVAL 498
Cdd:PRK05851 371 EIGEIEIRGASMMSGYLGQAPID----PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVRE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 499 AA--AVGKPDAKAGE-LPVAYIQLKPGASASEEELLEhasRHVPERAAVPKDIWLIE--SMPVTAVGKtfkpaLRLDAIR 573
Cdd:PRK05851 446 GAvvAVGTGEGSARPgLVIAAEFRGPDEAGARSEVVQ---RVASECGVVPSDVVFVApgSLPRTSSGK-----LRRLAVK 517
|
....*
gi 15599055 574 RVLEE 578
Cdd:PRK05851 518 RSLEA 522
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
215-568 |
8.43e-21 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 95.45 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDD-VLLCGLPLFHVN-GVMVTGLApfhRGAQVLLAGPQ 292
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrVAQVLSIAFDACiGEIFSTLC---NGGTLVLADPS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 gyrnptliqDFWKLVERyRVTSFSGVPTIYAALlqvpsDGRDLSSLRFALCGAAPMPVELIRQFeaRTGLKVIEGYGLTE 372
Cdd:cd17653 181 ---------DPFAHVAR-TVDALMSTPSILSTL-----SPQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 GTCGTSCnprgGERRPG---SIGLRLPYcqVKVAVLDGEgnyLRDAAPNEVGNLCLKGPTVFKGYLQQD-----RNRDIW 444
Cdd:cd17653 244 CTISSTM----TELLPGqpvTIGKPIPN--STCYILDAD---LQPVPEGVVGEICISGVQVARGYLGNPaltasKFVPDP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 445 IGDGW--FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHR-HPAVALAAAVgkpdaKAGELPVAYIQlkP 521
Cdd:cd17653 315 FWPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAI-----VVNGRLVAFVT--P 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15599055 522 gASASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd17653 388 -ETVDVDGLRSELAKHLP-SYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
215-561 |
1.53e-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: 95.25 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGY 294
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 -RNPTLiqdfW-KLVERYRVTSFSGVPTIYAALLQVPSDGR----DLSSLRFALCGAAPMPVELIRQFEART---GLK-- 363
Cdd:cd05908 185 iRRPIL----WlKKASEHKATIVSSPNFGYKYFLKTLKPEKandwDLSSIRMILNGAEPIDYELCHEFLDHMskyGLKrn 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 364 -VIEGYGLTEGTCGTSCNPRG---------------GERRPG------------SIGLRLPYCQVKVAvlDGEGNYLRDA 415
Cdd:cd05908 261 aILPVYGLAEASVGASLPKAQspfktitlgrrhvthGEPEPEvdkkdsecltfvEVGKPIDETDIRIC--DEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 416 ApneVGNLCLKGPTVFKGYLQQDR-NRDIWIGDGWFNTGDLGRIdEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHP 494
Cdd:cd05908 339 Y---IGHIQIRGKNVTPGYYNNPEaTAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELE 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599055 495 AVALA--AAVGKPDAKAGELPVAYIQLKpgaSASEEELLEHASR---HVPERAAVP-KDIWLIESMPVTAVGK 561
Cdd:cd05908 415 GVELGrvVACGVNNSNTRNEEIFCFIEH---RKSEDDFYPLGKKikkHLNKRGGWQiNEVLPIRRIPKTTSGK 484
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
32-567 |
2.26e-20 |
|
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: 94.70 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 32 ELLQRSARRHGQRIALSCllhgsaaeEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGG-EAAG 110
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVF--------EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGIlKAGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 111 IVNAINPLLEPEHIAELIRASNTRVLVTLAPFpgtdlwqkvaglraQLPELYAIVVVdpanllpapqrealkaqrgplpe 190
Cdd:cd17655 73 AYLPIDPDYPEERIQYILEDSGADILLTQSHL--------------QPPIAFIGLID----------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 191 gVLDFDTLIADcPADRLEsgRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMaeIMGLNADYGVDDVLLCGLplfhvn 270
Cdd:cd17655 116 -LLDEDTIYHE-ESENLE--PVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNL--VEWANKVIYQGEHLRVAL------ 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 271 gvmvtgLAPFHRGAQV------LLAG------PQGYRNPtlIQDFWKLVERYRVTSFSGVPTIYAALlqVPSDGRDLSSL 338
Cdd:cd17655 184 ------FASISFDASVteifasLLSGntlyivRKETVLD--GQALTQYIRQNRITIIDLTPAHLKLL--DAADDSEGLSL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 339 RFALCGAAPMPVELIRQFEARTGLKV--IEGYGLTEGT-CGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDgegNYLRDA 415
Cdd:cd17655 254 KHLIVGGEALSTELAKKIIELFGTNPtiTNAYGPTETTvDASIYQYEPETDQQVSVPIGKPLGNTRIYILD---QYGRPQ 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 416 APNEVGNLCLKGPTVFKGYLQQDR-------NRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLI-IRgGHNIDPQMIE 487
Cdd:cd17655 331 PVGVAGELYIGGEGVARGYLNRPEltaekfvDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVkIR-GYRIELGEIE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 488 EALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPgaSASEEELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd17655 410 ARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDY-MIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
214-568 |
3.30e-20 |
|
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: 94.15 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPK--LAPHSHFNEVAMA--EIMGLNAD--------YGVDdvllcgLPLFHVngvmvtgLAPFH 281
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKgvVIEHRALSTSALAhgRALGLTSEsrvlqfasYTFD------VSILEI-------FTTLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 282 RGAQVLLAgpqgyRNPTLIQDFWKLVERYRVTSFSGVPTIyAALLQvPSDgrdLSSLRFALCGAAPMPVELIRQFEARTg 361
Cdd:cd05918 171 AGGCLCIP-----SEEDRLNDLAGFINRLRVTWAFLTPSV-ARLLD-PED---VPSLRTLVLGGEALTQSDVDTWADRV- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 362 lKVIEGYGLTEGTCGTSCNPRGGERRPGSIGlrLPYCQVkVAVLDgEGNYLRDAAPNEVGNLCLKGPTVFKGYL-QQDRN 440
Cdd:cd05918 240 -RLINAYGPAECTIAATVSPVVPSTDPRNIG--RPLGAT-CWVVD-PDNHDRLVPIGAVGELLIEGPILARGYLnDPEKT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 441 RDIWIGD-GW------------FNTGDLGRIDEDGYIWLTGRSKDLI-IRgGHNIDPQMIEEALHRHPAVALAAAVG--- 503
Cdd:cd05918 315 AAAFIEDpAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVkIR-GQRVELGEIEHHLRQSLPGAKEVVVEvvk 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 504 KPDAKAGELPVAYIQLKPGASASEE-----------------ELLEHASRHVPeRAAVPkDIWL-IESMPVTAVGKTFKP 565
Cdd:cd05918 394 PKDGSSSPQLVAFVVLDGSSSGSGDgdslflepsdefralvaELRSKLRQRLP-SYMVP-SVFLpLSHLPLTASGKIDRR 471
|
...
gi 15599055 566 ALR 568
Cdd:cd05918 472 ALR 474
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
50-561 |
1.45e-19 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 92.72 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 50 LLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQThyVIwGGEAAGIVNAI----NPLLEPEHIA 125
Cdd:cd05943 87 AIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEA--VV-AMLATASIGAIwsscSPDFGVPGVL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 126 ELIRASNTRVLVTLAPF----PGTDLWQKVAGLRAQLPELYAIVVVD------PANLLPAPQREALKAQRGPLPEGVLDF 195
Cdd:cd05943 164 DRFGQIEPKVLFAVDAYtyngKRHDVREKVAELVKGLPSLLAVVVVPytvaagQPDLSKIAKALTLEDFLATGAAGELEF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 196 DTLiadcPADrlesgraiHPDDVasyFHTGGTTGTPKLAPHSHFNEV--AMAEIMgLNADYGVDDVLL----CGLPLFHv 269
Cdd:cd05943 244 EPL----PFD--------HPLYI---LYSSGTTGLPKCIVHGAGGTLlqHLKEHI-LHCDLRPGDRLFyyttCGWMMWN- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 270 ngVMVTGLAPfhrGAQ-VLLAGPQGYRNPTLiqdFWKLVERYRVTSFSGVPTIYAALLQ---VPSDGRDLSSLRFALCGA 345
Cdd:cd05943 307 --WLVSGLAV---GATiVLYDGSPFYPDTNA---LWDLADEEGITVFGTSAKYLDALEKaglKPAETHDLSSLRTILSTG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 346 APMPVE----LIRQFEARTGLKVIEGyglteGT----CGTSCNP----RGGErrpgsigLRLPYCQVKVAVLDGEGNYLR 413
Cdd:cd05943 379 SPLKPEsfdyVYDHIKPDVLLASISG-----GTdiisCFVGGNPllpvYRGE-------IQCRGLGMAVEAFDEEGKPVW 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 414 DaapnEVGNL-CLKG----PTVF----------KGYLqqDRNRDIWigdgwfNTGDLGRIDEDGYIWLTGRSKDLIIRGG 478
Cdd:cd05943 447 G----EKGELvCTKPfpsmPVGFwndpdgsryrAAYF--AKYPGVW------AHGDWIEITPRGGVVILGRSDGTLNPGG 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 479 HNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE-------ELLEHAS-RHVPERAAVPKDIwl 550
Cdd:cd05943 515 VRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDElrkrirsTIRSALSpRHVPAKIIAVPDI-- 592
|
570
....*....|.
gi 15599055 551 iesmPVTAVGK 561
Cdd:cd05943 593 ----PRTLSGK 599
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
486-561 |
1.99e-19 |
|
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: 82.59 E-value: 1.99e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599055 486 IEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEEELLEHASRHVPErAAVPKDIWLIESMPVTAVGK 561
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGP-YAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
215-493 |
1.06e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 89.88 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMGLNADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAgpqgy 294
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFA----- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPS-DGRDLSSLRFALCGAAPMPVELiRQFEARTGLKVI--EGYGLT 371
Cdd:PRK06334 257 YNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKkQESCLPSLRFVVIGGDAFKDSL-YQEALKTFPHIQlrQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 372 EGTCGTSCNPRGGERRPGSIGLrlPYCQVKVAVLDGEGNYlrDAAPNEVGNLCLKGPTVFKGYLQQDRNRDI--WIGDGW 449
Cdd:PRK06334 336 ECSPVITINTVNSPKHESCVGM--PIRGMDVLIVSEETKV--PVSSGETGLVLTRGTSLFSGYLGEDFGQGFveLGGETW 411
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15599055 450 FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRH 493
Cdd:PRK06334 412 YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-567 |
6.97e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 22 EQRDLPSSTYELLQRSARRHGQRIALSCLLH----GSAAEEPLRI---------SYAELFARVTQTANALHRLGLESHQA 88
Cdd:PRK12316 1976 ELALLDAGERQRILADWDRTPEAYPRGPGVHqriaEQAARAPEAIavvfgdqhlSYAELDSRANRLAHRLRARGVGPEVR 2055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 89 VSFLLPNLPQTHYVIWGG-EAAGIVNAINPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkvaglraqlpelyaivvv 167
Cdd:PRK12316 2056 VAIAAERSFELVVALLAVlKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT----------------------------- 2106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 168 dpanllpapQREALkaQRGPLPEGV--LDFDTL--IADCPADRLESgrAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVA 243
Cdd:PRK12316 2107 ---------QRHLL--ERLPLPAGVarLPLDRDaeWADYPDTAPAV--QLAGENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 244 MAEIMGLNADYGVDDVLLCGLPlFHVNGVMVTGLAPFHRGAQVLLaGPQGYRNPtliQDFWKLVERYRVTSFSGVPTIYA 323
Cdd:PRK12316 2174 HCQAAGERYELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLI-RDDELWDP---EQLYDEMERHGVTILDFPPVYLQ 2248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 324 ALLQVPSDGRDLSSLRFALCGAAPMPVELIRQ-FEARTGLKVIEGYGLTEGTCGTS---CNPRGGERRPGS-IGLRLPyc 398
Cdd:PRK12316 2249 QLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLlwkCRPQDPCGAAYVpIGRALG-- 2326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 399 QVKVAVLDGEGNYLrdaAPNEVGNLCLKGPTVFKGYLqqdrNR----------DIWIGDG--WFNTGDLGRIDEDGYIWL 466
Cdd:PRK12316 2327 NRRAYILDADLNLL---APGMAGELYLGGEGLARGYL----NRpgltaerfvpDPFSASGerLYRTGDLARYRADGVVEY 2399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 467 TGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKpDAKAGELPVAYIQLKPGASASEEELLEHASRHVPERaAVPK 546
Cdd:PRK12316 2400 LGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAY-MVPA 2477
|
570 580
....*....|....*....|.
gi 15599055 547 DIWLIESMPVTAVGKTFKPAL 567
Cdd:PRK12316 2478 HWVVLERLPLNPNGKLDRKAL 2498
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
215-496 |
4.72e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 85.17 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVA-MAEIMGLNADYGVDDVLLCGLPLFHVngvmvtglapFHRGAQVLLAGPQ- 292
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVAtVAGVMTVVPKLGKNDVYLAYLPLAHI----------LELAAESVMAAVGa 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 293 --GYRNP-TLIQDFWKL-------VERYRVTSFSGVPTIY-----AALLQVPSDG------------RDLSS-------- 337
Cdd:PLN02387 319 aiGYGSPlTLTDTSNKIkkgtkgdASALKPTLMTAVPAILdrvrdGVRKKVDAKGglakklfdiaykRRLAAiegswfga 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 338 -----------------------LRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEgTCGTSCNPRGGERRPGSIGLR 394
Cdd:PLN02387 399 wglekllwdalvfkkiravlggrIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTE-TCAGATFSEWDDTSVGRVGPP 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 395 LPYCQVKVAVLDgEGNYLRDAAPNEVGNLCLKGPTVFKGYLQ-QDRNRDIWIGDG----WFNTGDLGRIDEDGYIWLTGR 469
Cdd:PLN02387 478 LPCCYVKLVSWE-EGGYLISDKPMPRGEIVIGGPSVTLGYFKnQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDR 556
|
330 340
....*....|....*....|....*...
gi 15599055 470 SKDLI-IRGGHNIDPQMIEEALHRHPAV 496
Cdd:PLN02387 557 KKDIVkLQHGEYVSLGKVEAALSVSPYV 584
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
61-510 |
1.29e-16 |
|
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: 82.86 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 61 RISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQthYV-IWGGEAA-GIVNA-INPLLEPEHIAELIRASNTRVLV 137
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLE--FVaLWLGLAKiGVETAlINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 138 TlapfpgtdlwqkvaglraqlpelyaivvvdpaNLLpapqrEALKAQRGPLPEGVLDFDTliadcpadrlesgraihpDD 217
Cdd:cd05939 81 F--------------------------------NLL-----DPLLTQSSTEPPSQDDVNF------------------RD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 218 VASYFHTGGTTGTPKLAPHSHFNEVAMAeiMGLNADYGV--DDVLLCGLPLFH-VNGVMVTGLAPFHrGAQVLLagpqgy 294
Cdd:cd05939 106 KLFYIYTSGTTGLPKAAVIVHSRYYRIA--AGAYYAFGMrpEDVVYDCLPLYHsAGGIMGVGQALLH-GSTVVI------ 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RNPTLIQDFWKLVERYRVTSFSGVPTIYAALL-QVPSDGRDLSSLRFALcGAAPMPvELIRQFEARTGLKVI-EGYGLTE 372
Cdd:cd05939 177 RKKFSASNFWDDCVKYNCTIVQYIGEICRYLLaQPPSEEEQKHNVRLAV-GNGLRP-QIWEQFVRRFGIPQIgEFYGATE 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 GTCgtscNPRGGERRPGSIGL--RLP---YCQVKVAVLDGEGNYLRDA-------APNE----VGNLCLKGPTV-FKGYL 435
Cdd:cd05939 255 GNS----SLVNIDNHVGACGFnsRILpsvYPIRLIKVDEDTGELIRDSdglcipcQPGEpgllVGKIIQNDPLRrFDGYV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 436 QQDRN-----RDIWI-GDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHR----HPAVALAAAVGKP 505
Cdd:cd05939 331 NEGATnkkiaRDVFKkGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNvlglEDVVVYGVEVPGV 410
|
....*
gi 15599055 506 DAKAG 510
Cdd:cd05939 411 EGRAG 415
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
40-576 |
1.66e-16 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 83.31 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 40 RHGQRIALsclLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQThyVIwGGEAAGIVNAI---- 115
Cdd:PRK03584 96 RRDDRPAI---IFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPET--VV-AMLATASLGAIwssc 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 116 NPLLEPEHIAELIRASNTRVLVTLA--PFPGT--DLWQKVAGLRAQLPELYAIVVVDPANLLPApqrealkaqrGPLPEG 191
Cdd:PRK03584 170 SPDFGVQGVLDRFGQIEPKVLIAVDgyRYGGKafDRRAKVAELRAALPSLEHVVVVPYLGPAAA----------AAALPG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 192 VLDFDTLIADCPADRLESGRAI--HPDDVasyFHTGGTTGTPKLAPHS-------HFNEvamaeiMGLNADYGVDDVLL- 261
Cdd:PRK03584 240 ALLWEDFLAPAEAAELEFEPVPfdHPLWI---LYSSGTTGLPKCIVHGhggilleHLKE------LGLHCDLGPGDRFFw 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 262 ---CGLplfhvngVM----VTGLApfhRGAQVLL-AGPQGYRNPtliQDFWKLVERYRVTSFSGVPTIYAALLQ---VPS 330
Cdd:PRK03584 311 yttCGW-------MMwnwlVSGLL---VGATLVLyDGSPFYPDP---NVLWDLAAEEGVTVFGTSAKYLDACEKaglVPG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 331 DGRDLSSLRFALCGAAPMPVE----LIRQFEARTGLKVIEGyglteGTCGTSC----NP----RGGErrpgsigLRLPYC 398
Cdd:PRK03584 378 ETHDLSALRTIGSTGSPLPPEgfdwVYEHVKADVWLASISG-----GTDICSCfvggNPllpvYRGE-------IQCRGL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 399 QVKVAVLDGEGNYLRDaapnEVGNL-CLKG----PTVFKGYLQQDRNRdiwigDGWFNT-------GDLGRIDEDGYIWL 466
Cdd:PRK03584 446 GMAVEAWDEDGRPVVG----EVGELvCTKPfpsmPLGFWNDPDGSRYR-----DAYFDTfpgvwrhGDWIEITEHGGVVI 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 467 TGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE-------ELLEHAS-RHV 538
Cdd:PRK03584 517 YGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDAlrarirtTIRTNLSpRHV 596
|
570 580 590
....*....|....*....|....*....|....*....
gi 15599055 539 PER-AAVPkDIwliesmPVTAVGKTfkpaLRLdAIRRVL 576
Cdd:PRK03584 597 PDKiIAVP-DI------PRTLSGKK----VEL-PVKKLL 623
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
213-568 |
3.59e-16 |
|
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: 81.32 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 213 IHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAEIMG--LNADYGvDDVLLCgLPLFHVNGVMVTGLAPFHRGAQVLLAG 290
Cdd:cd05937 84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLShdLNLKNG-DRTYTC-MPLYHGTAAFLGACNCLMSGGTLALSR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 291 PQGYRNptliqdFWKLVERYRVTSFSGVPTIYAALLQVPSDGRDLSSLRFALCGAAPMPvELIRQFEARTGLKVI-EGYG 369
Cdd:cd05937 162 KFSASQ------FWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRP-DIWERFRERFNVPEIgEFYA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 370 LTEGTcGTSCNPRGGERRPGSIGLR-------LPYCQVKVAVLDGEGNYLRD--------AAPNEVG----NLCLKGPTV 430
Cdd:cd05937 235 ATEGV-FALTNHNVGDFGAGAIGHHglirrwkFENQVVLVKMDPETDDPIRDpktgfcvrAPVGEPGemlgRVPFKNREA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 431 FKGYL------QQDRNRDIW-IGDGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVG 503
Cdd:cd05937 314 FQGYLhnedatESKLVRDVFrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599055 504 ----KPDAKAGelpVAYIQLKPGASASEE----ELLEHASRHVPeRAAVPKDIWLIESMPVTAVGKTFKPALR 568
Cdd:cd05937 394 vkvpGHDGRAG---CAAITLEESSAVPTEftksLLASLARKNLP-SYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
216-497 |
2.20e-15 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 78.65 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 DDVASYFHTGGTTGTPKLAPHShFNEVAM-AEIMGLN-ADYGV---DDVLLC-GLPLFhvngvmVTGLApFHRGAQ---- 285
Cdd:COG1541 83 EEIVRIHASSGTTGKPTVVGYT-RKDLDRwAELFARSlRAAGVrpgDRVQNAfGYGLF------TGGLG-LHYGAErlga 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 286 -VLLAGPQgyrNPTLIqdfWKLVERYRVTSFSGVPTiYAALL--QVPSDGRDL--SSLRFALCGAAPMPVELIRQFEART 360
Cdd:COG1541 155 tVIPAGGG---NTERQ---LRLMQDFGPTVLVGTPS-YLLYLaeVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 361 GLKVIEGYGLTEGTCGTSCNPRGGErrpgsiGLRLPYCQVKVAVLDGEGnyLRDAAPNEVGNLCLkgpTVFkgylqqDRN 440
Cdd:COG1541 228 GIKAYDIYGLTEVGPGVAYECEAQD------GLHIWEDHFLVEIIDPET--GEPVPEGEEGELVV---TTL------TKE 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599055 441 -----RdiwigdgwFNTGDLGRIDED-----------GYIwlTGRSKD-LIIRGGhNIDPQMIEEALHRHPAVA 497
Cdd:COG1541 291 ampliR--------YRTGDLTRLLPEpcpcgrthpriGRI--LGRADDmLIIRGV-NVFPSQIEEVLLRIPEVG 353
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
18-461 |
3.90e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 78.93 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 18 RVPLEqrDLPSSTYELLQRSARRHGQRIALScllHGSAAEEPLR-ISYAELFARVTQTANALHRLGLESHQAVSFLLPNL 96
Cdd:PRK12582 41 RHPLG--PYPRSIPHLLAKWAAEAPDRPWLA---QREPGHGQWRkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 97 PQTHYVIWGGEAAGIVNA-INP--------LLEPEHIAELIRASntRVLV-TLAPFPGTdlwqkVAGLRAQLPELyaiVV 166
Cdd:PRK12582 116 IEHALMTLAAMQAGVPAApVSPayslmshdHAKLKHLFDLVKPR--VVFAqSGAPFARA-----LAALDLLDVTV---VH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 167 VDPAnllpapqrealkaqrgPLPEGVLDFDTLIADCPADRLESGRA-IHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMA 245
Cdd:PRK12582 186 VTGP----------------GEGIASIAFADLAATPPTAAVAAAIAaITPDTVAKYLFTSGSTGMPKAVINTQRMMCANI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 246 EIMGLNADYGVDD---VLLCGLPLFHVNGvmvtGLAPFHrgaQVLLAGPQGYRNP--TLIQDFWKLVERYRVTS---FSG 317
Cdd:PRK12582 250 AMQEQLRPREPDPpppVSLDWMPWNHTMG----GNANFN---GLLWGGGTLYIDDgkPLPGMFEETIRNLREISptvYGN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 318 VPTIYAALLQVPSDGRDL-----SSLRFALCGAAPMPVELIRQFEA----RTG--LKVIEGYGLTEgTCGTSCNPRGGER 386
Cdd:PRK12582 323 VPAGYAMLAEAMEKDDALrrsffKNLRLMAYGGATLSDDLYERMQAlavrTTGhrIPFYTGYGATE-TAPTTTGTHWDTE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 387 RPGSIGLRLPYCQVKVAVLdGEGNYLRdaapnevgnlcLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGR-IDED 461
Cdd:PRK12582 402 RVGLIGLPLPGVELKLAPV-GDKYEVR-----------VKGPNVTPGYHKDpELTAAAFDEEGFYRLGDAARfVDPD 466
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
18-461 |
4.87e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 78.38 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 18 RVPLEQRDLPSSTYELLQRSARRHGQRIALScllHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLP 97
Cdd:PRK08180 29 RSAEPLGDYPRRLTDRLVHWAQEAPDRVFLA---ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 98 QTHYVIWGGEAAGI-VNAINP--------LLEPEHIAELIR-----ASNTrvlvtlAPFpgtdlwqkVAGLRAQLPELYA 163
Cdd:PRK08180 106 EHALLALAAMYAGVpYAPVSPayslvsqdFGKLRHVLELLTpglvfADDG------AAF--------ARALAAVVPADVE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 164 IVVVdpanllpapqrealkaqRGPLPE-GVLDFDTLIADCPADRL-ESGRAIHPDDVASYFHTGGTTGTPKLAPHSH--- 238
Cdd:PRK08180 172 VVAV-----------------RGAVPGrAATPFAALLATPPTAAVdAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHrml 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 239 -FNEVAMAEIMGLNADYGVddVLLCGLPLFHV-NGVMVTGLAPFHRGAQVLLAG---PQGY----RNPTLIQDfwklver 309
Cdd:PRK08180 235 cANQQMLAQTFPFLAEEPP--VLVDWLPWNHTfGGNHNLGIVLYNGGTLYIDDGkptPGGFdetlRNLREISP------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 310 yrvTSFSGVPTIYAALLQVPSDGRDL-----SSLRFALCGAAPMPV----ELIRQFEARTGLKV--IEGYGLTEgTCGTS 378
Cdd:PRK08180 306 ---TVYFNVPKGWEMLVPALERDAALrrrffSRLKLLFYAGAALSQdvwdRLDRVAEATCGERIrmMTGLGMTE-TAPSA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 379 CNPRGGERRPGSIGLRLPYCQVKVAVLDG--EgnylrdaapnevgnLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDL 455
Cdd:PRK08180 382 TFTTGPLSRAGNIGLPAPGCEVKLVPVGGklE--------------VRVKGPNVTPGYWRApELTAEAFDEEGYYRSGDA 447
|
....*..
gi 15599055 456 GR-IDED 461
Cdd:PRK08180 448 VRfVDPA 454
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
203-561 |
5.00e-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: 77.83 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 203 PADRLE------SGRAI--HPDDVASYFHTGGTTGTPKLAPHSHFNEVAMaeIMGLNADYGVDD-----VLLCGLPLF-- 267
Cdd:cd17648 73 PDERIQfiledtGARVVitNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNL--RTSLSERYFGRDngdeaVLFFSNYVFdf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 268 HVNGVMVTGLapfhrGAQVLLAGPQGYRNPTliQDFWKLVERYRVTSFSGVPTiyaaLLQVPSDGRdLSSLRFALCGAAP 347
Cdd:cd17648 151 FVEQMTLALL-----NGQKLVVPPDEMRFDP--DRFYAYINREKVTYLSGTPS----VLQQYDLAR-LPHLKRVDAAGEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 348 MPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNP-RGGERRPGSIGLRLPycQVKVAVLDGEgnyLRDAAPNEVGNLCLK 426
Cdd:cd17648 219 FTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFfPGDQRFDKSLGRPVR--NTKCYVLNDA---MKRVPVGAVGELYLG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 427 GPTVFKGYLQQD---RNRDI--------WIGDG----WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALH 491
Cdd:cd17648 294 GDGVARGYLNRPeltAERFLpnpfqteqERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALA 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 492 RHPAVALAAAVGKPDAKAGELP-----VAYIQLKPGAsASEEELLEHASRHVPeRAAVPKDIWLIESMPVTAVGK 561
Cdd:cd17648 374 SYPGVRECAVVAKEDASQAQSRiqkylVGYYLPEPGH-VPESDLLSFLRAKLP-RYMVPARLVRLEGIPVTINGK 446
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
302-561 |
7.28e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 77.86 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 302 DFWKLVERYRVTSFSGVPTIYAALLQVPSDGR------DLSSLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTC 375
Cdd:PTZ00237 340 DLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATiirskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGI 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 376 gTSCNPRGGERRPGSiGLRLPYCQVKVAVLDGEGNYLRDaapNEVGNLCLKGP------TVFkgYLQQDRNRDIWIG-DG 448
Cdd:PTZ00237 420 -TYLYCYGHINIPYN-ATGVPSIFIKPSILSEDGKELNV---NEIGEVAFKLPmppsfaTTF--YKNDEKFKQLFSKfPG 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 449 WFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAYIQLKPGASASEE 528
Cdd:PTZ00237 493 YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSI 572
|
250 260 270
....*....|....*....|....*....|....*....
gi 15599055 529 ELLEHASR------HVPERAAVPKDIWLIESMPVTAVGK 561
Cdd:PTZ00237 573 DLNKLKNEinniitQDIESLAVLRKIIIVNQLPKTKTGK 611
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
215-567 |
8.30e-15 |
|
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: 77.09 E-value: 8.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHSHFNEVAMAeiMGLNADYGV---DDVLLCGLPLFHVNG--VMVTglapFHRGAQVLLA 289
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLS--HGLIKEYGItssDRVLQFASIAFDVAAeeIYVT----LLSGATLVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 290 GPQGYRNPTliqDFWKLVERYRVTSFSgVPTIY-----AALLQVPSDGrdLSSLRFALCGAAPMPVELIRQFEARTGLKV 364
Cdd:cd17644 179 PEEMRSSLE---DFVQYIQQWQLTVLS-LPPAYwhllvLELLLSTIDL--PSSLRLVIVGGEAVQPELVRQWQKNVGNFI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 365 --IEGYGLTEGTCGTS-CNPRG-GERRPGSIGLRLPYCQVKVAVLDgegNYLRDAAPNEVGNLCLKGPTVFKGYLQQDR- 439
Cdd:cd17644 253 qlINVYGPTEATIAATvCRLTQlTERNITSVPIGRPIANTQVYILD---ENLQPVPVGVPGELHIGGVGLARGYLNRPEl 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 440 NRDIWIGDGW--------FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGE 511
Cdd:cd17644 330 TAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNK 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599055 512 LPVAYIQLKPGASASEEELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd17644 410 RLVAYIVPHYEESPSTVELRQFLKAKLPDY-MIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
34-457 |
1.05e-14 |
|
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: 77.09 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 34 LQRSARRHGQRIalsCLLHGSAAEEPLRISYAELFARVTQTANALHRLGLESHQAVSFLLPNLPQTHYVIWGGEAAGIVN 113
Cdd:cd05921 1 LAHWARQAPDRT---WLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 114 A-INP--------LLEPEHIAELIRasntrvlvtlapfPGTDLWQKVAGLRAqlpelyAIVVVDPANLlpapqreALKAQ 184
Cdd:cd05921 78 ApVSPayslmsqdLAKLKHLFELLK-------------PGLVFAQDAAPFAR------ALAAIFPLGT-------PLVVS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 185 RGPLP-EGVLDFDTLIADCP-ADRLESGRAIHPDDVASYFHTGGTTGTPKLAPHSHFNEVAMAE-IMGLNADYGVDD-VL 260
Cdd:cd05921 132 RNAVAgRGAISFAELAATPPtAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAmLEQTYPFFGEEPpVL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 261 LCGLPLFHVNGVMVTGLAPFHRGAQVLLAGpqGYRNPTLIQDFWKLVERYRVTSFSGVPTIYAALLQVPSDGRDL----- 335
Cdd:cd05921 212 VDWLPWNHTFGGNHNFNLVLYNGGTLYIDD--GKPMPGGFEETLRNLREISPTVYFNVPAGWEMLVAALEKDEALrrrff 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 SSLRFALCGAAPMPVE----LIRQFEARTGLKV--IEGYGLTEgTCGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGEG 409
Cdd:cd05921 290 KRLKLMFYAGAGLSQDvwdrLQALAVATVGERIpmMAGLGATE-TAPTATFTHWPTERSGLIGLPAPGTELKLVPSGGKY 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 15599055 410 NyLRdaapnevgnlcLKGPTVFKGYLQQ-DRNRDIWIGDGWFNTGDLGR 457
Cdd:cd05921 369 E-VR-----------VKGPNVTPGYWRQpELTAQAFDEEGFYCLGDAAK 405
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
214-474 |
1.32e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 77.16 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPKLAPHSHfnEVAMAEIMGLNA-------DYGVDDVLLCGLPLFHVNGVMVTGLApFHRGAQV 286
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTH--EAVATFVRGVDLfmeqfedKMTHDDVYLSFLPLAHILDRMIEEYF-FRKGASV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 287 llagpqGYRN---PTLIQDFWKLveryRVTSFSGVPTIYAAL-------LQVPSDGRDL--------------------- 335
Cdd:PLN02430 295 ------GYYHgdlNALRDDLMEL----KPTLLAGVPRVFERIhegiqkaLQELNPRRRLifnalykyklawmnrgyshkk 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 336 ------------------SSLRFALCGAAPMPVElIRQFEARTGLK-VIEGYGLTEgTCG--TSCNPrGGERRPGSIGLR 394
Cdd:PLN02430 365 aspmadflafrkvkaklgGRLRLLISGGAPLSTE-IEEFLRVTSCAfVVQGYGLTE-TLGptTLGFP-DEMCMLGTVGAP 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 395 LPYCQVKVA-VLDGEGNYLRDaapNEVGNLCLKGPTVFKGYLQQDRNRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDL 473
Cdd:PLN02430 442 AVYNELRLEeVPEMGYDPLGE---PPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNL 518
|
.
gi 15599055 474 I 474
Cdd:PLN02430 519 I 519
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
215-473 |
1.47e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 76.98 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 215 PDDVASYFHTGGTTGTPKLAPHShfNEVAMAEIMGL-------NADYGVDDVLLCGLPLFHVNG-------VMVTGLAPF 280
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMIS--NESIVTLIAGVirllksaNAALTVKDVYLSYLPLAHIFDrvieecfIQHGAAIGF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 281 HRGAQVLLAGPQGYRNPTLIQDFWKLVERyrvtsfsgvptIYAALLQVPSDGRDLS------------------------ 336
Cdd:PLN02614 300 WRGDVKLLIEDLGELKPTIFCAVPRVLDR-----------VYSGLQKKLSDGGFLKkfvfdsafsykfgnmkkgqshvea 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 337 ------------------SLRFALCGAAPMPVELIRQFEARTGLKVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPYC 398
Cdd:PLN02614 369 splcdklvfnkvkqglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNV 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 399 QVKVAVLDgEGNYlrDA-APNEVGNLCLKGPTVFKGYLQ-QDRNRDIWIgDGWFNTGDLGRIDEDGYIWLTGRSKDL 473
Cdd:PLN02614 449 DIRLESVP-EMEY--DAlASTPRGEICIRGKTLFSGYYKrEDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNI 521
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
224-561 |
1.55e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 75.84 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 224 TGGTTGTPKLAPHShFNEVAmAEIMGLNADYGVDDVL----LCglPLFHVNGVMVTGLAPFHRGAQVLLAGPQgyrNPTL 299
Cdd:PRK08308 109 SSGTTGEPKLIRRS-WTEID-REIEAYNEALNCEQDEtpivAC--PVTHSYGLICGVLAALTRGSKPVIITNK---NPKF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 300 IqdfWKLVERYRVTSFSGVPTIYAALLQVPSDGRDLSSlrfALCGAAPMPVELIRQFEARTgLKVIEGYGLTEGTCgTSC 379
Cdd:PRK08308 182 A---LNILRNTPQHILYAVPLMLHILGRLLPGTFQFHA---VMTSGTPLPEAWFYKLRERT-TYMMQQYGCSEAGC-VSI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 380 NPRggERRPGSIGLRLPYCQVKVAvlDGEGNylrdaaPNEVgnlclkgptvfkgylqqdrnrDIWIGDGWFNTGDLGRID 459
Cdd:PRK08308 254 CPD--MKSHLDLGNPLPHVSVSAG--SDENA------PEEI---------------------VVKMGDKEIFTKDLGYKS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 460 EDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVAyiQLKPGASASEEELLEHASRHVP 539
Cdd:PRK08308 303 ERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA--KVISHEEIDPVQLREWCIQHLA 380
|
330 340
....*....|....*....|..
gi 15599055 540 ERaAVPKDIWLIESMPVTAVGK 561
Cdd:PRK08308 381 PY-QVPHEIESVTEIPKNANGK 401
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
252-565 |
4.33e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 75.91 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 252 ADYGVDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAgpQGYRNPTLIQDfwklVERYRVTSFSGVPTIYAALLQVPSd 331
Cdd:PRK07868 641 AALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALS--RGLDPDRFVQE----VRQYGVTVVSYTWAMLREVVDDPA- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 332 grdlsslrFALCGAAP--------MPVELIRQF-EARTGLKVIEGYGLTEGTCgTSCNPRGGerRPGSIGLRLP-YCQVK 401
Cdd:PRK07868 714 --------FVLHGNHPvrlfigsgMPTGLWERVvEAFAPAHVVEFFATTDGQA-VLANVSGA--KIGSKGRPLPgAGRVE 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 402 VA--------VLDGEGNYLRDAAPNEVGNLCLK--GPTVFKGYLQqdrnRDIWI-GDGWFNTGDLGRIDEDGYIWLTGRs 470
Cdd:PRK07868 783 LAaydpehdlILEDDRGFVRRAEVNEVGVLLARarGPIDPTASVK----RGVFApADTWISTEYLFRRDDDGDYWLVDR- 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 471 KDLIIRGGHN-IDPQMIEEALHRHPAVALAAAVGKPDAkAGELPVAYIQLKPGASASEEELLEH-ASRHVPERaavPKDI 548
Cdd:PRK07868 858 RGSVIRTARGpVYTEPVTDALGRIGGVDLAVTYGVEVG-GRQLAVAAVTLRPGAAITAADLTEAlASLPVGLG---PDIV 933
|
330
....*....|....*..
gi 15599055 549 WLIESMPVTAvgkTFKP 565
Cdd:PRK07868 934 HVVPEIPLSA---TYRP 947
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
214-511 |
6.11e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 74.88 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 214 HPDDVASYFHTGGTTGTPKLAPHShfNEVAMAEIMGLN-----ADYGV--DDVLLCGLPLFHVNGvMVTGLAPFHRGAQV 286
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILT--NRAIIAEVLSTDhllkvTDRVAteEDSYFSYLPLAHVYD-QVIETYCISKGASI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 287 llagpqgyrnptliqDFWKLVERY--------RVTSFSGVP----TIYAALLQVPSDGRDLSS----------------- 337
Cdd:PLN02861 295 ---------------GFWQGDIRYlmedvqalKPTIFCGVPrvydRIYTGIMQKISSGGMLRKklfdfaynyklgnlrkg 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 338 -------------------------LRFALCGAAPMPVElIRQFEARTGLKVI-EGYGLTEgTCGTSCNPRGGE-RRPGS 390
Cdd:PLN02861 360 lkqeeasprldrlvfdkikeglggrVRLLLSGAAPLPRH-VEEFLRVTSCSVLsQGYGLTE-SCGGCFTSIANVfSMVGT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 391 IGLRLPYCQVKVAVLDGEGNYLRDAAPNevGNLCLKGPTVFKGYLQ-QDRNRDIWIgDGWFNTGDLGRIDEDGYIWLTGR 469
Cdd:PLN02861 438 VGVPMTTIEARLESVPEMGYDALSDVPR--GEICLRGNTLFSGYHKrQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDR 514
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15599055 470 SKDLI-IRGGHNIDPQMIEEALHRHPAVA-----------LAAAVGKPDAKAGE 511
Cdd:PLN02861 515 KKNIFkLSQGEYVAVENLENTYSRCPLIAsiwvygnsfesFLVAVVVPDRQALE 568
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
223-567 |
1.51e-13 |
|
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: 73.28 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 223 HTGGTTGTPKLaphshfneVAMAE------IMGLNADYGV--DDVLLCGLPLFHVNGVMVTGLApFHRGAqVLLAGPQGY 294
Cdd:cd17654 125 HTSGTTGTPKI--------VAVPHkcilpnIQHFRSLFNItsEDILFLTSPLTFDPSVVEIFLS-LSSGA-TLLIVPTSV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 295 RN-PTLIQDFwkLVERYRVTSFSGVPTIYAALLQVPSDGRDLS---SLRFALCGAAPMPVELI----RQFEARTglKVIE 366
Cdd:cd17654 195 KVlPSKLADI--LFKRHRITVLQATPTLFRRFGSQSIKSTVLSatsSLRVLALGGEPFPSLVIlsswRGKGNRT--RIFN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 367 GYGLTEGTCGTSCNPRGGERRPGSIGLRlpycqvkvavLDGEGNYLRDAAPNEV-GNLCLKGptVFKGYLQQDRNrDIWI 445
Cdd:cd17654 271 IYGITEVSCWALAYKVPEEDSPVQLGSP----------LLGTVIEVRDQNGSEGtGQVFLGG--LNRVCILDDEV-TVPK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 446 GDgWFNTGDLGRIdEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVaLAAAVGKPDAkagELPVAYIQLKPGASA 525
Cdd:cd17654 338 GT-MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESSSSR 411
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15599055 526 SEEELlehaSRHVPERAAVPKDIWLIESMPVTAVGKTFKPAL 567
Cdd:cd17654 412 IHKEL----QLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
334-567 |
8.00e-13 |
|
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: 70.66 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 334 DLSSLRFALCGAapmpvELIRQFEaRTGLKVIEGYGLTEGTCGTSCNPRGGERrpGSIGLRLPYCQVKVAVLDgEGNYLR 413
Cdd:cd17645 213 DNQSLRVLLTGG-----DKLKKIE-RKGYKLVNNYGPTENTVVATSFEIDKPY--ANIPIGKPIDNTRVYILD-EALQLQ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 414 daaPNEV-GNLCLKGPTVFKGYL-QQDRNRDIWIGDGW------FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQM 485
Cdd:cd17645 284 ---PIGVaGELCIAGEGLARGYLnRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 486 IEEALHRHPAVALAAAVGKPDAKAGELPVAYIQlkPGASASEEELLEHASRHVPERaAVPKDIWLIESMPVTAVGKTFKP 565
Cdd:cd17645 361 IEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDLPDY-MIPTYFVHLKALPLTANGKVDRK 437
|
..
gi 15599055 566 AL 567
Cdd:cd17645 438 AL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
20-592 |
2.42e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 20 PLEQrdlpsSTYELLQRSARRHGQRIALSCLlhgsaaeePLRISYAELFARVTQTANALHRLGLESHQAVSFLLP-NLPQ 98
Cdd:PRK05691 3717 PLEQ-----SYVRLFEAQVAAHPQRIAASCL--------DQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAErGLDL 3783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 99 THYVIWGGEAAGIVNAINPLLEPEHIAELIRASNTRVLVTlapfpgtdlwqkVAGLRAQlpelyAIVVVDPANLLPAPQr 178
Cdd:PRK05691 3784 LGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVC------------SAACREQ-----ARALLDELGCANRPR- 3845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 179 ealkaqrgplpegVLDFDTLIADCPADRlESGRAIHPDDVASYFHTGGTTGTPK---------------LAPHSHFNEV- 242
Cdd:PRK05691 3846 -------------LLVWEEVQAGEVASH-NPGIYSGPDNLAYVIYTSGSTGLPKgvmveqrgmlnnqlsKVPYLALSEAd 3911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 243 AMAEIMGLNADYGVDDVLlcGLPLFhvngvmvtglapfhrGAQVLLAGPQGYRNPtliQDFWKLVERYRVTSFSGVPTIY 322
Cdd:PRK05691 3912 VIAQTASQSFDISVWQFL--AAPLF---------------GARVEIVPNAIAHDP---QGLLAHVQAQGITVLESVPSLI 3971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 323 AALLQvpSDGRDLSSLRFALCGAAPMPVELIRQFEAR-TGLKVIEGYGLTEGTCGTSCNPRGGERRPGS---IGLrlPYC 398
Cdd:PRK05691 3972 QGMLA--EDRQALDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPAECSDDVAFFRVDLASTRGSylpIGS--PTD 4047
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 399 QVKVAVLDGEGNYLRDAApneVGNLCLKGPTVFKGYLQQD-RNRDIWI-------GDGWFNTGDLGRIDEDGYIWLTGRS 470
Cdd:PRK05691 4048 NNRLYLLDEALELVPLGA---VGELCVAGTGVGRGYVGDPlRTALAFVphpfgapGERLYRTGDLARRRSDGVLEYVGRI 4124
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 471 KDLIIRGGHNIDPQMIEEALHRHPAVAlAAAVGKPDAKAGELPVAYiqLKPGASA-SEEELLEHASRHVpeRAAVPKDI- 548
Cdd:PRK05691 4125 DHQVKIRGYRIELGEIEARLHEQAEVR-EAAVAVQEGVNGKHLVGY--LVPHQTVlAQGALLERIKQRL--RAELPDYMv 4199
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 549 ---WLI-ESMPVTAVGKTFKPAL-RLD----------AIRRVLEEESRRI-AEDIRVEVV 592
Cdd:PRK05691 4200 plhWLWlDRLPLNANGKLDRKALpALDigqlqsqaylAPRNELEQTLATIwADVLKVERV 4259
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
177-558 |
4.73e-12 |
|
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: 69.02 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 177 QREALKAQRGPLPEG--VLDFDTLIAD-----CPADRLESGRaiHPDDVASYFHTGGTTGTPKLAPHSHfnevAMAEIMG 249
Cdd:cd17632 179 HRAALESARERLAAVgiPVTTLTLIAVrgrdlPPAPLFRPEP--DDDPLALLIYTSGSTGTPKGAMYTE----RLVATFW 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 250 LNADYGVDD-----VLLCGLPLFHVNG--VMVTGLApfhrgaqvllAGPQGYRNP-----TLIQDFwKLVeryRVTSFSG 317
Cdd:cd17632 253 LKVSSIQDIrppasITLNFMPMSHIAGriSLYGTLA----------RGGTAYFAAasdmsTLFDDL-ALV---RPTELFL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 318 VPTIYAALLQ--------VPSDGRDLSSL---------------RF--ALCGAAPMPVELIRQFEARTGLKVIEGYGLTE 372
Cdd:cd17632 319 VPRVCDMLFQryqaeldrRSVAGADAETLaervkaelrervlggRLlaAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 373 gTCGTSCNprGGERRPGSIGLRLpycqVKVAVLdgegNYLRDAAPNEVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGWFN 451
Cdd:cd17632 399 -AGAVILD--GVIVRPPVLDYKL----VDVPEL----GYFRTDRPHPRGELLVKTDTLFPGYYKRpEVTAEVFDEDGFYR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 452 TGD-LGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAV-------------ALAAAVGKPDAKAGElPVAyi 517
Cdd:cd17632 468 TGDvMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVrqifvygnserayLLAVVVPTQDALAGE-DTA-- 544
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15599055 518 QLKPGASASEEELLEHASRHVPEraaVPKDIwLIESMPVTA 558
Cdd:cd17632 545 RLRAALAESLQRIAREAGLQSYE---IPRDF-LIETEPFTI 581
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
216-567 |
6.49e-12 |
|
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: 68.27 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 216 DDVASYFHTGGTTGTPK--LAPHSHFNEVAMAEIMGLNADYGvDDVLLCGLPLFHVNgvmvtglapFHRGAQVLLAGPQG 293
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKgvQLEHKNMVNLLHFEREKTNINFS-DKVLQFATCSFDVC---------YQEIFSTLLSGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 294 YRNPTLIQ----DFWKLVERYRVTSFSgVPTiyaALLQVPSDGRDLSSlRFALC-------GAAPMPVELIRQFEARTGL 362
Cdd:cd17656 198 YIIREETKrdveQLFDLVKRHNIEVVF-LPV---AFLKFIFSEREFIN-RFPTCvkhiitaGEQLVITNEFKEMLHEHNV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 363 KVIEGYGLTEGTCGTSCNPRGGERRPGSIGLRLPYCQVKVAVLDGEGNYLRDAAPnevGNLCLKGPTVFKGYLQQDR-NR 441
Cdd:cd17656 273 HLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIV---GELYISGASVARGYLNRQElTA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 442 DIWIGDGW------FNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDAKAGELPVA 515
Cdd:cd17656 350 EKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCA 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15599055 516 YIQlkPGASASEEELLEHASRHVPERAAVPKDIWLiESMPVTAVGKTFKPAL 567
Cdd:cd17656 430 YFV--MEQELNISQLREYLAKQLPEYMIPSFFVPL-DQLPLTPNGKVDRKAL 478
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
212-568 |
1.53e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.90 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 212 AIHPDDVASYFHTGGTTGTPKLAPHSHF----NEVAMAEIMGLN-ADYGVDdvllcGLPLFHVNGvMVTGLAPFHRGAQV 286
Cdd:PRK07769 176 EANEDTIAYLQYTSGSTRIPAGVQITHLnlptNVLQVIDALEGQeGDRGVS-----WLPFFHDMG-LITVLLPALLGHYI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 287 LLAGPQGY-RNPTLIQDFWKLVERYRVTSFSGVPTI---YAALLQVPSDGR---DLSSLRFALCGAAPMPVELIRQFE-- 357
Cdd:PRK07769 250 TFMSPAAFvRRPGRWIRELARKPGGTGGTFSAAPNFafeHAAARGLPKDGEpplDLSNVKGLLNGSEPVSPASMRKFNea 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 358 -ARTGLK---VIEGYGLTEGTCGTSCNPRGGERR---------------------PGSIGlrlpycQV---KVAV----- 404
Cdd:PRK07769 330 fAPYGLPptaIKPSYGMAEATLFVSTTPMDEEPTviyvdrdelnagrfvevpadaPNAVA------QVsagKVGVsewav 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 405 -LDGE-GNYLRDaapNEVGNLCLKGPTVFKGY------------------LQQDRNRDIWIGDGWFNTGDLGrIDEDGYI 464
Cdd:PRK07769 404 iVDPEtASELPD---GQIGEIWLHGNNIGTGYwgkpeetaatfqnilksrLSESHAEGAPDDALWVRTGDYG-VYFDGEL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 465 WLTGRSKDLIIRGGHNIDPQMIE-EALHRHPAV--ALAAAVGKPdakAGELPVAYIQ-----LKPGASASEEELLEHASR 536
Cdd:PRK07769 480 YITGRVKDLVIIDGRNHYPQDLEyTAQEATKALrtGYVAAFSVP---ANQLPQVVFDdshagLKFDPEDTSEQLVIVAER 556
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15599055 537 ----HVPE--------RAAV-------PKDIWLIE--SMPVTAVGKTFKPALR 568
Cdd:PRK07769 557 apgaHKLDpqpiaddiRAAIavrhgvtVRDVLLVPagSIPRTSSGKIARRACR 609
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
212-497 |
1.21e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 51.09 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 212 AIHPDDVASYFHTGGTTGTPKLAPHSHfNEVAM-AEIM-------GLNADygvDDVLLC-GLPLFhvngvmvTGLAPFHR 282
Cdd:cd05913 74 AVPREKVVRIHASSGTTGKPTVVGYTK-NDLDVwAELVarcldaaGVTPG---DRVQNAyGYGLF-------TGGLGFHY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 283 GAQVLLAG--PQGYRNP----TLIQDFwklveryRVTSFSGVPTiYAALL--QVPSDGRDL--SSLRFALCGAAPMPVEL 352
Cdd:cd05913 143 GAERLGALviPAGGGNTerqlQLIKDF-------GPTVLCCTPS-YALYLaeEAEEEGIDPreLSLKVGIFGAEPWTEEM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 353 IRQFEARTGLKVIEGYGLTE----GTcGTSCNPRGGerrpgsIGLRLPYCQVKVaVLDGEGNYLRDAapnEVGNLCLKGP 428
Cdd:cd05913 215 RKRIERRLGIKAYDIYGLTEiigpGV-AFECEEKDG------LHIWEDHFIPEI-IDPETGEPVPPG---EVGELVFTTL 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599055 429 TVFKGYLQQDRNRDI----WIgdgwfnTGDLG----RIDEdgyiwLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVA 497
Cdd:cd05913 284 TKEAMPLIRYRTRDItrllPG------PCPCGrthrRIDR-----ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
362-474 |
1.21e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 51.64 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 362 LKVIEGYGLTEGTCGTSCNPRGGERrPGSIGLrlPYC-QVKVAVLDGEGNYLRDAAPNevGNLCLKGPTVFKGY-LQQDR 439
Cdd:PTZ00342 487 VNYYQGYGLTETTGPIFVQHADDNN-TESIGG--PISpNTKYKVRTWETYKATDTLPK--GELLIKSDSIFSGYfLEKEQ 561
|
90 100 110
....*....|....*....|....*....|....*
gi 15599055 440 NRDIWIGDGWFNTGDLGRIDEDGYIWLTGRSKDLI 474
Cdd:PTZ00342 562 TKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
180-567 |
1.24e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.09 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 180 ALKAQRGPLPEGV----LDFDT-LIADCPADRLEsgRAIHPDDVASYFHTGGTTGTPKLAPHSHfNEVAM-----AEIMG 249
Cdd:PRK05691 2294 ALFEALGELPAGVarwcLEDDAaALAAYSDAPLP--FLSLPQHQAYLIYTSGSTGKPKGVVVSH-GEIAMhcqavIERFG 2370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 250 LNADYgvddvllCGLPLFHVNGVMVTG--LAPFHRGAQVLLAGpQGYRNptlIQDFWKLVERYRVTSFSGVPTIYAALLQ 327
Cdd:PRK05691 2371 MRADD-------CELHFYSINFDAASErlLVPLLCGARVVLRA-QGQWG---AEEICQLIREQQVSILGFTPSYGSQLAQ 2439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 328 VPSDGRDLSSLRFALCGAAPMPVE-LIRQFEARTGLKVIEGYGLTEGTCG--TSCNPRGGERRPGS------IGLRLPYc 398
Cdd:PRK05691 2440 WLAGQGEQLPVRMCITGGEALTGEhLQRIRQAFAPQLFFNAYGPTETVVMplACLAPEQLEEGAASvpigrvVGARVAY- 2518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 399 qvkvaVLDGEGNYLRDAApneVGNLCLKGPTVFKGYLQQ-DRNRDIWIGDGW-------FNTGDLGRIDEDGYIWLTGRS 470
Cdd:PRK05691 2519 -----ILDADLALVPQGA---TGELYVGGAGLAQGYHDRpGLTAERFVADPFaadggrlYRTGDLVRLRADGLVEYVGRI 2590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 471 KDLIIRGGHNIDPQMIEEALHRHPAVAlAAAVGKPDAKAGELPVAYIQLKPGASASE------EELLEHASRHVPERAaV 544
Cdd:PRK05691 2591 DHQVKIRGFRIELGEIESRLLEHPAVR-EAVVLALDTPSGKQLAGYLVSAVAGQDDEaqaalrEALKAHLKQQLPDYM-V 2668
|
410 420
....*....|....*....|...
gi 15599055 545 PKDIWLIESMPVTAVGKTFKPAL 567
Cdd:PRK05691 2669 PAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
213-568 |
2.02e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.81 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 213 IHPDDVASYFHTGGTTGTPKLAPHSH----FNEVAMAEIMGLnADYGVDDVllCGLPLFHVNGVMVTGLaPFHRGAQVLL 288
Cdd:PRK12476 190 LDTDDVSHLQYTSGSTRPPVGVEITHravgTNLVQMILSIDL-LDRNTHGV--SWLPLYHDMGLSMIGF-PAVYGGHSTL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 289 AGPQGY-RNPT-LIQDFWKLVERYRVtsFSGVPTI---YAALLQVPSDGRDLSSLRFALC-GAAPMPVELIRQFEA---- 358
Cdd:PRK12476 266 MSPTAFvRRPQrWIKALSEGSRTGRV--VTAAPNFayeWAAQRGLPAEGDDIDLSNVVLIiGSEPVSIDAVTTFNKafap 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 359 ----RTGLKviEGYGLTEGTCGTSCNPRGGE-------RRPGSIGLRLPY------------C------QVKVAVLDGEG 409
Cdd:PRK12476 344 yglpRTAFK--PSYGIAEATLFVATIAPDAEpsvvyldREQLGAGRAVRVaadapnavahvsCgqvarsQWAVIVDPDTG 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 410 NYLRDAapnEVGNLCLKGPTVFKGYLQ-------------QDRNRDIWIGDG------WFNTGDLGrIDEDGYIWLTGRS 470
Cdd:PRK12476 422 AELPDG---EVGEIWLHGDNIGRGYWGrpeetertfgaklQSRLAEGSHADGaaddgtWLRTGDLG-VYLDGELYITGRI 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 471 KDLIIRGGHNIDPQMIE-EALHRHPAV--ALAAAVGKPdAKAGELPVAYIQLKPGASASE-EELLEHASRHVPERAAVP- 545
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEaTVAEASPMVrrGYVTAFTVP-AEDNERLVIVAERAAGTSRADpAPAIDAIRAAVSRRHGLAv 576
|
410 420
....*....|....*....|....*
gi 15599055 546 KDIWLIES--MPVTAVGKTFKPALR 568
Cdd:PRK12476 577 ADVRLVPAgaIPRTTSGKLARRACR 601
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
178-561 |
2.87e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 178 REALKAQRGPLPEGVLDFDTLIADCPaDRLESGRAIHPDdvASYF-HTGGTTGTPKLAPHSHFNEVAMAE-IM-GLNADY 254
Cdd:PRK05850 124 TEYVAPQPGQSAPPVIEVDLLDLDSP-RGSDARPRDLPS--TAYLqYTSGSTRTPAGVMVSHRNVIANFEqLMsDYFGDT 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 255 G----VDDVLLCGLPLFHVNGVMVTGLAPFHRGAQVLLAGPQGY-RNPTLiqdfW-KLVERYRvTSFSGVPTiYAALLQV 328
Cdd:PRK05850 201 GgvppPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFlQRPAR----WmQLLASNP-HAFSAAPN-FAFELAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 329 --PSD----GRDLSSLRFALCGAAPMPVELIRQFE---ARTGLK---VIEGYGLTEGTCGTSCNPRGG------------ 384
Cdd:PRK05850 275 rkTSDddmaGLDLGGVLGIISGSERVHPATLKRFAdrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesvrfdyekl 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 385 -----ERRPGSIGLRLPYCQVK----VAVLDGEGNylRDAAPNEVGNLCLKGPTVFKGYLQQDRNRDIWIG--------- 446
Cdd:PRK05850 355 saghaKRCETGGGTPLVSYGSPrsptVRIVDPDTC--IECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspg 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 447 --DG-WFNTGDLGRIDEDG-YIwlTGRSKDLIIRGGHNIDPQMIEEALH-----RhpavalAAAVGKPDAKAGELpVAYI 517
Cdd:PRK05850 433 tpEGpWLRTGDLGFISEGElFI--VGRIKDLLIVDGRNHYPDDIEATIQeitggR------VAAISVPDDGTEKL-VAII 503
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15599055 518 QLKPGASASEEELLEHAS--RHVPerAAVPK-------DIWLIE--SMPVTAVGK 561
Cdd:PRK05850 504 ELKKRGDSDEEAMDRLRTvkREVT--SAISKshglsvaDLVLVApgSIPITTSGK 556
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
433-567 |
4.27e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 43.28 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 433 GYLQQDRN---RDIWIG--DGWFNTGDLGRIDEDGYIWLTGRSKDLIIRGGHNIDPQMIEEALHRHPAVALAAAVGKPDA 507
Cdd:cd17647 352 NYLDKDNNepwRQFWLGprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599055 508 KAGELPVAYIQLKPGASASEEELLEHASRHVPERA--------------------------AVPKDIWLIESMPVTAVGK 561
Cdd:cd17647 432 DEEPTLVSYIVPRFDKPDDESFAQEDVPKEVSTDPivkgligyrklikdireflkkrlasyAIPSLIVVLDKLPLNPNGK 511
|
....*.
gi 15599055 562 TFKPAL 567
Cdd:cd17647 512 VDKPKL 517
|
|
| |
