|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
12-508 |
1.36e-34 |
|
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: 135.32 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 12 LFTNFQEAAANFSETPIIFDEplsafpelGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYL 91
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 92 GAVPVMTSYHLPTTTMEVFIDRLEDPFILFddetkkrvreisngtkskqipilylmeqpalsvsqsfldkneiSYMTHTS 171
Cdd:COG0318 73 GAVVVPLNPRLTAEELAYILEDSGARALVT-------------------------------------------ALILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 172 GTTGIPKLICHS-----AHSMGWRTKWQKTVFTKIsekkLIA---FHISPvhsrFNIGISSLMSMGFPMMPLANAQSSKV 243
Cdd:COG0318 110 GTTGRPKGVMLThrnllANAAAIAAALGLTPGDVV----LVAlplFHVFG----LTVGLLAPLLAGATLVLLPRFDPERV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 244 VHMLEAHRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRtsmAQDAVFLQVYGQSECGPMIlk 323
Cdd:COG0318 182 LELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEE---RFGVRIVEGYGLTETSPVV-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 324 ahTLESLKTSDARDMGVGLE-DMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMD 402
Cdd:COG0318 257 --TVNPEDPGERRPGSVGRPlPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 403 KHGHLFLKDRQVDLI----ETINSTlAIEDFLLdSLDFLAEVVI--VRDKNHSPQP--IIALAPDKEMDwnrwWEQVHE- 473
Cdd:COG0318 335 EDGYLYIVGRKKDMIisggENVYPA-EVEEVLA-AHPGVAEAAVvgVPDEKWGERVvaFVVLRPGAELD----AEELRAf 408
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 488214859 474 ----LPRLNVPiiRDF---DAIPRTATMKVQRLQIEKELKSQ 508
Cdd:COG0318 409 lrerLARYKVP--RRVefvDELPRTASGKIDRRALRERYAAG 448
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
7-508 |
4.80e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 128.77 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 7 YSPLNLFTNFQEAAANFSETPIIFDEplsafpelGLETTYKKccesVLKRAYQLAH----LGVKSGDKV--IIYKSSAFD 80
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFD--------GRRTTYAE----LDERVNRLANalraLGVKKGDRVavFDWNSHEYL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 81 TYLLAVSVsyLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDETKKRVREISNGTKSkqIPILYLMEQPALSVSQSF-- 158
Cdd:PRK06187 71 EAYFAVPK--IGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPT--VRTVIVEGDGPAAPLAPEvg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 159 -----------------LDKNEISYMTHTSGTTGIPK--------LICHSAHSMGWRTKWQKTVFtkisekkLIA---FH 210
Cdd:PRK06187 147 eyeellaaasdtfdfpdIDENDAAAMLYTSGTTGHPKgvvlshrnLFLHSLAVCAWLKLSRDDVY-------LVIvpmFH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 211 IspvhsrfnigisslMSMGFPMMPLANA---------QSSKVVHMLEAHRPI----------ALETHPNnfvqwrftakE 271
Cdd:PRK06187 220 V--------------HAWGLPYLALMAGakqviprrfDPENLLDLIETERVTfffavptiwqMLLKAPR----------A 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 272 HPEAFSGIRYYHSTFDAINNQTMKTFLRTSmaqDAVFLQVYGQSECGPMI----LKAHTLESLKTsdARDMGVGLEdMTS 347
Cdd:PRK06187 276 YFVDFSSLRLVIYGGAALPPALLREFKEKF---GIDLVQGYGMTETSPVVsvlpPEDQLPGQWTK--RRSAGRPLP-GVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 348 ARITDSVGNVLP--ENTDGHIQLlsKGRALT--YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ET 419
Cdd:PRK06187 350 ARIVDDDGDELPpdGGEVGEIIV--RGPWLMqgYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIisggEN 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 420 InSTLAIEDFLLDsLDFLAEV-VI-VRDKNHSPQP--IIALAPDKEMD-----------WNRWWeqvheLPRlNVPIIrd 484
Cdd:PRK06187 428 I-YPRELEDALYG-HPAVAEVaVIgVPDEKWGERPvaVVVLKPGATLDakelraflrgrLAKFK-----LPK-RIAFV-- 497
|
570 580
....*....|....*....|....
gi 488214859 485 fDAIPRTATMKVQRlqieKELKSQ 508
Cdd:PRK06187 498 -DELPRTSVGKILK----RVLREQ 516
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
163-497 |
8.56e-26 |
|
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: 107.76 E-value: 8.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 163 EISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAFHisPVhsrFNIGISSLMsmgfpMMPLANAQSS- 241
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTL--PL---FHIGGLFGL-----LGALLAGGTVv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 242 --------KVVHMLEAHRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRtsmAQDAVFLQVYG 313
Cdd:cd04433 71 llpkfdpeAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEE---APGIKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 314 QSECGPMIlkahTLESLKTSDARDMGVGL-EDMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDW 392
Cdd:cd04433 148 LTETGGTV----ATGPPDDDARKPGSVGRpVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 393 WDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFL-AEVVIVRDKNHSPQPI--IALAPDKEMDWN 465
Cdd:cd04433 224 YRTGDLGRLDEDGYLYIVGRLKDMIksggENV-YPAEVEAVLLGHPGVAeAAVVGVPDPEWGERVVavVVLRPGADLDAE 302
|
330 340 350
....*....|....*....|....*....|....
gi 488214859 466 RWWEQVHE-LPRLNVP-IIRDFDAIPRTATMKVQ 497
Cdd:cd04433 303 ELRAHVRErLAPYKVPrRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
36-498 |
2.62e-20 |
|
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: 93.44 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 36 AFPELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIY--KSSAFDTYLLAVSVsyLGAVPVMTSYHLptTTMEV-FID 112
Cdd:cd17631 13 ALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLskNSPEFLELLFAAAR--LGAVFVPLNFRL--TPPEVaYIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 113 RLEDPFILFDDetkkrvreisngtkskqipILYLMeqpalsvsqsfldkneisymtHTSGTTGIPKLICHSAHSMGWRTK 192
Cdd:cd17631 89 ADSGAKVLFDD-------------------LALLM---------------------YTSGTTGRPKGAMLTHRNLLWNAV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 193 WQKTVFTKISEKKLIA----FHISPVHsrfNIGISSLMsMGFPMMPLANAQSSKVVHMLEAHRPIALETHPnnfVQWRFT 268
Cdd:cd17631 129 NALAALDLGPDDVLLVvaplFHIGGLG---VFTLPTLL-RGGTVVILRKFDPETVLDLIERHRVTSFFLVP---TMIQAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 269 AkEHPEAfsgiryyhSTFDAinnQTMKTF-----------LRTSMAQDAVFLQVYGQSECGPMILkahtleSLKTSDARD 337
Cdd:cd17631 202 L-QHPRF--------ATTDL---SSLRAViyggapmperlLRALQARGVKFVQGYGMTETSPGVT------FLSPEDHRR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 338 -MG-VGLEDM-TSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQV 414
Cdd:cd17631 264 kLGsAGRPVFfVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 415 DLI----ETINStLAIEDFLLDsLDFLAEV-VI-VRDKN--HSPQPIIALAPDKEMDWNRWWEQVHE-LPRLNVPIIRDF 485
Cdd:cd17631 344 DMIisggENVYP-AEVEDVLYE-HPAVAEVaVIgVPDEKwgEAVVAVVVPRPGAELDEDELIAHCRErLARYKIPKSVEF 421
|
490
....*....|....
gi 488214859 486 -DAIPRTATMKVQR 498
Cdd:cd17631 422 vDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
16-417 |
1.84e-19 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 90.45 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 16 FQEAAANFSETPIIFDEPlsafpelGLETTYKKccesVLKRAYQLAH----LGVKSGDKVIIY--KSSAFDTYLLAVSvs 89
Cdd:pfam00501 1 LERQAARTPDKTALEVGE-------GRRLTYRE----LDERANRLAAglraLGVGKGDRVAILlpNSPEWVVAFLACL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 90 YLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDD--------ETKKRVREISNGTKSKQIPILYLMEQPALSVSQ----- 156
Cdd:pfam00501 68 KAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 157 --SFLDKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFT---KISEKKLIA-----FHISPVHSRFNIGISSLM 226
Cdd:pfam00501 148 ppPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfGLGPDDRVLstlplFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 227 SMGFpmMPLANAQSSK-VVHMLEAHRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSmaqD 305
Cdd:pfam00501 228 TVVL--PPGFPALDPAaLLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELF---G 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 306 AVFLQVYGQSECGPMilkAHTLESLKTSDARDMGVG--LEDmTSARITD-SVGNVLPENTDGhiQLLSKGRALT--YYKE 380
Cdd:pfam00501 303 GALVNGYGLTETTGV---VTTPLPLDEDLRSLGSVGrpLPG-TEVKIVDdETGEPVPPGEPG--ELCVRGPGVMkgYLND 376
|
410 420 430
....*....|....*....|....*....|....*...
gi 488214859 381 DARFQEN-VYGDWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:pfam00501 377 PELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
45-506 |
2.26e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 87.71 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 45 TYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLpttTMEVFIDRLEDP---FILF 121
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL---SREELLWQLDDAevkCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 122 DDETKKRVREIsngtkskqIPILY--LMEQPALSVS-QSFLDKNEISYMTHTSGTTGIPKLIC-----H------SAHSM 187
Cdd:PRK03640 106 DDDFEAKLIPG--------ISVKFaeLMNGPKEEAEiQEEFDLDEVATIMYTSGTTGKPKGVIqtygnHwwsavgSALNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 188 GWRTK--WqktvftkisekkLIA---FHISpvhsrfniGISSLMS---MGFPMMPLANAQSSKVVHMLEAHR-------P 252
Cdd:PRK03640 178 GLTEDdcW------------LAAvpiFHIS--------GLSILMRsviYGMRVVLVEKFDAEKINKLLQTGGvtiisvvS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 253 IALEthpnnfvqwRFTAKEHPEAfsgiryYHSTFDAI---NNQTMKTFLRTSMAQDAVFLQVYGQSEcgpmilkahTLES 329
Cdd:PRK03640 238 TMLQ---------RLLERLGEGT------YPSSFRCMllgGGPAPKPLLEQCKEKGIPVYQSYGMTE---------TASQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 330 LKTSDARDMgvgLEDMTSA---------RITDSvGNVLPENTDGHIqlLSKGRALT--YYKEDARFQENVYGDWWDSGDY 398
Cdd:PRK03640 294 IVTLSPEDA---LTKLGSAgkplfpcelKIEKD-GVVVPPFEEGEI--VVKGPNVTkgYLNREDATRETFQDGWFKTGDI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 399 GFMDKHGHLFLKDRQVDLI----ETINSTlAIEDFLLdSLDFLAEVVIV--RDKNHSPQPIIALAPDKEMDWNRWWEQVH 472
Cdd:PRK03640 368 GYLDEEGFLYVLDRRSDLIisggENIYPA-EIEEVLL-SHPGVAEAGVVgvPDDKWGQVPVAFVVKSGEVTEEELRHFCE 445
|
490 500 510
....*....|....*....|....*....|....*.
gi 488214859 473 E-LPRLNVPI-IRDFDAIPRTATMKVQRLQIEKELK 506
Cdd:PRK03640 446 EkLAKYKVPKrFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
45-506 |
1.19e-17 |
|
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: 85.09 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 45 TYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLpttTMEVFIDRLEDPFILFDDe 124
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRL---TPNELAFQLKDSDVKLDD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 125 tkkrvreisngtkskqipilylmeqpalsvsqsfldkneISYMTHTSGTTGIPKLICHSahsmgWRTKWQKTVFTKIS-- 202
Cdd:cd05912 79 ---------------------------------------IATIMYTSGTTGKPKGVQQT-----FGNHWWSAIGSALNlg 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 203 ----EKKLIA---FHISpvhsrfniGISSLMS---MGFPMMPLANAQSSKVVHMLEAHRPIALETHPNnFVQWrfTAKEH 272
Cdd:cd05912 115 ltedDNWLCAlplFHIS--------GLSILMRsviYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPT-MLQR--LLEIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 273 PEAfsgiryYHSTFdainnQTM--------KTFLRTSMAQDAVFLQVYGQSECGPMILKAHTLESL-KTSDArdmGVGLE 343
Cdd:cd05912 184 GEG------YPNNL-----RCIllgggpapKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALnKIGSA---GKPLF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 344 DMtSARITDSVGnvlPENTDGHIQLlsKGRALT--YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI---- 417
Cdd:cd05912 250 PV-ELKIEDDGQ---PPYEVGEILL--KGPNVTkgYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIisgg 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 418 ETINSTlAIEDFLLdSLDFLAEVVIV--RDKNHSPQPIIALAPDKEMDWNRWWEQVHE-LPRLNVPI-IRDFDAIPRTAT 493
Cdd:cd05912 324 ENIYPA-EIEEVLL-SHPAIKEAGVVgiPDDKWGQVPVAFVVSERPISEEELIAYCSEkLAKYKVPKkIYFVDELPRTAS 401
|
490
....*....|...
gi 488214859 494 MKVQRlqieKELK 506
Cdd:cd05912 402 GKLLR----HELK 410
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
110-496 |
1.50e-16 |
|
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: 81.99 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 110 FIDRLEDPFILFDDETKKRVreisnGTKSKQIPILYLMEQPALSVSQSFL---DKNEISYMTHTSGTTGIPKLICHSAHS 186
Cdd:cd05909 97 LFDVEYDARIVYLEDLRAKI-----SKADKCKAFLAGKFPPKWLLRIFGVapvQPDDPAVILFTSGSEGLPKGVVLSHKN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 187 MGWRTKWQKTVFTKISEKKLIAFhISPVHS-RFNIGISSLMSMGFPMMPLANA-QSSKVVHMLEAHRPIALETHPNNFVQ 264
Cdd:cd05909 172 LLANVEQITAIFDPNPEDVVFGA-LPFFHSfGLTGCLWLPLLSGIKVVFHPNPlDYKKIPELIYDKKATILLGTPTFLRG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 265 wrFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTsmaQDAVFLQVYGQSECGPMILKahtleSLKTSDARDMGVG--L 342
Cdd:cd05909 251 --YARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEK---FGIRILEGYGTTECSPVISV-----NTPQSPNKEGTVGrpL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 343 EDMtSARITDSVGNV-LPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQ---VDLIE 418
Cdd:cd05909 321 PGM-EVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLsrfAKIAG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 419 TINSTLAIEDFLLDSL--DFLAEVVIVRDKNHSPQpIIALAPDKEMDWNRWWEQV--HELPRLNVP-IIRDFDAIPRTAT 493
Cdd:cd05909 400 EMVSLEAIEDILSEILpeDNEVAVVSVPDGRKGEK-IVLLTTTTDTDPSSLNDILknAGISNLAKPsYIHQVEEIPLLGT 478
|
...
gi 488214859 494 MKV 496
Cdd:cd05909 479 GKP 481
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
41-505 |
4.17e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 74.54 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 41 GLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIY--KSSAFdtYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPF 118
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLmkNSAAF--LELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 119 ILFDDE--------TKKRVREISNGTKSKQIPILYLMEQPALSVSQSFLDKneisyMTHTSGTTGIPKLICHSAHSMGWR 190
Cdd:PRK06145 103 LLVDEEfdaivaleTPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVR-----LMYTSGTTDRPKGVMHSYGNLHWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 191 TKWQKTVFTKISEKKLIAfhISPVH--SRFNI-GISSLMSMGFpMMPLANAQSSKVVHMLEAHRPIALETHPnnFVQWRF 267
Cdd:PRK06145 178 SIDHVIALGLTASERLLV--VGPLYhvGAFDLpGIAVLWVGGT-LRIHREFDPEAVLAAIERHRLTCAWMAP--VMLSRV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 268 TAKEHPEAF--SGIRYYHSTFDAINNQTMKTFlrTSMAQDAVFLQVYGQSE-CGPMILKAHTLESLKT-SDARDMGvgle 343
Cdd:PRK06145 253 LTVPDRDRFdlDSLAWCIGGGEKTPESRIRDF--TRVFTRARYIDAYGLTEtCSGDTLMEAGREIEKIgSTGRALA---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 344 dMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ET 419
Cdd:PRK06145 327 -HVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIisggEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 420 INSTlAIEDFLLDsLDFLAEVVI--VRDKNHSPQP--IIALAPDKEMDWNRWWEQVHE-LPRLNVP---IIRdfDAIPRT 491
Cdd:PRK06145 406 IASS-EVERVIYE-LPEVAEAAVigVHDDRWGERItaVVVLNPGATLTLEALDRHCRQrLASFKVPrqlKVR--DELPRN 481
|
490
....*....|....
gi 488214859 492 ATMKVQRLQIEKEL 505
Cdd:PRK06145 482 PSGKVLKRVLRDEL 495
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-499 |
7.19e-14 |
|
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: 73.89 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 38 PELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIY--KSSAFDTYLLAVSVSYLGAVPVMTSYhlpttTMEVFIDRLE 115
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIAlpNGLEFVVAFLAAARAGAVVAPLNPAY-----KKAEFEFYLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 116 D---PFILFDDETKKrvrEISNGTKSKQIPILYLMEQPAlsVSQSFLDKNEISYMT---------------------HTS 171
Cdd:cd05926 84 DlgsKLVLTPKGELG---PASRAASKLGLAILELALDVG--VLIRAPSAESLSNLLadkknaksegvplpddlalilHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 172 GTTGIPKL-------ICHSAHSMgwrtkwqKTVFTKISEKKLIA----FHIspvhsrfnIG-ISSLMSmgfpmmPLAnAQ 239
Cdd:cd05926 159 GTTGRPKGvplthrnLAASATNI-------TNTYKLTPDDRTLVvmplFHV--------HGlVASLLS------TLA-AG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 240 SSKVVhmleAHRPIALETHP---NNFVQWrFTA------------KEHPE-AFSGIRYYHSTFDAINNQTMKTFLRTSMA 303
Cdd:cd05926 217 GSVVL----PPRFSASTFWPdvrDYNATW-YTAvptihqillnrpEPNPEsPPPKLRFIRSCSASLPPAVLEALEATFGA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 304 QdavFLQVYGQSECgpmilkAH--TLESLKTSDARDMGVGLEDMTSARITDSVGNVLPENTDGHIQLlsKGRALT--YYK 379
Cdd:cd05926 292 P---VLEAYGMTEA------AHqmTSNPLPPGPRKPGSVGKPVGVEVRILDEDGEILPPGVVGEICL--RGPNVTrgYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 380 -EDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLdSLDFLAEVVIVRdknhSPQPI- 453
Cdd:cd05926 361 nPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELInrggEKI-SPLEVDGVLL-SHPAVLEAVAFG----VPDEKy 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 488214859 454 -------IALAPDKEMDWNRWWEQV-HELPRLNVPI-IRDFDAIPRTATMKVQRL 499
Cdd:cd05926 435 geevaaaVVLREGASVTEEELRAFCrKHLAAFKVPKkVYFVDELPKTATGKIQRR 489
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
60-503 |
9.11e-14 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 73.61 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 60 LAHLGVKSGDKVIIYKSSAFDTY--LLAVSvsYLGAVpvmtsyHLPTTTM---EVFIDRLED--PFILF-DDET------ 125
Cdd:COG0365 56 LRALGVKKGDRVAIYLPNIPEAViaMLACA--RIGAV------HSPVFPGfgaEALADRIEDaeAKVLItADGGlrggkv 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 126 ---KKRVREISNGTKSKQIPILY-----------------LMEQPALSVSQSFLDKNEISYMTHTSGTTGIPKLICHSAH 185
Cdd:COG0365 128 idlKEKVDEALEELPSLEHVIVVgrtgadvpmegdldwdeLLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 186 S-MGWRTKWQKTVFtKISEKKL---------IAFHISPVHSRFNIGISSLMSMGFPMMPLANAqsskVVHMLEAHRPial 255
Cdd:COG0365 208 GyLVHAATTAKYVL-DLKPGDVfwctadigwATGHSYIVYGPLLNGATVVLYEGRPDFPDPGR----LWELIEKYGV--- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 256 ethpNNFvqwrFTA--------KEHPEA-----FSGIRYYHSTFDAINNQTMKTFlrtsmaQDAVFLQV---YGQSE-CG 318
Cdd:COG0365 280 ----TVF----FTAptairalmKAGDEPlkkydLSSLRLLGSAGEPLNPEVWEWW------YEAVGVPIvdgWGQTEtGG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 319 PMILKAHTLESLKTSdardMGV---GLEdmtsARITDSVGNVLPENTDGHIQLLSK--GRALTYYKEDARFQE---NVYG 390
Cdd:COG0365 346 IFISNLPGLPVKPGS----MGKpvpGYD----VAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYREtyfGRFP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 391 DWWDSGDYGFMDKHGHLFLKDRqVDliETIN------STLAIEDFLLdSLDFLAEVVIVrdknHSPQPI--------IAL 456
Cdd:COG0365 418 GWYRTGDGARRDEDGYFWILGR-SD--DVINvsghriGTAEIESALV-SHPAVAEAAVV----GVPDEIrgqvvkafVVL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 488214859 457 APDKE---------MDWNRwwEQV--HELPRlnvpIIRDFDAIPRTATMKVQRLQIEK 503
Cdd:COG0365 490 KPGVEpsdelakelQAHVR--EELgpYAYPR----EIEFVDELPKTRSGKIMRRLLRK 541
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
45-503 |
1.35e-13 |
|
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: 72.75 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 45 TYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVmtsyhlPTTTMEvfidrledpfilfdde 124
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYV------PLTTLL---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 125 tkkrvreisnGTKskqiPILYLMEqpALSVSQSFLDKNEISYMTHTSGTTGIPKLICHS-----AHSMGWRTkWQ----K 195
Cdd:cd05972 60 ----------GPK----DIEYRLE--AAGAKAIVTDAEDPALIYFTSGTTGLPKGVLHThsyplGHIPTAAY-WLglrpD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 196 TVFTKISEKKLIAFHISPVHSRFNIGISSLMSMGFPMMPlanaqsSKVVHMLEAHRPIALETHPnnfVQWRFTAKEHPEA 275
Cdd:cd05972 123 DIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDA------ERILELLERYGVTSFCGPP---TAYRMLIKQDLSS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 276 --FSGIRYYHSTFDAINNQTMKTFlrtsmaQDAVFLQV---YGQSECGPMILKAHTLESLKTSDARDMGvGLEdmtsARI 350
Cdd:cd05972 194 ykFSHLRLVVSAGEPLNPEVIEWW------RAATGLPIrdgYGQTETGLTVGNFPDMPVKPGSMGRPTP-GYD----VAI 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 351 TDSVGNVLPENTDGHIQLLSK--GRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA--- 425
Cdd:cd05972 263 IDDDGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGpfe 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 426 IEDFLLDSlDFLAEVVIVrdknHSPQPI--------IALAPDKEMDwnrwWEQVHELPRL--------NVPIIRDF-DAI 488
Cdd:cd05972 343 VESALLEH-PAVAEAAVV----GSPDPVrgevvkafVVLTSGYEPS----EELAEELQGHvkkvlapyKYPREIEFvEEL 413
|
490
....*....|....*
gi 488214859 489 PRTATMKVQRLQIEK 503
Cdd:cd05972 414 PKTISGKIRRVELRD 428
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
44-417 |
2.72e-13 |
|
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: 71.93 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 44 TTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDtYLLAVSVSYL-GAVPVMTS---------------YHLPTTtm 107
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNED-FIPAFWACVLaGFVPAPLTvpptydepnarlrklRHIWQL-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 108 evfidrLEDPFILFDDETKKRVREISNGTKSKQIPILY---LMEQPALSVSQSfLDKNEISYMTHTSGTTGIPKLICHSA 184
Cdd:cd05906 117 ------LGSPVVLTDAELVAEFAGLETLSGLPGIRVLSieeLLDTAADHDLPQ-SRPDDLALLMLTSGSTGFPKAVPLTH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 185 HSMGWRTK--------WQKTVF---------TKISEkkliaFHISPVH---SRFNIGISSLMsmgfpmmplanAQSSKVV 244
Cdd:cd05906 190 RNILARSAgkiqhnglTPQDVFlnwvpldhvGGLVE-----LHLRAVYlgcQQVHVPTEEIL-----------ADPLRWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 245 HMLEAHRpIALETHPN-NFVQWRFTAKEHPEA---FSGIRYYHSTFDAINNQTMKTFLRT---SMAQDAVFLQVYGQSEC 317
Cdd:cd05906 254 DLIDRYR-VTITWAPNfAFALLNDLLEEIEDGtwdLSSLRYLVNAGEAVVAKTIRRLLRLlepYGLPPDAIRPAFGMTET 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 318 GPMILKAHTLESLKTSDA-RDMGVGLE----DMtsaRITDSVGNVLPENTDGHIQLlsKGRALT--YYKEDARFQEN-VY 389
Cdd:cd05906 333 CSGVIYSRSFPTYDHSQAlEFVSLGRPipgvSM---RIVDDEGQLLPEGEVGRLQV--RGPVVTkgYYNNPEANAEAfTE 407
|
410 420
....*....|....*....|....*...
gi 488214859 390 GDWWDSGDYGFMDkHGHLFLKDRQVDLI 417
Cdd:cd05906 408 DGWFRTGDLGFLD-NGNLTITGRTKDTI 434
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
53-497 |
1.11e-12 |
|
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: 69.93 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 53 VLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEdPFILF-DDETKKRVRE 131
Cdd:cd05911 20 SRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK-PKVIFtDPDGLEKVKE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 132 ISNGTKSK-QIPILYLMEQPALSVSQS----------------FLDKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQ 194
Cdd:cd05911 99 AAKELGPKdKIIVLDDKPDGVLSIEDLlsptlgeededlppplKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 195 KTVFTKISEKKLIAFHISPVHSRFniGISSLMSM---GFP--MMP-------LANAQSSKVVHMLEAhrP---IALETHP 259
Cdd:cd05911 179 QTFLYGNDGSNDVILGFLPLYHIY--GLFTTLASllnGATviIMPkfdselfLDLIEKYKITFLYLV--PpiaAALAKSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 260 NnfVQwrftakehPEAFSGIRYYHSTFDAINNQtMKTFLRTsMAQDAVFLQVYGQSECGPMILKAHTLESLKTSdardmg 339
Cdd:cd05911 255 L--LD--------KYDLSSLRVILSGGAPLSKE-LQELLAK-RFPNATIKQGYGMTETGGILTVNPDGDDKPGS------ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 340 VG--LEDMTsARITDSVGN-VLPENTDGHIQLLSKGRALTYYK-----EDARFQENvygdWWDSGDYGFMDKHGHLFLKD 411
Cdd:cd05911 317 VGrlLPNVE-AKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNnpeatKETFDEDG----WLHTGDIGYFDEDGYLYIVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 412 RQVDLI----------EtinstlaIEDFLLdSLDFLAEV-VI-VRDKNHS--PQPIIALAPDKEM------DWNRwwEQV 471
Cdd:cd05911 392 RKKELIkykgfqvapaE-------LEAVLL-EHPGVADAaVIgIPDEVSGelPRAYVVRKPGEKLtekevkDYVA--KKV 461
|
490 500
....*....|....*....|....*..
gi 488214859 472 HELPRLNVPIIrdF-DAIPRTATMKVQ 497
Cdd:cd05911 462 ASYKQLRGGVV--FvDEIPKSASGKIL 486
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
43-503 |
2.75e-12 |
|
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: 68.81 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 43 ETTYKKCCESVLKRAYQLAHLGVKSGDKViiyKSSAFDTY-----LLAVSVsyLGAVPVMTSYHLPTTTMEVFIDRLEDP 117
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVKPGDRV---ATLAWNTHrhlelYYAVPG--MGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 118 FILFDDE----------TKKRVREI-----SNGTKSKQIPILY-----LMEQPALSVSQSFlDKNEISYMTHTSGTTGIP 177
Cdd:cd12119 100 VVFVDRDflplleaiapRLPTVEHVvvmtdDAAMPEPAGVGVLayeelLAAESPEYDWPDF-DENTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 178 K--LICHSA---HSMGWRTkwqkTVFTKISEKKLI-----AFHispVHSrFNIGISSLMSmGFPM-MPLANAQSSKVVHM 246
Cdd:cd12119 179 KgvVYSHRSlvlHAMAALL----TDGLGLSESDVVlpvvpMFH---VNA-WGLPYAAAMV-GAKLvLPGPYLDPASLAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 247 LEAHRPialethpnnfvqwRFTAK---------EHPEAfSGIRYYHSTFDAINNQTMKTFLRTSMAQDAV-FLQVYGQSE 316
Cdd:cd12119 250 IEREGV-------------TFAAGvptvwqgllDHLEA-NGRDLSSLRRVVIGGSAVPRSLIEAFEERGVrVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 317 CGPMILKAHTLESLkTSDARDMGVGLEDMT-------SARITDSVGNVLPE--NTDGHIQLLSKGRALTYYKEDARFQEN 387
Cdd:cd12119 316 TSPLGTVARPPSEH-SNLSEDEQLALRAKQgrpvpgvELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 388 VYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFL-AEVVIVRDKNHSPQP--IIALAPDK 460
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIksggEWI-SSVELENAIMAHPAVAeAAVIGVPHPKWGERPlaVVVLKEGA 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 488214859 461 EMD-----------WNRWWeqvheLPrLNVPIIrdfDAIPRTATMKVQRLQIEK 503
Cdd:cd12119 474 TVTaeellefladkVAKWW-----LP-DDVVFV---DEIPKTSTGKIDKKALRE 518
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
43-498 |
4.57e-12 |
|
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: 67.87 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 43 ETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSyhlptttmevfidrledpfilfd 122
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVIN----------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 123 detkkrvreisngTKSKQIPILYLME--QPALSVSqsflDKNEISYMTHTSGTTGIPKLICHS-AHSMGWRTKWQKTVFT 199
Cdd:cd05919 67 -------------PLLHPDDYAYIARdcEARLVVT----SADDIAYLLYSSGTTGPPKGVMHAhRDPLLFADAMAREALG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 200 KISEKKLiaFHISPVHSRFNIGiSSLMsmgFPMMPLANA-------QSSKVVHMLEAHRPIALETHPNNFVQWRFTAKEH 272
Cdd:cd05919 130 LTPGDRV--FSSAKMFFGYGLG-NSLW---FPLAVGASAvlnpgwpTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 273 PEAFSGIRYYHSTFDA----INNQTMKTFLRTsmaqdavFLQVYGQSECGpmilkaHTLESLKTSDARDMGVGLE-DMTS 347
Cdd:cd05919 204 PDALRSLRLCVSAGEAlprgLGERWMEHFGGP-------ILDGIGATEVG------HIFLSNRPGAWRLGSTGRPvPGYE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 348 ARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLiETIN----ST 423
Cdd:cd05919 271 IRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDM-LKVGgqwvSP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 424 LAIEDFLLDSLDFLAEVVIVRDKNH---SPQPIIALAPDKEMD--WNRWWEQ-------VHELPRLnvpiIRDFDAIPRT 491
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTglsRLTAFVVLKSPAAPQesLARDIHRhllerlsAHKVPRR----IAFVDELPRT 425
|
....*..
gi 488214859 492 ATMKVQR 498
Cdd:cd05919 426 ATGKLQR 432
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
57-443 |
1.05e-10 |
|
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: 63.55 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 57 AYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAV--PVMTSYHlptttmevfidRLEDPFILFDDETKKRVreisn 134
Cdd:cd05903 15 AAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVtnPILPFFR-----------EHELAFILRRAKAKVFV----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 135 gtkskqIPILYLMEQPALsvsqsflDKNEISYMTHTSGTTGIPKLICHSAHSM---------GWRTKWQKTVFTKisekk 205
Cdd:cd05903 79 ------VPERFRQFDPAA-------MPDAVALLLFTSGTTGEPKGVMHSHNTLsasirqyaeRLGLGPGDVFLVA----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 206 liafhiSPV--HSRFNIGISSLMSMGFPMMPLANAQSSKVVHMLEAHRPialeTH---PNNFVQWRFTA-KEHPEAFSGI 279
Cdd:cd05903 141 ------SPMahQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGV----TFmmgATPFLTDLLNAvEEAGEPLSRL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 280 RYYHSTFDAINNQTMKtflRTSMAQDAVFLQVYGQSECGPMILKAHTLESLK--TSDARdMGVGLEdmtsARITDSVGNV 357
Cdd:cd05903 211 RTFVCGGATVPRSLAR---RAAELLGAKVCSAYGSTECPGAVTSITPAPEDRrlYTDGR-PLPGVE----IKVVDDTGAT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 358 LPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDS 433
Cdd:cd05903 283 LAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIirggENI-PVLEVEDLLLGH 361
|
410
....*....|
gi 488214859 434 LDfLAEVVIV 443
Cdd:cd05903 362 PG-VIEAAVV 370
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
45-419 |
3.66e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 62.26 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 45 TYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDE 124
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 125 TKKRVREISNGTKSKQI---PILYLMEQPA-------LSVSQS------FLDKNEISYMTHTSGTTGIPKLICHSAHSMG 188
Cdd:PRK08316 118 LAPTAEAALALLPVDTLilsLVLGGREAPGgwldfadWAEAGSvaepdvELADDDLAQILYTSGTESLPKGAMLTHRALI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 189 WrtKWQKTVFT---KISEKKLIA---FHISPVHSRFN----IGISSLMsMGFPMMPLanaqsskVVHMLEAHRP------ 252
Cdd:PRK08316 198 A--EYVSCIVAgdmSADDIPLHAlplYHCAQLDVFLGpylyVGATNVI-LDAPDPEL-------ILRTIEAERItsffap 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 253 ----IALETHPNnFVQWRFTA----------------KEHPEAFSGIRYYhstfdainnqtmktflrtsmaqdavflQVY 312
Cdd:PRK08316 268 ptvwISLLRHPD-FDTRDLSSlrkgyygasimpvevlKELRERLPGLRFY---------------------------NCY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 313 GQSECGP--MILKAHTLESlKTSDARDMGVGLEdmtsARITDSVGNVLPENTDGHI-----QLLskgraLTYYKEDARFQ 385
Cdd:PRK08316 320 GQTEIAPlaTVLGPEEHLR-RPGSAGRPVLNVE----TRVVDDDGNDVAPGEVGEIvhrspQLM-----LGYWDDPEKTA 389
|
410 420 430
....*....|....*....|....*....|....
gi 488214859 386 ENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET 419
Cdd:PRK08316 390 EAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKT 423
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
7-498 |
3.95e-10 |
|
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: 61.93 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 7 YSPLNLFTNFQEAAANFSE-TPIIFDEPLSAFPElgletTYKKCCesvlKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLA 85
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDrTSIVYGDRRYTWRQ-----TYDRCR----RLASALAALGISRGDTVAVLAPNTPAMYELH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 86 VSVSYLGAVPVMTSYHLPTTTMEvFIDRLEDPFILFDDETKKRVREISNGTKSkqipilYLMEQPAlsvsqsflDKNEIS 165
Cdd:cd12118 72 FGVPMAGAVLNALNTRLDAEEIA-FILRHSEAKVLFVDREFEYEDLLAEGDPD------FEWIPPA--------DEWDPI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 166 YMTHTSGTTGIPKLICHS---------AHSMGWRTKwQKTVFTKIsekkLIAFHISpvhsrfnigisslmSMGFPMMPLA 236
Cdd:cd12118 137 ALNYTSGTTGRPKGVVYHhrgaylnalANILEWEMK-QHPVYLWT----LPMFHCN--------------GWCFPWTVAA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 237 NAQSS------------------KVVHMLEAhrPIALETHPNNFVQWR---------FTAKEHPEAfsgiryyhSTFDAI 289
Cdd:cd12118 198 VGGTNvclrkvdakaiydliekhKVTHFCGA--PTVLNMLANAPPSDArplphrvhvMTAGAPPPA--------AVLAKM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 290 NNQTMKTFlrtsmaqdavflQVYGQSEC-GPMILKAHTLE--SLKTSD-----ARDmGVGLEDMTSARITDSVGNV-LPE 360
Cdd:cd12118 268 EELGFDVT------------HVYGLTETyGPATVCAWKPEwdELPTEErarlkARQ-GVRYVGLEEVDVLDPETMKpVPR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 361 N--TDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSL 434
Cdd:cd12118 335 DgkTIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIisggENI-SSVEVEGVLYKHP 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488214859 435 DFLAEVVIVRDKNH---SPQPIIALAPDKE------MDWNRwweqvHELPRLNVPIIRDFDAIPRTATMKVQR 498
Cdd:cd12118 414 AVLEAAVVARPDEKwgeVPCAFVELKEGAKvteeeiIAFCR-----EHLAGFMVPKTVVFGELPKTSTGKIQK 481
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
45-419 |
4.30e-10 |
|
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: 61.75 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 45 TYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPV-MTSYHLPtttmEVFIDRLEdpfilfdd 123
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICpLFSAFGP----EAIRDRLE-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 124 etkkrvreisngtkskqipilyLMEQPALSVSQSFLDKNEI---SYMTHTSGTTGIPKLICHSAHSMgwrtkwqktVFTK 200
Cdd:cd05969 70 ----------------------NSEAKVLITTEELYERTDPedpTLLHYTSGTTGTPKGVLHVHDAM---------IFYY 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 201 ISEKKLIAFHISPVH-SRFNIGISSLMSMGFpMMPLANAQSSKVVH----------MLEAHRPIALETHPNNFVQWRFTA 269
Cdd:cd05969 119 FTGKYVLDLHPDDIYwCTADPGWVTGTVYGI-WAPWLNGVTNVVYEgrfdaeswygIIERVKVTVWYTAPTAIRMLMKEG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 270 KEHPEAF--SGIRYYHSTFDAINNQTmktfLRTSMAQDAV-FLQVYGQSECGPMILKAHTLESLKtsdARDMGVGLEDMT 346
Cdd:cd05969 198 DELARKYdlSSLRFIHSVGEPLNPEA----IRWGMEVFGVpIHDTWWQTETGSIMIANYPCMPIK---PGSMGKPLPGVK 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488214859 347 SArITDSVGNVLPENTDGHIQLLSKGRAL--TYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET 419
Cdd:cd05969 271 AA-VVDENGNELPPGTKGILALKPGWPSMfrGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKT 344
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
30-509 |
4.36e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 62.10 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 30 FDEPLSAFP--------ELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYH 101
Cdd:PRK12583 24 FDATVARFPdrealvvrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 102 LPTTTMEVFIDRLEDPFILFDDETKKR-----VREISNGTKSKQ--------IP----ILYLMEQP-------------- 150
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFKTSdyhamLQELLPGLAEGQpgalacerLPelrgVVSLAPAPppgflawhelqarg 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 151 ------ALSVSQSFLDKNEISYMTHTSGTTGIPKLICHSAHSM---GWRTKwQKTVFTkiSEKKLIAfhISPVHSRFNIG 221
Cdd:PRK12583 184 etvsreALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIlnnGYFVA-ESLGLT--EHDRLCV--PVPLYHCFGMV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 222 ISSL--MSMGFPMM-------PLANAQSskvvhmLEAHRPIALETHPNNFVqwrfTAKEHPEafsgiryyHSTFDAinnq 292
Cdd:PRK12583 259 LANLgcMTVGACLVypneafdPLATLQA------VEEERCTALYGVPTMFI----AELDHPQ--------RGNFDL---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 293 tmkTFLRTS-MAQDAVFLQV----------------YGQSECGPMILKAHTLESLktsDARDMGVG-----LEdmtsARI 350
Cdd:PRK12583 317 ---SSLRTGiMAGAPCPIEVmrrvmdemhmaevqiaYGMTETSPVSLQTTAADDL---ERRVETVGrtqphLE----VKV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 351 TDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI----ETINSTlA 425
Cdd:PRK12583 387 VDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDgWMHTGDLATMDEQGYVRIVGRSKDMIirggENIYPR-E 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 426 IEDFLLDSLDFLAEVVI-VRDKNHSPQPI--IALAPDKEM------DWNRWWEQVHELPRLnvpiIRDFDAIPRTATMKV 496
Cdd:PRK12583 466 IEEFLFTHPAVADVQVFgVPDEKYGEEIVawVRLHPGHAAseeelrEFCKARIAHFKVPRY----FRFVDEFPMTVTGKV 541
|
570
....*....|....*..
gi 488214859 497 QRLQIEK----ELKSQK 509
Cdd:PRK12583 542 QKFRMREisieELALPV 558
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
45-470 |
5.90e-10 |
|
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: 61.46 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 45 TYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVmTSYhlPTTTMEvfidrlEDPFILFDDE 124
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV-PIY--PTSSAE------QIAYILNDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 125 TKkrvreisngtkskqipilylmeqpALSVSqsflDKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEK 204
Cdd:cd05907 78 AK------------------------ALFVE----DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 205 KLIAF----HI--------SPVHSRFNIGISSLMSMGFPMMplanaqsSKVvhmleahrpialethpnnfvqwrftakeH 272
Cdd:cd05907 130 RHLSFlplaHVferraglyVPLLAGARIYFASSAETLLDDL-------SEV----------------------------R 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 273 PEAFSGI-RYYHSTFDAINNQTMKTFLRTsMAQDAV----------------------------FLQVYGQSECGPMIlk 323
Cdd:cd05907 175 PTVFLAVpRVWEKVYAAIKVKAVPGLKRK-LFDLAVggrlrfaasggaplpaellhffralgipVYEGYGLTETSAVV-- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 324 ahtleSLKTSDARDMGvgledmtsaritdSVGNVLPENT-----DGHIQLlsKGRALT--YYKEDARFQENVYGD-WWDS 395
Cdd:cd05907 252 -----TLNPPGDNRIG-------------TVGKPLPGVEvriadDGEILV--RGPNVMlgYYKNPEATAEALDADgWLHT 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 396 GDYGFMDKHGHLFLKDRQVDLIetINST------LAIEDFLLDSLdFLAEVVIVRDKnhspQP-IIAL-APDKEMdWNRW 467
Cdd:cd05907 312 GDLGEIDEDGFLHITGRKKDLI--ITSGgknispEPIENALKASP-LISQAVVIGDG----RPfLVALiVPDPEA-LEAW 383
|
...
gi 488214859 468 WEQ 470
Cdd:cd05907 384 AEE 386
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-506 |
3.20e-09 |
|
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: 59.11 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 15 NFQEAAANFSETPiifdeplsAFPELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAV 94
Cdd:cd05936 4 LLEEAARRFPDKT--------ALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 95 PVMTSyhlPTTTMEVFIDRLED--PFILFDDETKKRVREISNGTKSKQIPilylmeqpalsvsqsflDKNEISYMTHTSG 172
Cdd:cd05936 76 VVPLN---PLYTPRELEHILNDsgAKALIVAVSFTDLLAAGAPLGERVAL-----------------TPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 173 TTGIPKL-------ICHSAHSMGWRTKWQKTvftkiSEKKLIA----FHIspvhsrFNIGISSLMS--MGFPMMPLANAQ 239
Cdd:cd05936 136 TTGVPKGamlthrnLVANALQIKAWLEDLLE-----GDDVVLAalplFHV------FGLTVALLLPlaLGATIVLIPRFR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 240 SSKVVHMLEAHRP----------IALETHPNnfvqwrftakEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSmaqDAVFL 309
Cdd:cd05936 205 PIGVLKEIRKHRVtifpgvptmyIALLNAPE----------FKKRDFSSLRLCISGGAPLPVEVAERFEELT---GVPIV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 310 QVYGQSECGPMIlkahTLESLKTSD-ARDMGVGLEDmTSARITDSVGNVLPENTDGhiQLLSKGRALT--YYKEDARFQE 386
Cdd:cd05936 272 EGYGLTETSPVV----AVNPLDGPRkPGSIGIPLPG-TEVKIVDDDGEELPPGEVG--ELWVRGPQVMkgYWNRPEETAE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 387 NVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----------EtinstlaIEDFLLdSLDFLAEVVIV--RDKNH------ 448
Cdd:cd05936 345 AFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIivggfnvyprE-------VEEVLY-EHPAVAEAAVVgvPDPYSgeavka 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488214859 449 --SPQPIIALAPDKEMDWNRwwEQV--HELPRLnvpiIRDFDAIPRTATMKVQRlqieKELK 506
Cdd:cd05936 417 fvVLKEGASLTEEEIIAFCR--EQLagYKVPRQ----VEFRDELPKSAVGKILR----RELR 468
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
43-501 |
3.64e-09 |
|
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: 58.64 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 43 ETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVmtsyhlPTTTMevfIDRLEDPFILFD 122
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVV------PINPM---LKERELEYILND 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 123 DETKkrvreisngtkskqipilylmeqpaLSVSQSFLDknEISYMTHTSGTTGIPKLICHSaHSMGWRTKWQKTVFTKIS 202
Cdd:cd05935 72 SGAK-------------------------VAVVGSELD--DLALIPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 203 EKKLIA-----FHISP-VHSrfnigISSLMSMGFPMMPLANAQSSKVVHMLEAHRPIALETHPNNFVQWRFTAKEHPEAF 276
Cdd:cd05935 124 PSDVILaclplFHVTGfVGS-----LNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 277 SGIRYYHSTFDAINNQTMKTFLRTSMAQdavFLQVYGQSE-CGPMILKAHTLESLKTsdardMGVGLEDmTSARITD-SV 354
Cdd:cd05935 199 SSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTEtMSQTHTNPPLRPKLQC-----LGIP*FG-VDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 355 GNVLPENTDGHIQL----LSKGraltYYKedaRFQENVYGDWWDS-------GDYGFMDKHGHLFLKDRqvdLIETIN-S 422
Cdd:cd05935 270 GRELPPNEVGEIVVrgpqIFKG----YWN---RPEETEESFIEIKgrrffrtGDLGYMDEEGYFFFVDR---VKRMINvS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 423 TLAIEDFLLDSLDF----LAEVVIV----RDKNHSPQPIIALAPDKEM--------DWNRWWEQVHELPRlnvpIIRDFD 486
Cdd:cd05935 340 GFKVWPAEVEAKLYkhpaI*EVCVIsvpdERVGEEVKAFIVLRPEYRGkvteediiEWAREQMAAYKYPR----EVEFVD 415
|
490
....*....|....*
gi 488214859 487 AIPRTATMKVQRLQI 501
Cdd:cd05935 416 ELPRSASGKILWRLL 430
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
45-509 |
3.98e-09 |
|
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: 59.04 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 45 TYKKCCESVLKRAYQLAHLGVKSGDKVIIyKSSAFDTYLLAVSVSYLGA-VPVMTSyhlptttmevfidrledpfILFDD 123
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVF-QITHNNKFLYLFWACLLGGmIAVPVS-------------------IGSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 124 ETKKRVREISNgtkskqipilyLMEQPALSVSQSFLDKN--EISYMTHTSGTTGIPK-----------LICHSAHSMGWR 190
Cdd:cd05908 77 EHKLKLNKVWN-----------TLKNPYLITEEEVLCELadELAFIQFSSGSTGDPKgvmlthenlvhNMFAILNSTEWK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 191 TK-----WqktvFTKISEKKLIAFHISPVHSrfniGISSLMsmgfpmMPLANAQSSKVVHMLEAHRPIALETHPNNFVQW 265
Cdd:cd05908 146 TKdrilsW----MPLTHDMGLIAFHLAPLIA----GMNQYL------MPTRLFIRRPILWLKKASEHKATIVSSPNFGYK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 266 RFTAKEHPEA-----FSGIRYYHSTFDAINNQTMKTFLrTSMA----QDAVFLQVYGQSECG--------------PMIL 322
Cdd:cd05908 212 YFLKTLKPEKandwdLSSIRMILNGAEPIDYELCHEFL-DHMSkyglKRNAILPVYGLAEASvgaslpkaqspfktITLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 323 KAHTL--ESLKTSDARD------MGVGLE-DMTSARITDSVGNVLPENTDGHIQLlsKGRALT--YYKeDARFQENVYGD 391
Cdd:cd05908 291 RRHVThgEPEPEVDKKDsecltfVEVGKPiDETDIRICDEDNKILPDGYIGHIQI--RGKNVTpgYYN-NPEATAKVFTD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 392 --WWDSGDYGFMdKHGHLFLKDRQVDLIeTIN---------STLAIEdflLDSLDfLAEVVI--VRDKNHSPQPIIA--- 455
Cdd:cd05908 368 dgWLKTGDLGFI-RNGRLVITGREKDII-FVNgqnvyphdiERIAEE---LEGVE-LGRVVAcgVNNSNTRNEEIFCfie 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488214859 456 -------LAP-----DKEMDWNRWWeQVHELprlnVPIIRdfdaIPRTATMKVQRLQIEKELKSQK 509
Cdd:cd05908 442 hrkseddFYPlgkkiKKHLNKRGGW-QINEV----LPIRR----IPKTTSGKVKRYELAQRYQSGE 498
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
4-509 |
7.41e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 58.12 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 4 TITYSPLNLFTNFQEAAANFSETpiifdeplSAFPELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSA----- 78
Cdd:PRK06710 18 TISYDIQPLHKYVEQMASRYPEK--------KALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCpqavi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 79 --FDTYL---LAVSVSYL-------------GA---------VPVMTSYHLPTTTMEVFIDRLED--PF---ILFDDETK 126
Cdd:PRK06710 90 gyYGTLLaggIVVQTNPLytereleyqlhdsGAkvilcldlvFPRVTNVQSATKIEHVIVTRIADflPFpknLLYPFVQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 127 KRVREISNGTKSKQIPILYLMEQPALSVSQSFLD-KNEISYMTHTSGTTGIPK--LICH----SAHSMGWRTKWQKTVFT 199
Cdd:PRK06710 170 KQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDpENDLALLQYTGGTTGFPKgvMLTHknlvSNTLMGVQWLYNCKEGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 200 KISEKKLIAFHISPVHSRFNIGISSlmsmGFPMMPLANAQSSKVVHMLEAHRPIALETHPNNFVQWRFTAKEHPEAFSGI 279
Cdd:PRK06710 250 EVVLGVLPFFHVYGMTAVMNLSIMQ----GYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 280 RYYHSTFDAINNQTMKTFLRTSMAQdavFLQVYGQSECGPMilkAHTLESLKTSDARDMGVGLEDMTSARITDSVGNVLP 359
Cdd:PRK06710 326 RACISGSAPLPVEVQEKFETVTGGK---LVEGYGLTESSPV---THSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 360 ENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTL---AIEDFLLDSlDF 436
Cdd:PRK06710 400 PGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVyprEVEEVLYEH-EK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 437 LAEVVIV----RDKNHSPQPIIALAPDK---EMDWNRWWEQVheLPRLNVPIIRDF-DAIPRTATMKV-QRLQIEKELKS 507
Cdd:PRK06710 479 VQEVVTIgvpdPYRGETVKAFVVLKEGTecsEEELNQFARKY--LAAYKVPKVYEFrDELPKTTVGKIlRRVLIEEEKRK 556
|
..
gi 488214859 508 QK 509
Cdd:PRK06710 557 NE 558
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
310-443 |
7.73e-09 |
|
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: 58.20 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 310 QVYGQSEcgpmILKAHTLEslKTSDARDMGVGLE-DMTSARITDSvgnvlpentdGHIQLLSKGRALTYYKEDARFQENV 388
Cdd:cd17641 353 QLYGQTE----LAGAYTVH--RDGDVDPDTVGVPfPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDF 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488214859 389 YGD-WWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLAIEDFLLDSLDF---LAEVVIV 443
Cdd:cd17641 417 DEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFspyIAEAVVL 475
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
311-501 |
5.89e-08 |
|
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: 54.59 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 311 VYGQSECGPMILKAHTLESLktsDARDMGVG-LEDMTSARITDSVGN-VLPENTDGhiQLLSKGRALT--YYKEDARFQE 386
Cdd:cd05917 150 AYGMTETSPVSTQTRTDDSI---EKRVNTVGrIMPHTEAKIVDPEGGiVPPVGVPG--ELCIRGYSVMkgYWNDPEKTAE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 387 NVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI----ETINSTlAIEDFLLDSLDFL-AEVVIVRDKNHSPQ--PIIALAP 458
Cdd:cd05917 225 AIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIirggENIYPR-EIEEFLHTHPKVSdVQVVGVPDERYGEEvcAWIRLKE 303
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488214859 459 DKEMDwnrwWEQVHE-----LPRLNVP-IIRDFDAIPRTATMKVQRLQI 501
Cdd:cd05917 304 GAELT----EEDIKAyckgkIAHYKVPrYVFFVDEFPLTVSGKIQKFKL 348
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
41-500 |
1.69e-07 |
|
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: 53.45 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 41 GLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRledpfil 120
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDH------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 121 fddetkkrvreisngtkskqipilylmEQPALSVSqsflDKNEISYmthTSGTTGIPKLICHSAHSMGWRTKWQKTVFTK 200
Cdd:cd05934 74 ---------------------------SGAQLVVV----DPASILY---TSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 201 ISEKKLIAFhispvhsrfnigisslmsmgfpmMPL--ANAQSSKVVHMLEAHRPIALEThpnnfvqwRFTAKehpeAF-S 277
Cdd:cd05934 120 GEDDVYLTV-----------------------LPLfhINAQAVSVLAALSVGATLVLLP--------RFSAS----RFwS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 278 GIRYYHST-FDAINnqTMKTFLrtsMAQ-----DA--------------------------VFLQVYGQSECGPMILKAH 325
Cdd:cd05934 165 DVRRYGATvTNYLG--AMLSYL---LAQppspdDRahrlraaygapnppelheefeerfgvRLLEGYGMTETIVGVIGPR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 326 TleslktSDARDMGVG-LEDMTSARITDSVGNVLPENTDGHIQLLS---KGRALTYYKEDARFQENVYGDWWDSGDYGFM 401
Cdd:cd05934 240 D------EPRRPGSIGrPAPGYEVRIVDDDGQELPAGEPGELVIRGlrgWGFFKGYYNMPEATAEAMRNGWFHTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 402 DKHGHLFLKDRQVDLI----ETInSTLAIEDFLL--------------DSL--DFLAEVVIVRDknhsPQPiiaLAPDKE 461
Cdd:cd05934 314 DADGFFYFVDRKKDMIrrrgENI-SSAEVERAILrhpavreaavvavpDEVgeDEVKAVVVLRP----GET---LDPEEL 385
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488214859 462 MDWNRwwEQvheLPRLNVP-IIRDFDAIPRTATMKVQRLQ 500
Cdd:cd05934 386 FAFCE--GQ---LAYFKVPrYIRFVDDLPKTPTEKVAKAQ 420
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
96-412 |
2.19e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 53.28 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 96 VMTSYHLPTTTMEVFIDRLEDPFIL-FDDETKKRVreisngTKSKQIPILYLMEQPALSVSQSF----LDKNEISYMTHT 170
Cdd:PRK06334 118 VLTSKQLMQHLAQTHGEDAEYPFSLiYMEEVRKEL------SFWEKCRIGIYMSIPFEWLMRWFgvsdKDPEDVAVILFT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 171 SGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAFhISPVHSR-FNIGISSLMSMGFPMMPLANA-QSSKVVHMLE 248
Cdd:PRK06334 192 SGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSF-LPPFHAYgFNSCTLFPLLSGVPVVFAYNPlYPKKIVEMID 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 249 AHRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINN----QTMKTFLRTSMAQDavflqvYGQSECGPMIlKA 324
Cdd:PRK06334 271 EAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDslyqEALKTFPHIQLRQG------YGTTECSPVI-TI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 325 HTLESLKtsDARDMGVGLEDMTSARITDSVGNVLPENTDGHIqlLSKGRAL--TYYKEDAR--FQENVYGDWWDSGDYGF 400
Cdd:PRK06334 344 NTVNSPK--HESCVGMPIRGMDVLIVSEETKVPVSSGETGLV--LTRGTSLfsGYLGEDFGqgFVELGGETWYVTGDLGY 419
|
330
....*....|..
gi 488214859 401 MDKHGHLFLKDR 412
Cdd:PRK06334 420 VDRHGELFLKGR 431
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
43-507 |
2.22e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 53.33 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 43 ETTYKKCCESVLKRAYQLAH-LGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVfidRLEDPFI-- 119
Cdd:PRK06839 27 EMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIF---QLKDSGTtv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 120 LFDDETKKRVREISNGTKSKQIPILylMEQPALSVSQS---FLDKNE-----ISYmthTSGTTGIPKLICHSAHSMGWRT 191
Cdd:PRK06839 104 LFVEKTFQNMALSMQKVSYVQRVIS--ITSLKEIEDRKidnFVEKNEsasfiICY---TSGTTGKPKGAVLTQENMFWNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 192 KWQKTVFTKISEKKLIA----FHISpvhsrfNIGI---SSLMSMGFPMMPlANAQSSKVVHMLEAHRPIALETHPNNFVQ 264
Cdd:PRK06839 179 LNNTFAIDLTMHDRSIVllplFHIG------GIGLfafPTLFAGGVIIVP-RKFEPTKALSMIEKHKVTVVMGVPTIHQA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 265 WRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSMaqdaVFLQVYGQSECGPMILKAhtlesLKTSDARDMG-VGLE 343
Cdd:PRK06839 252 LINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGF----LFGQGFGMTETSPTVFML-----SEEDARRKVGsIGKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 344 DM-TSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----E 418
Cdd:PRK06839 323 VLfCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIisggE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 419 TInSTLAIEDfLLDSLDFLAE--VVIVRDKNHSPQPIIALAPDKEMDWNRWWEQVHELPRL-NVPIIRDF---DAIPRTA 492
Cdd:PRK06839 403 NI-YPLEVEQ-VINKLSDVYEvaVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLaKYKIPKEIvflKELPKNA 480
|
490
....*....|....*
gi 488214859 493 TMKVQRLQIEKELKS 507
Cdd:PRK06839 481 TGKIQKAQLVNQLKS 495
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
162-509 |
7.56e-07 |
|
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: 51.70 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 162 NEISYMTHTSGTTGIPKLICHSAHSMG---------WRTKWQKTVFTKISE----KKLIAFHISP--------VHS--RF 218
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGlglkvngryWLDLTASDIMWNTSDtgwiKSAWSSLFEPwiqgacvfVHHlpRF 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 219 --NIGISSLMSmgFPMMPLANAQSskVVHMLEAhrpialethpNNFVQWRFTAKEHpeafsgiryYHSTFDAINNQTMKT 296
Cdd:cd05928 254 dpLVILKTLSS--YPITTFCGAPT--VYRMLVQ----------QDLSSYKFPSLQH---------CVTGGEPLNPEVLEK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 297 FlrtsMAQDAVFL-QVYGQSECGpmiLKAHTLESLKTSDArDMGVGLEDMtSARITDSVGNVLPENTDGHIQL-LSKGRA 374
Cdd:cd05928 311 W----KAQTGLDIyEGYGQTETG---LICANFKGMKIKPG-SMGKASPPY-DVQIIDDNGNVLPPGTEGDIGIrVKPIRP 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 375 LT----YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIetINSTLAIEDFLLDSL----DFLAEVVIVRdk 446
Cdd:cd05928 382 FGlfsgYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVI--NSSGYRIGPFEVESAliehPAVVESAVVS-- 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488214859 447 nhSPQPI--------IALAPD-KEMDWNRWWEQVHE-LPRLNVPI-----IRDFDAIPRTATMKVQRlqieKELKSQK 509
Cdd:cd05928 458 --SPDPIrgevvkafVVLAPQfLSHDPEQLTKELQQhVKSVTAPYkyprkVEFVQELPKTVTGKIQR----NELRDKE 529
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
309-503 |
1.18e-06 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 51.25 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 309 LQVYGQSECGPMIlkahtleSLKTSDARDMGvgledmtsaritdSVGNVLPENT-----DGHIQLlsKGRALT--YYKED 381
Cdd:COG1022 375 LEGYGLTETSPVI-------TVNRPGDNRIG-------------TVGPPLPGVEvkiaeDGEILV--RGPNVMkgYYKNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 382 ARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLIetINST------LAIEDFLLDSlDFLAEVVIVRDKnhspQP-I 453
Cdd:COG1022 433 EATAEAFDADgWLHTGDIGELDEDGFLRITGRKKDLI--VTSGgknvapQPIENALKAS-PLIEQAVVVGDG----RPfL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 454 IAL-APDKEMdWNRWWEQvHELP----------------------RLN--VPI---IRDFDAIPR---------TATMKV 496
Cdd:COG1022 506 AALiVPDFEA-LGEWAEE-NGLPytsyaelaqdpevraliqeevdRANagLSRaeqIKRFRLLPKeftiengelTPTLKL 583
|
....*..
gi 488214859 497 QRLQIEK 503
Cdd:COG1022 584 KRKVILE 590
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
167-507 |
1.21e-06 |
|
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: 50.75 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 167 MTHTSGTTGIPKLICHS-----AHSMGWRTKWQKTvftkiSEKKLIafHISP---VHSRFNIGISSLMSMG-FPMMPLAN 237
Cdd:cd05941 94 ILYTSGTTGRPKGVVLThanlaANVRALVDAWRWT-----EDDVLL--HVLPlhhVHGLVNALLCPLFAGAsVEFLPKFD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 238 AqssKVVHMLEAHRPIA------------LETHPNNFVQWRFTAKEHPEafsGIRYYHSTFDAINNQTMKTFLRTSmaqD 305
Cdd:cd05941 167 P---KEVAISRLMPSITvfmgvptiytrlLQYYEAHFTDPQFARAAAAE---RLRLMVSGSAALPVPTLEEWEAIT---G 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 306 AVFLQVYGQSECGpMILkAHTLESlktsDARDMGVGLEDMT-SARITD-SVGNVLPENTDGHIQLLSKGRALTYYKEDAR 383
Cdd:cd05941 238 HTLLERYGMTEIG-MAL-SNPLDG----ERRPGTVGMPLPGvQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 384 FQENVYGD-WWDSGDYGFMDKHGHLFLKDRQ-VDLIET----InSTLAIEDfLLDSLDFLAEVVIV----RDKNHSPQPI 453
Cdd:cd05941 312 TKEEFTDDgWFKTGDLGVVDEDGYYWILGRSsVDIIKSggykV-SALEIER-VLLAHPGVSECAVIgvpdPDWGERVVAV 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214859 454 IALAPDKE----MDWNRWWEQV---HELPRLnvpiIRDFDAIPRTATMKVQRlqieKELKS 507
Cdd:cd05941 390 VVLRAGAAalslEELKEWAKQRlapYKRPRR----LILVDELPRNAMGKVNK----KELRK 442
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
160-447 |
1.42e-06 |
|
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: 50.52 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 160 DKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAF----HISPVHSRFNIGisslMSMGFPMMPL 235
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSIlplhHIYPLTFTLLLP----LLNGAHVVFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 236 ANAQSSKVVHMLEAH-RPIA----------------------------LETHPNNFVQWRFTAKEHPEAFSG-IRYYHST 285
Cdd:cd05914 163 DKIPSAKIIALAFAQvTPTLgvpvplviekifkmdiipkltlkkfkfkLAKKINNRKIRKLAFKKVHEAFGGnIKEFVIG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 286 FDAINNQTMKtFLRTSmaqDAVFLQVYGQSECGPMILKAHTlESLKTSDArdmGVGLEDMtSARITDSVgnvlPENTDGH 365
Cdd:cd05914 243 GAKINPDVEE-FLRTI---GFPYTIGYGMTETAPIISYSPP-NRIRLGSA---GKVIDGV-EVRIDSPD----PATGEGE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 366 IQLLSKGRALTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI----------ETINSTLAIEDFLLDSL 434
Cdd:cd05914 310 IIVRGPNVMKGYYKNPEATAEAFDKDgWFHTGDLGKIDAEGYLYIRGRKKEMIvlssgkniypEEIEAKINNMPFVLESL 389
|
330
....*....|...
gi 488214859 435 dflaevVIVRDKN 447
Cdd:cd05914 390 ------VVVQEKK 396
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
349-509 |
1.87e-06 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 50.52 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 349 RITDSVGNVLPE--NTDGHIQLLSKGRALTYYKEDARFQENvyGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInS 422
Cdd:PRK06018 368 KITDDAGKELPWdgKTFGRLKVRGPAVAAAYYRVDGEILDD--DGFFDTGDVATIDAYGYMRITDRSKDVIksggEWI-S 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 423 TLAIEDFLLDSLDF-LAEVVIVRDKNHSPQP--IIALAPDKE---------MDWN--RWWeqvheLPRlNVPIIrdfDAI 488
Cdd:PRK06018 445 SIDLENLAVGHPKVaEAAVIGVYHPKWDERPllIVQLKPGETatreeilkyMDGKiaKWW-----MPD-DVAFV---DAI 515
|
170 180
....*....|....*....|.
gi 488214859 489 PRTATMKVQRLQIEKELKSQK 509
Cdd:PRK06018 516 PHTATGKILKTALREQFKDYK 536
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
163-419 |
3.31e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 49.60 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 163 EISYMTHTSGTTGIPKLICHSAHSMGWRTKWQktvftkisekkLIAFHIsPVHSRFnigissLMSMgfpmmPLANAQSSK 242
Cdd:PRK06188 169 DIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQ-----------LAEWEW-PADPRF------LMCT-----PLSHAGGAF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 243 VV---------HMLEAHRP----IALETHpnnfvqwRFTAK-----------EHPEA----FSGIR--YYHSTfdAIN-- 290
Cdd:PRK06188 226 FLptllrggtvIVLAKFDPaevlRAIEEQ-------RITATflvptmiyallDHPDLrtrdLSSLEtvYYGAS--PMSpv 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 291 --NQTMKTFlrtsmaqDAVFLQVYGQSECgPMIL-----KAHTLES--LKTSDARDMgVGLEdmtsARITDSVGNVLPEN 361
Cdd:PRK06188 297 rlAEAIERF-------GPIFAQYYGQTEA-PMVItylrkRDHDPDDpkRLTSCGRPT-PGLR----VALLDEDGREVAQG 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488214859 362 TDGHI----QLLSKGraltYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET 419
Cdd:PRK06188 364 EVGEIcvrgPLVMDG----YWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVT 421
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
377-509 |
3.66e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 49.56 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 377 YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFLAEVVIVR--DK-NHS 449
Cdd:PRK08162 402 YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIisggENI-SSIEVEDVLYRHPAVLVAAVVAKpdPKwGEV 480
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488214859 450 PQPIIALAPDKE------MDWNRwweqvHELPRLNVPIIRDFDAIPRTATMKVQRLQIEKELKSQK 509
Cdd:PRK08162 481 PCAFVELKDGASateeeiIAHCR-----EHLAGFKVPKAVVFGELPKTSTGKIQKFVLREQAKSLK 541
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
349-450 |
4.06e-06 |
|
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: 49.62 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 349 RITDSVGNVLPENTDGHIQL---LSKGRALTYYKEDARFQENVYGD---WWDSGDYGFMDKHGHLFLKDRQVDLIETIN- 421
Cdd:cd05967 423 QVLDEDGEPVGPNELGNIVIklpLPPGCLLTLWKNDERFKKLYLSKfpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGh 502
|
90 100 110
....*....|....*....|....*....|....*
gi 488214859 422 --STLAIEDFLLDSLDfLAE--VVIVRD--KNHSP 450
Cdd:cd05967 503 rlSTGEMEESVLSHPA-VAEcaVVGVRDelKGQVP 536
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
339-498 |
4.60e-06 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 49.30 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 339 GVGLEdmtsARITDSVGNVLPENTDGHIQLLS-KGRAL--TYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQV 414
Cdd:PRK08008 346 GFCYE----AEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYYLDPKATAKVLEADgWLHTGDTGYVDEEGFFYFVDRRC 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 415 DLI----ETINSTlAIEDFLLDSLDFLAEVVI-----VRDKnhSPQPIIALAPDKEMDWNRWWEQVHE-LPRLNVPIIRD 484
Cdd:PRK08008 422 NMIkrggENVSCV-ELENIIATHPKIQDIVVVgikdsIRDE--AIKAFVVLNEGETLSEEEFFAFCEQnMAKFKVPSYLE 498
|
170
....*....|....*
gi 488214859 485 F-DAIPRTATMKVQR 498
Cdd:PRK08008 499 IrKDLPRNCSGKIIK 513
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
36-501 |
4.89e-06 |
|
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: 48.78 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 36 AFPELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGA--VPVMTSYhlptttmevfidr 113
Cdd:cd05945 9 AVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDASS------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 114 ledpfilfddeTKKRVREISNgtkskqipilylMEQPALSVSqsflDKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKW 193
Cdd:cd05945 76 -----------PAERIREILD------------AAKPALLIA----DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 194 QKTVFtKISEKKLIAFHiSPVHsrFNIgisSLMSMgFP-------MMPLANAQSSKVVHMLE--AHRPIA---------- 254
Cdd:cd05945 129 MLSDF-PLGPGDVFLNQ-APFS--FDL---SVMDL-YPalasgatLVPVPRDATADPKQLFRflAEHGITvwvstpsfaa 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 255 -LETHPNnfvqwrFTAKEHPeafsGIRyyHSTF--DAINNQTMKTFLRtsMAQDAVFLQVYGQSECGPMILKAH-TLESL 330
Cdd:cd05945 201 mCLLSPT------FTPESLP----SLR--HFLFcgEVLPHKTARALQQ--RFPDARIYNTYGPTEATVAVTYIEvTPEVL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 331 KTSDARDMGVGLEDMTsARITDSVGNVLPENTDGHIQLLSKGRALTYY----KEDARFQENVYGDWWDSGDYGFMDKHGH 406
Cdd:cd05945 267 DGYDRLPIGYAKPGAK-LVILDEDGRPVPPGEKGELVISGPSVSKGYLnnpeKTAAAFFPDEGQRAYRTGDLVRLEADGL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 407 LFL---KDRQVDL----IEtinstLA-IEDFLLDSlDFLAEVVIV-RDKNHSPQPIIAL----APDKEMDWNRWWEQV-H 472
Cdd:cd05945 346 LFYrgrLDFQVKLngyrIE-----LEeIEAALRQV-PGVKEAVVVpKYKGEKVTELIAFvvpkPGAEAGLTKAIKAELaE 419
|
490 500 510
....*....|....*....|....*....|..
gi 488214859 473 ELPRLNVPiiRDF---DAIPRTATMKVQRLQI 501
Cdd:cd05945 420 RLPPYMIP--RRFvylDELPLNANGKIDRKAL 449
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
348-498 |
1.07e-05 |
|
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: 47.86 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 348 ARITDSVGNVLPENTDGhiQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA-- 425
Cdd:cd05958 276 AKVVDDEGNPVPDGTIG--RLAVRGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIApp 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 426 -IEDFLLDSLDfLAEVVIV----RDKNHSPQPIIALAPDKEMDwnrwwEQ-VHEL-------------PRLnvpiIRDFD 486
Cdd:cd05958 354 eVEDVLLQHPA-VAECAVVghpdESRGVVVKAFVVLRPGVIPG-----PVlARELqdhakahiapykyPRA----IEFVT 423
|
170
....*....|..
gi 488214859 487 AIPRTATMKVQR 498
Cdd:cd05958 424 ELPRTATGKLQR 435
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
29-505 |
1.23e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 47.69 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 29 IFDEPLSAFPE------LGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIY------KSSAFdtYllavSVSYLGAVPV 96
Cdd:PRK05605 37 LYDNAVARFGDrpaldfFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVlpncpqHIVAF--Y----AVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 97 mtsYHLPTTTMEvfidRLEDPF-------ILFDDETKKRVREISNGTKSKQI-------------------PILYLMEQ- 149
Cdd:PRK05605 111 ---EHNPLYTAH----ELEHPFedhgarvAIVWDKVAPTVERLRRTTPLETIvsvnmiaampllqrlalrlPIPALRKAr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 150 PALSVS-------QSFLD----------------KNEISYMTHTSGTTGIPK--------LICHSAHSMGW---RTKWQK 195
Cdd:PRK05605 184 AALTGPapgtvpwETLVDaaiggdgsdvshprptPDDVALILYTSGTTGKPKgaqlthrnLFANAAQGKAWvpgLGDGPE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 196 TVFTKisekkLIAFHISPVhsrfNIGISSLMSMGFPMMPLANAQSSKVVHMLEAHRPIALETHPNNFVQWRFTAKEHPEA 275
Cdd:PRK05605 264 RVLAA-----LPMFHAYGL----TLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 276 FSGIRYyhsTFDAINNQTMKTFLRTSMAQDAVFLQVYGQSECGPMILkAHTLeslktSDARD---MGVGLEDmTSARITD 352
Cdd:PRK05605 335 LSGVRN---AFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIV-GNPM-----SDDRRpgyVGVPFPD-TEVRIVD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 353 --SVGNVLPENTDGhiQLLSKGRALT--YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET--INSTLA- 425
Cdd:PRK05605 405 peDPDETMPDGEEG--ELLVRGPQVFkgYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITggFNVYPAe 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 426 IEDFLLD-----------------SLDFLAEVVIVrdknhspqPIIALAPDKEMDWNRwweqvHELPRLNVP-IIRDFDA 487
Cdd:PRK05605 483 VEEVLREhpgvedaavvglpredgSEEVVAAVVLE--------PGAALDPEGLRAYCR-----EHLTRYKVPrRFYHVDE 549
|
570
....*....|....*...
gi 488214859 488 IPRTATMKVQRLQIEKEL 505
Cdd:PRK05605 550 LPRDQLGKVRRREVREEL 567
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
169-503 |
1.31e-05 |
|
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: 47.48 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 169 HTSGTTGIPKLICHSaHSMGWRTKWQKTVFTKISEKKLIAFHISPVHsrfnigISSLMSMGfpMMPLANAQSSKVVHMLE 248
Cdd:cd05944 9 HTGGTTGTPKLAQHT-HSNEVYNAWMLALNSLFDPDDVLLCGLPLFH------VNGSVVTL--LTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 249 AHRPIALEthpnNFvqWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSMA-------------QDAVFLQV---Y 312
Cdd:cd05944 80 YRNPGLFD----NF--WKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSgaaplpvelrarfEDATGLPVvegY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 313 GQSECGpmilKAHTLeSLKTSDARDMGVGLE---DMTSARITDSVGNVLPE---NTDGHIQLLSKG-RALTYYKEDARfq 385
Cdd:cd05944 154 GLTEAT----CLVAV-NPPDGPKRPGSVGLRlpyARVRIKVLDGVGRLLRDcapDEVGEICVAGPGvFGGYLYTEGNK-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 386 eNVYGD--WWDSGDYGFMDKHGHLFLKDRQVDLI----ETINSTLaIEDFLLDSLDFLAEVVIVRDKNHS---PQPIIAL 456
Cdd:cd05944 227 -NAFVAdgWLNTGDLGRLDADGYLFITGRAKDLIirggHNIDPAL-IEEALLRHPAVAFAGAVGQPDAHAgelPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488214859 457 APDKE------MDWNRwwEQVHElpRLNVPI-IRDFDAIPRTATMKVQRLQIEK 503
Cdd:cd05944 305 KPGAVveeeelLAWAR--DHVPE--RAAVPKhIEVLEELPVTAVGKVFKPALRA 354
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
350-498 |
1.87e-05 |
|
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: 46.87 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 350 ITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRqvdLIETIN------ST 423
Cdd:cd17635 183 LAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGR---SSESINcggvkiAP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 424 LAIEDFLLDSLDF-LAEVVIVRDKNHSPQPIIALAPDKEMDWNRWWEQVH----ELPRLNVP-IIRDFDAIPRTATMKVQ 497
Cdd:cd17635 260 DEVERIAEGVSGVqECACYEISDEEFGELVGLAVVASAELDENAIRALKHtirrELEPYARPsTIVIVTDIPRTQSGKVK 339
|
.
gi 488214859 498 R 498
Cdd:cd17635 340 R 340
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
16-498 |
4.82e-05 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 45.62 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 16 FQEAAANFSETPIIFDEplsafpelGLETTYKKCCEsvlkRAYQLAHL----GVKSGDKVIIY--KSSAFDTYLLAVSVS 89
Cdd:cd17645 4 FEEQVERTPDHVAVVDR--------GQSLTYKQLNE----KANQLARHlrgkGVKPDDQVGIMldKSLDMIAAILGVLKA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 90 YLGAVPVMTSYhlPTTTMEvfidrledpFILFDDETKkrvreisngtkskqipilYLMEQPalsvsqsfldkNEISYMTH 169
Cdd:cd17645 72 GGAYVPIDPDY--PGERIA---------YMLADSSAK------------------ILLTNP-----------DDLAYVIY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 170 TSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKliafhiSPVHSRFNIGiSSLMSMgFPMMpLANAQsskvVHMLEA 249
Cdd:cd17645 112 TSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK------SLVYASFSFD-ASAWEI-FPHL-TAGAA----LHVVPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 250 HRPIALETHPNNFVQWRFTAKEHPEAFSgiryyhSTFDAINNQTMKTF------LRTSMAQDAVFLQVYGQSECGPMilk 323
Cdd:cd17645 179 ERRLDLDALNDYFNQEGITISFLPTGAA------EQFMQLDNQSLRVLltggdkLKKIERKGYKLVNNYGPTENTVV--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 324 AHTLESLKTSDARDMGVGLeDMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYgfMDK 403
Cdd:cd17645 250 ATSFEIDKPYANIPIGKPI-DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGER--MYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 404 HGHL--FLKDRQVDLIETINSTLA----------IEDFLLD-SLDFLAEVVIVRDKNHSPQPIIALAPDKEMDWNRWWEQ 470
Cdd:cd17645 327 TGDLakFLPDGNIEFLGRLDQQVKirgyriepgeIEPFLMNhPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREW 406
|
490 500 510
....*....|....*....|....*....|
gi 488214859 471 VHE-LPRLNVP-IIRDFDAIPRTATMKVQR 498
Cdd:cd17645 407 LKNdLPDYMIPtYFVHLKALPLTANGKVDR 436
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
349-417 |
4.91e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 45.84 E-value: 4.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 349 RITDSVGNVLPENTDGHIQLLSKGRAL-TYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PRK12406 336 RFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMV 405
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
349-417 |
5.99e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 45.45 E-value: 5.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214859 349 RITDSVGNVLPENTDGHIqLLSKGRALTYYKEDARFQE--NVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PRK13391 339 HILDDDGAELPPGEPGTI-WFEGGRPFEYLNDPAKTAEarHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
346-505 |
6.60e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 45.42 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 346 TSARITDSV-GNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTL 424
Cdd:PRK06178 396 TEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSV 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 425 ---AIEDFLLDSLDFLAEVVIVR---DKNHSPQPIIALAPDKEMDWnrwwEQVHELPRLN-----VPIIRDFDAIPRTAT 493
Cdd:PRK06178 476 fpsEVEALLGQHPAVLGSAVVGRpdpDKGQVPVAFVQLKPGADLTA----AALQAWCRENmavykVPEIRIVDALPMTAT 551
|
170
....*....|..
gi 488214859 494 MKVQRLQIEKEL 505
Cdd:PRK06178 552 GKVRKQDLQALA 563
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
36-510 |
7.39e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 45.15 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 36 AFPELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVIIY--KSSAFDTYLLAVSVsyLGAVPVMTSYHLptTTMEVfidr 113
Cdd:PRK07786 35 ALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILmlNRTEFVESVLAANM--LGAIAVPVNFRL--TPPEI---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 114 ledPFILFDDETKKRVRE--------------------ISNGTKSKQIPILY--LMEQPALSVSQSFLDKNEISYMTHTS 171
Cdd:PRK07786 107 ---AFLVSDCGAHVVVTEaalapvatavrdivpllstvVVAGGSSDDSVLGYedLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 172 GTTGIPK--LICHS---AHSMGWRTKWQKTVFTKISEKKLIAFHISPVHSrfnigISSLMSMGFPMM--PLANAQSSKVV 244
Cdd:PRK07786 184 GTTGRPKgaVLTHAnltGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGS-----MLPGLLLGAPTViyPLGAFDPGQLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 245 HMLEAHRPIALETHPnnfVQWRF-----TAKEHPEAFSGIRYYHS-TFDAINNQTMKTFlrtsmaQDAVFLQVYGQSECG 318
Cdd:PRK07786 259 DVLEAEKVTGIFLVP---AQWQAvcaeqQARPRDLALRVLSWGAApASDTLLRQMAATF------PEAQILAAFGQTEMS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 319 PMILkahtleSLKTSDA-RDMG-VG-LEDMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDS 395
Cdd:PRK07786 330 PVTC------MLLGEDAiRKLGsVGkVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 396 GDYGFMDKHGHLFLKDRQVDLI----ETINSTlAIEDFLLDSLDFLAEVVIVR--DK-NHSPQPIIALAPDKEM----DW 464
Cdd:PRK07786 404 GDLVRQDEEGYVWVVDRKKDMIisggENIYCA-EVENVLASHPDIVEVAVIGRadEKwGEVPVAVAAVRNDDAAltleDL 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 488214859 465 NRWWEQvhELPRLNVP-IIRDFDAIPRTATMKVQRLQIEKELKSQKS 510
Cdd:PRK07786 483 AEFLTD--RLARYKHPkALEIVDALPRNPAGKVLKTELRERYGACVN 527
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
166-417 |
1.01e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 45.12 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 166 YMTHTSGTTGIPKLICHS--AHSMGWRTKWQktvFTKISEKKLIAF-HISPVHSRFNIGISSLMSMGFPMMpLANAQSSK 242
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSngPHLVGLKYYWR---SIIEKDIPTVVFsHSSIGWVSFHGFLYGSLSLGNTFV-MFEGGIIK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 243 VVHM-------LEAHRPIALETHPNNFvqwRFTAKEHPEAfsgiRYYHSTFDAIN-----------NQTMKTFLRTSMAQ 304
Cdd:PTZ00237 334 NKHIeddlwntIEKHKVTHTLTLPKTI---RYLIKTDPEA----TIIRSKYDLSNlkeiwcggeviEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 305 DAvfLQVYGQSECGPMILKAHTLESLKTSDARDMGVGLEDMtsarITDSVGNVLPENTDGHIQL---LSKGRALTYYKED 381
Cdd:PTZ00237 407 KS--SRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPS----ILSEDGKELNVNEIGEVAFklpMPPSFATTFYKND 480
|
250 260 270
....*....|....*....|....*....|....*...
gi 488214859 382 ARFQE--NVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PTZ00237 481 EKFKQlfSKFPGYYNSGDLGFKDENGYYTIVSRSDDQI 518
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1-453 |
1.22e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 44.61 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 1 MMETITYSPLNL----FTNFQEA---AANfSETPIIFdepLSAFPELGLETTYKKCCESVLKRAYQLAHLGVKSGDKVII 73
Cdd:PRK09192 4 MSPTPTTSSLPRryadFPTLVEAldyAAL-GEAGMNF---YDRRGQLEEALPYQTLRARAEAGARRLLALGLKPGDRVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 74 YKSSAFDTYLLAVSVSYLGAVPVmtSYHLPTT--TMEVFIDRLE------DP-FILFDDETKKRVREISNGTKSKQI-PI 143
Cdd:PRK09192 80 IAETDGDFVEAFFACQYAGLVPV--PLPLPMGfgGRESYIAQLRgmlasaQPaAIITPDELLPWVNEATHGNPLLHVlSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 144 LYLMEQPALSVSQSFLDKNEISYMTHTSGTTGIPK--LICHSA----------------------------HSMGwrtkw 193
Cdd:PRK09192 158 AWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRgvIITHRAlmanlraishdglkvrpgdrcvswlpfyHDMG----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 194 qktvftkisekkLIAFHISPVHSRfnIGISSLMSMGFPMMPLA-------N----AQSSKVVHMLEAHRPIALETHPNNF 262
Cdd:PRK09192 233 ------------LVGFLLTPVATQ--LSVDYLPTRDFARRPLQwldlisrNrgtiSYSPPFGYELCARRVNSKDLAELDL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 263 VQWRftakehpeaFSGIryyhsTFDAINNQTMKTF---LRTSMAQDAVFLQVYGQSE-----------CGpmiLKAHTLE 328
Cdd:PRK09192 299 SCWR---------VAGI-----GADMIRPDVLHQFaeaFAPAGFDDKAFMPSYGLAEatlavsfsplgSG---IVVEEVD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 329 -------------SLKTSDARDM---GVGLEDMTsARITDSVGNVLPENTDGHIqlLSKGRALT--YYKEDARFQENVYG 390
Cdd:PRK09192 362 rdrleyqgkavapGAETRRVRTFvncGKALPGHE-IEIRNEAGMPLPERVVGHI--CVRGPSLMsgYFRDEESQDVLAAD 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488214859 391 DWWDSGDYGFMdKHGHLFLKDRQVDLIetinstlaiedflldsldflaevvIVRDKNHSPQPI 453
Cdd:PRK09192 439 GWLDTGDLGYL-LDGYLYITGRAKDLI------------------------IINGRNIWPQDI 476
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
55-501 |
1.23e-04 |
|
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: 44.79 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 55 KRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDEtkKRVREISN 134
Cdd:cd05970 59 KTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE--DNIPEEIE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 135 GTKSkQIPILYLMEQPALSVSQSFLD---------------------KNE-ISYMTHTSGTTGIPKLICHS--------A 184
Cdd:cd05970 137 KAAP-ECPSKPKLVWVGDPVPEGWIDfrkliknaspdferptansypCGEdILLVYFSSGTTGMPKMVEHDftyplghiV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 185 HSMGWR-------------TKWQKTVFTKISEKKLIAFHISPV-HSRFNigisslmsmgfpmmplanaqSSKVVHMLEAH 250
Cdd:cd05970 216 TAKYWQnvregglhltvadTGWGKAVWGKIYGQWIAGAAVFVYdYDKFD--------------------PKALLEKLSKY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 251 RPIALETHPNNFvqwRFTAKEHPEA--FSGIRYYHSTFDAINNQTMKTFLRTSMAQdavFLQVYGQSECGPMILKAHTLE 328
Cdd:cd05970 276 GVTTFCAPPTIY---RFLIREDLSRydLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIATFPWME 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 329 SLKTSDARDM-GVGLEdmtsarITDSVGNVLPENTDGHIQL-LSKGRAL----TYYKEDARFQENVYGDWWDSGDYGFMD 402
Cdd:cd05970 350 PKPGSMGKPApGYEID------LIDREGRSCEAGEEGEIVIrTSKGKPVglfgGYYKDAEKTAEVWHDGYYHTGDAAWMD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 403 KHGHLFLKDRQVDLIETinSTLAIEDFLLDSLDFLAEVVIVRDKNHSPQPI--------IALAPDKE---------MDWN 465
Cdd:cd05970 424 EDGYLWFVGRTDDLIKS--SGYRIGPFEVESALIQHPAVLECAVTGVPDPIrgqvvkatIVLAKGYEpseelkkelQDHV 501
|
490 500 510
....*....|....*....|....*....|....*.
gi 488214859 466 RWWEQVHELPRlnvpIIRDFDAIPRTATMKVQRLQI 501
Cdd:cd05970 502 KKVTAPYKYPR----IVEFVDELPKTISGKIRRVEI 533
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
392-506 |
2.00e-04 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 43.97 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 392 WWDSGDYGFMDKHGHLFLKDRQVDLI----ETINSTlAIEDFLLDSLDFLAEVVI----------------VRDKNHSP- 450
Cdd:PRK06087 411 WYYSGDLCRMDEAGYIKITGRKKDIIvrggENISSR-EVEDILLQHPKIHDACVVampderlgerscayvvLKAPHHSLt 489
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488214859 451 -QPIIALAPDKEMDWNRWWEqvhelpRLNVpiirdFDAIPRTATMKVQRLQIEKELK 506
Cdd:PRK06087 490 lEEVVAFFSRKRVAKYKYPE------HIVV-----IDKLPRTASGKIQKFLLRKDIM 535
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
349-417 |
2.09e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 43.74 E-value: 2.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 349 RITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYG-DWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PRK08276 326 RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMI 395
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
270-417 |
3.12e-04 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 43.50 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 270 KEHPeaFSGIRYYHSTFDA-INNQTMKTF----LRTS----MA-QDAV-----------FLQVYGQSECGPMI-LKAHTL 327
Cdd:PRK08974 296 KKYP--FTAITGVNTLFNAlLNNEEFQELdfssLKLSvgggMAvQQAVaerwvkltgqyLLEGYGLTECSPLVsVNPYDL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 328 ESLKTSdardmgVGLE-DMTSARITDSVGNVLPENTDGhiQLLSKG-RALTYYKEDARFQENVYGD-WWDSGDYGFMDKH 404
Cdd:PRK08974 374 DYYSGS------IGLPvPSTEIKLVDDDGNEVPPGEPG--ELWVKGpQVMLGYWQRPEATDEVIKDgWLATGDIAVMDEE 445
|
170
....*....|...
gi 488214859 405 GHLFLKDRQVDLI 417
Cdd:PRK08974 446 GFLRIVDRKKDMI 458
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
43-180 |
3.87e-04 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 43.07 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 43 ETTYKKCCESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFD 122
Cdd:PRK05857 41 ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVA 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488214859 123 DETK---KRVREISNGTKSKQIPILYLMEQPALSVSQSFLDKN------EISYMTHTSGTTGIPKLI 180
Cdd:PRK05857 121 PGSKmasSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNadqgseDPLAMIFTSGTTGEPKAV 187
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
310-498 |
3.99e-04 |
|
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: 42.80 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 310 QVYGQSECGPMILKAHTLESLKTSDardMGVGLEDMTsARITDSVGNVLPENTDGHIQLLSKGRA--LTYYKEDARFQEN 387
Cdd:cd05971 237 EFYGQTECNLVIGNCSALFPIKPGS---MGKPIPGHR-VAIVDDNGTPLPPGEVGEIAVELPDPVafLGYWNNPSATEKK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 388 VYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA---IEDFLLDSLDFL------------AEVV---IVRDKNHS 449
Cdd:cd05971 313 MAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGpaeIEECLLKHPAVLmaavvgipdpirGEIVkafVVLNPGET 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488214859 450 PQPIIAlapdKEMDwnrwwEQV------HELPRLnvpiIRDFDAIPRTATMKVQR 498
Cdd:cd05971 393 PSDALA----REIQ-----ELVktrlaaHEYPRE----IEFVNELPRTATGKIRR 434
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
350-510 |
5.71e-04 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 42.66 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 350 ITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA--- 425
Cdd:PLN02330 375 IDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDgWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVApae 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 426 IEDFLLD--SLDFLAeVVIVRDKNHSPQPIIALAPDKEMDWNRwwEQVHELPRLNVP------IIRDFDAIPRTATMKV- 496
Cdd:PLN02330 455 LEAILLThpSVEDAA-VVPLPDEEAGEIPAACVVINPKAKESE--EDILNFVAANVAhykkvrVVQFVDSIPKSLSGKIm 531
|
170
....*....|....
gi 488214859 497 QRLQIEKELKSQKS 510
Cdd:PLN02330 532 RRLLKEKMLSINKA 545
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
169-503 |
6.16e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 42.63 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 169 HTSGTTGIPKLICHSaHS----MGW------RTKWQKTVFTKisekkLIAFHISPVHSRFnigisslmsmgfpMMPLANA 238
Cdd:PRK07529 220 HTGGTTGMPKLAQHT-HGnevaNAWlgalllGLGPGDTVFCG-----LPLFHVNALLVTG-------------LAPLARG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 239 QSskVVhmleahrpiaLET-----HPN---NFvqWRFTAKEHPEAFSGIryyhstfdainnqtmKTFLrtsmaqdAVFLQ 310
Cdd:PRK07529 281 AH--VV----------LATpqgyrGPGviaNF--WKIVERYRINFLSGV---------------PTVY-------AALLQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 311 VygqsecgPmiLKAHTLESLKT--SDARDMGVGL----EDMTSARITDSVGnvLPENT--------DGHIQLLSKGRALT 376
Cdd:PRK07529 325 V-------P--VDGHDISSLRYalCGAAPLPVEVfrrfEAATGVRIVEGYG--LTEATcvssvnppDGERRIGSVGLRLP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 377 Y-------------YKEDARFQE---------NVY---------------GDWWDSGDYGFMDKHGHLFLKDRQVDLI-- 417
Cdd:PRK07529 394 YqrvrvvilddagrYLRDCAVDEvgvlciagpNVFsgyleaahnkglwleDGWLNTGDLGRIDADGYFWLTGRAKDLIir 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 418 --ETINSTlAIEDFLLDSLDFLAEVVIVRDKNHS---PQPIIALAPDKE------MDWNRwwEQVHElpRLNVPI-IRDF 485
Cdd:PRK07529 474 ggHNIDPA-AIEEALLRHPAVALAAAVGRPDAHAgelPVAYVQLKPGASateaelLAFAR--DHIAE--RAAVPKhVRIL 548
|
410
....*....|....*...
gi 488214859 486 DAIPRTATMKVQRLQIEK 503
Cdd:PRK07529 549 DALPKTAVGKIFKPALRR 566
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
348-419 |
6.42e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 42.19 E-value: 6.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488214859 348 ARITDSVGNVLPENTDGHIQLlSKG-----RAltYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET 419
Cdd:PRK04319 387 AAIVDDQGNELPPNRMGNLAI-KKGwpsmmRG--IWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKT 460
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
289-446 |
7.86e-04 |
|
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: 41.96 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 289 INNQTMKTFLrtsmAQDAVFLQVYGQSEC-GPmilkaHTLESLKtsdardmgvgledmtSARITdSVGNVLP-------- 359
Cdd:cd05933 332 ISRETLEFFL----SLNIPIMELYGMSETsGP-----HTISNPQ---------------AYRLL-SCGKALPgcktkihn 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 360 ENTDGHIQLLSKGRA--LTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI-----ETINStLAIEDFLL 431
Cdd:cd05933 387 PDADGIGEICFWGRHvfMGYLNMEDKTEEAIDEDgWLHSGDLGKLDEDGFLYITGRIKELIitaggENVPP-VPIEDAVK 465
|
170
....*....|....*
gi 488214859 432 DSLDFLAEVVIVRDK 446
Cdd:cd05933 466 KELPIISNAMLIGDK 480
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
377-504 |
8.11e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 41.98 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 377 YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA---IEDFLLDSLDFLAEVVIVRDKNHSPQPI 453
Cdd:PRK07867 367 YYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGtapIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488214859 454 IA---LAPDKEMDWNRWWEQVHELPRLN---VP-IIRDFDAIPRTATMKVQRLQIEKE 504
Cdd:PRK07867 447 MAalvLAPGAKFDPDAFAEFLAAQPDLGpkqWPsYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
377-498 |
8.46e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 42.14 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 377 YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFLAEVVIVRDKNH---S 449
Cdd:PLN02479 416 YLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIisggENI-SSLEVENVVYTHPAVLEASVVARPDERwgeS 494
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488214859 450 PQPIIALAPDKE-MDWNRWWEQV-----HELPRLNVPIIRDFDAIPRTATMKVQR 498
Cdd:PLN02479 495 PCAFVTLKPGVDkSDEAALAEDImkfcrERLPAYWVPKSVVFGPLPKTATGKIQK 549
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
50-185 |
1.33e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 41.01 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 50 CESVLKRAYQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDETKKrv 129
Cdd:PRK09029 35 CARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALVLEGENT-- 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488214859 130 reisngtkskQIPILYLMEQPALSVSQSFLDKNEISYMTHTSGTTGIPKLICHS--AH 185
Cdd:PRK09029 113 ----------FSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTaqAH 160
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
352-443 |
1.75e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 40.75 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 352 DSVGNVLP-------ENTDGHIQLLSKGRALTYYKEDARFQEnvygdWWDSGDYGFMDKHGHLFLKDRQVDLI----ETI 420
Cdd:PRK07445 283 NSSGQVLPhaqitipANQTGNITIQAQSLALGYYPQILDSQG-----IFETDDLGYLDAQGYLHILGRNSQKIitggENV 357
|
90 100
....*....|....*....|...
gi 488214859 421 NStLAIEDFLLDSlDFLAEVVIV 443
Cdd:PRK07445 358 YP-AEVEAAILAT-GLVQDVCVL 378
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
349-498 |
2.76e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 40.30 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 349 RITDSVGNVLPENTDGHIqLLSKGRALTYYKeDARFQENVYGdWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTL 424
Cdd:PRK07788 388 KILDENGNEVPRGVVGRI-FVGNGFPFEGYT-DGRDKQIIDG-LLSSGDVGYFDEDGLLFVDGRDDDMIvsggENV-FPA 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 425 AIEDFLLDSLDFL-AEVVIVRDKNHS--------PQPIIALAPDKEMDWNRwweqvHELPRLNVPiiRD---FDAIPRTA 492
Cdd:PRK07788 464 EVEDLLAGHPDVVeAAVIGVDDEEFGqrlrafvvKAPGAALDEDAIKDYVR-----DNLARYKVP--RDvvfLDELPRNP 536
|
....*.
gi 488214859 493 TMKVQR 498
Cdd:PRK07788 537 TGKVLK 542
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
349-417 |
2.88e-03 |
|
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: 40.05 E-value: 2.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214859 349 RITDSVGNVLPENTDGHIQLL-SKGRALTYYKEDARFQENVYGdwWDS-GDYGFMDKHGHLFLKDRQVDLI 417
Cdd:cd05929 308 HILDEDGNEVPPGEIGEVYFAnGPGFEYTNDPEKTAAARNEGG--WSTlGDVGYLDEDGYLYLTDRRSDMI 376
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
341-417 |
4.19e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 39.59 E-value: 4.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488214859 341 GLEdmtsARITDSVGNVLPENTDGHIQLlsKGRALT-YYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PRK07768 368 GLE----VRVVDEDGQVLPPRGVGVIEL--RGESVTpGYLTMDGFIPAQDADgWLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
292-419 |
5.16e-03 |
|
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: 39.18 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214859 292 QTMKTFLRTSmaqDAVFLQVYGQSEcgpmilkAHTLESLKTSDARDMGVGLED-MTSARITDSVGNVLPENTDGHI---- 366
Cdd:cd17637 126 ETIQRFEETT---GATFWSLYGQTE-------TSGLVTLSPYRERPGSAGRPGpLVRVRIVDDNDRPVPAGETGEIvvrg 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488214859 367 QLLSKGraltYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQV--DLIET 419
Cdd:cd17637 196 PLVFQG----YWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKPekELIKP 246
|
|
| |
