|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
12-498 |
4.88e-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: 133.40 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 12 LFTNFQEAAANFSETPIIFDEplsafpelGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYL 91
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 92 GAVPVMTSYHLPTTTMEVFIDRLEDPFILFddetkkrvreisngtkskqipilylmeqpdlsvsqsfldkneiSYMTHTS 171
Cdd:COG0318 73 GAVVVPLNPRLTAEELAYILEDSGARALVT-------------------------------------------ALILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 172 GTTGIPKLICHSAHSMGWRTKWQKTVFtKISEKkLIAFHISPVYSRFNIGISSLMSM--GFPMMPLANAQSSKVVHMLEV 249
Cdd:COG0318 110 GTTGRPKGVMLTHRNLLANAAAIAAAL-GLTPG-DVVLVALPLFHVFGLTVGLLAPLlaGATLVLLPRFDPERVLELIER 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 250 HRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRtsmAQNAVFLQVYGQSECGPMIlkahTLES 329
Cdd:COG0318 188 ERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEE---RFGVRIVEGYGLTETSPVV----TVNP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 330 LKISDARDMGVGLE-DMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLF 408
Cdd:COG0318 261 EDPGERRPGSVGRPlPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 409 LKDRQVDLI----ETINSTlAIEDFLLdSLDFLAEVVI--VRDKNHSPQP--IIALAPDKEMDwnrwWEQVHE-----LP 475
Cdd:COG0318 341 IVGRKKDMIisggENVYPA-EVEEVLA-AHPGVAEAAVvgVPDEKWGERVvaFVVLRPGAELD----AEELRAflrerLA 414
|
490 500
....*....|....*....|....*.
gi 488252875 476 RLNVPiiRDF---DAIPRTATMKVQR 498
Cdd:COG0318 415 RYKVP--RRVefvDELPRTASGKIDR 438
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
7-498 |
4.24e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 129.15 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 7 YSPLNLFTNFQEAAANFSETPIIFDEplsafpelGLETTYKKccesVLKRACQLAH----LGVKSGDKV--IIYKSSAFD 80
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFD--------GRRTTYAE----LDERVNRLANalraLGVKKGDRVavFDWNSHEYL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 81 TYLLAVSVsyLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDETKKRVREISNGTKSkqIPILYLMEQPDLSVSQSF-- 158
Cdd:PRK06187 71 EAYFAVPK--IGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPT--VRTVIVEGDGPAAPLAPEvg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 159 -----------------LDKNEISYMTHTSGTTGIPK--------LICHSAHSMGWRTKWQKTVFtkisekkLIA---FH 210
Cdd:PRK06187 147 eyeellaaasdtfdfpdIDENDAAAMLYTSGTTGHPKgvvlshrnLFLHSLAVCAWLKLSRDDVY-------LVIvpmFH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 211 IspvysrfnigisslMSMGFPMMPLANA---------QSSKVVHMLEVHRPI----------ALETHPNnfvqwrftakE 271
Cdd:PRK06187 220 V--------------HAWGLPYLALMAGakqviprrfDPENLLDLIETERVTfffavptiwqMLLKAPR----------A 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 272 HPEAFSGIRYYHSTFDAINNQTMKTFLRTSMAQnavFLQVYGQSECGPMI----LKAHTLESLKIsdARDMGVGLEdMTS 347
Cdd:PRK06187 276 YFVDFSSLRLVIYGGAALPPALLREFKEKFGID---LVQGYGMTETSPVVsvlpPEDQLPGQWTK--RRSAGRPLP-GVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 348 ARITDSVGNVLP--ENTDGHIQLlsKGRALT--YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ET 419
Cdd:PRK06187 350 ARIVDDDGDELPpdGGEVGEIIV--RGPWLMqgYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIisggEN 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 420 InSTLAIEDFLLDsLDFLAEV-VI-VRDKNHSPQP--IIALAPDKEMD-----------WNRWWeqvheLPRlNVPIIrd 484
Cdd:PRK06187 428 I-YPRELEDALYG-HPAVAEVaVIgVPDEKWGERPvaVVVLKPGATLDakelraflrgrLAKFK-----LPK-RIAFV-- 497
|
570
....*....|....
gi 488252875 485 fDAIPRTATMKVQR 498
Cdd:PRK06187 498 -DELPRTSVGKILK 510
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
163-497 |
3.89e-25 |
|
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: 106.22 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 163 EISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAFHisPVysrFNIGISSLMsmgfpMMPLANAQSS- 241
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTL--PL---FHIGGLFGL-----LGALLAGGTVv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 242 --------KVVHMLEVHRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRtsmAQNAVFLQVYG 313
Cdd:cd04433 71 llpkfdpeAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEE---APGIKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 314 QSECGPMIlkahTLESLKISDARDMGVGL-EDMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDW 392
Cdd:cd04433 148 LTETGGTV----ATGPPDDDARKPGSVGRpVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 393 WDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFL-AEVVIVRDKNHSPQPI--IALAPDKEMDWN 465
Cdd:cd04433 224 YRTGDLGRLDEDGYLYIVGRLKDMIksggENV-YPAEVEAVLLGHPGVAeAAVVGVPDPEWGERVVavVVLRPGADLDAE 302
|
330 340 350
....*....|....*....|....*....|....
gi 488252875 466 RWWEQVHE-LPRLNVP-IIRDFDAIPRTATMKVQ 497
Cdd:cd04433 303 ELRAHVRErLAPYKVPrRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
16-417 |
1.81e-20 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 93.53 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 16 FQEAAANFSETPIIFDEPlsafpelGLETTYKKccesVLKRACQLAH----LGVKSGDKVIIY--KSSAFDTYLLAVSvs 89
Cdd:pfam00501 1 LERQAARTPDKTALEVGE-------GRRLTYRE----LDERANRLAAglraLGVGKGDRVAILlpNSPEWVVAFLACL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 90 YLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDD--------ETKKRVREISNGTKSKQIPILYLMEQPDLSVSQ----- 156
Cdd:pfam00501 68 KAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 157 --SFLDKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFT---KISEKKLIA-----FHIspvYSRFNIGISSLM 226
Cdd:pfam00501 148 ppPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfGLGPDDRVLstlplFHD---FGLSLGLLGPLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 227 SmGFP--MMPLANAQSSK-VVHMLEVHRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSma 303
Cdd:pfam00501 225 A-GATvvLPPGFPALDPAaLLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELF-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 304 qNAVFLQVYGQSECGPMilkAHTLESLKISDARDMGVG--LEDmTSARITD-SVGNVLPENTDGhiQLLSKGRALT--YY 378
Cdd:pfam00501 302 -GGALVNGYGLTETTGV---VTTPLPLDEDLRSLGSVGrpLPG-TEVKIVDdETGEPVPPGEPG--ELCVRGPGVMkgYL 374
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 488252875 379 KEDARFQEN-VYGDWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:pfam00501 375 NDPELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
36-498 |
2.39e-19 |
|
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: 90.36 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 36 AFPELGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIY--KSSAFDTYLLAVSVsyLGAVPVMTSYHLptTTMEV-FID 112
Cdd:cd17631 13 ALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLskNSPEFLELLFAAAR--LGAVFVPLNFRL--TPPEVaYIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 113 RLEDPFILFDDetkkrvreisngtkskqipILYLMeqpdlsvsqsfldkneisymtHTSGTTGIPKLICHSAHSMGWRTK 192
Cdd:cd17631 89 ADSGAKVLFDD-------------------LALLM---------------------YTSGTTGRPKGAMLTHRNLLWNAV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 193 WQKTVFTKISEKKLIafHISPVYSRFNIGISSLMSM--GFPMMPLANAQSSKVVHMLEVHRPIALETHPnnfVQWRFTAk 270
Cdd:cd17631 129 NALAALDLGPDDVLL--VVAPLFHIGGLGVFTLPTLlrGGTVVILRKFDPETVLDLIERHRVTSFFLVP---TMIQALL- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 271 EHPEAfsgiryyhSTFDAinnQTMKTF-----------LRTSMAQNAVFLQVYGQSECGPMILkahtleSLKISDARD-M 338
Cdd:cd17631 203 QHPRF--------ATTDL---SSLRAViyggapmperlLRALQARGVKFVQGYGMTETSPGVT------FLSPEDHRRkL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 339 G-VGLEDM-TSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDL 416
Cdd:cd17631 266 GsAGRPVFfVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 417 I----ETINStLAIEDFLLDsLDFLAEV-VI-VRDKN--HSPQPIIALAPDKEMDWNRWWEQVHE-LPRLNVPIIRDF-D 486
Cdd:cd17631 346 IisggENVYP-AEVEDVLYE-HPAVAEVaVIgVPDEKwgEAVVAVVVPRPGAELDEDELIAHCRErLARYKIPKSVEFvD 423
|
490
....*....|..
gi 488252875 487 AIPRTATMKVQR 498
Cdd:cd17631 424 ALPRNATGKILK 435
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
45-498 |
9.97e-18 |
|
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: 9.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 45 TYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLpttTMEVFIDRLEDPFILFDDe 124
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRL---TPNELAFQLKDSDVKLDD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 125 tkkrvreisngtkskqipilylmeqpdlsvsqsfldkneISYMTHTSGTTGIPKLICHSahsmgWRTKWQKTVFTKIS-- 202
Cdd:cd05912 79 ---------------------------------------IATIMYTSGTTGKPKGVQQT-----FGNHWWSAIGSALNlg 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 203 ----EKKLIA---FHISpvysrfniGISSLMS---MGFPMMPLANAQSSKVVHMLEVHRPIALETHPNnFVQWrfTAKEH 272
Cdd:cd05912 115 ltedDNWLCAlplFHIS--------GLSILMRsviYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPT-MLQR--LLEIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 273 PEAfsgiryYHSTFdainnQTM--------KTFLRTSMAQNAVFLQVYGQSECGPMILKAHTLESL-KISDArdmGVGLE 343
Cdd:cd05912 184 GEG------YPNNL-----RCIllgggpapKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALnKIGSA---GKPLF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 344 DMtSARITDSVGnvlPENTDGHIQLlsKGRALT--YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI---- 417
Cdd:cd05912 250 PV-ELKIEDDGQ---PPYEVGEILL--KGPNVTkgYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIisgg 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 418 ETINSTlAIEDFLLdSLDFLAEVVIV--RDKNHSPQPIIALAPDKEMDWNRWWEQVHE-LPRLNVPI-IRDFDAIPRTAT 493
Cdd:cd05912 324 ENIYPA-EIEEVLL-SHPAIKEAGVVgiPDDKWGQVPVAFVVSERPISEEELIAYCSEkLAKYKVPKkIYFVDELPRTAS 401
|
....*
gi 488252875 494 MKVQR 498
Cdd:cd05912 402 GKLLR 406
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
45-498 |
1.13e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 85.40 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 45 TYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLpttTMEVFIDRLEDP---FILF 121
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL---SREELLWQLDDAevkCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 122 DDETKKRVREIsngtkskqIPILY--LMEQPDLSVS-QSFLDKNEISYMTHTSGTTGIPKLIC-----H------SAHSM 187
Cdd:PRK03640 106 DDDFEAKLIPG--------ISVKFaeLMNGPKEEAEiQEEFDLDEVATIMYTSGTTGKPKGVIqtygnHwwsavgSALNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 188 GWRTK--WqktvftkisekkLIA---FHISpvysrfniGISSLMS---MGFPMMPLANAQSSKVVHMLEVHR-------P 252
Cdd:PRK03640 178 GLTEDdcW------------LAAvpiFHIS--------GLSILMRsviYGMRVVLVEKFDAEKINKLLQTGGvtiisvvS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 253 IALEthpnnfvqwRFTAKEHPEAfsgiryYHSTFDAI---NNQTMKTFLRTSMAQNAVFLQVYGQSECGPMILkahTLes 329
Cdd:PRK03640 238 TMLQ---------RLLERLGEGT------YPSSFRCMllgGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIV---TL-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 330 lkisDARDMgvgLEDMTSA---------RITDSvGNVLPENTDGHIqlLSKGRALT--YYKEDARFQENVYGDWWDSGDY 398
Cdd:PRK03640 298 ----SPEDA---LTKLGSAgkplfpcelKIEKD-GVVVPPFEEGEI--VVKGPNVTkgYLNREDATRETFQDGWFKTGDI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 399 GFMDKHGHLFLKDRQVDLI----ETINSTlAIEDFLLdSLDFLAEVVIV--RDKNHSPQPIIALAPDKEMDWNRWWEQVH 472
Cdd:PRK03640 368 GYLDEEGFLYVLDRRSDLIisggENIYPA-EIEEVLL-SHPGVAEAGVVgvPDDKWGQVPVAFVVKSGEVTEEELRHFCE 445
|
490 500
....*....|....*....|....*...
gi 488252875 473 E-LPRLNVPI-IRDFDAIPRTATMKVQR 498
Cdd:PRK03640 446 EkLAKYKVPKrFYFVEELPRNASGKLLR 473
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
41-496 |
4.67e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 80.70 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 41 GLETTYKKCCESVLKRACQLAHLGVKSGDKVIIY--KSSAFdtYLLAVSVSYLGAVPVMTSYHLPTTTME---------- 108
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLmkNSAAF--LELAFAASYLGAVFLPINYRLAADEVAyilgdagakl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 109 VFIDR-------LEDPFILFDDETKKRVREISNGtkSKQIPILYLMEQPDLSvsqsfldkneisYMTHTSGTTGIPKLIC 181
Cdd:PRK06145 103 LLVDEefdaivaLETPKIVIDAAAQADSRRLAQG--GLEIPPQAAVAPTDLV------------RLMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 182 HSAHSMGWRTKWQKTVFTKISEKKLIAfhISPVY--SRFNI-GISSLMSMGFpMMPLANAQSSKVVHMLEVHRPIALETH 258
Cdd:PRK06145 169 HSYGNLHWKSIDHVIALGLTASERLLV--VGPLYhvGAFDLpGIAVLWVGGT-LRIHREFDPEAVLAAIERHRLTCAWMA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 259 PnnFVQWRFTAKEHPEAF--SGIRYYHSTFDAINNQTMKTFlrTSMAQNAVFLQVYGQSE-CGPMILKAHTLESLKI-SD 334
Cdd:PRK06145 246 P--VMLSRVLTVPDRDRFdlDSLAWCIGGGEKTPESRIRDF--TRVFTRARYIDAYGLTEtCSGDTLMEAGREIEKIgST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 335 ARDMGvgledMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQV 414
Cdd:PRK06145 322 GRALA-----HVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 415 DLI----ETINSTlAIEDFLLDsLDFLAEVVI--VRDKNHSPQP--IIALAPDKEMDWNRWWEQVHE-LPRLNVP---II 482
Cdd:PRK06145 397 DMIisggENIASS-EVERVIYE-LPEVAEAAVigVHDDRWGERItaVVVLNPGATLTLEALDRHCRQrLASFKVPrqlKV 474
|
490
....*....|....
gi 488252875 483 RdfDAIPRTATMKV 496
Cdd:PRK06145 475 R--DELPRNPSGKV 486
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
37-496 |
4.96e-15 |
|
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: 77.37 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 37 FPELGLETTYKKccesVLKRACQLA---HLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSY--------HLPTT 105
Cdd:cd05909 1 EDTLGTSLTYRK----LLTGAIALArklAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYtaglrelrACIKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 106 -------TMEVFIDRL---------EDPFILFDDETKKRVreisnGTKSKQIPILYLMEQPDLSVSQSFL---DKNEISY 166
Cdd:cd05909 77 agiktvlTSKQFIEKLklhhlfdveYDARIVYLEDLRAKI-----SKADKCKAFLAGKFPPKWLLRIFGVapvQPDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 167 MTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAFhiSPVYSRF--NIGISSLMSMGFPMMPLANA-QSSKV 243
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGA--LPFFHSFglTGCLWLPLLSGIKVVFHPNPlDYKKI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 244 VHMLEVHRPIALETHPNNFVQwrFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTsmaQNAVFLQVYGQSECGPMILK 323
Cdd:cd05909 230 PELIYDKKATILLGTPTFLRG--YARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEK---FGIRILEGYGTTECSPVISV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 324 ahtleSLKISDARDMGVG--LEDMtSARITDSVGNV-LPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGF 400
Cdd:cd05909 305 -----NTPQSPNKEGTVGrpLPGM-EVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 401 MDKHGHLFLKDRQ---VDLIETINSTLAIEDFLLDSL--DFLAEVVIVRDKNHSPQpIIALAPDKEMDWNRWWEQV--HE 473
Cdd:cd05909 379 IDGEGFLTITGRLsrfAKIAGEMVSLEAIEDILSEILpeDNEVAVVSVPDGRKGEK-IVLLTTTTDTDPSSLNDILknAG 457
|
490 500
....*....|....*....|....
gi 488252875 474 LPRLNVP-IIRDFDAIPRTATMKV 496
Cdd:cd05909 458 ISNLAKPsYIHQVEEIPLLGTGKP 481
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-503 |
1.93e-14 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 75.92 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 54 LKRACQLAH----LGVKSGDKVIIYKSSAFDTY--LLAVSvsYLGAVpvmtsyHLPTTTM---EVFIDRLED--PFILF- 121
Cdd:COG0365 46 RREVNRFANalraLGVKKGDRVAIYLPNIPEAViaMLACA--RIGAV------HSPVFPGfgaEALADRIEDaeAKVLIt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 122 DDET---------KKRVREISNGTKSKQIPILY-----------------LMEQPDLSVSQSFLDKNEISYMTHTSGTTG 175
Cdd:COG0365 118 ADGGlrggkvidlKEKVDEALEELPSLEHVIVVgrtgadvpmegdldwdeLLAAASAEFEPEPTDADDPLFILYTSGTTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 176 IPKLICHSAHS-MGWRTKWQKTVFtKISEKKL---------IAFHISPVYSRFNIGISSLMSMGFPMMPLANAqsskvvh 245
Cdd:COG0365 198 KPKGVVHTHGGyLVHAATTAKYVL-DLKPGDVfwctadigwATGHSYIVYGPLLNGATVVLYEGRPDFPDPGR------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 246 MLEVhrpiaLETH-PNNFvqwrFTA--------KEHPEA-----FSGIRYYHSTFDAINNQTMKTFlrtsmaQNAVFLQV 311
Cdd:COG0365 270 LWEL-----IEKYgVTVF----FTAptairalmKAGDEPlkkydLSSLRLLGSAGEPLNPEVWEWW------YEAVGVPI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 312 ---YGQSE-CGPMILKAHTLEsLKISDardMGV---GLEdmtsARITDSVGNVLPENTDGHIQLLSK--GRALTYYKEDA 382
Cdd:COG0365 335 vdgWGQTEtGGIFISNLPGLP-VKPGS---MGKpvpGYD----VAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 383 RFQE---NVYGDWWDSGDYGFMDKHGHLFLKDRqVDliETIN------STLAIEDFLLdSLDFLAEVVIVrdknHSPQPI 453
Cdd:COG0365 407 RYREtyfGRFPGWYRTGDGARRDEDGYFWILGR-SD--DVINvsghriGTAEIESALV-SHPAVAEAAVV----GVPDEI 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488252875 454 --------IALAPDKE---------MDWNRwwEQV--HELPRlnvpIIRDFDAIPRTATMKVQRLQIEK 503
Cdd:COG0365 479 rgqvvkafVVLKPGVEpsdelakelQAHVR--EELgpYAYPR----EIEFVDELPKTRSGKIMRRLLRK 541
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
45-503 |
3.10e-14 |
|
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: 74.68 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 45 TYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVmtsyhlPTTTMEvfidrledpfilfdde 124
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYV------PLTTLL---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 125 tkkrvreisnGTKskqiPILYLMEQPDLSVSQSflDKNEISYMTHTSGTTGIPKLICHS-----AHSMGWRTkWQ----K 195
Cdd:cd05972 60 ----------GPK----DIEYRLEAAGAKAIVT--DAEDPALIYFTSGTTGLPKGVLHThsyplGHIPTAAY-WLglrpD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 196 TVFTKISEKKLIAFHISPVYSRFNIGISSLMSMGFPMMPlanaqsSKVVHMLEVHRPIALETHPnnfVQWRFTAKEHPEA 275
Cdd:cd05972 123 DIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDA------ERILELLERYGVTSFCGPP---TAYRMLIKQDLSS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 276 --FSGIRYYHSTFDAINNQTMKTFLRTSmaqNAVFLQVYGQSECGPMILKAHTLESLKISDARDMGvGLEdmtsARITDS 353
Cdd:cd05972 194 ykFSHLRLVVSAGEPLNPEVIEWWRAAT---GLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTP-GYD----VAIIDD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 354 VGNVLPENTDGHIQLLSK--GRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA---IED 428
Cdd:cd05972 266 DGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGpfeVES 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 429 FLLDSlDFLAEVVIVrdknHSPQPI--------IALAPDKEMDwnrwWEQVHELPRL--------NVPIIRDF-DAIPRT 491
Cdd:cd05972 346 ALLEH-PAVAEAAVV----GSPDPVrgevvkafVVLTSGYEPS----EELAEELQGHvkkvlapyKYPREIEFvEELPKT 416
|
490
....*....|..
gi 488252875 492 ATMKVQRLQIEK 503
Cdd:cd05972 417 ISGKIRRVELRD 428
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
53-497 |
8.62e-14 |
|
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: 73.40 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 53 VLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEdPFILF-DDETKKRVRE 131
Cdd:cd05911 20 SRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK-PKVIFtDPDGLEKVKE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 132 ISNGTKSK-QIPILYLMEQPDLSVSQS----------------FLDKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQ 194
Cdd:cd05911 99 AAKELGPKdKIIVLDDKPDGVLSIEDLlsptlgeededlppplKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 195 KTVFTKISEKKLIAFHISPVYSRFniGISSLMSM---GFP--MMP-------LANAQSSKVVHMLEVhrP---IALETHP 259
Cdd:cd05911 179 QTFLYGNDGSNDVILGFLPLYHIY--GLFTTLASllnGATviIMPkfdselfLDLIEKYKITFLYLV--PpiaAALAKSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 260 NnfVQwrftakehPEAFSGIRYYHSTFDAINNQtMKTFLRTsMAQNAVFLQVYGQSECGPMIlkAHTLESLKISDArdmg 339
Cdd:cd05911 255 L--LD--------KYDLSSLRVILSGGAPLSKE-LQELLAK-RFPNATIKQGYGMTETGGIL--TVNPDGDDKPGS---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 340 VG--LEDMTsARITDSVGN-VLPENTDGHIQLLSKGRALTYYK-----EDARFQENvygdWWDSGDYGFMDKHGHLFLKD 411
Cdd:cd05911 317 VGrlLPNVE-AKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNnpeatKETFDEDG----WLHTGDIGYFDEDGYLYIVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 412 RQVDLI----------EtinstlaIEDFLLdSLDFLAEV-VI-VRDKNHS--PQPIIALAPDKEM------DWNRwwEQV 471
Cdd:cd05911 392 RKKELIkykgfqvapaE-------LEAVLL-EHPGVADAaVIgIPDEVSGelPRAYVVRKPGEKLtekevkDYVA--KKV 461
|
490 500
....*....|....*....|....*..
gi 488252875 472 HELPRLNVPIIrdF-DAIPRTATMKVQ 497
Cdd:cd05911 462 ASYKQLRGGVV--FvDEIPKSASGKIL 486
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-499 |
2.29e-13 |
|
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: 72.35 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 38 PELGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIY--KSSAFDTYLLAVSVSYLGAVPVMTSYhlpttTMEVFIDRLE 115
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIAlpNGLEFVVAFLAAARAGAVVAPLNPAY-----KKAEFEFYLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 116 D---PFILFDDETKKrvrEISNGTKSKQIPIL-------------------YLMEQPDLSVSQSFLDKNEISYMTHTSGT 173
Cdd:cd05926 84 DlgsKLVLTPKGELG---PASRAASKLGLAILelaldvgvlirapsaeslsNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 174 TGIPKL-------ICHSAHSMgwrtkwqKTVFTKISEKKLIA----FHIspvysrfnIG-ISSLMSmgfpmmPLAnAQSS 241
Cdd:cd05926 161 TGRPKGvplthrnLAASATNI-------TNTYKLTPDDRTLVvmplFHV--------HGlVASLLS------TLA-AGGS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 242 KVVhmlevhrPIALETHP--NNFVQWR---FTA------------KEHPE-AFSGIRYYHSTFDAINNQTMKTFLRTSMA 303
Cdd:cd05926 219 VVL-------PPRFSASTfwPDVRDYNatwYTAvptihqillnrpEPNPEsPPPKLRFIRSCSASLPPAVLEALEATFGA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 304 QnavFLQVYGQSECgpmilkAH--TLESLKISDARDMGVGLEDMTSARITDSVGNVLPENTDGHIQLlsKGRALT--YYK 379
Cdd:cd05926 292 P---VLEAYGMTEA------AHqmTSNPLPPGPRKPGSVGKPVGVEVRILDEDGEILPPGVVGEICL--RGPNVTrgYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 380 -EDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLdSLDFLAEVVIVRdknhSPQPI- 453
Cdd:cd05926 361 nPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELInrggEKI-SPLEVDGVLL-SHPAVLEAVAFG----VPDEKy 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 488252875 454 -------IALAPDKEMDWNRWWEQV-HELPRLNVPI-IRDFDAIPRTATMKVQRL 499
Cdd:cd05926 435 geevaaaVVLREGASVTEEELRAFCrKHLAAFKVPKkVYFVDELPKTATGKIQRR 489
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
44-417 |
1.01e-12 |
|
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: 70.39 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 44 TTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDtYLLAVSVSYL-GAVPVMTS---------------YHLPTTtm 107
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNED-FIPAFWACVLaGFVPAPLTvpptydepnarlrklRHIWQL-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 108 evfidrLEDPFILFDDETKKRVREISNGTKSKQIPILYLME------QPDLSVSQSfldkNEISYMTHTSGTTGIPKLIC 181
Cdd:cd05906 117 ------LGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEElldtaaDHDLPQSRP----DDLALLMLTSGSTGFPKAVP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 182 HSAHSMGWRTK--------WQKTVF---------TKISEkkliaFHISPVY---SRFNIGISSLMsmgfpmmplanAQSS 241
Cdd:cd05906 187 LTHRNILARSAgkiqhnglTPQDVFlnwvpldhvGGLVE-----LHLRAVYlgcQQVHVPTEEIL-----------ADPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 242 KVVHMLEVHRpIALETHPN-NFVQWRFTAKEHPEA---FSGIRYYHSTFDAINNQTMKTFLRT---SMAQNAVFLQVYGQ 314
Cdd:cd05906 251 RWLDLIDRYR-VTITWAPNfAFALLNDLLEEIEDGtwdLSSLRYLVNAGEAVVAKTIRRLLRLlepYGLPPDAIRPAFGM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 315 SECGPMILKAHTLESLKISDA-RDMGVGLE----DMtsaRITDSVGNVLPENTDGHIQLlsKGRALT--YYKEDARFQEN 387
Cdd:cd05906 330 TETCSGVIYSRSFPTYDHSQAlEFVSLGRPipgvSM---RIVDDEGQLLPEGEVGRLQV--RGPVVTkgYYNNPEANAEA 404
|
410 420 430
....*....|....*....|....*....|.
gi 488252875 388 -VYGDWWDSGDYGFMDkHGHLFLKDRQVDLI 417
Cdd:cd05906 405 fTEDGWFRTGDLGFLD-NGNLTITGRTKDTI 434
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
43-498 |
6.94e-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: 67.49 E-value: 6.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 43 ETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSyhlptttmevfidrledpfilfd 122
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVIN----------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 123 detkkrvreisngTKSKQIPILYLMEqpDLSVSQSFLDKNEISYMTHTSGTTGIPKLICHS-AHSMGWRTKWQKTVFTKI 201
Cdd:cd05919 67 -------------PLLHPDDYAYIAR--DCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAhRDPLLFADAMAREALGLT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 202 SEKKLiaFHISPVYSRFNIGiSSLMsmgFPMMPLANA-------QSSKVVHMLEVHRPIALETHPNNFVQWRFTAKEHPE 274
Cdd:cd05919 132 PGDRV--FSSAKMFFGYGLG-NSLW---FPLAVGASAvlnpgwpTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 275 AFSGIRYYHSTFDA----INNQTMKTFLRTsmaqnavFLQVYGQSECGpmilkaHTLESLKISDARDMGVGLE-DMTSAR 349
Cdd:cd05919 206 ALRSLRLCVSAGEAlprgLGERWMEHFGGP-------ILDGIGATEVG------HIFLSNRPGAWRLGSTGRPvPGYEIR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 350 ITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLiETIN----STLA 425
Cdd:cd05919 273 LVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDM-LKVGgqwvSPVE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 426 IEDFLLDSLDFLAEVVIVRDKNH---SPQPIIALAPDKEMD--WNRWWEQ-------VHELPRLnvpiIRDFDAIPRTAT 493
Cdd:cd05919 352 VESLIIQHPAVAEAAVVAVPESTglsRLTAFVVLKSPAAPQesLARDIHRhllerlsAHKVPRR----IAFVDELPRTAT 427
|
....*
gi 488252875 494 MKVQR 498
Cdd:cd05919 428 GKLQR 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
45-419 |
1.40e-11 |
|
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: 66.37 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 45 TYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVmtsyhlPTttmevfidrledpFILFDDE 124
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC------PL-------------FSAFGPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 125 tkkrvreisngtkskqiPILYLMEQPD---LSVSQSFLDKNEI---SYMTHTSGTTGIPKLICHSAHSMgwrtkwqktVF 198
Cdd:cd05969 63 -----------------AIRDRLENSEakvLITTEELYERTDPedpTLLHYTSGTTGTPKGVLHVHDAM---------IF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 199 TKISEKKLIAFHISPVY-SRFNIGISSLMSMGFpMMPLANAQSSKVVH----------MLEVHRPIALETHPNNFVQWRF 267
Cdd:cd05969 117 YYFTGKYVLDLHPDDIYwCTADPGWVTGTVYGI-WAPWLNGVTNVVYEgrfdaeswygIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 268 TAKEHPEAF--SGIRYYHSTFDAINNQT----MKTFlrtsmaqNAVFLQVYGQSECGPMILKAHTLESLKISDardMGVG 341
Cdd:cd05969 196 EGDELARKYdlSSLRFIHSVGEPLNPEAirwgMEVF-------GVPIHDTWWQTETGSIMIANYPCMPIKPGS---MGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 342 LEDMTSArITDSVGNVLPENTDGHIQLLSKGRAL--TYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET 419
Cdd:cd05969 266 LPGVKAA-VVDENGNELPPGTKGILALKPGWPSMfrGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKT 344
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
30-509 |
3.61e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 65.56 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 30 FDEPLSAFP--------ELGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYH 101
Cdd:PRK12583 24 FDATVARFPdrealvvrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 102 LPTTTMEVFIDRLEDPFILFDDETKKR-----VREISNGTKSKQ--------IP----ILYLMEQP-------------- 150
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFKTSdyhamLQELLPGLAEGQpgalacerLPelrgVVSLAPAPppgflawhelqarg 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 151 ------DLSVSQSFLDKNEISYMTHTSGTTGIPKLICHSAHSM---GWRTKwQKTVFTkiSEKKLIAfhISPVYSRFNIG 221
Cdd:PRK12583 184 etvsreALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIlnnGYFVA-ESLGLT--EHDRLCV--PVPLYHCFGMV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 222 ISSL--MSMGFPMM-------PLANAQSskvvhmLEVHRPIALETHPNNFVqwrfTAKEHPEafsgiryyHSTFDAinnq 292
Cdd:PRK12583 259 LANLgcMTVGACLVypneafdPLATLQA------VEEERCTALYGVPTMFI----AELDHPQ--------RGNFDL---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 293 tmkTFLRTS-MAQNAVFLQV----------------YGQSECGPMILKAHTLESLKIsdaRDMGVG-----LEdmtsARI 350
Cdd:PRK12583 317 ---SSLRTGiMAGAPCPIEVmrrvmdemhmaevqiaYGMTETSPVSLQTTAADDLER---RVETVGrtqphLE----VKV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 351 TDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI----ETINSTlA 425
Cdd:PRK12583 387 VDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDgWMHTGDLATMDEQGYVRIVGRSKDMIirggENIYPR-E 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 426 IEDFLLDSLDFLAEVVI-VRDKNHSPQPI--IALAPDKEM------DWNRWWEQVHELPRLnvpiIRDFDAIPRTATMKV 496
Cdd:PRK12583 466 IEEFLFTHPAVADVQVFgVPDEKYGEEIVawVRLHPGHAAseeelrEFCKARIAHFKVPRY----FRFVDEFPMTVTGKV 541
|
570
....*....|...
gi 488252875 497 QRLQIEKAPIVKL 509
Cdd:PRK12583 542 QKFRMREISIEEL 554
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
43-503 |
4.73e-11 |
|
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: 64.96 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 43 ETTYKKCCESVLKRACQLAHLGVKSGDKViiyKSSAFDTY-----LLAVSVsyLGAVPVMTSYHLPTTTMEVFIDRLEDP 117
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVKPGDRV---ATLAWNTHrhlelYYAVPG--MGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 118 FILFDDE----------TKKRVREI-----SNGTKSKQIPILY-----LMEQPDLSVSQSFlDKNEISYMTHTSGTTGIP 177
Cdd:cd12119 100 VVFVDRDflplleaiapRLPTVEHVvvmtdDAAMPEPAGVGVLayeelLAAESPEYDWPDF-DENTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 178 K--LICHSA---HSMGWRTkwqkTVFTKISEKKLI-----AFHISPvysrFNIGISSLMSmGFPM-MPLANAQSSKVVHM 246
Cdd:cd12119 179 KgvVYSHRSlvlHAMAALL----TDGLGLSESDVVlpvvpMFHVNA----WGLPYAAAMV-GAKLvLPGPYLDPASLAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 247 LEVHRPialethpnnfvqwRFTAK---------EHPEAfSGIRYYHSTFDAINNQTMKTFLRTSMAQNAV-FLQVYGQSE 316
Cdd:cd12119 250 IEREGV-------------TFAAGvptvwqgllDHLEA-NGRDLSSLRRVVIGGSAVPRSLIEAFEERGVrVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 317 CGPMILKAHTLESLkISDARDMGVGLEDMT-------SARITDSVGNVLPE--NTDGHIQLLSKGRALTYYKEDARFQEN 387
Cdd:cd12119 316 TSPLGTVARPPSEH-SNLSEDEQLALRAKQgrpvpgvELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 388 VYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFL-AEVVIVRDKNHSPQP--IIALAPDK 460
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIksggEWI-SSVELENAIMAHPAVAeAAVIGVPHPKWGERPlaVVVLKEGA 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 488252875 461 EMD-----------WNRWWeqvheLPrLNVPIIrdfDAIPRTATMKVQRLQIEK 503
Cdd:cd12119 474 TVTaeellefladkVAKWW-----LP-DDVVFV---DEIPKTSTGKIDKKALRE 518
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
56-443 |
9.18e-11 |
|
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: 63.94 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 56 RACQLAH----LGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAV--PVMTSYHlptttmevfidRLEDPFILFDDETKKRV 129
Cdd:cd05903 10 RADRLAAglaaLGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVtnPILPFFR-----------EHELAFILRRAKAKVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 130 reisngtkskqIPILY----LMEQPDlsvsqsfldknEISYMTHTSGTTGIPKLICHSAHSM---------GWRTKWQKT 196
Cdd:cd05903 79 -----------VPERFrqfdPAAMPD-----------AVALLLFTSGTTGEPKGVMHSHNTLsasirqyaeRLGLGPGDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 197 VFTKISekklIAFHISPVYsrfniGISSLMSMGFPMMPLANAQSSKVVHMLEVHRPialeTH---PNNFVQWRFTA-KEH 272
Cdd:cd05903 137 FLVASP----MAHQTGFVY-----GFTLPLLLGAPVVLQDIWDPDKALALMREHGV----TFmmgATPFLTDLLNAvEEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 273 PEAFSGIRYYHSTFDAINNQTMKtflRTSMAQNAVFLQVYGQSECGPMILKAHTLESLKI--SDARdMGVGLEdmtsARI 350
Cdd:cd05903 204 GEPLSRLRTFVCGGATVPRSLAR---RAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRlyTDGR-PLPGVE----IKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 351 TDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAI 426
Cdd:cd05903 276 VDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIirggENI-PVLEV 354
|
410
....*....|....*..
gi 488252875 427 EDFLLDSLDfLAEVVIV 443
Cdd:cd05903 355 EDLLLGHPG-VIEAAVV 370
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-498 |
4.56e-10 |
|
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: 61.81 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 15 NFQEAAANFSETPiifdeplsAFPELGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAV 94
Cdd:cd05936 4 LLEEAARRFPDKT--------ALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 95 PVMTSyhlPTTTMEVFIDRLED--PFILFDDETKKRVREISNGTKSKQIPilylmEQPDLSVsqsfldkneISYmthTSG 172
Cdd:cd05936 76 VVPLN---PLYTPRELEHILNDsgAKALIVAVSFTDLLAAGAPLGERVAL-----TPEDVAV---------LQY---TSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 173 TTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAFHISPVYSRFNIGISSLMS--MGFPMMPLANAQSSKVVHMLEVH 250
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPlaLGATIVLIPRFRPIGVLKEIRKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 251 RP----------IALETHPNnfvqwrftakEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSmaqNAVFLQVYGQSECGPM 320
Cdd:cd05936 216 RVtifpgvptmyIALLNAPE----------FKKRDFSSLRLCISGGAPLPVEVAERFEELT---GVPIVEGYGLTETSPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 321 IlkahTLESLKISD-ARDMGVGLEDmTSARITDSVGNVLPENTDGhiQLLSKGRALT--YYKEDARFQENVYGDWWDSGD 397
Cdd:cd05936 283 V----AVNPLDGPRkPGSIGIPLPG-TEVKIVDDDGEELPPGEVG--ELWVRGPQVMkgYWNRPEETAEAFVDGWLRTGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 398 YGFMDKHGHLFLKDRQVDLI----------EtinstlaIEDFLLdSLDFLAEVVIV--RDKNH--------SPQPIIALA 457
Cdd:cd05936 356 IGYMDEDGYFFIVDRKKDMIivggfnvyprE-------VEEVLY-EHPAVAEAAVVgvPDPYSgeavkafvVLKEGASLT 427
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 488252875 458 PDKEMDWNRwwEQV--HELPRLnvpiIRDFDAIPRTATMKVQR 498
Cdd:cd05936 428 EEEIIAFCR--EQLagYKVPRQ----VEFRDELPKSAVGKILR 464
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
45-419 |
7.05e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 61.10 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 45 TYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDE 124
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 125 TKKRVREISNGTKSKQI---PILYLMEQP-------DLSVSQS------FLDKNEISYMTHTSGTTGIPKLICHSAHSMG 188
Cdd:PRK08316 118 LAPTAEAALALLPVDTLilsLVLGGREAPggwldfaDWAEAGSvaepdvELADDDLAQILYTSGTESLPKGAMLTHRALI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 189 WrtKWQKTVFTKISEKKLIAFHISPVY----------SRFNIGISSLMsMGFPMMPLanaqsskVVHMLEVHRP------ 252
Cdd:PRK08316 198 A--EYVSCIVAGDMSADDIPLHALPLYhcaqldvflgPYLYVGATNVI-LDAPDPEL-------ILRTIEAERItsffap 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 253 ----IALETHPNnFVQWRFTA----------------KEHPEAFSGIRYYhstfdainnqtmktflrtsmaqnavflQVY 312
Cdd:PRK08316 268 ptvwISLLRHPD-FDTRDLSSlrkgyygasimpvevlKELRERLPGLRFY---------------------------NCY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 313 GQSECGP--MILKAHTLESlKISDARDMGVGLEdmtsARITDSVGNVLPENTDGHI-----QLLskgraLTYYKEDARFQ 385
Cdd:PRK08316 320 GQTEIAPlaTVLGPEEHLR-RPGSAGRPVLNVE----TRVVDDDGNDVAPGEVGEIvhrspQLM-----LGYWDDPEKTA 389
|
410 420 430
....*....|....*....|....*....|....
gi 488252875 386 ENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET 419
Cdd:PRK08316 390 EAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKT 423
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
45-470 |
7.10e-09 |
|
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: 57.99 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 45 TYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVmTSYhlPTTTMEvfidrlEDPFILFDDE 124
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV-PIY--PTSSAE------QIAYILNDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 125 TKkrvreisngtkskqipiLYLMEQPDlsvsqsfldknEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEK 204
Cdd:cd05907 78 AK-----------------ALFVEDPD-----------DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 205 KLIAF----HI--------SPVYSRFNIGISSLMSMGFPMMplanaqssKVVH---MLEVhrPIALETHPNNFVQwrfta 269
Cdd:cd05907 130 RHLSFlplaHVferraglyVPLLAGARIYFASSAETLLDDL--------SEVRptvFLAV--PRVWEKVYAAIKV----- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 270 KEHPEAFSGIryyhstFDAINNQTMK--------------TFLRtsmAQNAVFLQVYGQSECGPMILkAHTLESLKIsda 335
Cdd:cd05907 195 KAVPGLKRKL------FDLAVGGRLRfaasggaplpaellHFFR---ALGIPVYEGYGLTETSAVVT-LNPPGDNRI--- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 336 rdmgvgledmtsaritDSVGNVLPENT-----DGHIQLlsKGRALT--YYKEDARFQENVYGD-WWDSGDYGFMDKHGHL 407
Cdd:cd05907 262 ----------------GTVGKPLPGVEvriadDGEILV--RGPNVMlgYYKNPEATAEALDADgWLHTGDLGEIDEDGFL 323
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488252875 408 FLKDRQVDLIetINST------LAIEDFLLDSLdFLAEVVIVRDKnhspQP-IIAL-APDKEMdWNRWWEQ 470
Cdd:cd05907 324 HITGRKKDLI--ITSGgknispEPIENALKASP-LISQAVVIGDG----RPfLVALiVPDPEA-LEAWAEE 386
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
45-501 |
2.23e-08 |
|
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: 56.34 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 45 TYKKCCESVLKRACQLAHLGVKSGDKVIIyKSSAFDTYLLAVSVSYLGA-VPVMTSY-HLPTTTMEVF--IDRLEDPFIL 120
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVF-QITHNNKFLYLFWACLLGGmIAVPVSIgSNEEHKLKLNkvWNTLKNPYLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 121 FDDETKKRVreisngtkskqipilylmeqpdlsvsqsfldKNEISYMTHTSGTTGIPK-----------LICHSAHSMGW 189
Cdd:cd05908 96 TEEEVLCEL-------------------------------ADELAFIQFSSGSTGDPKgvmlthenlvhNMFAILNSTEW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 190 RTK-----WqktvFTKISEKKLIAFHISPVYSrfniGISSLMsmgfpmMPLANAQSSKVVHMLEVHRPIALETHPNNFVQ 264
Cdd:cd05908 145 KTKdrilsW----MPLTHDMGLIAFHLAPLIA----GMNQYL------MPTRLFIRRPILWLKKASEHKATIVSSPNFGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 265 WRFTAKEHPEA-----FSGIRYYHSTFDAINNQTMKTFLRT----SMAQNAVfLQVYGQSECG--------------PMI 321
Cdd:cd05908 211 KYFLKTLKPEKandwdLSSIRMILNGAEPIDYELCHEFLDHmskyGLKRNAI-LPVYGLAEASvgaslpkaqspfktITL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 322 LKAHTL--ESLKISDARD------MGVGLE-DMTSARITDSVGNVLPENTDGHIQLlsKGRALT--YYKeDARFQENVYG 390
Cdd:cd05908 290 GRRHVThgEPEPEVDKKDsecltfVEVGKPiDETDIRICDEDNKILPDGYIGHIQI--RGKNVTpgYYN-NPEATAKVFT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 391 D--WWDSGDYGFMdKHGHLFLKDRQVDLIeTIN---------STLAIEdflLDSLDfLAEVVI--VRDKNHSPQPIIA-- 455
Cdd:cd05908 367 DdgWLKTGDLGFI-RNGRLVITGREKDII-FVNgqnvyphdiERIAEE---LEGVE-LGRVVAcgVNNSNTRNEEIFCfi 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 488252875 456 --------LAP-----DKEMDWNRWWeQVHELprlnVPIIRdfdaIPRTATMKVQRLQI 501
Cdd:cd05908 441 ehrkseddFYPlgkkiKKHLNKRGGW-QINEV----LPIRR----IPKTTSGKVKRYEL 490
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
7-498 |
2.28e-08 |
|
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: 56.54 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 7 YSPLNLFTNFQEAAANFSE-TPIIFDEPLSAFPElgletTYKKCCesvlKRACQLAHLGVKSGDKVIIYKSSAFDTYLLA 85
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDrTSIVYGDRRYTWRQ-----TYDRCR----RLASALAALGISRGDTVAVLAPNTPAMYELH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 86 VSVSYLGAVPVMTSYHLPTTTMEvFIDRLEDPFILFDDETKKRVREISNGTKSkqipilYLMEQPDlsvsqsflDKNEIS 165
Cdd:cd12118 72 FGVPMAGAVLNALNTRLDAEEIA-FILRHSEAKVLFVDREFEYEDLLAEGDPD------FEWIPPA--------DEWDPI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 166 YMTHTSGTTGIPK--LICH-SA--------------------------HSMGWRTKWQ----------------KTVFTK 200
Cdd:cd12118 137 ALNYTSGTTGRPKgvVYHHrGAylnalanilewemkqhpvylwtlpmfHCNGWCFPWTvaavggtnvclrkvdaKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 201 ISEKKLIAFHISPVysrfnigissLMSMgfpmmpLANAQSSkvvhmleVHRPIaleTHPNNFvqwrFTAKEHPEAfsgir 280
Cdd:cd12118 217 IEKHKVTHFCGAPT----------VLNM------LANAPPS-------DARPL---PHRVHV----MTAGAPPPA----- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 281 yyhSTFDAINNQTMKTFlrtsmaqnavflQVYGQSEC-GPMILKAHTLE--SLKISD-----ARDmGVGLEDMTSARITD 352
Cdd:cd12118 262 ---AVLAKMEELGFDVT------------HVYGLTETyGPATVCAWKPEwdELPTEErarlkARQ-GVRYVGLEEVDVLD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 353 SVGNV-LPEN--TDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLA 425
Cdd:cd12118 326 PETMKpVPRDgkTIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIisggENI-SSVE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 426 IEDFLLDSLDFLAEVVIVRDKNH---SPQPIIALAPDKE------MDWNRwweqvHELPRLNVPIIRDFDAIPRTATMKV 496
Cdd:cd12118 405 VEGVLYKHPAVLEAAVVARPDEKwgeVPCAFVELKEGAKvteeeiIAFCR-----EHLAGFMVPKTVVFGELPKTSTGKI 479
|
..
gi 488252875 497 QR 498
Cdd:cd12118 480 QK 481
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
43-501 |
2.39e-08 |
|
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: 56.33 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 43 ETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVmtsyhlPTTTMevfIDRLEDPFILFD 122
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVV------PINPM---LKERELEYILND 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 123 DETKkrvreisngtkskqipilylmeqpdLSVSQSFLDknEISYMTHTSGTTGIPKLICHSaHSMGWRTKWQKTVFTKIS 202
Cdd:cd05935 72 SGAK-------------------------VAVVGSELD--DLALIPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 203 EKKLIA-----FHISPVYSRFNIGisslMSMGFPMMPLANAQSSKVVHMLEVHRPIALETHPNNFVQWRFTAKEHPEAFS 277
Cdd:cd05935 124 PSDVILaclplFHVTGFVGSLNTA----VYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 278 GIRYYHSTFDAINNQTMKTFLRTSMAQnavFLQVYGQSE-CGPMILKAHTLESLKIsdardMGVGLEDmTSARITD-SVG 355
Cdd:cd05935 200 SLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTEtMSQTHTNPPLRPKLQC-----LGIP*FG-VDARVIDiETG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 356 NVLPENTDGHIQL----LSKGraltYYKedaRFQENVYGDWWDS-------GDYGFMDKHGHLFLKDRqvdLIETIN-ST 423
Cdd:cd05935 271 RELPPNEVGEIVVrgpqIFKG----YWN---RPEETEESFIEIKgrrffrtGDLGYMDEEGYFFFVDR---VKRMINvSG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 424 LAIEDFLLDSLDF----LAEVVIV----RDKNHSPQPIIALAPDKEM--------DWNRWWEQVHELPRlnvpIIRDFDA 487
Cdd:cd05935 341 FKVWPAEVEAKLYkhpaI*EVCVIsvpdERVGEEVKAFIVLRPEYRGkvteediiEWAREQMAAYKYPR----EVEFVDE 416
|
490
....*....|....
gi 488252875 488 IPRTATMKVQRLQI 501
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
162-459 |
2.97e-08 |
|
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: 56.32 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 162 NEISYMTHTSGTTGIPKLICHSAHSMG---------WRTKWQKTVFTKISEKKLIAFHISPVYS--------------RF 218
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGlglkvngryWLDLTASDIMWNTSDTGWIKSAWSSLFEpwiqgacvfvhhlpRF 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 219 --NIGISSLMSmgFPMMPLANAQSskvvhmleVHRPIALEthpnNFVQWRFTAKEHpeafsgiryYHSTFDAINNQTMKT 296
Cdd:cd05928 254 dpLVILKTLSS--YPITTFCGAPT--------VYRMLVQQ----DLSSYKFPSLQH---------CVTGGEPLNPEVLEK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 297 FlrtsMAQNAVFL-QVYGQSECGpmiLKAHTLESLKISDArDMGVGLEDMtSARITDSVGNVLPENTDGHIQL-LSKGRA 374
Cdd:cd05928 311 W----KAQTGLDIyEGYGQTETG---LICANFKGMKIKPG-SMGKASPPY-DVQIIDDNGNVLPPGTEGDIGIrVKPIRP 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 375 LT----YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIetINSTLAIEDFLLDSL----DFLAEVVIVRdk 446
Cdd:cd05928 382 FGlfsgYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVI--NSSGYRIGPFEVESAliehPAVVESAVVS-- 457
|
330 340
....*....|....*....|.
gi 488252875 447 nhSPQPI--------IALAPD 459
Cdd:cd05928 458 --SPDPIrgevvkafVVLAPQ 476
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
310-443 |
3.34e-08 |
|
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: 55.89 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 310 QVYGQSEcgpmILKAHTLESLKISDARDMGVGLEDmTSARITDSvgnvlpentdGHIQLLSKGRALTYYKEDARFQENVY 389
Cdd:cd17641 353 QLYGQTE----LAGAYTVHRDGDVDPDTVGVPFPG-TEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDFD 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488252875 390 GD-WWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLAIEDFLLDSLDF---LAEVVIV 443
Cdd:cd17641 418 EDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFspyIAEAVVL 475
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
4-498 |
4.23e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 55.81 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 4 TITYSPLNLFTNFQEAAANFSETpiifdeplSAFPELGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSA----- 78
Cdd:PRK06710 18 TISYDIQPLHKYVEQMASRYPEK--------KALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCpqavi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 79 --FDTYL---LAVSVSYL-------------GA---------VPVMTSYHLPTTTMEVFIDRLED--PF---ILFDDETK 126
Cdd:PRK06710 90 gyYGTLLaggIVVQTNPLytereleyqlhdsGAkvilcldlvFPRVTNVQSATKIEHVIVTRIADflPFpknLLYPFVQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 127 KRVREISNGTKSKQIPILYLMEQP-DLSVSQSFLDKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKK 205
Cdd:PRK06710 170 KQSNLVVKVSESETIHLWNSVEKEvNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 206 LIAFHISPVYSRFniGISSLMSM----GFPMMPLANAQSSKVVHMLEVHRPIALETHPNNFVQWRFTAKEHPEAFSGIRY 281
Cdd:PRK06710 250 EVVLGVLPFFHVY--GMTAVMNLsimqGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 282 YHSTFDAINNQTMKTFLRTSMAQnavFLQVYGQSECGPmILKAHTLESLKISDArdMGVGLEDMTSARITDSVGNVLPEN 361
Cdd:PRK06710 328 CISGSAPLPVEVQEKFETVTGGK---LVEGYGLTESSP-VTHSNFLWEKRVPGS--IGVPWPDTEAMIMSLETGEALPPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 362 TDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTL---AIEDFLLDSlDFLA 438
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVyprEVEEVLYEH-EKVQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488252875 439 EVVIV----RDKNHSPQPIIALAPDK---EMDWNRWWEQVheLPRLNVPIIRDF-DAIPRTATMKVQR 498
Cdd:PRK06710 481 EVVTIgvpdPYRGETVKAFVVLKEGTecsEEELNQFARKY--LAAYKVPKVYEFrDELPKTTVGKILR 546
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
311-501 |
7.16e-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: 54.21 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 311 VYGQSECGPMILKAHTLESLkisDARDMGVG-LEDMTSARITDSVGN-VLPENTDGhiQLLSKGRALT--YYKEDARFQE 386
Cdd:cd05917 150 AYGMTETSPVSTQTRTDDSI---EKRVNTVGrIMPHTEAKIVDPEGGiVPPVGVPG--ELCIRGYSVMkgYWNDPEKTAE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 387 NVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI----ETINSTlAIEDFLLDSLDFL-AEVVIVRDKNHSPQ--PIIALAP 458
Cdd:cd05917 225 AIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIirggENIYPR-EIEEFLHTHPKVSdVQVVGVPDERYGEEvcAWIRLKE 303
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488252875 459 DKEMDwnrwWEQVHE-----LPRLNVP-IIRDFDAIPRTATMKVQRLQI 501
Cdd:cd05917 304 GAELT----EEDIKAyckgkIAHYKVPrYVFFVDEFPLTVSGKIQKFKL 348
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
160-447 |
1.28e-07 |
|
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: 53.99 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 160 DKNEISYMTHTSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAF----HISPVYSRFNIGIS---SLMSMGFPM 232
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSIlplhHIYPLTFTLLLPLLngaHVVFLDKIP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 233 MPLANAQS-SKVVHMLEVHRPIALE---------------------THPNNFVQWRFTAKEHPEAFSG-IRYYHSTFDAI 289
Cdd:cd05914 167 SAKIIALAfAQVTPTLGVPVPLVIEkifkmdiipkltlkkfkfklaKKINNRKIRKLAFKKVHEAFGGnIKEFVIGGAKI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 290 NNQTMKtFLRTSmaqNAVFLQVYGQSECGPMILKAHTlESLKISDArdmGVGLEDMtSARITDSVgnvlPENTDGHIQLL 369
Cdd:cd05914 247 NPDVEE-FLRTI---GFPYTIGYGMTETAPIISYSPP-NRIRLGSA---GKVIDGV-EVRIDSPD----PATGEGEIIVR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 370 SKGRALTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI----------ETINSTLAIEDFLLDSLdfla 438
Cdd:cd05914 314 GPNVMKGYYKNPEATAEAFDKDgWFHTGDLGKIDAEGYLYIRGRKKEMIvlssgkniypEEIEAKINNMPFVLESL---- 389
|
....*....
gi 488252875 439 evVIVRDKN 447
Cdd:cd05914 390 --VVVQEKK 396
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
41-500 |
2.02e-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: 53.06 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 41 GLETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFIL 120
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 121 FDDETkkrvreisngtkskqipILYlmeqpdlsvsqsfldkneisymthTSGTTGIPKLICHSAHSMGWRTKWQKTVFTK 200
Cdd:cd05934 81 VDPAS-----------------ILY------------------------TSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 201 ISEKKLIAFhispvysrfnigisslmsmgfpmMPL--ANAQSSKVVHMLEVHRPIALEThpnnfvqwRFTAKehpeAF-S 277
Cdd:cd05934 120 GEDDVYLTV-----------------------LPLfhINAQAVSVLAALSVGATLVLLP--------RFSAS----RFwS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 278 GIRYYHST-FDAINnqTMKTFLrtsMAQ-------------------------------NAVFLQVYGQSECGPMILKAH 325
Cdd:cd05934 165 DVRRYGATvTNYLG--AMLSYL---LAQppspddrahrlraaygapnppelheefeerfGVRLLEGYGMTETIVGVIGPR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 326 TleslkiSDARDMGVG-LEDMTSARITDSVGNVLPENTDGHIQLLS---KGRALTYYKEDARFQENVYGDWWDSGDYGFM 401
Cdd:cd05934 240 D------EPRRPGSIGrPAPGYEVRIVDDDGQELPAGEPGELVIRGlrgWGFFKGYYNMPEATAEAMRNGWFHTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 402 DKHGHLFLKDRQVDLI----ETInSTLAIEDFLL--------------DSL--DFLAEVVIVRDknhsPQPiiaLAPDKE 461
Cdd:cd05934 314 DADGFFYFVDRKKDMIrrrgENI-SSAEVERAILrhpavreaavvavpDEVgeDEVKAVVVLRP----GET---LDPEEL 385
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488252875 462 MDWNRwwEQvheLPRLNVP-IIRDFDAIPRTATMKVQRLQ 500
Cdd:cd05934 386 FAFCE--GQ---LAYFKVPrYIRFVDDLPKTPTEKVAKAQ 420
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
309-503 |
4.16e-07 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 52.41 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 309 LQVYGQSECGPMILkAHTLESLKIsdardmgvgledmtsaritDSVGNVLPENT-----DGHIQLlsKGRALT--YYKED 381
Cdd:COG1022 375 LEGYGLTETSPVIT-VNRPGDNRI-------------------GTVGPPLPGVEvkiaeDGEILV--RGPNVMkgYYKNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 382 ARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLIetINST------LAIEDFLLDSlDFLAEVVIVRDKnhspQP-I 453
Cdd:COG1022 433 EATAEAFDADgWLHTGDIGELDEDGFLRITGRKKDLI--VTSGgknvapQPIENALKAS-PLIEQAVVVGDG----RPfL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 454 IAL-APDKEMdWNRWWEQvHELP----------------------RLN--VPI---IRDFDAIPR---------TATMKV 496
Cdd:COG1022 506 AALiVPDFEA-LGEWAEE-NGLPytsyaelaqdpevraliqeevdRANagLSRaeqIKRFRLLPKeftiengelTPTLKL 583
|
....*..
gi 488252875 497 QRLQIEK 503
Cdd:COG1022 584 KRKVILE 590
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
96-412 |
2.37e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.20 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 96 VMTSYHLPTTTMEVFIDRLEDPFIL-FDDETKKRVR---EISNGTKSKqIPILYLMEQPDLSVSqsflDKNEISYMTHTS 171
Cdd:PRK06334 118 VLTSKQLMQHLAQTHGEDAEYPFSLiYMEEVRKELSfweKCRIGIYMS-IPFEWLMRWFGVSDK----DPEDVAVILFTS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 172 GTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKLIAFhISPVYSR-FNIGISSLMSMGFPMMPLANA-QSSKVVHMLEV 249
Cdd:PRK06334 193 GTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSF-LPPFHAYgFNSCTLFPLLSGVPVVFAYNPlYPKKIVEMIDE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 250 HRPIALETHPNNFVQWRFTAKEHPEAFSGIRYYHSTFDAINN----QTMKTFLRTSMAQNavflqvYGQSECGPMIlKAH 325
Cdd:PRK06334 272 AKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDslyqEALKTFPHIQLRQG------YGTTECSPVI-TIN 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 326 TLESLKISDArdMGVGLEDMTSARITDSVGNVLPENTDGHIqlLSKGRAL--TYYKEDAR--FQENVYGDWWDSGDYGFM 401
Cdd:PRK06334 345 TVNSPKHESC--VGMPIRGMDVLIVSEETKVPVSSGETGLV--LTRGTSLfsGYLGEDFGqgFVELGGETWYVTGDLGYV 420
|
330
....*....|.
gi 488252875 402 DKHGHLFLKDR 412
Cdd:PRK06334 421 DRHGELFLKGR 431
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
43-501 |
2.57e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 49.86 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 43 ETTYKKCCESVLKRACQLAH-LGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVfidRLEDPFI-- 119
Cdd:PRK06839 27 EMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIF---QLKDSGTtv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 120 LFDDETKKRVREISNGTKSKQIPILY--LMEQPDLSVSqSFLDKNE-----ISYmthTSGTTGIPKLICHSAHSMGWRTK 192
Cdd:PRK06839 104 LFVEKTFQNMALSMQKVSYVQRVISItsLKEIEDRKID-NFVEKNEsasfiICY---TSGTTGKPKGAVLTQENMFWNAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 193 WQKTVFTKISEKKLIA----FHISpvysrfNIGI---SSLMSMGFPMMPlANAQSSKVVHMLEVHRPIALETHPNNFVQW 265
Cdd:PRK06839 180 NNTFAIDLTMHDRSIVllplFHIG------GIGLfafPTLFAGGVIIVP-RKFEPTKALSMIEKHKVTVVMGVPTIHQAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 266 RFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSMaqnaVFLQVYGQSECGP---MILKahtleslkiSDARDM--GV 340
Cdd:PRK06839 253 INCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGF----LFGQGFGMTETSPtvfMLSE---------EDARRKvgSI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 341 GLEDM-TSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI-- 417
Cdd:PRK06839 320 GKPVLfCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIis 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 418 --ETInSTLAIEDfLLDSLDFLAE--VVIVRDKNHSPQPIIALAPDKEMDWNRWWEQVHELPRL-NVPIIRDF---DAIP 489
Cdd:PRK06839 400 ggENI-YPLEVEQ-VINKLSDVYEvaVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLaKYKIPKEIvflKELP 477
|
490
....*....|..
gi 488252875 490 RTATMKVQRLQI 501
Cdd:PRK06839 478 KNATGKIQKAQL 489
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
159-450 |
3.89e-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: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 159 LDKNEISYMTHTSGTTGIPKLICH--------SAHSMgwRTKW---QKTVFTKISEKKLIAFHISPVYSRFNIGISSLMS 227
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVVRdngghavaLNWSM--RNIYgikPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 228 MGFPM-MPLANAQSSkvvhMLEVHRPIALETHPNNFvqwRFTAKEHPEAFSGIRYYHSTFDAInnqtmktFL-------- 298
Cdd:cd05967 305 EGKPVgTPDPGAFWR----VIEKYQVNALFTAPTAI---RAIRKEDPDGKYIKKYDLSSLRTL-------FLagerldpp 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 299 RTSMAQNAVFLQV---YGQSECG-PMILKAHTLESLKI---SDARDM-GVGLEdmtsarITDSVGNVLPENTDGHIQL-- 368
Cdd:cd05967 371 TLEWAENTLGVPVidhWWQTETGwPITANPVGLEPLPIkagSPGKPVpGYQVQ------VLDEDGEPVGPNELGNIVIkl 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 369 -LSKGRALTYYKEDARFQENVYGD---WWDSGDYGFMDKHGHLFLKDRQVDLIETIN---STLAIEDFLLDSLDfLAE-- 439
Cdd:cd05967 445 pLPPGCLLTLWKNDERFKKLYLSKfpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGhrlSTGEMEESVLSHPA-VAEca 523
|
330
....*....|...
gi 488252875 440 VVIVRD--KNHSP 450
Cdd:cd05967 524 VVGVRDelKGQVP 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 488252875 339 GVGLEdmtsARITDSVGNVLPENTDGHIQLLS-KGRAL--TYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQV 414
Cdd:PRK08008 346 GFCYE----AEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYYLDPKATAKVLEADgWLHTGDTGYVDEEGFFYFVDRRC 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 415 DLI----ETINSTlAIEDFLLDSLDFLAEVVI-----VRDKnhSPQPIIALAPDKEMDWNRWWEQVHE-LPRLNVPIIRD 484
Cdd:PRK08008 422 NMIkrggENVSCV-ELENIIATHPKIQDIVVVgikdsIRDE--AIKAFVVLNEGETLSEEEFFAFCEQnMAKFKVPSYLE 498
|
170
....*....|....*
gi 488252875 485 F-DAIPRTATMKVQR 498
Cdd:PRK08008 499 IrKDLPRNCSGKIIK 513
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
16-498 |
8.41e-06 |
|
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: 48.32 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 16 FQEAAANFSETPIIFDEplsafpelGLETTYKKCCEsvlkRACQLAHL----GVKSGDKVIIY--KSSAFDTYLLAVSVS 89
Cdd:cd17645 4 FEEQVERTPDHVAVVDR--------GQSLTYKQLNE----KANQLARHlrgkGVKPDDQVGIMldKSLDMIAAILGVLKA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 90 YLGAVPVMTSYhlPTTTMEvfidrledpFILFDDETKkrvreisngtkskqipilYLMEQPDlsvsqsfldknEISYMTH 169
Cdd:cd17645 72 GGAYVPIDPDY--PGERIA---------YMLADSSAK------------------ILLTNPD-----------DLAYVIY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 170 TSGTTGIPKLICHSAHSMGWRTKWQKTVFTKISEKKliafhiSPVYSRFNIGiSSLMSMgFPMMpLANAQsskvVHMLEV 249
Cdd:cd17645 112 TSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK------SLVYASFSFD-ASAWEI-FPHL-TAGAA----LHVVPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 250 HRPIALETHPNNFVQWRFTAKEHPEAFSgiryyhSTFDAINNQTMKTF------LRTSMAQNAVFLQVYGQSECGPMILK 323
Cdd:cd17645 179 ERRLDLDALNDYFNQEGITISFLPTGAA------EQFMQLDNQSLRVLltggdkLKKIERKGYKLVNNYGPTENTVVATS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 324 AHT-LESLKISDARDMgvgleDMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYgfMD 402
Cdd:cd17645 253 FEIdKPYANIPIGKPI-----DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGER--MY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 403 KHGHL--FLKDRQVDLIETINSTLA----------IEDFLLD-SLDFLAEVVIVRDKNHSPQPIIALAPDKEMDWNRWWE 469
Cdd:cd17645 326 RTGDLakFLPDGNIEFLGRLDQQVKirgyriepgeIEPFLMNhPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELRE 405
|
490 500 510
....*....|....*....|....*....|.
gi 488252875 470 QVHE-LPRLNVP-IIRDFDAIPRTATMKVQR 498
Cdd:cd17645 406 WLKNdLPDYMIPtYFVHLKALPLTANGKVDR 436
|
|
| 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 488252875 348 ARITDSVGNVLPENTDGhiQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA-- 425
Cdd:cd05958 276 AKVVDDEGNPVPDGTIG--RLAVRGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIApp 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 426 -IEDFLLDSLDfLAEVVIV----RDKNHSPQPIIALAPDKEMDwnrwwEQ-VHEL-------------PRLnvpiIRDFD 486
Cdd:cd05958 354 eVEDVLLQHPA-VAECAVVghpdESRGVVVKAFVVLRPGVIPG-----PVlARELqdhakahiapykyPRA----IEFVT 423
|
170
....*....|..
gi 488252875 487 AIPRTATMKVQR 498
Cdd:cd05958 424 ELPRTATGKLQR 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
348-503 |
1.29e-05 |
|
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: 47.67 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 348 ARITD-SVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQ-VDLIET----I 420
Cdd:cd05941 275 ARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDgWFKTGDLGVVDEDGYYWILGRSsVDIIKSggykV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 421 nSTLAIEDfLLDSLDFLAEVVIV----RDKNHSPQPIIALAPDKE----MDWNRWWEQV---HELPRLnvpiIRDFDAIP 489
Cdd:cd05941 355 -SALEIER-VLLAHPGVSECAVIgvpdPDWGERVVAVVVLRAGAAalslEELKEWAKQRlapYKRPRR----LILVDELP 428
|
170
....*....|....
gi 488252875 490 RTATMKVQRLQIEK 503
Cdd:cd05941 429 RNAMGKVNKKELRK 442
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1-184 |
1.36e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 47.69 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 1 MMETITYSPLNL----FTNFQEA---AANfSETPIIFdepLSAFPELGLETTYKKCCESVLKRACQLAHLGVKSGDKVII 73
Cdd:PRK09192 4 MSPTPTTSSLPRryadFPTLVEAldyAAL-GEAGMNF---YDRRGQLEEALPYQTLRARAEAGARRLLALGLKPGDRVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 74 YKSSAFDTYLLAVSVSYLGAVPVmtSYHLPTT--TMEVFIDRLE------DP-FILFDDETKKRVREISNGTKSKQI--- 141
Cdd:PRK09192 80 IAETDGDFVEAFFACQYAGLVPV--PLPLPMGfgGRESYIAQLRgmlasaQPaAIITPDELLPWVNEATHGNPLLHVlsh 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488252875 142 PILYLMEQPDLSVSQsfLDKNEISYMTHTSGTTGIPK--LICHSA 184
Cdd:PRK09192 158 AWFKALPEADVALPR--PTPDDIAYLQYSSGSTRFPRgvIITHRA 200
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
166-417 |
1.51e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 47.81 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 166 YMTHTSGTTGIPKLICHS--AHSMGWRTKWQktvFTKISEKKLIAF-HISPVYSRFNIGISSLMSMGFPMMpLANAQSSK 242
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSngPHLVGLKYYWR---SIIEKDIPTVVFsHSSIGWVSFHGFLYGSLSLGNTFV-MFEGGIIK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 243 VVHMlEVHRPIALETHP-NNFVQW----RFTAKEHPEAfsgiRYYHSTFDAIN-----------NQTMKTFLRTSMaqNA 306
Cdd:PTZ00237 334 NKHI-EDDLWNTIEKHKvTHTLTLpktiRYLIKTDPEA----TIIRSKYDLSNlkeiwcggeviEESIPEYIENKL--KI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 307 VFLQVYGQSECGPMILKAHTLESLKISDARDMGVGLEDMtsarITDSVGNVLPENTDGHIQL---LSKGRALTYYKEDAR 383
Cdd:PTZ00237 407 KSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPS----ILSEDGKELNVNEIGEVAFklpMPPSFATTFYKNDEK 482
|
250 260 270
....*....|....*....|....*....|....*.
gi 488252875 384 FQE--NVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PTZ00237 483 FKQlfSKFPGYYNSGDLGFKDENGYYTIVSRSDDQI 518
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
36-419 |
1.77e-05 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 47.12 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 36 AFPELGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLE 115
Cdd:cd05923 21 ADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 116 DPFILFDDetkkrVREISNGTKSKQIPILYLMEQPDLSVSQSFLD--------KNEISYMTHTSGTTGIPK--LICHsah 185
Cdd:cd05923 101 MTAAVIAV-----DAQVMDAIFQSGVRVLALSDLVGLGEPESAGPliedpprePEQPAFVFYTSGTTGLPKgaVIPQ--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 186 smgwRTKWQKTVFTKISEKKLIAFH-----ISPVYSrfNIGISSL--MSMGF-----PMMPLANAQSSKVVHMLEVHRPI 253
Cdd:cd05923 173 ----RAAESRVLFMSTQAGLRHGRHnvvlgLMPLYH--VIGFFAVlvAALALdgtyvVVEEFDPADALKLIEQERVTSLF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 254 ALETHpnnfvqwrFTAKEHPEAFSGIRYY---HSTF--DAINNQTMKtflRTSMAQNAVFLQVYGQSEcgpmilkahTLE 328
Cdd:cd05923 247 ATPTH--------LDALAAAAEFAGLKLSslrHVTFagATMPDAVLE---RVNQHLPGEKVNIYGTTE---------AMN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 329 SLKISDARDMGVGLEDMTS----ARITDSVGNVLPENTDGHIQL-LSKGRALTYY--KEDARFQENVYGdWWDSGDYGFM 401
Cdd:cd05923 307 SLYMRDARTGTEMRPGFFSevriVRIGGSPDEALANGEEGELIVaAAADAAFTGYlnQPEATAKKLQDG-WYRTGDVGYV 385
|
410
....*....|....*...
gi 488252875 402 DKHGHLFLKDRQVDLIET 419
Cdd:cd05923 386 DPSGDVRILGRVDDMIIS 403
|
|
| 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 488252875 350 ITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRqvdLIETIN------ST 423
Cdd:cd17635 183 LAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGR---SSESINcggvkiAP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 424 LAIEDFLLDSLDF-LAEVVIVRDKNHSPQPIIALAPDKEMDWNRWWEQVH----ELPRLNVP-IIRDFDAIPRTATMKVQ 497
Cdd:cd17635 260 DEVERIAEGVSGVqECACYEISDEEFGELVGLAVVASAELDENAIRALKHtirrELEPYARPsTIVIVTDIPRTQSGKVK 339
|
.
gi 488252875 498 R 498
Cdd:cd17635 340 R 340
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
349-503 |
2.05e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 47.05 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 349 RITDSVGNVLPE--NTDGHIQLLSKGRALTYYKEDARFQENvyGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInS 422
Cdd:PRK06018 368 KITDDAGKELPWdgKTFGRLKVRGPAVAAAYYRVDGEILDD--DGFFDTGDVATIDAYGYMRITDRSKDVIksggEWI-S 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 423 TLAIEDFLLDSLDF-LAEVVIVRDKNHSPQP--IIALAPDKE---------MDWN--RWWeqvheLPRlNVPIIrdfDAI 488
Cdd:PRK06018 445 SIDLENLAVGHPKVaEAAVIGVYHPKWDERPllIVQLKPGETatreeilkyMDGKiaKWW-----MPD-DVAFV---DAI 515
|
170
....*....|....*
gi 488252875 489 PRTATMKVQRLQIEK 503
Cdd:PRK06018 516 PHTATGKILKTALRE 530
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
36-178 |
2.08e-05 |
|
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: 46.86 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 36 AFPELGLETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGA--VPVMTSYhlptttmevfidr 113
Cdd:cd05945 9 AVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDASS------------- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488252875 114 ledpfilfddeTKKRVREISNgtkskqipilylMEQPDLSVSqsflDKNEISYMTHTSGTTGIPK 178
Cdd:cd05945 76 -----------PAERIREILD------------AAKPALLIA----DGDDNAYIIFTSGSTGRPK 113
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
307-419 |
2.34e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 46.90 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 307 VFLQVYGQSECgPMIL-----KAHTLESLKI--SDARDMgVGLEdmtsARITDSVGNVLPENTDGHI----QLLSKGral 375
Cdd:PRK06188 308 IFAQYYGQTEA-PMVItylrkRDHDPDDPKRltSCGRPT-PGLR----VALLDEDGREVAQGEVGEIcvrgPLVMDG--- 378
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488252875 376 tYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIET 419
Cdd:PRK06188 379 -YWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVT 421
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
153-505 |
2.87e-05 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 46.79 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 153 SVSQSFLDKNEISYMTHTSGTTGIPK--LICHS--AHSMGWRTKWQKTVfTKISEKKLIAFHISPVYSRFNIGISSLMSM 228
Cdd:PRK08751 199 SMPTLQIEPDDIAFLQYTGGTTGVAKgaMLTHRnlVANMQQAHQWLAGT-GKLEEGCEVVITALPLYHIFALTANGLVFM 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 229 GFpmmplanaqsSKVVHMleVHRPIALETHPNNFVQWRFTAkehpeaFSGIRYYHST------FDAINNQTMKTFLRTSM 302
Cdd:PRK08751 278 KI----------GGCNHL--ISNPRDMPGFVKELKKTRFTA------FTGVNTLFNGllntpgFDQIDFSSLKMTLGGGM 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 303 A-QNAV-----------FLQVYGQSECGPmilkAHTLESLKISDaRDMGVGLE-DMTSARITDSVGNVLPENTDGhiQLL 369
Cdd:PRK08751 340 AvQRSVaerwkqvtgltLVEAYGLTETSP----AACINPLTLKE-YNGSIGLPiPSTDACIKDDAGTVLAIGEIG--ELC 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 370 SKGRALT--YYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLIETINSTL---AIEDfLLDSLDFLAEVVIV 443
Cdd:PRK08751 413 IKGPQVMkgYWKRPEETAKVMDADgWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVypnEIED-VIAMMPGVLEVAAV 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488252875 444 RDKNHSPQPIIALAPDKEmDWNRWWEQVHELPRLNV-----PIIRDFDA-IPRTATMKVQRLQIEKAP 505
Cdd:PRK08751 492 GVPDEKSGEIVKVVIVKK-DPALTAEDVKAHARANLtgykqPRIIEFRKeLPKTNVGKILRRELRDAA 558
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
377-500 |
2.94e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 46.48 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 377 YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFLAEVVIVR--DK-NHS 449
Cdd:PRK08162 402 YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIisggENI-SSIEVEDVLYRHPAVLVAAVVAKpdPKwGEV 480
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488252875 450 PQPIIALAPDKE------MDWNRwweqvHELPRLNVPIIRDFDAIPRTATMKVQRLQ 500
Cdd:PRK08162 481 PCAFVELKDGASateeeiIAHCR-----EHLAGFKVPKAVVFGELPKTSTGKIQKFV 532
|
|
| 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 488252875 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 488252875 349 RITDSVGNVLPENTDGHIqLLSKGRALTYYKEDARFQE--NVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PRK13391 339 HILDDDGAELPPGEPGTI-WFEGGRPFEYLNDPAKTAEarHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
55-501 |
7.96e-05 |
|
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: 45.18 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 55 KRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDEtkKRVREISN 134
Cdd:cd05970 59 KTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE--DNIPEEIE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 135 GTKSkQIPILYLMEQPDLSVSQSFLD---------------------KNE-ISYMTHTSGTTGIPKLICHS--------A 184
Cdd:cd05970 137 KAAP-ECPSKPKLVWVGDPVPEGWIDfrkliknaspdferptansypCGEdILLVYFSSGTTGMPKMVEHDftyplghiV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 185 HSMGWR-------------TKWQKTVFTKIsekkliafhispvYSRFNIGiSSLMSMGFPMMPLANaqsskvvhMLEVHR 251
Cdd:cd05970 216 TAKYWQnvregglhltvadTGWGKAVWGKI-------------YGQWIAG-AAVFVYDYDKFDPKA--------LLEKLS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 252 PIALETHPNNFVQWRFTAKEHPEA--FSGIRYYHSTFDAINNQTMKTFLRTSMAQnavFLQVYGQSECgpmILKAHTLES 329
Cdd:cd05970 274 KYGVTTFCAPPTIYRFLIREDLSRydLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTET---TLTIATFPW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 330 LKI---SDARDM-GVGLEdmtsarITDSVGNVLPENTDGHIQL-LSKGRAL----TYYKEDARFQENVYGDWWDSGDYGF 400
Cdd:cd05970 348 MEPkpgSMGKPApGYEID------LIDREGRSCEAGEEGEIVIrTSKGKPVglfgGYYKDAEKTAEVWHDGYYHTGDAAW 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 401 MDKHGHLFLKDRQVDLIETinSTLAIEDFLLDSLDFLAEVVIVRDKNHSPQPI--------IALAPDKE---------MD 463
Cdd:cd05970 422 MDEDGYLWFVGRTDDLIKS--SGYRIGPFEVESALIQHPAVLECAVTGVPDPIrgqvvkatIVLAKGYEpseelkkelQD 499
|
490 500 510
....*....|....*....|....*....|....*...
gi 488252875 464 WNRWWEQVHELPRlnvpIIRDFDAIPRTATMKVQRLQI 501
Cdd:cd05970 500 HVKKVTAPYKYPR----IVEFVDELPKTISGKIRRVEI 533
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
43-180 |
1.01e-04 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 45.00 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 43 ETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFD 122
Cdd:PRK05857 41 ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVA 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488252875 123 DETK---------------KRVREISNGTKSKQIP-ILYLMEQPDLSVSQSFLdkneisyMTHTSGTTGIPKLI 180
Cdd:PRK05857 121 PGSKmassavpealhsipvIAVDIAAVTRESEHSLdAASLAGNADQGSEDPLA-------MIFTSGTTGEPKAV 187
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
169-506 |
1.08e-04 |
|
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: 44.39 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 169 HTSGTTGIPKLICHSaHSMGWRTKWQKTVFTKISEKKLIAFHIsPVYSRFNigisslmSMGFPMMPLANAQSSKVVHMLE 248
Cdd:cd05944 9 HTGGTTGTPKLAQHT-HSNEVYNAWMLALNSLFDPDDVLLCGL-PLFHVNG-------SVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 249 VHRPIALEthpnNFvqWRFTAKEHPEAFSGIRYYHSTFDAINNQTMKTFLRTSMAQNAVF----------------LQVY 312
Cdd:cd05944 80 YRNPGLFD----NF--WKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLpvelrarfedatglpvVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 313 GQSECGPMILKAHTLESLKISdardmGVGLE---DMTSARITDSVGNVLPE---NTDGHIQLLSKG-RALTYYKEDARfq 385
Cdd:cd05944 154 GLTEATCLVAVNPPDGPKRPG-----SVGLRlpyARVRIKVLDGVGRLLRDcapDEVGEICVAGPGvFGGYLYTEGNK-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 386 eNVYGD--WWDSGDYGFMDKHGHLFLKDRQVDLI----ETINSTLaIEDFLLDSLDFLAEVVIVRDKNHS---PQPIIAL 456
Cdd:cd05944 227 -NAFVAdgWLNTGDLGRLDADGYLFITGRAKDLIirggHNIDPAL-IEEALLRHPAVAFAGAVGQPDAHAgelPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488252875 457 APDKE------MDWNRwwEQVHElpRLNVPI-IRDFDAIPRTATMKVQRLQIEKAPI 506
Cdd:cd05944 305 KPGAVveeeelLAWAR--DHVPE--RAAVPKhIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
43-184 |
1.45e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 44.57 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 43 ETTYKKCCESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSyhlPTTTMEVFIDRLE--DPFIL 120
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCS---PDFGVPGVLDRFGqiEPKVL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 121 FDDE----TKKR------VREISNGTKSKQ----IPILYLMEQPDLSVSQSFLDKNEIS-------------------YM 167
Cdd:cd05943 175 FAVDaytyNGKRhdvrekVAELVKGLPSLLavvvVPYTVAAGQPDLSKIAKALTLEDFLatgaagelefeplpfdhplYI 254
|
170
....*....|....*..
gi 488252875 168 THTSGTTGIPKLICHSA 184
Cdd:cd05943 255 LYSSGTTGLPKCIVHGA 271
|
|
| 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 488252875 349 RITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYG-DWWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PRK08276 326 RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMI 395
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
346-503 |
2.20e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 43.88 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 346 TSARITDSV-GNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTL 424
Cdd:PRK06178 396 TEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSV 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 425 ---AIEDFLLDSLDFLAEVVIVR---DKNHSPQPIIALAPDKEMDWnrwwEQVHELPRLN-----VPIIRDFDAIPRTAT 493
Cdd:PRK06178 476 fpsEVEALLGQHPAVLGSAVVGRpdpDKGQVPVAFVQLKPGADLTA----AALQAWCRENmavykVPEIRIVDALPMTAT 551
|
170
....*....|
gi 488252875 494 MKVQRLQIEK 503
Cdd:PRK06178 552 GKVRKQDLQA 561
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
169-506 |
2.99e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 43.41 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 169 HTSGTTGIPKLICHSaHS----MGW------RTKWQKTVFTKisekkLIAFHISPVYSRFnigisslmsmgfpMMPLANA 238
Cdd:PRK07529 220 HTGGTTGMPKLAQHT-HGnevaNAWlgalllGLGPGDTVFCG-----LPLFHVNALLVTG-------------LAPLARG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 239 QSskVVhmlevhrpiaLET-----HPN---NFvqWRFTAKEHPEAFSGIryyhstfdainnqtmKTFLrtsmaqnAVFLQ 310
Cdd:PRK07529 281 AH--VV----------LATpqgyrGPGviaNF--WKIVERYRINFLSGV---------------PTVY-------AALLQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 311 VygqsecgPmiLKAHTLESLK--ISDARDMGVGL----EDMTSARITDSVGnvLPENT--------DGHIQLLSKGRALT 376
Cdd:PRK07529 325 V-------P--VDGHDISSLRyaLCGAAPLPVEVfrrfEAATGVRIVEGYG--LTEATcvssvnppDGERRIGSVGLRLP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 377 Y-------------YKEDARFQE---------NVY---------------GDWWDSGDYGFMDKHGHLFLKDRQVDLI-- 417
Cdd:PRK07529 394 YqrvrvvilddagrYLRDCAVDEvgvlciagpNVFsgyleaahnkglwleDGWLNTGDLGRIDADGYFWLTGRAKDLIir 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 418 --ETINSTlAIEDFLLDSLDFLAEVVIVRDKNHS---PQPIIALAPDKE------MDWNRwwEQVHElpRLNVPI-IRDF 485
Cdd:PRK07529 474 ggHNIDPA-AIEEALLRHPAVALAAAVGRPDAHAgelPVAYVQLKPGASateaelLAFAR--DHIAE--RAAVPKhVRIL 548
|
410 420
....*....|....*....|.
gi 488252875 486 DAIPRTATMKVQRLQIEKAPI 506
Cdd:PRK07529 549 DALPKTAVGKIFKPALRRDAI 569
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
332-418 |
3.80e-04 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 43.04 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 332 ISDARDMGVGLEDMTSARITDSVGNVLPENTDGHIQLLSKGRALTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLK 410
Cdd:PLN02330 357 IAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDgWLHTGDIGYIDDDGDIFIV 436
|
....*...
gi 488252875 411 DRQVDLIE 418
Cdd:PLN02330 437 DRIKELIK 444
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
270-417 |
3.90e-04 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 43.12 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 270 KEHPeaFSGIRYYHSTFDA-INNQTMKTF----LRTS----MA-QNAV-----------FLQVYGQSECGPMI------L 322
Cdd:PRK08974 296 KKYP--FTAITGVNTLFNAlLNNEEFQELdfssLKLSvgggMAvQQAVaerwvkltgqyLLEGYGLTECSPLVsvnpydL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 323 KAHTleslkisdardMGVGLE-DMTSARITDSVGNVLPENTDGhiQLLSKG-RALTYYKEDARFQENVYGD-WWDSGDYG 399
Cdd:PRK08974 374 DYYS-----------GSIGLPvPSTEIKLVDDDGNEVPPGEPG--ELWVKGpQVMLGYWQRPEATDEVIKDgWLATGDIA 440
|
170
....*....|....*...
gi 488252875 400 FMDKHGHLFLKDRQVDLI 417
Cdd:PRK08974 441 VMDEEGFLRIVDRKKDMI 458
|
|
| 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 488252875 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 |
6.79e-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: 42.34 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 289 INNQTMKTFLrtsmAQNAVFLQVYGQSEC-GPmilkaHTLESLKisdardmgvgledmtSARITdSVGNVLP-------- 359
Cdd:cd05933 332 ISRETLEFFL----SLNIPIMELYGMSETsGP-----HTISNPQ---------------AYRLL-SCGKALPgcktkihn 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 360 ENTDGHIQLLSKGRA--LTYYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI-----ETINStLAIEDFLL 431
Cdd:cd05933 387 PDADGIGEICFWGRHvfMGYLNMEDKTEEAIDEDgWLHSGDLGKLDEDGFLYITGRIKELIitaggENVPP-VPIEDAVK 465
|
170
....*....|....*
gi 488252875 432 DSLDFLAEVVIVRDK 446
Cdd:cd05933 466 KELPIISNAMLIGDK 480
|
|
| 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 488252875 377 YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTLAIEDFLLDSLDFLAEVVIVRDKNH---S 449
Cdd:PLN02479 416 YLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIisggENI-SSLEVENVVYTHPAVLEASVVARPDERwgeS 494
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488252875 450 PQPIIALAPDKE-MDWNRWWEQV-----HELPRLNVPIIRDFDAIPRTATMKVQR 498
Cdd:PLN02479 495 PCAFVTLKPGVDkSDEAALAEDImkfcrERLPAYWVPKSVVFGPLPKTATGKIQK 549
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
50-185 |
1.52e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 41.01 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 50 CESVLKRACQLAHLGVKSGDKVIIYKSSAFDTYLLAVSVSYLGAVPVMTSYHLPTTTMEVFIDRLEDPFILFDDETKKrv 129
Cdd:PRK09029 35 CARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALVLEGENT-- 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488252875 130 reisngtkskQIPILYLMEQPDLSVSQSFLDKNEISYMTHTSGTTGIPKLICHS--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 488252875 352 DSVGNVLP-------ENTDGHIQLLSKGRALTYYKEDARFQEnvygdWWDSGDYGFMDKHGHLFLKDRQVDLI----ETI 420
Cdd:PRK07445 283 NSSGQVLPhaqitipANQTGNITIQAQSLALGYYPQILDSQG-----IFETDDLGYLDAQGYLHILGRNSQKIitggENV 357
|
90 100
....*....|....*....|...
gi 488252875 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 488252875 349 RITDSVGNVLPENTDGHIqLLSKGRALTYYKeDARFQENVYGdWWDSGDYGFMDKHGHLFLKDRQVDLI----ETInSTL 424
Cdd:PRK07788 388 KILDENGNEVPRGVVGRI-FVGNGFPFEGYT-DGRDKQIIDG-LLSSGDVGYFDEDGLLFVDGRDDDMIvsggENV-FPA 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 425 AIEDFLLDSLDFL-AEVVIVRDKNHS--------PQPIIALAPDKEMDWNRwweqvHELPRLNVPiiRD---FDAIPRTA 492
Cdd:PRK07788 464 EVEDLLAGHPDVVeAAVIGVDDEEFGqrlrafvvKAPGAALDEDAIKDYVR-----DNLARYKVP--RDvvfLDELPRNP 536
|
....*.
gi 488252875 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 488252875 349 RITDSVGNVLPENTDGHIQLL-SKGRALTYYKEDARFQENVYGdwWDS-GDYGFMDKHGHLFLKDRQVDLI 417
Cdd:cd05929 308 HILDEDGNEVPPGEIGEVYFAnGPGFEYTNDPEKTAAARNEGG--WSTlGDVGYLDEDGYLYLTDRRSDMI 376
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
377-501 |
3.72e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.05 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 377 YYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQVDLIETINSTLA---IEDFLLDSLDFLAEVVIVRDKNHSPQPI 453
Cdd:PRK07867 367 YYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGtapIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488252875 454 IA---LAPDKEMDWNRWWEQVHELPRLN---VP-IIRDFDAIPRTATMKVQRLQI 501
Cdd:PRK07867 447 MAalvLAPGAKFDPDAFAEFLAAQPDLGpkqWPsYVRVCAELPRTATFKVLKRQL 501
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
292-419 |
4.07e-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: 39.56 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252875 292 QTMKTFLRTSmaqNAVFLQVYGQSEcgpmilkAHTLESLKISDARDMGVGLED-MTSARITDSVGNVLPENTDGHI---- 366
Cdd:cd17637 126 ETIQRFEETT---GATFWSLYGQTE-------TSGLVTLSPYRERPGSAGRPGpLVRVRIVDDNDRPVPAGETGEIvvrg 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488252875 367 QLLSKGraltYYKEDARFQENVYGDWWDSGDYGFMDKHGHLFLKDRQV--DLIET 419
Cdd:cd17637 196 PLVFQG----YWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKPekELIKP 246
|
|
| 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 488252875 341 GLEdmtsARITDSVGNVLPENTDGHIQLlsKGRALT-YYKEDARFQENVYGD-WWDSGDYGFMDKHGHLFLKDRQVDLI 417
Cdd:PRK07768 368 GLE----VRVVDEDGQVLPPRGVGVIEL--RGESVTpGYLTMDGFIPAQDADgWLDTGDLGYLTEEGEVVVCGRVKDVI 440
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