|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-519 |
0e+00 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 582.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 46 CQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSI 125
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 126 TRPKLIFCDGKCFQRLSIIARIL--KSHVYTLKDHRLGMPRVEDLLEPT-TAELYYVPETLLLGGDHTVAILCTSGTTGL 202
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELgpKDKIIVLDDKPDGVLSIEDLLSPTlGEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 203 PKAVCISNSACLFDFGFVTG--------QDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYtPEYMIQLVEKYKVTL 274
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTflygndgsNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFD-SELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 275 LTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCyvanLLKLQEFLIT----GQISYGYALTECGGVAANM--GVAKPS 348
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPL----SKELQELLAKrfpnATIKQGYGMTETGGILTVNpdGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 349 SVGRIVPGVRVKILDEAGRS-LGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKED 427
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 428 LLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRlVVDHKQLHCGVFFL 507
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKK-VASYKQLRGGVVFV 474
|
490
....*....|..
gi 24648260 508 PELPKTGSGKVL 519
Cdd:cd05911 475 DEIPKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
30-533 |
8.14e-94 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 293.64 E-value: 8.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 30 IGKILFAFMRNHPNSICqISDtEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHA 109
Cdd:COG0318 1 LADLLRRAAARHPDRPA-LVF-GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 110 VSPWQDEDTIKHLFSITRPKLIFcdgkcfqrlsiiarilkshvytlkdhrlgmprvedllepttaelyyvpetlllggdh 189
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALV--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 190 TVAILCTSGTTGLPKAVCIS------NSACLFDFGFVTGQDVLLSFSTIDWSAGM-FNMLFSCCHGSTRIITDRpYTPEY 262
Cdd:COG0318 102 TALILYTSGTTGRPKGVMLThrnllaNAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGATLVLLPR-FDPER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLitG-QISYGYALTECGGVAA- 340
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF--GvRIVEGYGLTETSPVVTv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 341 ---NMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNES-KRMQDyqGWFHTGDMGYFDNE 416
Cdd:COG0318 259 npeDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATaEAFRD--GWLRTGDLGRLDED 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 417 NYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL--- 493
Cdd:COG0318 337 GYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLary 416
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24648260 494 -VVDHkqlhcgVFFLPELPKTGSGKVLRQQARDQALGKKWA 533
Cdd:COG0318 417 kVPRR------VEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
189-519 |
1.48e-84 |
|
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: 265.69 E-value: 1.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 189 HTVAILCTSGTTGLPKAVCIS------NSACLFDFGFVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPyTPEY 262
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLShrnllaAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF-DPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEfLITGQISYGYALTECGGVAANM 342
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 343 GV----AKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPnESKRMQDYQGWFHTGDMGYFDNENY 418
Cdd:cd04433 159 PPdddaRKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 419 LHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL----V 494
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLapykV 317
|
330 340
....*....|....*....|....*
gi 24648260 495 VDHkqlhcgVFFLPELPKTGSGKVL 519
Cdd:cd04433 318 PRR------VVFVDALPRTASGKID 336
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
35-522 |
6.46e-79 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 256.39 E-value: 6.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 35 FAFMRNHPNSICQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQ 114
Cdd:cd05904 12 FLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 115 DEDTIKHLFSITRPKLIFCDGKCFQRLSIIArilkSHVYTLKDHRLGMPRVEDLLEPTTAELYYVPEtllLGGDHTVAIL 194
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELAEKLASLA----LPVVLLDSAEFDSLSFSDLLFEADEAEPPVVV---IKQDDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 195 CTSGTTGLPKAVCISN-----SACLFDFGF---VTGQDVLLSFstidwsAGMFNM----LFSCC---HGSTRIITDRpYT 259
Cdd:cd05904 165 YSSGTTGRSKGVMLTHrnliaMVAQFVAGEgsnSDSEDVFLCV------LPMFHIyglsSFALGllrLGATVVVMPR-FD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 260 PEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGgscyvANLLK--LQEF---LITGQISYGYALTE 334
Cdd:cd05904 238 LEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGA-----APLGKelIEAFrakFPNVDLGQGYGMTE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 CGGVAANM-----GVAKPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTG 408
Cdd:cd05904 313 STGVVAMCfapekDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 409 DMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEY 488
Cdd:cd05904 393 DLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDF 472
|
490 500 510
....*....|....*....|....*....|....
gi 24648260 489 VAKRlVVDHKQLHcGVFFLPELPKTGSGKVLRQQ 522
Cdd:cd05904 473 VAKQ-VAPYKKVR-KVAFVDAIPKSPSGKILRKE 504
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
39-520 |
2.74e-70 |
|
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: 231.73 E-value: 2.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 39 RNHPNSICQIsdTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPwqdedt 118
Cdd:cd17631 6 RRHPDRTALV--FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 119 ikhlfsitrpklifcdgkcfqrlsiiarilkshvytlkdhRLGMPRVEDLLEPTTAelyyvpeTLLLggDHTVAILCTSG 198
Cdd:cd17631 78 ----------------------------------------RLTPPEVAYILADSGA-------KVLF--DDLALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 199 TTGLPKAVCIS-------NSACLFDFGfVTGQDVLLS----FSTIdwSAGMFnMLFSCCHGSTRIITDRPyTPEYMIQLV 267
Cdd:cd17631 109 TTGRPKGAMLThrnllwnAVNALAALD-LGPDDVLLVvaplFHIG--GLGVF-TLPTLLRGGTVVILRKF-DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 268 EKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFliTGQISYGYALTECGGVAANMG---- 343
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSpedh 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 344 VAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKR-MQDyqGWFHTGDMGYFDNENYLHIV 422
Cdd:cd17631 262 RRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAaFRD--GWFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 423 ERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdpAAAAVVKIPGSRLTEMDIVEYVAKRLVVDH- 497
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVpdekWGEA----VVAVVVPRPGAELDEDELIAHCRERLARYKi 415
|
490 500
....*....|....*....|....
gi 24648260 498 -KQlhcgVFFLPELPKTGSGKVLR 520
Cdd:cd17631 416 pKS----VEFVDALPRNATGKILK 435
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
14-525 |
1.20e-69 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 232.80 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 14 IWSGPRPasFFD-ADCSIGKILFAFMRNHPnsicQISDTegTALTN---GEAITFA------IRIAQQLKAMGLKQDDVV 83
Cdd:cd17642 1 IIVGPGP--FYPlEDGTAGEQLHKAMKRYA----SVPGT--IAFTDahtGVNYSYAeylemsVRLAEALKKYGLKQNDRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 84 GIVGTNT-TYLMPVVLGCLLNGTpfhaVSPWQD---EDTIKHLFSITRPKLIFCDGKCFQRLSIIARILK--------SH 151
Cdd:cd17642 73 AVCSENSlQFFLPVIAGLFIGVG----VAPTNDiynERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKiiktiiilDS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 152 VYTLKDHRLGMPRVEDLLEPTTAELYYVPETLllGGDHTVA-ILCTSGTTGLPKAVCIS--NSACLFD------FGFVTG 222
Cdd:cd17642 149 KEDYKGYQCLYTFITQNLPPGFNEYDFKPPSF--DRDEQVAlIMNSSGSTGLPKGVQLThkNIVARFShardpiFGNQII 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 223 QDVLLsFSTIDW--SAGMFNMLFSCCHGStRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIR 300
Cdd:cd17642 227 PDTAI-LTVIPFhhGFGMFTTLGYLICGF-RVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 301 FVSVGGG--SCYVANLLKlQEFLITGqISYGYALTECGG--VAANMGVAKPSSVGRIVPGVRVKILD-EAGRSLGHGETG 375
Cdd:cd17642 305 EIASGGAplSKEVGEAVA-KRFKLPG-IRQGYGLTETTSaiLITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 376 EILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEAC 455
Cdd:cd17642 383 ELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAG 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 456 VFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRlVVDHKQLHCGVFFLPELPKTGSGKVLRQQARD 525
Cdd:cd17642 463 VAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQ-VSTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
52-524 |
1.21e-68 |
|
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: 228.22 E-value: 1.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTN-GEAITF------AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFS 124
Cdd:cd05936 14 DKTALIFmGRKLTYreldalAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 125 ITRPKLIFCDgkcfqrlsiiarilkshvytlkdHRLgmprvEDLLEPTTAELYYVPETlllgGDHTVAILCTSGTTGLPK 204
Cdd:cd05936 94 DSGAKALIVA-----------------------VSF-----TDLLAAGAPLGERVALT----PEDVAVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 205 AVCISN-------SACLFDFGFV-TGQDVLLS----FSTIDWSAGMFNMLFScchGSTRIITDRPyTPEYMIQLVEKYKV 272
Cdd:cd05936 142 GAMLTHrnlvanaLQIKAWLEDLlEGDDVVLAalplFHVFGLTVALLLPLAL---GATIVLIPRF-RPIGVLKEIRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 273 TLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEflITG-QISYGYALTECGGVAA-N--MGVAKPS 348
Cdd:cd05936 218 TIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEE--LTGvPIVEGYGLTETSPVVAvNplDGPRKPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 349 SVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNES-KRMQDyqGWFHTGDMGYFDNENYLHIVERKED 427
Cdd:cd05936 296 SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETaEAFVD--GWLRTGDIGYMDEDGYFFIVDRKKD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 428 LLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL---VVDHKqlhcgV 504
Cdd:cd05936 374 MIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLagyKVPRQ-----V 448
|
490 500
....*....|....*....|
gi 24648260 505 FFLPELPKTGSGKVLRQQAR 524
Cdd:cd05936 449 EFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
24-531 |
8.59e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 219.67 E-value: 8.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 24 FDADCSIGKILFAFMRNHPNSicqisdtegTALT-NGEAITFAI------RIAQQLKAMGLKQDDVVGIVGTNTTYLMPV 96
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDK---------EAVYfDGRRTTYAEldervnRLANALRALGVKKGDRVAVFDWNSHEYLEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 97 VLGCLLNGTPFHAV----SPWQDEDTIKHlfsiTRPKLIFCDGKcFqrLSIIARILK-----SHVYTLKDHRLGMPRV-- 165
Cdd:PRK06187 73 YFAVPKIGAVLHPInirlKPEEIAYILND----AEDRVVLVDSE-F--VPLLAAILPqlptvRTVIVEGDGPAAPLAPev 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 166 ---EDLL--EPTTAELYYVPEtlllggdHTVAILC-TSGTTGLPKAVCIS------NSACLFDFGFVTGQDVLLS----F 229
Cdd:PRK06187 146 geyEELLaaASDTFDFPDIDE-------NDAAAMLyTSGTTGHPKGVVLShrnlflHSLAVCAWLKLSRDDVYLVivpmF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 230 STIDWSAGMFNMLfsccHGSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSC 309
Cdd:PRK06187 219 HVHAWGLPYLALM----AGAKQVIPRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 310 YVAnLLK--LQEFLItgQISYGYALTECGGVAA--------NMGVAKPSSVGRIVPGVRVKILDEAGRSLGH--GETGEI 377
Cdd:PRK06187 294 PPA-LLRefKEKFGI--DLVQGYGMTETSPVVSvlppedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 378 LVHNGKVWNGYYANPNESKR-MQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACV 456
Cdd:PRK06187 371 IVRGPWLMQGYWNRPEATAEtIDG--GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 457 FGL----WNEVdgdPAAAAVVKiPGSRLTEMDIVEYVAKRL----VVDHkqlhcgVFFLPELPKTGSGKVLRQQARDQAL 528
Cdd:PRK06187 449 IGVpdekWGER---PVAVVVLK-PGATLDAKELRAFLRGRLakfkLPKR------IAFVDELPRTSVGKILKRVLREQYA 518
|
...
gi 24648260 529 GKK 531
Cdd:PRK06187 519 EGK 521
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
34-429 |
7.36e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.10 E-value: 7.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 34 LFAFMRNHPNSICQISDtEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPW 113
Cdd:pfam00501 1 LERQAARTPDKTALEVG-EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 114 QDEDTIKHLFSITRPKLIFCDG-KCFQRLSIIARILKSHVYTLKDHRLGMPRVEDLLEPTTAELYYVPETLLLGGDHTVA 192
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDaLKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVCISNSACLF----------DFGFVTGQDVLLSFSTIDWSAGMFNMLFSC-CHGSTRIITDR--PYT 259
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLVAnvlsikrvrpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPlLAGATVVLPPGfpALD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 260 PEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLItGQISYGYALTECGGVA 339
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 340 ANMG-----VAKPSSVGRIVPGVRVKILDEA-GRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYF 413
Cdd:pfam00501 319 TTPLpldedLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRR 398
|
410
....*....|....*.
gi 24648260 414 DNENYLHIVERKEDLL 429
Cdd:pfam00501 399 DEDGYLEIVGRKKDQI 414
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
46-524 |
1.12e-62 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 214.46 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 46 CQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSI 125
Cdd:PLN02246 41 CLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 126 TRPKLIFCDGKCFQRLSIIARILKSHVYTLKDHRLGMPRVEDLLEPTTAELyyvPEtLLLGGDHTVAILCTSGTTGLPKA 205
Cdd:PLN02246 121 SGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENEL---PE-VEISPDDVVALPYSSGTTGLPKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 206 V------CISNSACLFDfG-----FVTGQDVLL---------SFSTIdwsagmfnMLFSCCHGSTRIITDRPYTPEyMIQ 265
Cdd:PLN02246 197 VmlthkgLVTSVAQQVD-GenpnlYFHSDDVILcvlpmfhiySLNSV--------LLCGLRVGAAILIMPKFEIGA-LLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 266 LVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGgscyvANLLK-LQEFL-------ITGQisyGYALTECGG 337
Cdd:PLN02246 267 LIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGA-----APLGKeLEDAFraklpnaVLGQ---GYGMTEAGP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 338 VAAnMGVA--------KPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTG 408
Cdd:PLN02246 339 VLA-MCLAfakepfpvKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 409 DMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEY 488
Cdd:PLN02246 418 DIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQF 497
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648260 489 VAKRlVVDHKQLHcGVFFLPELPKTGSGKVLRQQAR 524
Cdd:PLN02246 498 VAKQ-VVFYKRIH-KVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
39-526 |
2.16e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 212.84 E-value: 2.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 39 RNHPNSICQIsdTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDT 118
Cdd:PRK07656 16 RRFGDKEAYV--FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 119 IKHLFSITRPKLIFC-------DGKCFQRLSIIARILKSHVYTLKDHRLGMPRVEDLLEPTtAELYYVPEtllLGGDHTV 191
Cdd:PRK07656 94 AAYILARGDAKALFVlglflgvDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAG-DPAERAPE---VDPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 192 AILCTSGTTGLPKAV------CISNSACLFDFGFVTGQD----VLLSFSTIDWSAGMfnmLFSCCHGSTrIITDRPYTPE 261
Cdd:PRK07656 170 DILFTSGTTGRPKGAmlthrqLLSNAADWAEYLGLTEGDrylaANPFFHVFGYKAGV---NAPLMRGAT-ILPLPVFDPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 262 YMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVAAn 341
Cdd:PRK07656 246 EVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTT- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 342 M----GVAK--PSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDN 415
Cdd:PRK07656 325 FnrldDDRKtvAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 416 ENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL-- 493
Cdd:PRK07656 405 EGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLak 484
|
490 500 510
....*....|....*....|....*....|....*
gi 24648260 494 --VVDHkqlhcgVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:PRK07656 485 ykVPRS------IEFLDELPKNATGKVLKRALREK 513
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
67-534 |
1.60e-57 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 201.11 E-value: 1.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNG---TP-FHAVSPwqdeDTIKHLFSITRPKLIFCD------GK 136
Cdd:COG0365 51 RFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGavhSPvFPGFGA----EALADRIEDAEAKVLITAdgglrgGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 137 CFQRLSIIARILKS-----HVYTLK--DHRLGMPRV---EDLLEPTTAELYYVPetllLGGDHTVAILCTSGTTGLPKAV 206
Cdd:COG0365 127 VIDLKEKVDEALEElpsleHVIVVGrtGADVPMEGDldwDELLAAASAEFEPEP----TDADDPLFILYTSGTTGKPKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 207 CISNS----ACLFDFGFVTG---QDVLLSFSTIDWSAGMFNMLFSC-CHGSTRIITD-RPYTP--EYMIQLVEKYKVTLL 275
Cdd:COG0365 203 VHTHGgylvHAATTAKYVLDlkpGDVFWCTADIGWATGHSYIVYGPlLNGATVVLYEgRPDFPdpGRLWELIEKYGVTVF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 276 TVVPQQVASLLKTPT--LNKQRLASIR-FVSVG---------------GgsCYVANllklqeflITGQisygyalTECGG 337
Cdd:COG0365 283 FTAPTAIRALMKAGDepLKKYDLSSLRlLGSAGeplnpevwewwyeavG--VPIVD--------GWGQ-------TETGG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 338 -VAANMGV--AKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGkvW----NGYYANPNESKR--MQDYQGWFHTG 408
Cdd:COG0365 346 iFISNLPGlpVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGP--WpgmfRGYWNDPERYREtyFGRFPGWYRTG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 409 DMGYFDNENYLHIVERKEDLLRFHGaqY--SPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTE---M 483
Cdd:COG0365 424 DGARRDEDGYFWILGRSDDVINVSG--HriGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDelaK 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24648260 484 DIVEYVAKRL----VVDHkqlhcgVFFLPELPKTGSGKVLRQQARDQALGKKWAD 534
Cdd:COG0365 502 ELQAHVREELgpyaYPRE------IEFVDELPKTRSGKIMRRLLRKIAEGRPLGD 550
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
52-526 |
3.61e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 196.69 E-value: 3.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLI 131
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 132 FCDGKCFQRLSIIARILK------SHVYTLKDHRLGMPRVEDLLEPTTAElyyVPETLLLGGDhTVAILCTSGTTGLPKA 205
Cdd:PRK08316 113 LVDPALAPTAEAALALLPvdtlilSLVLGGREAPGGWLDFADWAEAGSVA---EPDVELADDD-LAQILYTSGTESLPKG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 206 VCISNSA-------CLFDFGFvTGQDVLLSFSTIDWSAGMFNMLFSCCH-GSTRIITDRPyTPEYMIQLVEKYKVTLLTV 277
Cdd:PRK08316 189 AMLTHRAliaeyvsCIVAGDM-SADDIPLHALPLYHCAQLDVFLGPYLYvGATNVILDAP-DPELILRTIEAERITSFFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 278 VPQQVASLLKTPTLNKQRLASIRfvsvgggSCY-------VANLLKLQEFLITGQISYGYALTECGGVAANMG----VAK 346
Cdd:PRK08316 267 PPTVWISLLRHPDFDTRDLSSLR-------KGYygasimpVEVLKELRERLPGLRFYNCYGQTEIAPLATVLGpeehLRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 347 PSSVGRIVPGVRVKILDEAGRSLGHGETGEIlVHNG-KVWNGYYANPNESKR-MQDyqGWFHTGDMGYFDNENYLHIVER 424
Cdd:PRK08316 340 PGSAGRPVLNVETRVVDDDGNDVAPGEVGEI-VHRSpQLMLGYWDDPEKTAEaFRG--GWFHSGDLGVMDEEGYITVVDR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 425 KEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVvdHKQLHCGV 504
Cdd:PRK08316 417 KKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLA--GFKVPKRV 494
|
490 500
....*....|....*....|..
gi 24648260 505 FFLPELPKTGSGKVLRQQARDQ 526
Cdd:PRK08316 495 IFVDELPRNPSGKILKRELRER 516
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-524 |
8.52e-55 |
|
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: 190.20 E-value: 8.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 190 TVAILCTSGTTGLPKAVCISNSACLF------DFGFVTGQDVLLS---FSTIDwsAGMFNMLFSCCHGSTRIITDRpYTP 260
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHANLTFagyysaRRFGLGEDDVYLTvlpLFHIN--AQAVSVLAALSVGATLVLLPR-FSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 261 EYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSvgggsCYVANLLKLQEF-------LITGqisygYALT 333
Cdd:cd05934 160 SRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAY-----GAPNPPELHEEFeerfgvrLLEG-----YGMT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 334 E--CGGVAANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVW---NGYYANPNES-KRMQDyqGWFHT 407
Cdd:cd05934 230 EtiVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWgffKGYYNMPEATaEAMRN--GWFHT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 408 GDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVE 487
Cdd:cd05934 308 GDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFA 387
|
330 340 350
....*....|....*....|....*....|....*..
gi 24648260 488 YVAKRLvvDHKQLHCGVFFLPELPKTGSGKVLRQQAR 524
Cdd:cd05934 388 FCEGQL--AYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
48-521 |
3.39e-53 |
|
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: 187.90 E-value: 3.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 48 ISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITR 127
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 128 PKLIFCDGKCFQ-----RLSIIARILKSHVYTLKDHRlgMPRVEDLLEPTTAELYYVPETLLLGGDhTVAILCTSGTTGL 202
Cdd:cd05926 87 SKLVLTPKGELGpasraASKLGLAILELALDVGVLIR--APSAESLSNLLADKKNAKSEGVPLPDD-LALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 203 PKAV------------CISNSACLfdfgfvTGQD----VLLSFSTIDWSAGMFNMLFScchGSTRIITDRpYTPEYMIQL 266
Cdd:cd05926 164 PKGVplthrnlaasatNITNTYKL------TPDDrtlvVMPLFHVHGLVASLLSTLAA---GGSVVLPPR-FSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 267 VEKYKVTLLTVVPQQVASLLKTP-TLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISyGYALTE-CGGVAAN--- 341
Cdd:cd05926 234 VRDYNATWYTAVPTIHQILLNRPePNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLE-AYGMTEaAHQMTSNplp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 342 MGVAKPSSVGRIVpGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHI 421
Cdd:cd05926 313 PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 422 VERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLV---VDHK 498
Cdd:cd05926 392 TGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAafkVPKK 471
|
490 500
....*....|....*....|...
gi 24648260 499 qlhcgVFFLPELPKTGSGKVLRQ 521
Cdd:cd05926 472 -----VYFVDELPKTATGKIQRR 489
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
39-525 |
2.00e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 187.06 E-value: 2.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 39 RNHPNSICQIsDTEGTaLTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGC--------LLNgTPFhav 110
Cdd:PRK07788 60 RRAPDRAALI-DERGT-LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAgkvgariiLLN-TGF--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 111 SPWQDEDTIKHLfsitRPKLIFCDGKCFQRLSIIA------RILKSHVYTLKDHRLGMPRVEDLLEPTTAELYYVPETll 184
Cdd:PRK07788 134 SGPQLAEVAARE----GVKALVYDDEFTDLLSALPpdlgrlRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPPK-- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 185 lggdHTVAILCTSGTTGLPKAVCISNSACLFDFGFVTGQDVLLSFSTIDWSAGMFNML-FSCC-----HGSTrIITDRPY 258
Cdd:PRK07788 208 ----PGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATgWAHLtlamaLGST-VVLRRRF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVPQQVASLLKTP--TLNKQRLASIRFVSVGGgSCYVANLLK--LQEFlitGQISYG-YALT 333
Cdd:PRK07788 283 DPEATLEDIAKHKATALVVVPVMLSRILDLGpeVLAKYDTSSLKIIFVSG-SALSPELATraLEAF---GPVLYNlYGST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 334 ECGgVAAnmgVAK-------PSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGyYANPNeSKRMQDyqGWFH 406
Cdd:PRK07788 359 EVA-FAT---IATpedlaeaPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEG-YTDGR-DKQIID--GLLS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 407 TGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIV 486
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIK 510
|
490 500 510
....*....|....*....|....*....|....*....
gi 24648260 487 EYVAKRLvVDHKqLHCGVFFLPELPKTGSGKVLRQQARD 525
Cdd:PRK07788 511 DYVRDNL-ARYK-VPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
53-530 |
4.36e-50 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 180.56 E-value: 4.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 53 GTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIF 132
Cdd:PLN02330 53 GKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 CDGKCFQRLsiiaRILKSHVYTLKDHRL-GMPRVEDLLEPTTAELYYVPETLLLGGDhTVAILCTSGTTGLPKAVCISNS 211
Cdd:PLN02330 133 TNDTNYGKV----KGLGLPVIVLGEEKIeGAVNWKELLEAADRAGDTSDNEEILQTD-LCALPFSSGTTGISKGVMLTHR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 212 -------ACLFDFGF-VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVA 283
Cdd:PLN02330 208 nlvanlcSSLFSVGPeMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIIL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 284 SLLKTPTLNKQRLASIRFVSVGGGSCYVA-NLLKLQEFLITG-QISYGYALTE--C-----GGVAANMGVAKPSSVGRIV 354
Cdd:PLN02330 288 NLVKNPIVEEFDLSKLKLQAIMTAAAPLApELLTAFEAKFPGvQVQEAYGLTEhsCitlthGDPEKGHGIAKKNSVGFIL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 355 PGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHG 433
Cdd:PLN02330 368 PNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 434 AQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRlVVDHKQLHCgVFFLPELPKT 513
Cdd:PLN02330 448 FQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAAN-VAHYKKVRV-VQFVDSIPKS 525
|
490
....*....|....*..
gi 24648260 514 GSGKVLRQQARDQALGK 530
Cdd:PLN02330 526 LSGKIMRRLLKEKMLSI 542
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
162-522 |
6.58e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 178.90 E-value: 6.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 162 MPRVEDLLEPTTAElyyvPETLLLGGDHTVAILC-TSGTTGLPKAVCISNSACLFD-----FGF-VTGQDVLLSFSTIDW 234
Cdd:PRK06839 126 VISITSLKEIEDRK----IDNFVEKNESASFIICyTSGTTGKPKGAVLTQENMFWNalnntFAIdLTMHDRSIVLLPLFH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 235 SAGMFNMLFSCCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANL 314
Cdd:PRK06839 202 IGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELM 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 315 LKLQEF-LITGQisyGYALTECGG----VAANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYY 389
Cdd:PRK06839 282 REFIDRgFLFGQ---GFGMTETSPtvfmLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYW 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 390 ANPNESKR-MQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPA 468
Cdd:PRK06839 359 NRPDATEEtIQD--GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIP 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24648260 469 AAAVVKIPGSRLTEMDIVEYVAKRLVvdHKQLHCGVFFLPELPKTGSGKVLRQQ 522
Cdd:PRK06839 437 IAFIVKKSSSVLIEKDVIEHCRLFLA--KYKIPKEIVFLKELPKNATGKIQKAQ 488
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
48-531 |
2.66e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 177.40 E-value: 2.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 48 ISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITR 127
Cdd:PRK08276 4 IMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 128 PKLIFCDGKCFQRLSIIARILKSHVytlkDHRLGMPRVEDLLEPTTAELYYVPETLL----LGGDhtvaILCTSGTTGLP 203
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGV----PLLLVVAGPVPGFRSYEEALAAQPDTPIadetAGAD----MLYSSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 204 KAV-----------CISNSACLFDFGFVTGQD-VLLSFSTIDWSA-GMFNMlFSCCHGSTRIITDRpYTPEYMIQLVEKY 270
Cdd:PRK08276 156 KGIkrplpgldpdeAPGMMLALLGFGMYGGPDsVYLSPAPLYHTApLRFGM-SALALGGTVVVMEK-FDAEEALALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 271 KVTLLTVVPQQVASLLKTPTLNKQR--LASIRFVSVGGGSCYVAnlLKLQEFLITGQISYG-YALTECGGVA---ANMGV 344
Cdd:PRK08276 234 RVTHSQLVPTMFVRMLKLPEEVRARydVSSLRVAIHAAAPCPVE--VKRAMIDWWGPIIHEyYASSEGGGVTvitSEDWL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 345 AKPSSVGRIVPGVrVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVER 424
Cdd:PRK08276 312 AHPGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 425 KEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTE---MDIVEYVAKRL-------V 494
Cdd:PRK08276 391 KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDalaAELIAWLRGRLahykcprS 470
|
490 500 510
....*....|....*....|....*....|....*..
gi 24648260 495 VDhkqlhcgvfFLPELPKTGSGKVLRQQARDQALGKK 531
Cdd:PRK08276 471 ID---------FEDELPRTPTGKLYKRRLRDRYWEGR 498
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
65-525 |
5.52e-48 |
|
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: 174.36 E-value: 5.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 65 AIRIAQQLKAMGLKQDDVVGIVGTNT-----TYLMPVVLGCLLNgTPFHAVSPWQDEDTIKHlfsiTRPKLIFCDGKCFQ 139
Cdd:cd12119 35 ARRLANALRRLGVKPGDRVATLAWNThrhleLYYAVPGMGAVLH-TINPRLFPEQIAYIINH----AEDRVVFVDRDFLP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 140 RLSIIARILKS--HVYTLKD----HRLGMPRV---EDLL--EPTTAELYYVPEtlllggdHTVAILC-TSGTTGLPKAVC 207
Cdd:cd12119 110 LLEAIAPRLPTveHVVVMTDdaamPEPAGVGVlayEELLaaESPEYDWPDFDE-------NTAAAICyTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 208 ISN--------SACLFDFGFVTGQDVLLSFSTidwsagMF-----NMLFSCCH-GSTRIITDRPYTPEYMIQLVEKYKVT 273
Cdd:cd12119 183 YSHrslvlhamAALLTDGLGLSESDVVLPVVP------MFhvnawGLPYAAAMvGAKLVLPGPYLDPASLAELIEREGVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 274 LLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLItgQISYGYALTE---CGGVA----------A 340
Cdd:cd12119 257 FAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGV--RVIHAWGMTEtspLGTVArppsehsnlsE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 341 NMGVAKPSSVGRIVPGVRVKILDEAGRSLGH-GET-GEILVHNGKVWNGYYANPNESKRMQDyQGWFHTGDMGYFDNENY 418
Cdd:cd12119 335 DEQLALRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTE-DGWLRTGDVATIDEDGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 419 LHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdPAAAAVVKiPGSRLTEMDIVEYVAKRlv 494
Cdd:cd12119 414 LTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVphpkWGER---PLAVVVLK-EGATVTAEELLEFLADK-- 487
|
490 500 510
....*....|....*....|....*....|.
gi 24648260 495 VDHKQLHCGVFFLPELPKTGSGKVLRQQARD 525
Cdd:cd12119 488 VAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
2-525 |
3.42e-46 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 170.02 E-value: 3.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 2 NRSTTQFDKYTKIWSGPRPASFFDADCSIGKILFAFMR-NHPNSICQISDTEGTALTNGEAITFAIRIAQQL-KAMGLKQ 79
Cdd:PLN02574 12 NNPPFWYSPETGIYSSKHPPVPLPSDPNLDAVSFIFSHhNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLyHVMGVRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 80 DDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSI--IARILKSHVYTLKD 157
Cdd:PLN02574 92 GDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPlgVPVIGVPENYDFDS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 158 HRLGMPRVEDLLepttaelYYVPETL---LLGGDHTVAILCTSGTTGLPKAVCISNSaclfdfGFVTGQDVLLSFSTIDW 234
Cdd:PLN02574 172 KRIEFPKFYELI-------KEDFDFVpkpVIKQDDVAAIMYSSGTTGASKGVVLTHR------NLIAMVELFVRFEASQY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 235 SA-GMFNMLFSC---CH--------------GSTrIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTptlnKQRL 296
Cdd:PLN02574 239 EYpGSDNVYLAAlpmFHiyglslfvvgllslGST-IVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKK----AKGV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 297 ASIRFVSVGGGSCYVANLLK--LQEFLIT---GQISYGYALTECGGVAA----NMGVAKPSSVGRIVPGVRVKILD-EAG 366
Cdd:PLN02574 314 CGEVLKSLKQVSCGAAPLSGkfIQDFVQTlphVDFIQGYGMTESTAVGTrgfnTEKLSKYSSVGLLAPNMQAKVVDwSTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 367 RSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIA 446
Cdd:PLN02574 394 CLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24648260 447 ELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRlVVDHKQLHcGVFFLPELPKTGSGKVLRQQARD 525
Cdd:PLN02574 474 SHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQ-VAPYKKVR-KVVFVQSIPKSPAGKILRRELKR 550
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
185-528 |
1.02e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 168.80 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 185 LGGDHTVAILCTSGTTGLPKAVCISNSACLFDFGFV------TGQDVLLSFSTIDWSAGMFNMLFSC-CHGSTRIITDRP 257
Cdd:PRK12583 198 LDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVaeslglTEHDRLCVPVPLYHCFGMVLANLGCmTVGACLVYPNEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 258 YTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGG 337
Cdd:PRK12583 278 FDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSP 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 338 VAANMGVAKP-----SSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGY 412
Cdd:PRK12583 358 VSLQTTAADDlerrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLAT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 413 FDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKR 492
Cdd:PRK12583 438 MDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKAR 517
|
330 340 350
....*....|....*....|....*....|....*.
gi 24648260 493 LVvdHKQLHCGVFFLPELPKTGSGKVLRQQARDQAL 528
Cdd:PRK12583 518 IA--HFKVPRYFRFVDEFPMTVTGKVQKFRMREISI 551
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
55-524 |
6.79e-45 |
|
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: 164.09 E-value: 6.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 55 ALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCD 134
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 135 GKcFQRLSIIArilkshvytlkdhrlgMPrvedllepttaelyyvpetlllggDHTVAILCTSGTTGLPKAVCISNSACL 214
Cdd:cd05903 81 ER-FRQFDPAA----------------MP------------------------DAVALLLFTSGTTGEPKGVMHSHNTLS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 215 FD-------FGFvTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLK 287
Cdd:cd05903 120 ASirqyaerLGL-GPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 288 TPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITgQISYGYALTECGGVAANMGVAKPS----SVGRIVPGVRVKILD 363
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTECPGAVTSITPAPEDrrlyTDGRPLPGVEIKVVD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 364 EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRmQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQ 443
Cdd:cd05903 278 DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-AAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 444 VIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDHK---QLHcgvfFLPELPKTGSGKVLR 520
Cdd:cd05903 357 LLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYwpeRLV----HVDDLPRTPSGKVQK 432
|
....
gi 24648260 521 QQAR 524
Cdd:cd05903 433 FRLR 436
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-518 |
2.17e-43 |
|
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: 157.44 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVAILCTSGTTGLPKAVC------ISNSACLFDFGFVTGQDVLLS----FSTIDWSAGMFNMLfscCHGSTRIITDRP 257
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATlthhniVNNGYFIGERLGLTEQDRLCIpvplFHCFGSVLGVLACL---THGATMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 258 YTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGG 337
Cdd:cd05917 79 FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 338 VAANMGVAKPS-----SVGRIVPGVRVKILDEAGRS-LGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMG 411
Cdd:cd05917 159 VSTQTRTDDSIekrvnTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 412 YFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAK 491
Cdd:cd05917 239 VMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKG 318
|
330 340
....*....|....*....|....*..
gi 24648260 492 RLVvdHKQLHCGVFFLPELPKTGSGKV 518
Cdd:cd05917 319 KIA--HYKVPRYVFFVDEFPLTVSGKI 343
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
196-522 |
2.34e-43 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 159.57 E-value: 2.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSACLFD-----FGF-VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEYMIQLVEK 269
Cdd:cd05935 92 TSGTTGLPKGCMHTHFSAAANalqsaVWTgLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 270 YKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEflITGqISY--GYALTE-CGGVAAN-MGVA 345
Cdd:cd05935 172 YKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLK--LTG-LRFveGYGLTEtMSQTHTNpPLRP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 346 KPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQG---WFHTGDMGYFDNENYLHI 421
Cdd:cd05935 249 KLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFF 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 422 VERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSR--LTEMDIVEYvAKRLVVDHKQ 499
Cdd:cd05935 329 VDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRgkVTEEDIIEW-AREQMAAYKY 407
|
330 340
....*....|....*....|...
gi 24648260 500 LHcGVFFLPELPKTGSGKVLRQQ 522
Cdd:cd05935 408 PR-EVEFVDELPRSASGKILWRL 429
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
34-525 |
3.60e-43 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 160.81 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 34 LFAFMRNH---PNSICqISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGI-VGTNTTYLMpVVLGCLLNGTPFHA 109
Cdd:PRK07514 5 LFDALRAAfadRDAPF-IETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVqVEKSPEALA-LYLATLRAGAVFLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 110 VSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSIIARILK-SHVYTLKDHRLGmprveDLLEPTTAElyyvP---ETLLL 185
Cdd:PRK07514 83 LNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGaPHVETLDADGTG-----SLLEAAAAA----PddfETVPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 GGDHTVAILCTSGTTGLPKA------VCISNSACLFDFGFVTGQDVLLSFSTIDWSAGmfnmLFSCCH-----GSTRIIT 254
Cdd:PRK07514 154 GADDLAAILYTSGTTGRSKGamlshgNLLSNALTLVDYWRFTPDDVLIHALPIFHTHG----LFVATNvallaGASMIFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 255 DRpYTPEYMIQLVEKykVTLLTVVPQQVASLLKTPTLNKQRLASIR-FVSvggGScyvANLL--KLQEFLI-TGQ-ISYG 329
Cdd:PRK07514 230 PK-FDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRlFIS---GS---APLLaeTHREFQErTGHaILER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 330 YALTEcggvaANM-------GVAKPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDY 401
Cdd:PRK07514 301 YGMTE-----TNMntsnpydGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 402 QGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLT 481
Cdd:PRK07514 376 DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24648260 482 EMDIVEYVAKRLvVDHKQLHcGVFFLPELPKTGSGKV----LRQQARD 525
Cdd:PRK07514 456 EAAILAALKGRL-ARFKQPK-RVFFVDELPRNTMGKVqknlLREQYAD 501
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-520 |
1.47e-42 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 154.97 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAV------CISNSACLFDFGFVTGQDVLLS----FSTIDWSAGMFNMLFScchGSTrIITDRPYTPEY 262
Cdd:cd17638 5 IMFTSGTTGRSKGVmcahrqTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAGIVACLLT---GAT-VVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVA--- 339
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATmcr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 340 -ANMGVAKPSSVGRIVPGVRVKILDEagrslghgetGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENY 418
Cdd:cd17638 161 pGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 419 LHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVvdHK 498
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLA--NY 308
|
330 340
....*....|....*....|..
gi 24648260 499 QLHCGVFFLPELPKTGSGKVLR 520
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
65-531 |
2.16e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 158.71 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 65 AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNG---TPFHavspWQdedtikhlFSITRPKLIFCDGKcfqrl 141
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGayaVPVN----WH--------FKPEEIAYILEDSG----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 142 siiARILKSHVYTLKDHRLGMPR-VEDLLEPTTAEL---YYVPETLLLGGDHTVA---------------------ILCT 196
Cdd:PRK12406 84 ---ARVLIAHADLLHGLASALPAgVTVLSVPTPPEIaaaYRISPALLTPPAGAIDwegwlaqqepydgppvpqpqsMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 197 SGTTGLPKAVCISN----SACLFD------FGFVTGQDVLLS---FSTIDWSAGMFNMLFscchGSTRIITDRpYTPEYM 263
Cdd:PRK12406 161 SGTTGHPKGVRRAAptpeQAAAAEqmraliYGLKPGIRALLTgplYHSAPNAYGLRAGRL----GGVLVLQPR-FDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 264 IQLVEKYKVTLLTVVPQQVASLLKTPTLNKQR--LASIRFVSVGGGSCYVAnlLKLQEFLITGQISYG-YALTECGGVA- 339
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKLPEEVRAKydVSSLRHVIHAAAPCPAD--VKRAMIEWWGPVIYEyYGSTESGAVTf 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 340 --ANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNEN 417
Cdd:PRK12406 314 atSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDADG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 418 YLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL---- 493
Cdd:PRK12406 394 YLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLagyk 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24648260 494 VVDHkqlhcgVFFLPELPKTGSGKVLRQQARD---QALGKK 531
Cdd:PRK12406 474 VPKH------IEIMAELPREDSGKIFKRRLRDpywANAGRK 508
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
110-524 |
2.47e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 157.22 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 110 VSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSIIARILKSHVYT-----LKDHRLGMPRVEdllepttaelyyvpetll 184
Cdd:cd05922 52 LNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDPGTVldadgIRAARASAPAHE------------------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 185 LGGDHTVAILCTSGTTGLPKAVCISNSACLFDFGFV------TGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPY 258
Cdd:cd05922 114 VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIaeylgiTADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVPQqVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGV 338
Cdd:cd05922 194 LDDAFWEDLREHGATGLAGVPS-TYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 339 AANMG----VAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFD 414
Cdd:cd05922 273 MTYLPperiLEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 415 NENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwNEVDGDPAAAAVVKIPGsrLTEMDIVEYVAKRLV 494
Cdd:cd05922 353 EDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL-PDPLGEKLALFVTAPDK--IDPKDVLRSLAERLP 429
|
410 420 430
....*....|....*....|....*....|
gi 24648260 495 VdHKqLHCGVFFLPELPKTGSGKVLRQQAR 524
Cdd:cd05922 430 P-YK-VPATVRVVDELPLTASGKVDYAALR 457
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
172-525 |
7.45e-42 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 155.20 E-value: 7.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 172 TTAELYYVPETLLLGGDHTVAILCTSGTTGLPKAVCIS-----NSA--CLFDFGFvTGQDVLLSFSTIDWSAGMFNMLFS 244
Cdd:cd05912 61 TPNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTfgnhwWSAigSALNLGL-TEDDNWLCALPLFHISGLSILMRS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 245 CCHGSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTptLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITG 324
Cdd:cd05912 140 VIYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQRLLEI--LGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 325 QISYGYALTECGGVAAN--MGVAKPSSVGRIVPGVRVKILDEAGRSLGHGEtgeILVHNGKVWNGYYANPNESKRMQDyQ 402
Cdd:cd05912 217 YQSYGMTETCSQIVTLSpeDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGPNVTKGYLNRPDATEESFE-N 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 403 GWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdPAAAAVVKIPgs 478
Cdd:cd05912 293 GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIpddkWGQV---PVAFVVSERP-- 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24648260 479 rLTEMDIVEYVAKRLVvdHKQLHCGVFFLPELPKTGSGKVLRQQARD 525
Cdd:cd05912 368 -ISEEELIAYCSEKLA--KYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
29-473 |
1.27e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 157.95 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 29 SIGKILFAFMRNHPNSICQISDTEG--TALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNG-- 104
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGav 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 105 -TPFHAVSPwqdEDTIKHLFSITRPKLIFCDGKcFQR---LSIIARI--LKsHVYTLKD-HRLGMPRV---EDLLEP--T 172
Cdd:COG1022 92 tVPIYPTSS---AEEVAYILNDSGAKVLFVEDQ-EQLdklLEVRDELpsLR-HIVVLDPrGLRDDPRLlslDELLALgrE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 173 TAELYYVPETLLLGGDHTVAILC-TSGTTGLPKAVC------ISNSACLFDFGFVTGQDVLLSFSTIDWSAGMFNMLFSC 245
Cdd:COG1022 167 VADPAELEARRAAVKPDDLATIIyTSGTTGRPKGVMlthrnlLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 246 CHGSTRIITDRPytpEYMIQLVEKYKVTLLTVVP-----------QQVASLlktpTLNKQRLASiRFVSVG--------- 305
Cdd:COG1022 247 AAGATVAFAESP---DTLAEDLREVKPTFMLAVPrvwekvyagiqAKAEEA----GGLKRKLFR-WALAVGrryararla 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 306 GGSC--------YVANLL---KLQE-------FLITG-----------------QISYGYALTE-CGGVAAN-MGVAKPS 348
Cdd:COG1022 319 GKSPslllrlkhALADKLvfsKLREalggrlrFAVSGgaalgpelarffralgiPVLEGYGLTEtSPVITVNrPGDNRIG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 349 SVGRIVPGVRVKIldeagrslghGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDL 428
Cdd:COG1022 399 TVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDL 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24648260 429 LRF-HGAQYSPQEIEQVIAELPDVIEACVFGlwnevDGDPAAAAVV 473
Cdd:COG1022 469 IVTsGGKNVAPQPIENALKASPLIEQAVVVG-----DGRPFLAALI 509
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
26-526 |
1.32e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 156.68 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 26 ADCSIGKILFAFMRNHPNSICqISDTEGTaLTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTN-TTYLMPVVLGCL--L 102
Cdd:PRK06188 10 SGATYGHLLVSALKRYPDRPA-LVLGDTR-LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNrPEVLMAIGAAQLagL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 103 NGTPFHAVSPWQDedtikHLFSITRPK---LIFCDGKCFQRlsiiARILKSHVYTLKdHRLGMPRVEDLLEPTTAELYYV 179
Cdd:PRK06188 88 RRTALHPLGSLDD-----HAYVLEDAGistLIVDPAPFVER----ALALLARVPSLK-HVLTLGPVPDGVDLLAAAAKFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 180 PETLLLGGDHT--VAILCTSGTTGLPKAVCISNSAclfdfgfVTGQDVLLsFSTIDWSAgmfNMLFSCC----H------ 247
Cdd:PRK06188 158 PAPLVAAALPPdiAGLAYTGGTTGKPKGVMGTHRS-------IATMAQIQ-LAEWEWPA---DPRFLMCtplsHaggaff 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 248 ------GSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGScyvANLLKLQEFL 321
Cdd:PRK06188 227 lptllrGGTVIVLAK-FDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASP---MSPVRLAEAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 322 -ITGQI-SYGYALTECGGVAANMG--------VAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYAN 391
Cdd:PRK06188 303 eRFGPIfAQYYGQTEAPMVITYLRkrdhdpddPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 392 PNESKR-MQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAA 470
Cdd:PRK06188 383 PEETAEaFRD--GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTA 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24648260 471 AVVKIPGSRLTEMDIVEYVAKRLVVDH--KQlhcgVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:PRK06188 461 VVVLRPGAAVDAAELQAHVKERKGSVHapKQ----VDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
39-520 |
1.37e-41 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 157.22 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 39 RNHPNSIcQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVgivgtntTYLMP-------VVLGCLLNGTPFHAVS 111
Cdd:PRK06087 34 RAMPDKI-AVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRV-------AFQLPgwceftiIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 112 PWQDEDTIKHLFSITRPKLIFCDGKcFQRLSIIARIL--KSHVYTLKdHRLGMprveDLLEPTTAELYY---------VP 180
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAPTL-FKQTRPVDLILplQNQLPQLQ-QIVGV----DKLAPATSSLSLsqiiadyepLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 181 ETLLLGGDHTVAILCTSGTTGLPKAVCISNSACLF-DFGFV-----TGQDVLLSFSTIDWSAGMFN-----MLFscchGS 249
Cdd:PRK06087 180 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAsERAYCarlnlTWQDVFMMPAPLGHATGFLHgvtapFLI----GA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 250 TRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGS--------CYVANLLKLQEFL 321
Cdd:PRK06087 256 RSVLLDI-FTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTipkkvareCQQRGIKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 322 ITGQISYGYA-LTECggVAANMGVAkpssvGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQD 400
Cdd:PRK06087 335 STESSPHAVVnLDDP--LSRFMHTD-----GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 401 YQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVV-KIPGSR 479
Cdd:PRK06087 408 EEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHS 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24648260 480 LTEMDIVEY-----VAKRLVVDHKQLhcgvffLPELPKTGSGKVLR 520
Cdd:PRK06087 488 LTLEEVVAFfsrkrVAKYKYPEHIVV------IDKLPRTASGKIQK 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
48-524 |
7.26e-41 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 154.45 E-value: 7.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 48 ISDTEGTaLTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITR 127
Cdd:cd05959 23 FIDDAGS-LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 128 PKLIFCDGKCFQRLSIIARILKSHVYTL-----KDHRLGMPRVEDLLePTTAELYYVPETlllGGDHTVAILCTSGTTGL 202
Cdd:cd05959 102 ARVVVVSGELAPVLAAALTKSEHTLVVLivsggAGPEAGALLLAELV-AAEAEQLKPAAT---HADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 203 PKAVC-----ISNSACLF--DFGFVTGQDVLLSFSTIDWSAGMFN-MLFSCCHGSTRII-TDRPyTPEYMIQLVEKYKVT 273
Cdd:cd05959 178 PKGVVhlhadIYWTAELYarNVLGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLmPERP-TPAAVFKRIRRYRPT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 274 LLTVVPQQVASLLKTPTLNKQRLASIRfVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGV-AANM-GVAKPSSVG 351
Cdd:cd05959 257 VFFGVPTLYAAMLAAPNLPSRDLSSLR-LCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIfLSNRpGRVRYGTTG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 352 RIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMqdYQG-WFHTGDMGYFDNENYLHIVERKEDLLR 430
Cdd:cd05959 336 KPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDT--FQGeWTRTGDKYVRDDDGFYTYAGRADDMLK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 431 FHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEM---DIVEYVAKRLvVDHKQLHcGVFFL 507
Cdd:cd05959 414 VSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAleeELKEFVKDRL-APYKYPR-WIVFV 491
|
490
....*....|....*..
gi 24648260 508 PELPKTGSGKVLRQQAR 524
Cdd:cd05959 492 DELPKTATGKIQRFKLR 508
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
196-526 |
1.02e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 154.43 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSaclfDFGFV------------TGQDVLLSFSTIDWSAGMfNMLFSCCHGSTRIIT-DRPYTPEY 262
Cdd:PRK07470 171 TSGTTGRPKAAVLTHG----QMAFVitnhladlmpgtTEQDASLVVAPLSHGAGI-HQLCQVARGAATVLLpSERFDPAE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVAN----LLKLQEFLItgqiSYgYALTECGGv 338
Cdd:PRK07470 246 VWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADqkraLAKLGKVLV----QY-FGLGEVTG- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 339 aaNMGVAKPS-------------SVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPN-ESKRMQDyqGW 404
Cdd:PRK07470 320 --NITVLPPAlhdaedgpdarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEaNAKAFRD--GW 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 405 FHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMD 484
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAE 475
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24648260 485 IVEYVAKRlvVDHKQLHCGVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:PRK07470 476 LLAWLDGK--VARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
65-522 |
1.08e-40 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 152.60 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 65 AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPF----HAVSPWQDEDTIKHLfsitRPKLIFCDgKCFQR 140
Cdd:TIGR01923 9 AAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIamlnTRLTENERTNQLEDL----DVQLLLTD-SLLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 141 LSIIARILkshvytlkdHRLGMPRvedlLEPTTAELYYvpetlllGGDHTVAILCTSGTTGLPKAVCIS-----NSA--C 213
Cdd:TIGR01923 84 KDFQADSL---------DRIEAAG----RYETSLSASF-------NMDQIATLMFTSGTTGKPKAVPHTfrnhyASAvgS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 214 LFDFGFVTGQDVLLSFSTIDWSAgmFNMLFSCC-HGSTRIITDRPYTPEYMIQlveKYKVTLLTVVPQQVASLLKTpTLN 292
Cdd:TIGR01923 144 KENLGFTEDDNWLLSLPLYHISG--LSILFRWLiEGATLRIVDKFNQLLEMIA---NERVTHISLVPTQLNRLLDE-GGH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 293 KQRLASIRFvsvgGGSCYVANLLKL-QEFLITGQISYGyaLTE-CGGVAA--NMGVAKPSSVGRIVPGVRVKILDEagrs 368
Cdd:TIGR01923 218 NENLRKILL----GGSAIPAPLIEEaQQYGLPIYLSYG--MTEtCSQVTTatPEMLHARPDVGRPLAGREIKIKVD---- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 369 lGHGETGEILVHNGKVWNGYYaNPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAEL 448
Cdd:TIGR01923 288 -NKEGHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQH 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24648260 449 PDVIEACVFGL----WNEVdgdPAAAAVVKIPGSRLTemdIVEYVAKRLvvDHKQLHCGVFFLPELPKTGSGKVLRQQ 522
Cdd:TIGR01923 366 PGIQEAVVVPKpdaeWGQV---PVAYIVSESDISQAK---LIAYLTEKL--AKYKVPIAFEKLDELPYNASGKILRNQ 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
67-525 |
1.96e-40 |
|
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: 151.34 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGT---P-FHAVSPwqdeDTIKHLFSITRPKLIFCDGkcfqrls 142
Cdd:cd05972 12 KAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAvyvPlTTLLGP----KDIEYRLEAAGAKAIVTDA------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 143 iiarilkshvytlkdhrlgmprvEDlleptTAELYYvpetlllggdhtvailcTSGTTGLPKAVCISNSACLfdfGF-VT 221
Cdd:cd05972 81 -----------------------ED-----PALIYF-----------------TSGTTGLPKGVLHTHSYPL---GHiPT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 222 GQDVL------LSFSTID-------WSAGMFNMLfsccHGSTRIITD-RPYTPEYMIQLVEKYKVTLLTVVPQqVASLLK 287
Cdd:cd05972 113 AAYWLglrpddIHWNIADpgwakgaWSSFFGPWL----LGATVFVYEgPRFDAERILELLERYGVTSFCGPPT-AYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 288 TPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFL-ITgqISYGYALTECGGVAAN---MGVaKPSSVGRIVPGVRVKILD 363
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATgLP--IRDGYGQTETGLTVGNfpdMPV-KPGSMGRPTPGYDVAIID 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 364 EAGRSLGHGETGEILVHNGKV--WNGYYANPnESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEI 441
Cdd:cd05972 265 DDGRELPPGEEGDIAIKLPPPglFLGYVGDP-EKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 442 EQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPG---SRLTEMDIVEYVAKRL-------VVDhkqlhcgvfFLPELP 511
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepSEELAEELQGHVKKVLapykyprEIE---------FVEELP 414
|
490
....*....|....
gi 24648260 512 KTGSGKVLRQQARD 525
Cdd:cd05972 415 KTISGKIRRVELRD 428
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
59-526 |
2.05e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 152.73 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 59 GEAITFAI---RI---AQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIF 132
Cdd:PRK06145 25 DQEISYAEfhqRIlqaAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 CDGKCFQRLSIIARILKSHVYTLKD-HRLGMPRVEdlleptTAELYYVPETLLlggdhtVAILCTSGTTGLPKAVCISNS 211
Cdd:PRK06145 105 VDEEFDAIVALETPKIVIDAAAQADsRRLAQGGLE------IPPQAAVAPTDL------VRLMYTSGTTDRPKGVMHSYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 212 ACL---FD----FGfVTGQDVLLSFSTIdWSAGMFNM--LFSCCHGSTrIITDRPYTPEYMIQLVEKYKVTLLTVVPQQV 282
Cdd:PRK06145 173 NLHwksIDhviaLG-LTASERLLVVGPL-YHVGAFDLpgIAVLWVGGT-LRIHREFDPEAVLAAIERHRLTCAWMAPVML 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 283 ASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTE-CGG---VAANMGVAKPSSVGRIVPGVR 358
Cdd:PRK06145 250 SRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTEtCSGdtlMEAGREIEKIGSTGRALAHVE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 359 VKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRmQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSP 438
Cdd:PRK06145 330 IRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAE-AFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIAS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 439 QEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLvvdhkqlhcGVFFLP-------ELP 511
Cdd:PRK06145 409 SEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRL---------ASFKVPrqlkvrdELP 479
|
490
....*....|....*
gi 24648260 512 KTGSGKVLRQQARDQ 526
Cdd:PRK06145 480 RNPSGKVLKRVLRDE 494
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
53-526 |
2.23e-40 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 153.38 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 53 GTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGT---PF-HAVSPWQdedtIKHLFSITRP 128
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAiavPInTALRGPQ----LEHILRNSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 129 KLIFCDGKcfqrlsiiariLKSHVYTLKDHRLGMPRV----EDLLEPTTAELYYVPETLL---------LGGDhTVAILC 195
Cdd:PRK06155 120 RLLVVEAA-----------LLAALEAADPGDLPLPAVwlldAPASVSVPAGWSTAPLPPLdapapaaavQPGD-TAAILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNsACLFDFGFVTGQ-------DVLLS----FSTidwsaGMFNMLFSC-CHGSTRIITDR----PYT 259
Cdd:PRK06155 188 TSGTTGPSKGVCCPH-AQFYWWGRNSAEdleigadDVLYTtlplFHT-----NALNAFFQAlLAGATYVLEPRfsasGFW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 260 PEymiqlVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRfVSVGGGscyVANLLKLQEFLITG-QISYGYALTECGGV 338
Cdd:PRK06155 262 PA-----VRRHGATVTYLLGAMVSILLSQPARESDRAHRVR-VALGPG---VPAALHAAFRERFGvDLLDGYGSTETNFV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 339 -AANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHN---GKVWNGYYANPNesKRMQDYQG-WFHTGDMGYF 413
Cdd:PRK06155 333 iAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPE--KTVEAWRNlWFHTGDRVVR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 414 DNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL 493
Cdd:PRK06155 411 DADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRL 490
|
490 500 510
....*....|....*....|....*....|....*..
gi 24648260 494 ----VVDHkqlhcgVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:PRK06155 491 ayfaVPRY------VEFVAALPKTENGKVQKFVLREQ 521
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
65-473 |
8.58e-40 |
|
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: 150.05 E-value: 8.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 65 AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNG---TPFHAVSPwqdEDTIKHLFSITRPKLIFCDGKcfqrl 141
Cdd:cd05907 15 VRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGavpVPIYPTSS---AEQIAYILNDSEAKALFVEDP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 142 siiarilkshvytlkdhrlgmprvedllepttaelyyvpetlllggDHTVAILCTSGTTGLPKAVCIS------NSACLF 215
Cdd:cd05907 87 ----------------------------------------------DDLATIIYTSGTTGRPKGVMLShrnilsNALALA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 216 DFGFVTGQDVLLSFSTIDWSAG--MFNMLFSCCHGSTRIITDrpytPEYMIQLVEKYKVTLLTVVPQQV------ASLLK 287
Cdd:cd05907 121 ERLPATEGDRHLSFLPLAHVFErrAGLYVPLLAGARIYFASS----AETLLDDLSEVRPTVFLAVPRVWekvyaaIKVKA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 288 TPTLNKQ-----RLASIRFVSVGGGSCYVANLLKLQEFLITgqISYGYALTECGGVAA-NMGVA-KPSSVGRIVPGVRVK 360
Cdd:cd05907 197 VPGLKRKlfdlaVGGRLRFAASGGAPLPAELLHFFRALGIP--VYEGYGLTETSAVVTlNPPGDnRIGTVGKPLPGVEVR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 361 IldeagrslghGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQY-SPQ 439
Cdd:cd05907 275 I----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNiSPE 344
|
410 420 430
....*....|....*....|....*....|....
gi 24648260 440 EIEQVIAELPDVIEACVFGlwnevDGDPAAAAVV 473
Cdd:cd05907 345 PIENALKASPLISQAVVIG-----DGRPFLVALI 373
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
236-520 |
2.61e-39 |
|
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: 145.88 E-value: 2.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 236 AGMfNMLFSCCH-GSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSvggGSCYVANL 314
Cdd:cd17637 54 AGL-NLALATFHaGGANVVMEK-FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL---GLDAPETI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 315 LKLQEflITGQISY-GYALTECGGVAANMGVA-KPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANP 392
Cdd:cd17637 129 QRFEE--TTGATFWsLYGQTETSGLVTLSPYReRPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 393 NESKRMQDyQGWFHTGDMGYFDNENYLHIVERK--EDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEvdgd 466
Cdd:cd17637 207 ELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVpdpkWGE---- 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24648260 467 pAAAAVVKI-PGSRLTEMDIVEYVAKRLVVDHKQLHcgVFFLPELPKTGSGKVLR 520
Cdd:cd17637 282 -GIKAVCVLkPGATLTADELIEFVGSRIARYKKPRY--VVFVEALPKTADGSIDR 333
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
193-525 |
3.07e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 150.29 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVCISNSAclfdfGFVTGQDVLlsfSTIDW--------SAGMF------NMLFSCCHGSTrIITDRPY 258
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPG-----GIGTLKAIL---DRTPWraeeptviVAPMFhawgfsQLVLAASLACT-IVTRRRF 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVPQQVASLLKTPT--LNKQRLASIRFVSVGGGSCYVANLLKLQEFLitGQISYG-YALTEC 335
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF--GDVIYNnYNATEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 336 GGVA----ANMGVAkPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYyaNPNESKRMQDyqGWFHTGDMG 411
Cdd:PRK13382 350 GMIAtatpADLRAA-PDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 412 YFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAK 491
Cdd:PRK13382 425 YLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRD 504
|
330 340 350
....*....|....*....|....*....|....
gi 24648260 492 RLvVDHKqLHCGVFFLPELPKTGSGKVLRQQARD 525
Cdd:PRK13382 505 NL-ANYK-VPRDIVVLDELPRGATGKILRRELQA 536
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
39-520 |
6.24e-39 |
|
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: 147.78 E-value: 6.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 39 RNHPNSICqiSDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDT 118
Cdd:cd05945 2 AANPDRPA--VVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 119 IKHLFSITRPKLIFCDGkcfqrlsiiarilkshvytlkdhrlgmprvedllepttAELYYvpetlllggdhtvaILCTSG 198
Cdd:cd05945 80 IREILDAAKPALLIADG--------------------------------------DDNAY--------------IIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 199 TTGLPKAVCIS--NSACLFD----FGFVTGQDVLLSFS--TIDWSagMFNMLFSCCHGSTRIITDRPYTpEYMIQLVE-- 268
Cdd:cd05945 108 STGRPKGVQIShdNLVSFTNwmlsDFPLGPGDVFLNQApfSFDLS--VMDLYPALASGATLVPVPRDAT-ADPKQLFRfl 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 269 -KYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTEC-GGVAAN----- 341
Cdd:cd05945 185 aEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEAtVAVTYIevtpe 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 342 -MGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKR---MQDYQGWFHTGDMGYFDNEN 417
Cdd:cd05945 265 vLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVRLEADG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 418 YLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGS-RLTEMDIVEYVAKRL--- 493
Cdd:cd05945 345 LLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAeAGLTKAIKAELAERLppy 424
|
490 500
....*....|....*....|....*..
gi 24648260 494 VVDHKQLHcgvffLPELPKTGSGKVLR 520
Cdd:cd05945 425 MIPRRFVY-----LDELPLNANGKIDR 446
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
248-531 |
4.02e-38 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 147.51 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 248 GSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFvSVGGGSCY---VANllKLQEflITG 324
Cdd:PRK08974 276 GGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKL-SVGGGMAVqqaVAE--RWVK--LTG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 325 Q-ISYGYALTECGG-VAAN-MGVAKPS-SVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQD 400
Cdd:PRK08974 351 QyLLEGYGLTECSPlVSVNpYDLDYYSgSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIK 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 401 yQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSrL 480
Cdd:PRK08974 431 -DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPS-L 508
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24648260 481 TEMDIVEYvAKRLVVDHK--QLhcgVFFLPELPKTGSGKVLRQQARDQALGKK 531
Cdd:PRK08974 509 TEEELITH-CRRHLTGYKvpKL---VEFRDELPKSNVGKILRRELRDEARAKV 557
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
54-522 |
2.48e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 143.95 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 54 TALTNG-EAITF------AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGC--------LLNGTPFHAVSPWQDEDT 118
Cdd:PRK03640 19 TAIEFEeKKVTFmelheaVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALqqlgavavLLNTRLSREELLWQLDDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 119 ikhlfsitRPKLIFCDGKCFQRLSIIARIlkshvytlkdhrlgmpRVEDLLEPTTAELYYVPETLLlggDHTVAILCTSG 198
Cdd:PRK03640 99 --------EVKCLITDDDFEAKLIPGISV----------------KFAELMNGPKEEAEIQEEFDL---DEVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 199 TTGLPKAV----------CISNSACLfdfGfVTGQDVLLS----FSTIDWSAGMFNMLFSCchgstRIITDRPYTPEYMI 264
Cdd:PRK03640 152 TTGKPKGViqtygnhwwsAVGSALNL---G-LTEDDCWLAavpiFHISGLSILMRSVIYGM-----RVVLVEKFDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 265 QLVEKYKVTLLTVVPQQVASLL-KTPtlNKQRLASIRFVSVGGGScyvANLLKLQEFLITG----QiSYGyaLTE-CGGV 338
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRLLeRLG--EGTYPSSFRCMLLGGGP---APKPLLEQCKEKGipvyQ-SYG--MTEtASQI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 339 AA---NMGVAKPSSVGRIVPGVRVKILDEaGRSLGHGETGEILVHNGKVWNGYYANPN-ESKRMQDyqGWFHTGDMGYFD 414
Cdd:PRK03640 295 VTlspEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDaTRETFQD--GWFKTGDIGYLD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 415 NENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKipGSRLTEMDIVEYVAKRLV 494
Cdd:PRK03640 372 EEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLA 449
|
490 500
....*....|....*....|....*...
gi 24648260 495 vdHKQLHCGVFFLPELPKTGSGKVLRQQ 522
Cdd:PRK03640 450 --KYKVPKRFYFVEELPRNASGKLLRHE 475
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
59-521 |
2.88e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 145.18 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 59 GEAITFAI------RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIF 132
Cdd:PRK06710 47 GKDITFSVfhdkvkRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 CDGKCFQRLSIIARILK-SHVYTLKDHRLgMPRVEDLLEP-------------TTAELYYVPETLLLGGDHTVAILC--- 195
Cdd:PRK06710 127 CLDLVFPRVTNVQSATKiEHVIVTRIADF-LPFPKNLLYPfvqkkqsnlvvkvSESETIHLWNSVEKEVNTGVEVPCdpe 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 --------TSGTTGLPKAVCISNSACLFD--------FGFVTGQDVLLSFSTIDWSAGMFNML-FSCCHGSTRIITDRpY 258
Cdd:PRK06710 206 ndlallqyTGGTTGFPKGVMLTHKNLVSNtlmgvqwlYNCKEGEEVVLGVLPFFHVYGMTAVMnLSIMQGYKMVLIPK-F 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRfVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGV 338
Cdd:PRK06710 285 DMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIR-ACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 339 A-ANMGVAK--PSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKR-MQDyqGWFHTGDMGYF 413
Cdd:PRK06710 364 ThSNFLWEKrvPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAvLQD--GWLHTGDVGYM 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 414 DNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL 493
Cdd:PRK06710 442 DEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYL 521
|
490 500
....*....|....*....|....*...
gi 24648260 494 VVdhKQLHCGVFFLPELPKTGSGKVLRQ 521
Cdd:PRK06710 522 AA--YKVPKVYEFRDELPKTTVGKILRR 547
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
192-525 |
7.87e-37 |
|
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: 141.66 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 192 AILCTSGTTGLPKAVCI------SNSACLFDFGFVTGQDVLLSFSTIDWSAGMFNMLF-SCCHGSTRIITdRPYTPEYMI 264
Cdd:cd05941 93 LILYTSGTTGRPKGVVLthanlaANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLcPLFAGASVEFL-PKFDPKEVA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 265 QLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIR---------FVSvggGScyvANLLK--LQEFL-ITGQ-ISYGYA 331
Cdd:cd05941 172 ISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARaaaaerlrlMVS---GS---AALPVptLEEWEaITGHtLLERYG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 332 LTECGGVAAN--MGVAKPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTG 408
Cdd:cd05941 246 MTEIGMALSNplDGERRPGTVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 409 DMGYFDNENYLHIVER-KEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSR-LTEMDIV 486
Cdd:cd05941 326 DLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAaLSLEELK 405
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24648260 487 EYVAKRLVVdHK---QLHcgvfFLPELPKTGSGKVLRQQARD 525
Cdd:cd05941 406 EWAKQRLAP-YKrprRLI----LVDELPRNAMGKVNKKELRK 442
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
192-525 |
2.05e-36 |
|
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: 141.36 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 192 AILCTSGTTGLPK-------AVCISNS---ACLFDFGFVTGQdVLLSfstidwSAGMF-NMLFSCCH-----GSTRIITD 255
Cdd:cd05929 129 KMLYSGGTTGRPKgikrglpGGPPDNDtlmAAALGFGPGADS-VYLS------PAPLYhAAPFRWSMtalfmGGTLVLME 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 256 RpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTP--TLNKQRLASIRFVSVGGGSCYVAnlLKLQEFLITGQISYG-YAL 332
Cdd:cd05929 202 K-FDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPeaVRNAYDLSSLKRVIHAAAPCPPW--VKEQWIDWGGPIIWEyYGG 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 333 TECGGVAANMG---VAKPSSVGRIVPGvRVKILDEAGRSLGHGETGEILVHNGKVWNgYYANPNESKRMQDYQGWFHTGD 409
Cdd:cd05929 279 TEGQGLTIINGeewLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 410 MGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYV 489
Cdd:cd05929 357 VGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELI 436
|
330 340 350
....*....|....*....|....*....|....*....
gi 24648260 490 A---KRLvvDHKQLHCGVFFLPELPKTGSGKVLRQQARD 525
Cdd:cd05929 437 AflrDRL--SRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
59-522 |
3.22e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 142.10 E-value: 3.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 59 GEAITFA------IRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIF 132
Cdd:PRK06178 56 GHVITYAeldelsDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 CdgkcFQRLSIIARILKS-----HVYT------------------LKDHRLGMPRVEDLLE----PTTAELYYVPETlll 185
Cdd:PRK06178 136 A----LDQLAPVVEQVRAetslrHVIVtsladvlpaeptlplpdsLRAPRLAAAGAIDLLPalraCTAPVPLPPPAL--- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 ggDHTVAILCTSGTTGLPKAvCISNSACLFD----FGFVTGQ----DVLLSFSTIDWSAGM-FNMLFSCCHGSTRIITDR 256
Cdd:PRK06178 209 --DALAALNYTGGTTGMPKG-CEHTQRDMVYtaaaAYAVAVVggedSVFLSFLPEFWIAGEnFGLLFPLFSGATLVLLAR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 257 pYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVgggscyVANLLKLQEFL------ITGQI---- 326
Cdd:PRK06178 286 -WDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRV------VSFVKKLNPDYrqrwraLTGSVlaea 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 327 SYGyaLTE---CGGVAANMG------VAKPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPN-ES 395
Cdd:PRK06178 359 AWG--MTEthtCDTFTAGFQdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEaTA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 396 KRMQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKI 475
Cdd:PRK06178 437 EALRD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLK 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24648260 476 PGSRLTEMDIVEYVAKRLVVdHKQLHcgVFFLPELPKTGSGKVLRQQ 522
Cdd:PRK06178 515 PGADLTAAALQAWCRENMAV-YKVPE--IRIVDALPMTATGKVRKQD 558
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
196-530 |
4.56e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 141.25 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAvCI-------SNSACLFDFGFVTGQDVLLSFSTIDWSAGMFNMLFSCCH-GSTRIIT---DRpytpEYMI 264
Cdd:PRK08314 198 TSGTTGVPKG-CMhthrtvmANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYaGATVVLMprwDR----EAAA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 265 QLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSvGGGSCY---VANLLKLQefliTGqISY--GYALTECGG-V 338
Cdd:PRK08314 273 RLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIG-GGGAAMpeaVAERLKEL----TG-LDYveGYGLTETMAqT 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 339 AAN-MGVAKPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNES---------KRmqdyqgWFHT 407
Cdd:PRK08314 347 HSNpPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATaeafieidgKR------FFRT 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 408 GDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSR--LTEMDI 485
Cdd:PRK08314 421 GDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEI 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24648260 486 VE--------YVAKRLVVdhkqlhcgvfFLPELPKTGSGKVLRQQARDQALGK 530
Cdd:PRK08314 501 IAwarehmaaYKYPRIVE----------FVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
56-524 |
5.66e-36 |
|
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: 139.13 E-value: 5.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLlngtpfhavspwqdedtikhlfsitrpklifcdg 135
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCL---------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 136 kcfqRLSIIARILKShvytlkdhRLGMPRVEDLLEPTTAELYYVpetlllGGDHTVAILCTSGTTGLPKAVC-------- 207
Cdd:cd05919 57 ----ARGAIAVVINP--------LLHPDDYAYIARDCEARLVVT------SADDIAYLLYSSGTTGPPKGVMhahrdpll 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 208 ISNSACLFDFGfVTGQDVLLSFSTIDWSAGMFNML-FSCCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLL 286
Cdd:cd05919 119 FADAMAREALG-LTPGDRVFSSAKMFFGYGLGNSLwFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 287 KTPTLNKQRLASIRFVsVGGGSCYVANLLKLQEFLITGQISYGYALTECGGV--AANMGVAKPSSVGRIVPGVRVKILDE 364
Cdd:cd05919 198 DSCAGSPDALRSLRLC-VSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIflSNRPGAWRLGSTGRPVPGYEIRLVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 365 AGRSLGHGETGEILVHNGKVWNGYYANPNES-KRMQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQ 443
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSrATFNG--GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 444 VIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEM---DIVEYVAKRLVVdHK---QLHcgvfFLPELPKTGSGK 517
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSA-HKvprRIA----FVDELPRTATGK 429
|
....*..
gi 24648260 518 VLRQQAR 524
Cdd:cd05919 430 LQRFKLR 436
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
322-530 |
6.03e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 141.05 E-value: 6.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 322 ITG-QISYGYALTECGGVAA--NMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRM 398
Cdd:PRK05677 349 VTGcAICEGYGMTETSPVVSvnPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 399 QDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGS 478
Cdd:PRK05677 429 LDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGE 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24648260 479 RLTEMDIVEYVAKRLVVDHKQLHcgVFFLPELPKTGSGKVLRQQARDQALGK 530
Cdd:PRK05677 509 TLTKEQVMEHMRANLTGYKVPKA--VEFRDELPTTNVGKILRRELRDEELKK 558
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
166-536 |
2.24e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 139.14 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 166 EDLLEPTTAELYYV--PEtlllggDHTVAILCTSGTTGLPKAVCISNS-------ACLFDFGFVTGQDVLLSFSTIDWSA 236
Cdd:PRK07786 156 EDLLAEAGPAHAPVdiPN------DSPALIMYTSGTTGRPKGAVLTHAnltgqamTCLRTNGADINSDVGFVGVPLFHIA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 237 GMFNMLFSCCHGSTRIItdRP---YTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLAsIRFVSVGGGSCYVAN 313
Cdd:PRK07786 230 GIGSMLPGLLLGAPTVI--YPlgaFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 314 LLKLQEFLITGQISYGYALTECGGVAANM----GVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYY 389
Cdd:PRK07786 307 LRQMAATFPEAQILAAFGQTEMSPVTCMLlgedAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYW 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 390 ANPNESKRMQDyQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdg 465
Cdd:PRK07786 387 NNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRadekWGEV-- 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648260 466 dPAAAAVVKIPGSRLTEMDIVEYVAKRLV-VDHKQlhcGVFFLPELPKTGSGKVLRQQARDQALGKKWADHG 536
Cdd:PRK07786 464 -PVAVAAVRNDDAALTLEDLAEFLTDRLArYKHPK---ALEIVDALPRNPAGKVLKTELRERYGACVNVERR 531
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
67-518 |
3.27e-35 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 137.27 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIvgtnttylmpvvlgcLLNGTPfhavspwqdeDTIkhlfsitrpklifcdgkcfqrLSIIAr 146
Cdd:cd05930 24 RLARYLRERGVGPGDLVAV---------------LLERSL----------EMV---------------------VAILA- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 147 ILKS-HVYTLKDHRLGMPRVEDLLEPTTAELyyvpetLLLGGDHTVAILCTSGTTGLPKAVCISNSA---CLFDFG---F 219
Cdd:cd05930 57 VLKAgAAYVPLDPSYPAERLAYILEDSGAKL------VLTDPDDLAYVIYTSGSTGKPKGVMVEHRGlvnLLLWMQeayP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 220 VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDR--PYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLnkQRLA 297
Cdd:cd05930 131 LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL--AALP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 298 SIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVAANMGVAK------PSSVGRIVPGVRVKILDEAGRSLGH 371
Cdd:cd05930 209 SLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPddeedgRVPIGRPIPNTRVYVLDENLRPVPP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 372 GETGEILVHNGKVWNGYYANPNESK------------RMqdyqgwFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQ 439
Cdd:cd05930 289 GVPGELYIGGAGLARGYLNRPELTAerfvpnpfgpgeRM------YRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 440 EIEQVIAELPDVIEACVFgLWNEVDGDPA-AAAVVKIPGSRLTEMDIVEYVAKRL----VVDHkqlhcgVFFLPELPKTG 514
Cdd:cd05930 363 EIEAALLAHPGVREAAVV-AREDGDGEKRlVAYVVPDEGGELDEEELRAHLAERLpdymVPSA------FVVLDALPLTP 435
|
....
gi 24648260 515 SGKV 518
Cdd:cd05930 436 NGKV 439
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
37-531 |
1.16e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 136.74 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 37 FMRNHPNSICQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSpwqde 116
Cdd:PRK13391 6 HAQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 117 dtiKHLfsiTRPKLIFCDGKCFQRLSI-------IARILKSHVYTLKdHRL------GMPRVEDLlEPTTAELyyvPETL 183
Cdd:PRK13391 81 ---SHL---TPAEAAYIVDDSGARALItsaakldVARALLKQCPGVR-HRLvldgdgELEGFVGY-AEAVAGL---PATP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 184 L----LGGDhtvaILCTSGTTGLPKAVC-------ISNSACLFDF-----GFVTGQdVLLSFSTIDWSAGMFNMLFSCCH 247
Cdd:PRK13391 150 IadesLGTD----MLYSSGTTGRPKGIKrplpeqpPDTPLPLTAFlqrlwGFRSDM-VYLSPAPLYHSAPQRAVMLVIRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 248 GSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQR--LASIRFVSVGGGSCYVanllKLQEFLIT-- 323
Cdd:PRK13391 225 GGTVIVMEH-FDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKydLSSLEVAIHAAAPCPP----QVKEQMIDww 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 324 GQISYG-YALTECGGVAA---NMGVAKPSSVGRIVPGVrVKILDEAGRSLGHGETGEILVHNGKVWNgYYANPNESKRMQ 399
Cdd:PRK13391 300 GPIIHEyYAATEGLGFTAcdsEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEAR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 400 DYQG-WFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGS 478
Cdd:PRK13391 378 HPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGV 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24648260 479 RLTE---MDIVEYVAKRLvvDHKQLHCGVFFLPELPKTGSGKVLRQQARDQALGKK 531
Cdd:PRK13391 458 DPGPalaAELIAFCRQRL--SRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGNK 511
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
186-526 |
1.57e-34 |
|
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: 136.86 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 GGDHTVAILCTSGTTGLPKAVCISNsacLFDFG-FVTG---QDVL-----LSFSTIDWSAGMFNMLF-SCCHGSTRIITD 255
Cdd:cd05970 183 CGEDILLVYFSSGTTGMPKMVEHDF---TYPLGhIVTAkywQNVRegglhLTVADTGWGKAVWGKIYgQWIAGAAVFVYD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 256 -RPYTPEYMIQLVEKYKVTLLtVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFliTG-QISYGYALT 333
Cdd:cd05970 260 yDKFDPKALLEKLSKYGVTTF-CAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEK--TGiKLMEGFGQT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 334 ECGGVAANMGV--AKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGK-----VWNGYYANPNE-SKRMQDyqGWF 405
Cdd:cd05970 337 ETTLTIATFPWmePKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKtAEVWHD--GYY 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 406 HTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKI----PGSRLT 481
Cdd:cd05970 415 HTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAkgyePSEELK 494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24648260 482 EmDIVEYVaKRLVVDHKQLHCgVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:cd05970 495 K-ELQDHV-KKVTAPYKYPRI-VEFVDELPKTISGKIRRVEIRER 536
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
186-525 |
3.19e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 134.48 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 GGDHTVAILCTSGTTGLPKAvcisnsaCLFDFGFVTG-------------QDVLLSFSTIDWS--AGMFNMLFSCCHGST 250
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKG-------ALHAHRVLLGhlpgvqfpfnlfpRDGDLYWTPADWAwiGGLLDVLLPSLYFGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 251 RIITDRP--YTPEYMIQLVEKYKVTLLTVVP------QQVASLLKTPTLNKQRLASirfvsvgGGSCYVANLLKLQEFLI 322
Cdd:cd05971 159 PVLAHRMtkFDPKAALDLMSRYGVTTAFLPPtalkmmRQQGEQLKHAQVKLRAIAT-------GGESLGEELLGWAREQF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 323 TGQISYGYALTECG---GVAANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVH--NGKVWNGYYANPnESKR 397
Cdd:cd05971 232 GVEVNEFYGQTECNlviGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNP-SATE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 398 MQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPG 477
Cdd:cd05971 311 KKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPG 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24648260 478 ---SRLTEMDIVEYVAKRLVVDHKQLHcgVFFLPELPKTGSGKVLRQQARD 525
Cdd:cd05971 391 etpSDALAREIQELVKTRLAAHEYPRE--IEFVNELPRTATGKIRRRELRA 439
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
263-525 |
1.00e-33 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 134.76 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRfVSVGGGscyvanlLKLQE------FLITG-QISYGYALTEC 335
Cdd:PRK07059 293 FIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLI-VANGGG-------MAVQRpvaerwLEMTGcPITEGYGLSET 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 336 GGVA-AN-MGVAKPS-SVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGY 412
Cdd:PRK07059 365 SPVAtCNpVDATEFSgTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGV 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 413 FDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSrLTEMDIVEYVAKR 492
Cdd:PRK07059 445 MDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA-LTEEDVKAFCKER 523
|
250 260 270
....*....|....*....|....*....|...
gi 24648260 493 LVVDHKQLHcgVFFLPELPKTGSGKVLRQQARD 525
Cdd:PRK07059 524 LTNYKRPKF--VEFRTELPKTNVGKILRRELRD 554
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
53-527 |
1.07e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 134.62 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 53 GTALTNGEAITFAIRIAQQL-KAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKH-LFSITRPKL 130
Cdd:PRK08751 48 GKTITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHqLIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 131 IFCDGKCFQRLSIIARILKSHVYT--LKDhRLGMPR------VEDLLEPTTAElYYVP------ETLLLGGDHTVAIL-- 194
Cdd:PRK08751 128 VVIDNFGTTVQQVIADTPVKQVITtgLGD-MLGFPKaalvnfVVKYVKKLVPE-YRINgairfrEALALGRKHSMPTLqi 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 195 ---------CTSGTTGLPKAVCISN----------SACLFDFGFVT-GQDVLLS----FSTIDWSAGmfNMLFSCCHGST 250
Cdd:PRK08751 206 epddiaflqYTGGTTGVAKGAMLTHrnlvanmqqaHQWLAGTGKLEeGCEVVITalplYHIFALTAN--GLVFMKIGGCN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 251 RIITDRPYTPEYMIQLvEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFvSVGGGSCyVANLLKLQEFLITG-QISYG 329
Cdd:PRK08751 284 HLISNPRDMPGFVKEL-KKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKM-TLGGGMA-VQRSVAERWKQVTGlTLVEA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 330 YALTECGGVAANMGVAKPS---SVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFH 406
Cdd:PRK08751 361 YGLTETSPAACINPLTLKEyngSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLH 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 407 TGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKiPGSRLTEMDIV 486
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVK-KDPALTAEDVK 519
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24648260 487 EYVAKRLvVDHKQLHCgVFFLPELPKTGSGKVLRQQARDQA 527
Cdd:PRK08751 520 AHARANL-TGYKQPRI-IEFRKELPKTNVGKILRRELRDAA 558
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
196-520 |
1.36e-33 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 129.83 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSACLFDF-----GF-VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTrIITDRPYTPEYMIQLVEK 269
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFvcnedLFnISGEDAILAPGPLSHSLFLYGAISALYLGGT-FIGQRKFNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 270 YKVTLLTVVPQQVASLLKTPTLNkqrlASIRFVSVGGGSCY---------VANLLKLQEFLITGQISYGYALtecggvaA 340
Cdd:cd17633 87 YNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFestkkklknIFPKANLIEFYGTSELSFITYN-------F 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 341 NMGVAKPSSVGRIVPGVRVKILDEAGrslghGETGEILVHNGKVWNGYYanpneskRMQDYQ--GWFHTGDMGYFDNENY 418
Cdd:cd17633 156 NQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYV-------RGGFSNpdGWMSVGDIGYVDEEGY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 419 LHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdpaaaAVVKIPGSRLTEMDIVEYVAKRLV 494
Cdd:cd17633 224 LYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdarFGEI-------AVALYSGDKLTYKQLKRFLKQKLS 296
|
330 340
....*....|....*....|....*...
gi 24648260 495 VDH--KQLHcgvfFLPELPKTGSGKVLR 520
Cdd:cd17633 297 RYEipKKII----FVDSLPYTSSGKIAR 320
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
188-520 |
3.35e-33 |
|
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: 131.80 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVAILCTSGTTGLPKAVCI------SNSACLFDFGFVTGQDVLLSFSTIDWSAGM-FNMLFSCCHGSTRIITDRPYTP 260
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLtyrnivSNVDGVKEVVLLGKGDKILSILPLHHIYPLtFTLLLPLLNGAHVVFLDKIPSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 261 EYMIQLVEKYKVTLLTVVPQQVASLLKTPTLN-------KQRLASIRFVS---------------------VGGGSCYVA 312
Cdd:cd05914 169 KIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPkltlkkfKFKLAKKINNRkirklafkkvheafggnikefVIGGAKINP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 313 NLLklqEFLITGQISY--GYALTECGGVAANMGVA--KPSSVGRIVPGVRVKILDEAGRSlghgETGEILVHNGKVWNGY 388
Cdd:cd05914 249 DVE---EFLRTIGFPYtiGYGMTETAPIISYSPPNriRLGSAGKVIDGVEVRIDSPDPAT----GEGEIIVRGPNVMKGY 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 389 YANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVER-KEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFglwnEVDGDP 467
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRkKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV----VQEKKL 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24648260 468 AAAAVV----------KIPGSRLTEMD--IVEYVAKrlVVDHKQLHCGVFFLPELPKTGSGKVLR 520
Cdd:cd05914 398 VALAYIdpdfldvkalKQRNIIDAIKWevRDKVNQK--VPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
196-527 |
8.12e-33 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 127.83 E-value: 8.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSACLFDF-------GFVTGQDVLLSFSTIDWSaGMFnMLFSCCHGSTRIITDRPYTPEYmiQLVE 268
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAaglhsrlGFGGGDSWLLSLPLYHVG-GLA-ILVRSLLAGAELVLLERNQALA--EDLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 269 KYKVTLLTVVPQQVASLLKTPtLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGyaLTECGG-VAAN-MGVAK 346
Cdd:cd17630 84 PPGVTHVSLVPTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYG--MTETASqVATKrPDGFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 347 PSSVGRIVPGVRVKILDeagrslghgeTGEILVHNGKVWNGYYANPNESKRmqDYQGWFHTGDMGYFDNENYLHIVERKE 426
Cdd:cd17630 161 RGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLVPEF--NEDGWFTTKDLGELHADGRLTVLGRAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 427 DLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVkiPGSRLTEMDIVEYVAKRLVVDH--KQLHcgv 504
Cdd:cd17630 229 NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDKLARFKlpKRIY--- 303
|
330 340
....*....|....*....|...
gi 24648260 505 fFLPELPKTGSGKVLRQQARDQA 527
Cdd:cd17630 304 -PVPELPRTGGGKVDRRALRAWL 325
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-520 |
8.50e-33 |
|
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: 128.15 E-value: 8.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 190 TVAILCTSGTTGLPKAVCISNSACLFDFGFV-------TGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEY 262
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILqkeglnwVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVAnllKLQEFLITG--QISYGYALTECGGVAA 340
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAA---DVRFIEATGltNTAQVYGLSETGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 341 ---NMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQdYQGWFHTGDMGYFDNEN 417
Cdd:cd17635 160 lptDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 418 YLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVK--------IPGSRLTEMDIVE-- 487
Cdd:cd17635 239 FLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeldenaIRALKHTIRRELEpy 318
|
330 340 350
....*....|....*....|....*....|...
gi 24648260 488 YVAKRLVvdhkqlhcgvfFLPELPKTGSGKVLR 520
Cdd:cd17635 319 ARPSTIV-----------IVTDIPRTQSGKVKR 340
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
52-524 |
1.02e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 132.39 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFA------IRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFhAVSPWQDEDTIKHLFSI 125
Cdd:PRK07529 49 DADPLDRPETWTYAelladvTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 126 TRPKLI-----FCDGKCFQRLSIIARILKsHVYT-----LKDH---------RLGMPRVEDLLEPTTAELYYVPETLLL- 185
Cdd:PRK07529 128 AGAKVLvtlgpFPGTDIWQKVAEVLAALP-ELRTvvevdLARYlpgpkrlavPLIRRKAHARILDFDAELARQPGDRLFs 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 ----GGDHTVAILCTSGTTGLPKAVC------ISNSACLFDFGFVTGQDVLLsfstidwsAG--MF--NMLFSCC----- 246
Cdd:PRK07529 207 grpiGPDDVAAYFHTGGTTGMPKLAQhthgneVANAWLGALLLGLGPGDTVF--------CGlpLFhvNALLVTGlapla 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 247 -HGSTRIITDRPY-TPEYMI---QLVEKYKVTLLTVVPQQVASLLKTPTlNKQRLASIRFVSVGGGSCYVANLLKLQEfl 321
Cdd:PRK07529 279 rGAHVVLATPQGYrGPGVIAnfwKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGAAPLPVEVFRRFEA-- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 322 ITG-QISYGYALTECG-GVAANM--GVAKPSSVGRIVPG--VRVKILDEAGRSL---GHGETGEILVHNGKVWNGYyANP 392
Cdd:PRK07529 356 ATGvRIVEGYGLTEATcVSSVNPpdGERRIGSVGLRLPYqrVRVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGY-LEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 393 NESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAV 472
Cdd:PRK07529 435 AHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYV 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24648260 473 VKIPGSRLTEMDIVEYvAKRLVVDHKQLHCGVFFLPELPKTGSGKVLRQQAR 524
Cdd:PRK07529 515 QLKPGASATEAELLAF-ARDHIAERAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
193-528 |
3.14e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 129.54 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVCISNS---ACLFDFGFVTGQDVLLSFsTIDwsAGMF-------NMLFSCCHGSTRIITDrPYTPEY 262
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERnlqQTAHNFGVLGRVDAHSSF-LCD--APMFhiiglitSVRPVLAVGGSILVSN-GFEPKR 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLV--EKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKlqeFLITG-QISYGYALTECG--- 336
Cdd:PRK09088 216 TLGRLgdPALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILG---WLDDGiPMVDGFGMSEAGtvf 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 337 GVAANMGV--AKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFD 414
Cdd:PRK09088 293 GMSVDCDVirAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 415 NENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdpAAAAVVKIPGSRLTEMDIVEYVA 490
Cdd:PRK09088 373 ADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMadaqWGEV----GYLAIVPADGAPLDLERIRSHLS 448
|
330 340 350
....*....|....*....|....*....|....*...
gi 24648260 491 KRLVvdHKQLHCGVFFLPELPKTGSGKVLRQQARDQAL 528
Cdd:PRK09088 449 TRLA--KYKVPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
187-534 |
3.20e-32 |
|
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: 130.90 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 187 GDHTVAILCTSGTTGLPKAV-------CISNSACLFD-FGFVTGqDVLLSFSTIDWSAGMfnmLFSC----CHGSTRIIT 254
Cdd:cd05967 229 ATDPLYILYTSGTTGKPKGVvrdngghAVALNWSMRNiYGIKPG-DVWWAASDVGWVVGH---SYIVygplLHGATTVLY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 255 D-RP-YTPE--YMIQLVEKYKVTLLTVVPQQVASLLKTPT----LNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQI 326
Cdd:cd05967 305 EgKPvGTPDpgAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 327 SYgYALTECG-GVAAN-MGVA----KPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVH----NGKVwNGYYANPNESK 396
Cdd:cd05967 385 DH-WWQTETGwPITANpVGLEplpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKlplpPGCL-LTLWKNDERFK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 397 R--MQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVK 474
Cdd:cd05967 463 KlyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVL 542
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 475 IPGSRLTEMDIVEYVAKrLVVDhkqlHCG-------VFFLPELPKTGSGKVLRQQARDQALGKKWAD 534
Cdd:cd05967 543 KEGVKITAEELEKELVA-LVRE----QIGpvaafrlVIFVKRLPKTRSGKILRRTLRKIADGEDYTI 604
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
29-526 |
3.27e-32 |
|
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: 130.09 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 29 SIGKILFAFMRNHPNSICQISDTEGT--ALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNG-- 104
Cdd:cd05906 11 TLLELLLRAAERGPTKGITYIDADGSeeFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 105 ----TPFHAVSPWQDEDT-IKHLFSITRPKLIFCDgkcFQRLSIIARILKshVYTLKDHRLGMprVEDLLEptTAELYYV 179
Cdd:cd05906 91 paplTVPPTYDEPNARLRkLRHIWQLLGSPVVLTD---AELVAEFAGLET--LSGLPGIRVLS--IEELLD--TAADHDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 180 PEtllLGGDHTVAILCTSGTTGLPKAVCISNSACL-------FDFGFvTGQDVLLSFSTIDWSAGMFNM-LFSCCHGSTR 251
Cdd:cd05906 162 PQ---SRPDDLALLMLTSGSTGFPKAVPLTHRNILarsagkiQHNGL-TPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 252 IitdrpYTP-EYMIQ-------LVEKYKVT-------LLTVVPQQVASLlKTPTLNkqrLASIRFVsVGGGSCYVA---- 312
Cdd:cd05906 238 V-----HVPtEEILAdplrwldLIDRYRVTitwapnfAFALLNDLLEEI-EDGTWD---LSSLRYL-VNAGEAVVAktir 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 313 NLLK-LQEF-LITGQISYGYALTE-CGGVAANMGVAKP--------SSVGRIVPGVRVKILDEAGRSLGHGETGEILVHN 381
Cdd:cd05906 308 RLLRlLEPYgLPPDAIRPAFGMTEtCSGVIYSRSFPTYdhsqalefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 382 GKVWNGYYANP--NESKRMQDyqGWFHTGDMGYFDNENyLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIE--ACVF 457
Cdd:cd05906 388 PVVTKGYYNNPeaNAEAFTED--GWFRTGDLGFLDNGN-LTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 458 GLWNEvDGDPAAAAVVKIP-----GSRLTEMDIVEYVAKRLVvdhkqlhcGV---FFLP----ELPKTGSGKVLRQQARD 525
Cdd:cd05906 465 AVRDP-GAETEELAIFFVPeydlqDALSETLRAIRSVVSREV--------GVspaYLIPlpkeEIPKTSLGKIQRSKLKA 535
|
.
gi 24648260 526 Q 526
Cdd:cd05906 536 A 536
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-520 |
7.98e-32 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 127.63 E-value: 7.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCllngtpfhavspWQDEDTIKHLFSITRPKLIfcdg 135
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGI------------WRLGAVYQPLFTAFGPKAI---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 136 kcfqrlsiiarilkshvytlkDHRLGMPRVEdLLEPTTAELYYVPETLLLggdhtvaILCTSGTTGLPKAVCISNSAcLF 215
Cdd:cd05973 65 ---------------------EHRLRTSGAR-LVVTDAANRHKLDSDPFV-------MMFTSGTTGLPKGVPVPLRA-LA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 216 DFGF-------VTGQDVLLSFSTIDWSAGMFNMLFS-CCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLK 287
Cdd:cd05973 115 AFGAylrdavdLRPEDSFWNAADPGWAYGLYYAITGpLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 288 TPTLNKQRL-ASIRFVSVGGG-------SCYVANLLKLqeflitgqISYGYALTECGGVAANM-GVAKP---SSVGRIVP 355
Cdd:cd05973 195 AGAEVPARPkGRLRRVSSAGEpltpeviRWFDAALGVP--------IHDHYGQTELGMVLANHhALEHPvhaGSAGRAMP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 356 GVRVKILDEAGRSLGHGETG--EILVHNGKV-W-NGYYANPNESKRmqdyQGWFHTGDMGYFDNENYLHIVERKEDLLRF 431
Cdd:cd05973 267 GWRVAVLDDDGDELGPGEPGrlAIDIANSPLmWfRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRADDVITM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 432 HGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEM---DIVEYVAKRLVVdH---KQLHcgvf 505
Cdd:cd05973 343 SGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSA-HaypRTIH---- 417
|
490
....*....|....*
gi 24648260 506 FLPELPKTGSGKVLR 520
Cdd:cd05973 418 FVDELPKTPSGKIQR 432
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
196-522 |
1.37e-31 |
|
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: 127.63 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSACLFDFGFVTGQ--------DVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEYMIQLV 267
Cdd:cd05923 158 TSGTTGLPKGAVIPQRAAESRVLFMSTQaglrhgrhNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 268 EKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLiTGQISYGYALTEcggvAAN---MGV 344
Cdd:cd05923 238 EQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL-PGEKVNIYGTTE----AMNslyMRD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 345 AKPSSVGRivPGV--RVKILDEAGRS---LGHGETGEILV--HNGKVWNGYYANPN-ESKRMQDyqGWFHTGDMGYFDNE 416
Cdd:cd05923 313 ARTGTEMR--PGFfsEVRIVRIGGSPdeaLANGEEGELIVaaAADAAFTGYLNQPEaTAKKLQD--GWYRTGDVGYVDPS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 417 NYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGsRLTEMDIVEYVAKRLVVD 496
Cdd:cd05923 389 GDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRASELAD 467
|
330 340
....*....|....*....|....*.
gi 24648260 497 HKQLHcGVFFLPELPKTGSGKVLRQQ 522
Cdd:cd05923 468 FKRPR-RYFFLDELPKNAMNKVLRRQ 492
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
67-528 |
3.97e-31 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 125.69 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGtpfhAVS-PwqdedtikhLFSItrpkliFCDGKCFQRLSII- 144
Cdd:cd05969 12 RFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIG----AVIcP---------LFSA------FGPEAIRDRLENSe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 145 ARILKSHvytlkdhrlgmprvEDLLEPTTaelyyvPETLLLggdhtvaILCTSGTTGLPKAVCISNSACLFDFgfVTGQD 224
Cdd:cd05969 73 AKVLITT--------------EELYERTD------PEDPTL-------LHYTSGTTGTPKGVLHVHDAMIFYY--FTGKY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 225 VL------LSFSTID--WSAGMFNMLFSC-CHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKT--PTLNK 293
Cdd:cd05969 124 VLdlhpddIYWCTADpgWVTGTVYGIWAPwLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdELARK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 294 QRLASIRFVSVGGGscYV-ANLLKLQEFLITGQISYGYALTECGGVA-ANMGV--AKPSSVGRIVPGVRVKILDEAGRSL 369
Cdd:cd05969 204 YDLSSLRFIHSVGE--PLnPEAIRWGMEVFGVPIHDTWWQTETGSIMiANYPCmpIKPGSMGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 370 GHGETGEILVHNG--KVWNGYYanpNESKRMQDY--QGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVI 445
Cdd:cd05969 282 PPGTKGILALKPGwpSMFRGIW---NDEERYKNSfiDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 446 AELPDVIEACVFGLWNEVDGD-PAAAAVVKI---PGSRLTEmDIVEYVAKRL--VVDHKQLHcgvfFLPELPKTGSGKVL 519
Cdd:cd05969 359 MEHPAVAEAGVIGKPDPLRGEiIKAFISLKEgfePSDELKE-EIINFVRQKLgaHVAPREIE----FVDNLPKTRSGKIM 433
|
....*....
gi 24648260 520 RQQARDQAL 528
Cdd:cd05969 434 RRVLKAKEL 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
188-530 |
6.76e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 126.65 E-value: 6.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVAILCTSGTTGLPKAVCISNSACLFDF--------GFVTGQDVLLSFSTIDWSAGM-FNMLFSCCHGSTRIITDRPY 258
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTHRNLFANAaqgkawvpGLGDGPERVLAALPMFHAYGLtLCLTLAVSIGGELVLLPAPD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMiQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFvSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGV 338
Cdd:PRK05605 299 IDLIL-DAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRN-AFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPI 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 339 AAN--MGVA-KPSSVGRIVPGVRVKILD--EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQdYQGWFHTGDMGYF 413
Cdd:PRK05605 377 IVGnpMSDDrRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVM 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 414 DNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL 493
Cdd:PRK05605 456 EEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHL 535
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 24648260 494 V---VDHKqlhcgVFFLPELPKTGSGKVLRQQARDQALGK 530
Cdd:PRK05605 536 TrykVPRR-----FYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
260-518 |
6.28e-30 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 119.71 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 260 PEYMIQLVEKYKVTLLTVVPQQVASLLKtptLNKQRLASIRfvsvgggSCYVANLLKLQEFLIT------GQISYGYALT 333
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIDQIVE---LNADGLYDLS-------SLRSSPAAPEWNDMATvdtspwGRKPGGYGQT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 334 ECGGVA--ANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNE-SKRMQDyqGWFHTGDM 410
Cdd:cd17636 147 EVMGLAtfAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVnARRTRG--GWHHTNDL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 411 GYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVA 490
Cdd:cd17636 225 GRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCR 304
|
250 260
....*....|....*....|....*...
gi 24648260 491 KRLVVDHKQLHcgVFFLPELPKTGSGKV 518
Cdd:cd17636 305 ARIASYKKPKS--VEFADALPRTAGGAD 330
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
67-456 |
3.06e-29 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 119.68 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAM-GLKQDDVVGIVGTNTTYLMPVVLGCLLNG---TPFHAVSPwqdEDTIKHLFSITRPKLIFCDGKCFQRLS 142
Cdd:TIGR01733 11 RLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGaayVPLDPAYP---AERLAFILEDAGARLLLTDSALASRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 143 IIARilkshvytlkdhrLGMPRVEDLLEPTTAELYYVPETLLLGGDHTVAILCTSGTTGLPKAVCISN-SACLF-----D 216
Cdd:TIGR01733 88 GLVL-------------PVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHrSLVNLlawlaR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 217 FGFVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRII---TDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKtptLNK 293
Cdd:TIGR01733 155 RYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVppeDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA---ALP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 294 QRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVA-------ANMGVAKPSSVGRIVPGVRVKILDEAG 366
Cdd:TIGR01733 232 PALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWStatlvdpDDAPRESPVPIGRPLANTRLYVLDDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 367 RSLGHGETGEILVHNGKVWNGYYANPNESK--------RMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSP 438
Cdd:TIGR01733 312 RPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIEL 391
|
410
....*....|....*...
gi 24648260 439 QEIEQVIAELPDVIEACV 456
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
174-521 |
3.08e-29 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.94 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 174 AELYYVPEtllLGGDHTVAILCTSGTTGLPKAVCISNSACLFDFGFVTGQ------DVLLSFST---IDW--SAGMfnML 242
Cdd:PRK08008 162 ATLCYAPP---LSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQcalrddDVYLTVMPafhIDCqcTAAM--AA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 243 FSCchGSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVsvgggsCYVANLLK------ 316
Cdd:PRK08008 237 FSA--GATFVLLEK-YSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREV------MFYLNLSDqekdaf 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 317 LQEFLITGQISYGYALTECGGVAANMGVAK--PSsVGRIVPGVRVKILDEAGRSLGHGETGEILVHN--GK-VWNGYYAN 391
Cdd:PRK08008 308 EERFGVRLLTSYGMTETIVGIIGDRPGDKRrwPS-IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpGKtIFKEYYLD 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 392 PNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAA 471
Cdd:PRK08008 387 PKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24648260 472 VVKIPGSRLTEMDIVEYVAKRLVvdhkQLHCGVF--FLPELPKTGSGKVLRQ 521
Cdd:PRK08008 467 VVLNEGETLSEEEFFAFCEQNMA----KFKVPSYleIRKDLPRNCSGKIIKK 514
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-527 |
1.18e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 116.81 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 187 GDHTVAILCTSGTTGLPKAVC------ISNSACLFDFGFVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRP--Y 258
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQhthsneVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPagY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQ----LVEKYKVTLLTVVPQQVASLLKTPTlnKQRLASIRFVSVGGGSCYVANLLKLQEFliTG-QISYGYALT 333
Cdd:cd05944 81 RNPGLFDnfwkLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDA--TGlPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 334 ECG-GVAANM--GVAKPSSVGRIVP--GVRVKILDEAGRSL---GHGETGEILVHNGKVWNGY-YANPNESKRMQDyqGW 404
Cdd:cd05944 157 EATcLVAVNPpdGPKRPGSVGLRLPyaRVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYlYTEGNKNAFVAD--GW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 405 FHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMD 484
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24648260 485 IVEYVAKRlVVDHKQLHCGVFFLPELPKTGSGKVLRQQARDQA 527
Cdd:cd05944 315 LLAWARDH-VPERAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
50-518 |
1.43e-28 |
|
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: 118.97 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 50 DTEGTALTNGEAITFAIRIAQQLKAMGlKQDDVVGIVGTNTTYLMPVVLGCLLNG-TPfhAVSPW-QDEDTIKHLFSITR 127
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALARKLAKMT-KEGENVGVMLPPSAGGALANFALALSGkVP--VMLNYtAGLRELRACIKLAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 128 PKLIFCdGKCFQRLsiiariLKSHVYTLKDHRLGMPRVEDLLEPTT--------AELYYVPETLLL-------GGDHTVA 192
Cdd:cd05909 79 IKTVLT-SKQFIEK------LKLHHLFDVEYDARIVYLEDLRAKISkadkckafLAGKFPPKWLLRifgvapvQPDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVCISNS-------ACLFDFGFVTgQDVLLS----FSTIDWSAGMFNMLFS----CCHGStriitdrP 257
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKnllanveQITAIFDPNP-EDVVFGalpfFHSFGLTGCLWLPLLSgikvVFHPN-------P 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 258 YTPEYMIQLVEKYKVTLLtvvpqqvaslLKTPTL--------NKQRLASIRFVSVGGGscyvanllKLQEFLITG----- 324
Cdd:cd05909 224 LDYKKIPELIYDKKATIL----------LGTPTFlrgyaraaHPEDFSSLRLVVAGAE--------KLKDTLRQEfqekf 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 325 --QISYGYALTECGGVAA----NMGvAKPSSVGRIVPGVRVKILDEAGRS-LGHGETGEILVHNGKVWNGYYANPNE-SK 396
Cdd:cd05909 286 giRILEGYGTTECSPVISvntpQSP-NKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELtSF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 397 RMQDyqGWFHTGDMGYFDNENYLHIVERkedLLRFH---GAQYSPQEIEQVIAE-LPDVIEACVFGLwneVDGDPAAAAV 472
Cdd:cd05909 365 AFGD--GWYDTGDIGKIDGEGFLTITGR---LSRFAkiaGEMVSLEAIEDILSEiLPEDNEVAVVSV---PDGRKGEKIV 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24648260 473 VKIPGSRLTEMDIVEY-----VAKRLVVDHkqlhcgVFFLPELPKTGSGKV 518
Cdd:cd05909 437 LLTTTTDTDPSSLNDIlknagISNLAKPSY------IHQVEEIPLLGTGKP 481
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
185-528 |
2.16e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 119.00 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 185 LGGDHTVAILCTSGTTGLPKAV------CISNSACLFDFGFVTGQDVLLSFSTIDWSAG-MFNMLFSCCHGSTRIITDRp 257
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVmhtantLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAVLQDI- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 258 YTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISyGYALTECGG 337
Cdd:PRK13295 273 WDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVS-AWGMTENGA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 338 VAanmgVAKPSSV--------GRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYanpnesKRMQ----DYQGWF 405
Cdd:PRK13295 352 VT----LTKLDDPderasttdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYL------KRPQlngtDADGWF 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 406 HTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDI 485
Cdd:PRK13295 422 DTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEM 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 486 VEY-----VAK-----RLVVdhkqlhcgvffLPELPKTGSGKV----LRQQARDQAL 528
Cdd:PRK13295 502 VEFlkaqkVAKqyipeRLVV-----------RDALPRTPSGKIqkfrLREMLRGEDA 547
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
191-527 |
2.48e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 118.77 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 191 VAIL-CTSGTTGLPKAVCISNS----------ACLFDFG------FVTGQDVLLS----FSTIDWSAGMFNMLFScchGS 249
Cdd:PRK12492 209 IAVLqYTGGTTGLAKGAMLTHGnlvanmlqvrACLSQLGpdgqplMKEGQEVMIAplplYHIYAFTANCMCMMVS---GN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 250 TRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEflITG-QISY 328
Cdd:PRK12492 286 HNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQ--LTGcTIVE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 329 GYALTECGGVAANM---GVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWF 405
Cdd:PRK12492 364 GYGLTETSPVASTNpygELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWF 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 406 HTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVV-KIPGSRLTEM- 483
Cdd:PRK12492 444 KTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVaRDPGLSVEELk 523
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24648260 484 -----DIVEYVAKRLVVdhkqlhcgvfFLPELPKTGSGKVLRQQARDQA 527
Cdd:PRK12492 524 ayckeNFTGYKVPKHIV----------LRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
161-523 |
2.93e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 118.37 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 161 GMPRVEDLL----EPTTAELYYVPETLllGGDHTVAILCTSGTTGLPKAVC-----ISNSA---------------C--- 213
Cdd:PRK08315 170 GMLNFDELLalgrAVDDAELAARQATL--DPDDPINIQYTSGTTGFPKGATlthrnILNNGyfigeamklteedrlCipv 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 214 -LFD-FGFVTGqdVLLSFStidwsagmfnmlfsccHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTL 291
Cdd:PRK08315 248 pLYHcFGMVLG--NLACVT----------------HGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDF 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 292 NKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVAANMGVAKP-----SSVGRIVPGVRVKILD-EA 365
Cdd:PRK08315 310 ARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPlekrvTTVGRALPHLEVKIVDpET 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 366 GRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVI 445
Cdd:PRK08315 390 GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 446 AELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL----VVDHkqlhcgVFFLPELPKTGSGKV--- 518
Cdd:PRK08315 470 YTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIahykIPRY------IRFVDEFPMTVTGKIqkf 543
|
....*.
gi 24648260 519 -LRQQA 523
Cdd:PRK08315 544 kMREMM 549
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
34-521 |
3.61e-28 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 117.69 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 34 LFA-FMRNHPNSICQISdtEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSP 112
Cdd:cd12117 2 LFEeQAARTPDAVAVVY--GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 113 WQDEDTIKHLFSITRPKLIFCDGKCFQRLsiiarilkshvytlkdhRLGMPRVEDLLEPTTAELyyVPETLLLGGDHTVA 192
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRA-----------------GGLEVAVVIDEALDAGPA--GNPAVPVSPDDLAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVCISNSACL-----FDFGFVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDR--PYTPEYMIQ 265
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVrlvknTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKgtLLDPDALGA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 266 LVEKYKVTLL---TVVPQQVASllktptLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVAANM 342
Cdd:cd12117 221 LIAEEGVTVLwltAALFNQLAD------EDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSH 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 343 GVAKPSSV------GRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKR--MQD-YQG---WFHTGDM 410
Cdd:cd12117 295 VVTELDEVagsipiGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAErfVADpFGPgerLYRTGDL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 411 GYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVfGLWNEVDGDPA-AAAVVkiPGSRLTEMDIVEYV 489
Cdd:cd12117 375 ARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVV-VVREDAGGDKRlVAYVV--AEGALDAAELRAFL 451
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648260 490 AKRL----VVDHkqlhcgVFFLPELPKTGSGKVLRQ 521
Cdd:cd12117 452 RERLpaymVPAA------FVVLDELPLTANGKVDRR 481
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
48-523 |
1.25e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 115.83 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 48 ISDTEGTaLTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITR 127
Cdd:cd12114 6 VICGDGT-LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 128 PKL-IFCDGKCFQRlsiIARILKSHVYTLKDHRLGMPrVEDLLEPTtaELYYVpetlllggdhtvaiLCTSGTTGLPKAV 206
Cdd:cd12114 85 ARLvLTDGPDAQLD---VAVFDVLILDLDALAAPAPP-PPVDVAPD--DLAYV--------------IFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 207 CISNSACL---FDFG--F-VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITD--RPYTPEYMIQLVEKYKVTLLTVV 278
Cdd:cd12114 145 MISHRAALntiLDINrrFaVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDeaRRRDPAHWAELIERHGVTLWNSV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 279 PQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQ-ISYGYAlTEcGGVAAN---MGVAKPS--SV-- 350
Cdd:cd12114 225 PALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARlISLGGA-TE-ASIWSIyhpIDEVPPDwrSIpy 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 351 GRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKR--MQDYQG--WFHTGDMGYFDNENYLHIVERKE 426
Cdd:cd12114 303 GRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 427 DLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDHKQLHcgVFF 506
Cdd:cd12114 383 GQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSR--VIA 460
|
490
....*....|....*..
gi 24648260 507 LPELPKTGSGKVLRQQA 523
Cdd:cd12114 461 LEALPLTANGKVDRAAL 477
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
53-522 |
2.12e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 115.09 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 53 GTALTNGEAITFAIRIAQQLKAMGLkqddvVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIF 132
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAERVAGARR-----VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 CDgkcfqrlsiiarilkshvytLKDHRLGMPRVEDLLEPTTAELYYVPETlllggDHTVAILCTSGTTGLPKAVCISNSA 212
Cdd:PRK07787 98 GP--------------------APDDPAGLPHVPVRLHARSWHRYPEPDP-----DAPALIVYTSGTTGPPKGVVLSRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 213 ------CLFDFGFVTGQDVLLSfstidwsaG--MFN-------MLFSCCHGSTRIITDRPyTPEYMIQLVEKyKVTLLTV 277
Cdd:PRK07787 153 iaadldALAEAWQWTADDVLVH--------GlpLFHvhglvlgVLGPLRIGNRFVHTGRP-TPEAYAQALSE-GGTLYFG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 278 VPQQVASLLKTPTLNKqRLASIRFVSVGGGSCYVANLLKLQEflITGQ-ISYGYALTEC---GGVAANmGVAKPSSVGRI 353
Cdd:PRK07787 223 VPTVWSRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAA--LTGHrPVERYGMTETlitLSTRAD-GERRPGWVGLP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 354 VPGVRVKILDEAGRSLGH-GET-GEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKE-DLLR 430
Cdd:PRK07787 299 LAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 431 FHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVkiPGSRLTEMDIVEYVAKRLVVdHKQLHcGVFFLPEL 510
Cdd:PRK07787 379 SGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSV-HKRPR-EVRFVDAL 454
|
490
....*....|..
gi 24648260 511 PKTGSGKVLRQQ 522
Cdd:PRK07787 455 PRNAMGKVLKKQ 466
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
193-522 |
2.85e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 115.09 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAV--------CISNSACLFDfgfvtgQDVLLSFSTIDWSAGMFN------MLFSCCHGSTrIITDRPY 258
Cdd:PRK13383 179 VLLTSGTTGKPKGVprapqlrsAVGVWVTILD------RTRLRTGSRISVAMPMFHglglgmLMLTIALGGT-VLTHRHF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQR--LASIRFVsVGGGSCYVANLLklQEFLIT-GQISY-GYALTE 334
Cdd:PRK13383 252 DAEAALAQASLHRADAFTAVPVVLARILELPPRVRARnpLPQLRVV-MSSGDRLDPTLG--QRFMDTyGDILYnGYGSTE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 CG-GVAANMGVAK--PSSVGRIVPGVRVKILDEAGRSLGHGETGEILVhnGKVWNGYYANPNESKRMQDyqGWFHTGDMG 411
Cdd:PRK13383 329 VGiGALATPADLRdaPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFV--GGELAGTRYTDGGGKAVVD--GMTSTGDMG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 412 YFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAK 491
Cdd:PRK13383 405 YLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKD 484
|
330 340 350
....*....|....*....|....*....|.
gi 24648260 492 RlvVDHKQLHCGVFFLPELPKTGSGKVLRQQ 522
Cdd:PRK13383 485 R--VSRFEQPRDINIVSSIPRNPTGKVLRKE 513
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
38-529 |
2.90e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.95 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 38 MRNHPNSICqISDTEGTALTNGEAITFAIRIAQQLKAmGLKQDDVVGIVGTNTTYLMPVVLGCLLNG-TP----FHAvsp 112
Cdd:PRK08633 625 AKRNWSRLA-VADSTGGELSYGKALTGALALARLLKR-ELKDEENVGILLPPSVAGALANLALLLAGkVPvnlnYTA--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 113 wqDEDTIKHLFSITRPKLIFCDGKCFQRLSIIARILKS----HVYTLKDHRLGMPRVEDLLEPTTAELyyVP----ETLL 184
Cdd:PRK08633 700 --SEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELpenvKVIYLEDLKAKISKVDKLTALLAARL--LParllKRLY 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 185 LGG---DHTVAILCTSGTTGLPKAV------CISNSACLFDFGFVTGQDVLLSFSTIDWSAGM-FNMLFSCCHGSTRIIT 254
Cdd:PRK08633 776 GPTfkpDDTATIIFSSGSEGEPKGVmlshhnILSNIEQISDVFNLRNDDVILSSLPFFHSFGLtVTLWLPLLEGIKVVYH 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 255 DRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGggscyvANLLKL-------QEFLITgqIS 327
Cdd:PRK08633 856 PDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAG------AEKLKPevadafeEKFGIR--IL 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 328 YGYALTECGGVAA-NM------GVA-----KPSSVGRIVPGVRVKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNE 394
Cdd:PRK08633 928 EGYGATETSPVASvNLpdvlaaDFKrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 395 SK---RMQDYQGWFHTGDMGYFDNENYLHIVERkedLLRF---------HGAqyspqeIEQVIAELpdvieacvfglwne 462
Cdd:PRK08633 1008 TAeviKDIDGIGWYVTGDKGHLDEDGFLTITDR---YSRFakiggemvpLGA------VEEELAKA-------------- 1064
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24648260 463 VDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDH-----KQLHCGVFFLP-------ELPKTGSGKVLRQQARDQALG 529
Cdd:PRK08633 1065 LGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEElkraiKESGLPNLWKPsryfkveALPLLGSGKLDLKGLKELALA 1143
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
67-525 |
3.02e-27 |
|
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: 114.70 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDgkcfqrlsiiar 146
Cdd:cd12118 41 RLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD------------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 147 ilKSHVYtlkdhrlgmprvEDLL---EPTTAELYYVPEtlllggDHTVAILCTSGTTGLPKAVCISNSAClfdfgFVTGQ 223
Cdd:cd12118 109 --REFEY------------EDLLaegDPDFEWIPPADE------WDPIALNYTSGTTGRPKGVVYHHRGA-----YLNAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 224 DVLLSF-----STIDWSAGMFNmlfscCHGSTRI----------ITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKT 288
Cdd:cd12118 164 ANILEWemkqhPVYLWTLPMFH-----CNGWCFPwtvaavggtnVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 289 PTLNKQRLASIRFVSVGGGSCYVANLLKLQEflITGQISYGYALTECGGVAAnMGVAKPSSVGriVP-----------GV 357
Cdd:cd12118 239 PPSDARPLPHRVHVMTAGAPPPAAVLAKMEE--LGFDVTHVYGLTETYGPAT-VCAWKPEWDE--LPteerarlkarqGV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 358 RVKILDEA-------GRSLGH-GET-GEILVHNGKVWNGYYANPnESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDL 428
Cdd:cd12118 314 RYVGLEEVdvldpetMKPVPRdGKTiGEIVFRGNIVMKGYLKNP-EATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 429 LRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdPAAAAVVKiPGSRLTEMDIVEYVAKRLVvdHKQLHCGV 504
Cdd:cd12118 393 IISGGENISSVEVEGVLYKHPAVLEAAVVARpdekWGEV---PCAFVELK-EGAKVTEEEIIAFCREHLA--GFMVPKTV 466
|
490 500
....*....|....*....|.
gi 24648260 505 FFLPeLPKTGSGKVLRQQARD 525
Cdd:cd12118 467 VFGE-LPKTSTGKIQKFVLRD 486
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
67-538 |
3.74e-27 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 115.50 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSIIAR 146
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 147 ILKSHVYTLKDHRLGMPRVEDLLEPTTAELYYvpETLLLGGDHTVAILC----------------TSGTTGLPKAVCISN 210
Cdd:PLN03102 131 LLSSEDSNLNLPVIFIHEIDFPKRPSSEELDY--ECLIQRGEPTPSLVArmfriqdehdpislnyTSGTTADPKGVVISH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 211 SACLFDfgfvtgqdvLLSfSTIDWSAGMFNM------LFSC----------CHGSTRIITDRPYTPEyMIQLVEKYKVTL 274
Cdd:PLN03102 209 RGAYLS---------TLS-AIIGWEMGTCPVylwtlpMFHCngwtftwgtaARGGTSVCMRHVTAPE-IYKNIEMHNVTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 275 LTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEflITGQISYGYALTECGG----------------- 337
Cdd:PLN03102 278 MCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGpvlfcewqdewnrlpen 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 338 ----VAANMGVakpSSVGRIVPGVR-VKILDEAGRSlghGET-GEILVHNGKVWNGYYANPNESKRMQDYqGWFHTGDMG 411
Cdd:PLN03102 356 qqmeLKARQGV---SILGLADVDVKnKETQESVPRD---GKTmGEIVIKGSSIMKGYLKNPKATSEAFKH-GWLNTGDVG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 412 YFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFG----LWNEVdgdPAAAAVVK---------IPGS 478
Cdd:PLN03102 429 VIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAmphpTWGET---PCAFVVLEkgettkedrVDKL 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 479 RLTEMDIVEYVAKRLvvDHKQLHCGVFFLPELPKTGSGKVLRQQARDQALGKKWADHGNG 538
Cdd:PLN03102 506 VTRERDLIEYCRENL--PHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVEDEDNV 563
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
192-526 |
3.79e-26 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 112.17 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 192 AILCTSGTTGLPKAVciSNSACLFDFGFV---------TGQDVLLSFSTIDWSAGMFNMLFSC-CHGSTRIITDRP-YTP 260
Cdd:cd05928 178 AIYFTSGTTGSPKMA--EHSHSSLGLGLKvngrywldlTASDIMWNTSDTGWIKSAWSSLFEPwIQGACVFVHHLPrFDP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 261 EYMIQLVEKYKVTLLTVVPQQVASLLKtptlnkQRLASIRFVSVGggSCYVANLLKLQEFL-----ITG-QISYGYALTE 334
Cdd:cd05928 256 LVILKTLSSYPITTFCGAPTVYRMLVQ------QDLSSYKFPSLQ--HCVTGGEPLNPEVLekwkaQTGlDIYEGYGQTE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 CGGVAAN---MGVaKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKV-----WNGYYANPneSKRMQDYQGWFH 406
Cdd:cd05928 328 TGLICANfkgMKI-KPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIrpfglFSGYVDNP--EKTAATIRGDFY 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 407 -TGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPG------SR 479
Cdd:cd05928 405 lTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQflshdpEQ 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24648260 480 LTEmDIVEYVaKRLVVDHKQLHcGVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:cd05928 485 LTK-ELQQHV-KSVTAPYKYPR-KVEFVQELPKTVTGKIQRNELRDK 528
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
30-527 |
4.12e-26 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 111.78 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 30 IGKILFAFMRNHPNSIcqisdtegtALTNGEA-ITFA------IRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCL- 101
Cdd:COG1021 27 LGDLLRRRAERHPDRI---------AVVDGERrLSYAeldrraDRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 102 -----LNGTPFHAVSpwqdEdtIKHLFSITRPKLIFCDGKC----FQRLsiiARILKSHVYTLKdHRLgmprVEDLLEPT 172
Cdd:COG1021 98 agaipVFALPAHRRA----E--ISHFAEQSEAVAYIIPDRHrgfdYRAL---ARELQAEVPSLR-HVL----VVGDAGEF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 173 TA--ELYYVPETLLL----GGDhtVAILCTS-GTTGLPKAvcI-------------SNSACLFDfgfvtGQDVLLSFSTI 232
Cdd:COG1021 164 TSldALLAAPADLSEprpdPDD--VAFFQLSgGTTGLPKL--IprthddylysvraSAEICGLD-----ADTVYLAALPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 233 dwsagMFNMLFSC-------CHGSTRIITDRPYtPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVG 305
Cdd:COG1021 235 -----AHNFPLSSpgvlgvlYAGGTVVLAPDPS-PDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 306 GGSC--YVANLLKlQEFLITGQISYGYAltEcgG------------VAANmgvakpsSVGR-IVPGVRVKILDEAGRSLG 370
Cdd:COG1021 309 GAKLspELARRVR-PALGCTLQQVFGMA--E--GlvnytrlddpeeVILT-------TQGRpISPDDEVRIVDEDGNPVP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 371 HGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPD 450
Cdd:COG1021 377 PGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 451 VIEACVFGLWNEVDGDPAAAAVVkIPGSRLTEMDIVEYVAKRLVVDHK---QLHcgvfFLPELPKTGSGKVLRQQARDQA 527
Cdd:COG1021 457 VHDAAVVAMPDEYLGERSCAFVV-PRGEPLTLAELRRFLRERGLAAFKlpdRLE----FVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
163-527 |
4.80e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 111.66 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 163 PRVEDLLEPTTAELYYVPetllLGGDHTVAILCTSGTTGLPKAVCISN-------SACLFDFGfVTGQDV-LLSFSTIDW 234
Cdd:PRK13388 129 PAYAELVAAAGALTPHRE----VDAMDPFMLIFTSGTTGAPKAVRCSHgrlafagRALTERFG-LTRDDVcYVSMPLFHS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 235 SAGMFNMLFSCCHGSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRfvsVGGGScyVANL 314
Cdd:PRK13388 204 NAVMAGWAPAVASGAAVALPAK-FSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLR---VAFGN--EASP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 315 LKLQEFL--ITGQISYGYALTECGGVAANMGVAKPSSVGRIVPGVR-----------VKILDEAGRSLGHGET-GEILVH 380
Cdd:PRK13388 278 RDIAEFSrrFGCQVEDGYGSSEGAVIVVREPGTPPGSIGRGAPGVAiynpetltecaVARFDAHGALLNADEAiGELVNT 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 381 NG-KVWNGYYANPN-ESKRMQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFG 458
Cdd:PRK13388 358 AGaGFFEGYYNNPEaTAERMRH--GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24648260 459 LWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDHKQLHCGVFFLPELPKTGSGKVLRQQARDQA 527
Cdd:PRK13388 436 VPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-529 |
6.02e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 113.03 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLI 131
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 132 FCDGKCFQRLSiiarilkshvytlkdhRLGMPRVedLLEptTAELYYVPETLL---LGGDHTVAILCTSGTTGLPKAVCI 208
Cdd:COG1020 578 LTQSALAARLP----------------ELGVPVL--ALD--ALALAAEPATNPpvpVTPDDLAYVIYTSGSTGRPKGVMV 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 209 SNSA--CLFD-----FGFvTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDR--PYTPEYMIQLVEKYKVTLLTVVP 279
Cdd:COG1020 638 EHRAlvNLLAwmqrrYGL-GPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPeaRRDPAALAELLARHRVTVLNLTP 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 280 QQVASLLKTPTlnkQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTE------CGGVAANMGVAKPSSVGRI 353
Cdd:COG1020 717 SLLRALLDAAP---EALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTEttvdstYYEVTPPDADGGSVPIGRP 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 354 VPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYY-----------ANPNES--KRMqdyqgwFHTGDMGYFdnenylh 420
Cdd:COG1020 794 IANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLnrpeltaerfvADPFGFpgARL------YRTGDLARW------- 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 421 iveRKEDLLRFHG---AQ-----Y--SPQEIEQVIAELPDVIEACVFgLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVA 490
Cdd:COG1020 861 ---LPDGNLEFLGradDQvkirgFriELGEIEAALLQHPGVREAVVV-AREDAPGDKRLVAYVVPEAGAAAAAALLRLAL 936
|
490 500 510
....*....|....*....|....*....|....*....
gi 24648260 491 KRLVVDHKQLHCgVFFLPELPKTGSGKVLRQQARDQALG 529
Cdd:COG1020 937 ALLLPPYMVPAA-VVLLLPLPLTGNGKLDRLALPAPAAA 974
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
27-522 |
1.89e-25 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 109.34 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 27 DCSIGKILFAFMRNHPNSICQISDteGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGT- 105
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 106 PFHAVsPWQDEDTIKHLFSITRPKLIfcdgkcfqrlsIIARilkshVYTLKDHRlgmPRVEDLLEPttaelyyVPETLLL 185
Cdd:cd05920 92 PVLAL-PSHRRSELSAFCAHAEAVAY-----------IVPD-----RHAGFDHR---ALARELAES-------IPEVALF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 ggdhtvaiLCTSGTTGLPKAV---------CISNSA--CLFDfgfvtGQDVLLsfstidwsAGM---FNMLFSC------ 245
Cdd:cd05920 145 --------LLSGGTTGTPKLIprthndyayNVRASAevCGLD-----QDTVYL--------AVLpaaHNFPLACpgvlgt 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 246 -CHGSTRIITDRPyTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGScYVANLLKLQEFLITG 324
Cdd:cd05920 204 lLAGGRVVLAPDP-SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGAR-LSPALARRVPPVLGC 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 325 QISYGYALTEcgGVAANMGVAKPSSV-----GR-IVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRM 398
Cdd:cd05920 282 TLQQVFGMAE--GLLNYTRLDDPDEViihtqGRpMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 399 QDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVkIPGS 478
Cdd:cd05920 360 FTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVV-LRDP 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24648260 479 RLTEMDIVEYVAKRLVVDHKqLHCGVFFLPELPKTGSGKVLRQQ 522
Cdd:cd05920 439 PPSAAQLRRFLRERGLAAYK-LPDRIEFVDSLPLTAVGKIDKKA 481
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
8-534 |
2.33e-25 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 110.27 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 8 FDKYTKI--WSG--PRPASFFDADCSIGKILF----AFMRNHPNSICQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQ 79
Cdd:cd05968 36 YEPPYQTldLSGgkPWAAWFVGGRMNIVEQLLdkwlADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 80 DDVVGIVGTNTTYLMPVVLGCLLNGTpfhAVSPwqdedtikhLFS-------ITR-----PKLIFC-DGkcFQR------ 140
Cdd:cd05968 116 GDRVGIYLPMIPEIVPAFLAVARIGG---IVVP---------IFSgfgkeaaATRlqdaeAKALITaDG--FTRrgrevn 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 141 LSIIARILKSHVYTLKD---HR-----LGMPRVEDLLEPTTAELYYvPETLLLGGDHTVAILCTSGTTGLPKAvCISNSA 212
Cdd:cd05968 182 LKEEADKACAQCPTVEKvvvVRhlgndFTPAKGRDLSYDEEKETAG-DGAERTESEDPLMIIYTSGTTGKPKG-TVHVHA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 213 CL-----FDFGF---VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRII----TDRPyTPEYMIQLVEKYKVTLLTVVPQ 280
Cdd:cd05968 260 GFplkaaQDMYFqfdLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgaPDHP-KADRLWRMVEDHEITHLGLSPT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 281 QVASLL--KTPTLNKQRLASIR-----------------FVSVGGGSCYVANLLKLQEflITGQISYGYALTECggvaan 341
Cdd:cd05968 339 LIRALKprGDAPVNAHDLSSLRvlgstgepwnpepwnwlFETVGKGRNPIINYSGGTE--ISGGILGNVLIKPI------ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 342 mgvaKPSSVGRIVPGVRVKILDEAGRSLgHGETGEILVHngKVW----NGYYANPNES-----KRMQDYqgWFHtGDMGY 412
Cdd:cd05968 411 ----KPSSFNGPVPGMKADVLDESGKPA-RPEVGELVLL--APWpgmtRGFWRDEDRYletywSRFDNV--WVH-GDFAY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 413 FDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGsrLTEMDIVEYVAKR 492
Cdd:cd05968 481 YDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPG--VTPTEALAEELME 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 24648260 493 LVVDH--KQLHC-GVFFLPELPKTGSGKVLRQQARDQALGKKWAD 534
Cdd:cd05968 559 RVADElgKPLSPeRILFVKDLPKTRNAKVMRRVIRAAYLGKELGD 603
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
186-528 |
3.36e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 109.00 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 GGDHTVAILCTSGTTGLPKAVCISNSACLFD-------FGFVTGQDVLLS---FST----IDWSAGMfnmlfsCCHGStr 251
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCTHRKVASAgvmlaqrFGLGPDDVCYVSmplFHSnavmAGWAVAL------AAGAS-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 252 IITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGS------------CYVANllklqe 319
Cdd:PRK07867 222 IALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGApgdiarfarrfgCVVVD------ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 320 flitgqisyGYALTEcGGVA-ANMGVAKPSSVGRIVPGVRV-----------KILDEAGRSLGHGETGEILVHNGKVW-N 386
Cdd:PRK07867 296 ---------GFGSTE-GGVAiTRTPDTPPGALGPLPPGVAIvdpdtgtecppAEDADGRLLNADEAIGELVNTAGPGGfE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 387 GYYANPN-ESKRMQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDG 465
Cdd:PRK07867 366 GYYNDPEaDAERMRG--GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVG 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648260 466 DPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDHKQLHCGVFFLPELPKTGSGKVLRQQARDQAL 528
Cdd:PRK07867 444 DQVMAALVLAPGAKFDPDAFAEFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
180-522 |
4.83e-25 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 107.78 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 180 PETLLLGGDHTVAILCTSGTTGLPKAVCIS--NSACLF-----DFGFvTGQDVLLSF--STIDWSA-GMFNMLFsccHGS 249
Cdd:cd17643 85 PSLLLTDPDDLAYVIYTSGSTGRPKGVVVShaNVLALFaatqrWFGF-NEDDVWTLFhsYAFDFSVwEIWGALL---HGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 250 TRIITdrPY----TPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQE--FLIT 323
Cdd:cd17643 161 RLVVV--PYevarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGrfGLDR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 324 GQISYGYALTE-CGGV------AANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYY------- 389
Cdd:cd17643 239 PQLVNMYGITEtTVHVtfrpldAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLgrpelta 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 390 ----ANP--NESKRMqdyqgwFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVfGLWNEV 463
Cdd:cd17643 319 erfvANPfgGPGSRM------YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAV-IVREDE 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24648260 464 DGDPA-AAAVVKIPGSRLTEMDIVEYVAKRLvVDHkqLHCGVF-FLPELPKTGSGKVLRQQ 522
Cdd:cd17643 392 PGDTRlVAYVVADDGAAADIAELRALLKELL-PDY--MVPARYvPLDALPLTVNGKLDRAA 449
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
196-524 |
5.29e-25 |
|
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: 107.56 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKA----------VC---------------ISNSACLFdFGFvtGQDVLLSFStidWSAGMFNMLFScchgst 250
Cdd:cd05958 105 TSGTTGAPKAtmhfhrdplaSAdryavnvlrlreddrFVGSPPLA-FTF--GLGGVLLFP---FGVGASGVLLE------ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 251 riitdrPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRfVSVGGGSCYVANLLKLQEFLITGQISYGY 330
Cdd:cd05958 173 ------EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLR-KCVSAGEALPAALHRAWKEATGIPIIDGI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 331 ALTECGGV--AANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGkvwNGYYANPNESKRMQDYQGWFHTG 408
Cdd:cd05958 246 GSTEMFHIfiSARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 409 DMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEY 488
Cdd:cd05958 323 DTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLAREL 402
|
330 340 350
....*....|....*....|....*....|....*...
gi 24648260 489 V--AKRLVVDHKQLHcGVFFLPELPKTGSGKVLRQQAR 524
Cdd:cd05958 403 QdhAKAHIAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
52-520 |
6.46e-25 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 107.75 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLI 131
Cdd:cd17646 20 EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 132 FCDGKcfqrlsiiarilkshvytLKDHRLGMPRVEDLLEPTTAELYYVPETLLLGGDHTVAILCTSGTTGLPKAVCISNS 211
Cdd:cd17646 100 LTTAD------------------LAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 212 ACL-------FDFGFVTGQDVL----LSFSTIDWSagmfnMLFSCCHGSTRIITdRPYT---PEYMIQLVEKYKVTLLTV 277
Cdd:cd17646 162 GIVnrllwmqDEYPLGPGDRVLqktpLSFDVSVWE-----LFWPLVAGARLVVA-RPGGhrdPAYLAALIREHGVTTCHF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 278 VPQQVASLLKTPTLnkQRLASIRFVSVGGGSCYVANLLKLQEfLITGQISYGYALTEcggVAANM------GVAKPSSV- 350
Cdd:cd17646 236 VPSMLRVFLAEPAA--GSCASLRRVFCSGEALPPELAARFLA-LPGAELHNLYGPTE---AAIDVthwpvrGPAETPSVp 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 351 -GRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYY-----------ANP-NESKRMqdyqgwFHTGDMGYFDNEN 417
Cdd:cd17646 310 iGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLgrpaltaerfvPDPfGPGSRM------YRTGDLARWRPDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 418 YLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFglwneVDGDPAAAA------VVKIPGSRLTEMDIVEYVAK 491
Cdd:cd17646 384 ALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVV-----ARAAPAGAArlvgyvVPAAGAAGPDTAALRAHLAE 458
|
490 500
....*....|....*....|....*....
gi 24648260 492 RLVvdHKQLHCGVFFLPELPKTGSGKVLR 520
Cdd:cd17646 459 RLP--EYMVPAAFVVLDALPLTANGKLDR 485
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
193-524 |
6.53e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 108.17 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAV---------------CISNSACLFDfgfVTGQDVLLSFSTIDWSA-----GMFNMLfscchGSTRI 252
Cdd:PRK13390 153 MLYSSGTTGFPKGIqpdlpgrdvdapgdpIVAIARAFYD---ISESDIYYSSAPIYHAAplrwcSMVHAL-----GGTVV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 253 ITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQR--LASIRFVSVGGGSCYVANLLKLQEFLitGQISYGY 330
Cdd:PRK13390 225 LAKR-FDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRydVSSLRAVIHAAAPCPVDVKHAMIDWL--GPIVYEY 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 331 -ALTECGG---VAANMGVAKPSSVGRIVPGVrVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQD--YQGW 404
Cdd:PRK13390 302 ySSTEAHGmtfIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHpaHPFW 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 405 FHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTE-- 482
Cdd:PRK13390 381 TTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDel 460
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24648260 483 -MDIVEYVAKRLVvdHKQLHCGVFFLPELPKTGSGKVLRQQAR 524
Cdd:PRK13390 461 aRELIDYTRSRIA--HYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
196-527 |
8.79e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 107.56 E-value: 8.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSACL--F-----DFGfVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITdRPYTPEYMIQLVE 268
Cdd:PRK07638 151 TSGSTGKPKAFLRAQQSWLhsFdcnvhDFH-MKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLM-RKFIPNQVLDKLE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 269 KYKVTLLTVVPQQVASLLKtptLNKQRLASIRFVSVGG-------GSCYVANL-LKLQEFLITGQISYGYALTEcggvaa 340
Cdd:PRK07638 229 TENISVMYTVPTMLESLYK---ENRVIENKMKIISSGAkweaeakEKIKNIFPyAKLYEFYGASELSFVTALVD------ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 341 NMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYyANPNESKRMQDYQGWFHTGDMGYFDNENYLH 420
Cdd:PRK07638 300 EESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIY 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 421 IVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdpaAAAVVKipgSRLTEMDIVEYVAKRLVVD 496
Cdd:PRK07638 379 IVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVpdsyWGEK-----PVAIIK---GSATKQQLKSFCLQRLSSF 450
|
330 340 350
....*....|....*....|....*....|...
gi 24648260 497 H--KQLHcgvfFLPELPKTGSGKVLRQQARDQA 527
Cdd:PRK07638 451 KipKEWH----FVDEIPYTNSGKIARMEAKSWI 479
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
56-475 |
1.56e-24 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 106.92 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDG 135
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 136 KCfqrlsiiarilkshvytlkdhrlgmprvEDLlepttaelyyvpetlllggdhtVAILCTSGTTGLPKAVCISNSACLF 215
Cdd:cd17639 86 KP----------------------------DDL----------------------ACIMYTSGSTGNPKGVMLTHGNLVA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 216 D--------FGFVTGQDVLLSFSTIdwsAGMFNMLF-SCC--------HGSTRIITD----------RPYTPEYMI---Q 265
Cdd:cd17639 116 GiaglgdrvPELLGPDDRYLAYLPL---AHIFELAAeNVClyrggtigYGSPRTLTDkskrgckgdlTEFKPTLMVgvpA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 266 LVEKYKVTLLTVVPQ------------------QVASLLKTPTLNKQRLASIRFVSVG-------GGSCYVAnllKLQEF 320
Cdd:cd17639 193 IWDTIRKGVLAKLNPmgglkrtlfwtayqsklkALKEGPGTPLLDELVFKKVRAALGGrlrymlsGGAPLSA---DTQEF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 321 L--ITGQISYGYALTE--CGGVAANMGVAKPSSVGRIVPGVRVKILD--EAGRSLGHGET-GEILVHNGKVWNGYYANPN 393
Cdd:cd17639 270 LniVLCPVIQGYGLTEtcAGGTVQDPGDLETGRVGPPLPCCEIKLVDweEGGYSTDKPPPrGEILIRGPNVFKGYYKNPE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 394 ESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQE-IEQVIAELPDVIEACVFglwnevdGDPAAAAV 472
Cdd:cd17639 350 KTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEkLESIYRSNPLVNNICVY-------ADPDKSYP 422
|
...
gi 24648260 473 VKI 475
Cdd:cd17639 423 VAI 425
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
65-526 |
2.00e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 106.76 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 65 AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSII 144
Cdd:PRK06018 49 ALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 145 ARILKSH----VYTLKDHrlgMPRV--------EDLLEPTTAELYY--VPEtlllggdHTVAILC-TSGTTGLPKAVCIS 209
Cdd:PRK06018 129 ADKLPSVeryvVLTDAAH---MPQTtlknavayEEWIAEADGDFAWktFDE-------NTAAGMCyTSGTTGDPKGVLYS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 210 NSACLFDFGFVTGQDVLlSFSTID--------WSAGMFNMLFSCCHGSTRIITDRPYTPEYMI-QLVEKYKVTLLTVVPQ 280
Cdd:PRK06018 199 HRSNVLHALMANNGDAL-GTSAADtmlpvvplFHANSWGIAFSAPSMGTKLVMPGAKLDGASVyELLDTEKVTFTAGVPT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 281 QVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLItgQISYGYALTECGGVAAnMGVAKPS------------ 348
Cdd:PRK06018 278 VWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGV--EVRHAWGMTEMSPLGT-LAALKPPfsklpgdarldv 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 349 --SVGRIVPGVRVKILDEAGRSLGH-GET-GEILVHNGKVWNGYYanpNESKRMQDYQGWFHTGDMGYFDNENYLHIVER 424
Cdd:PRK06018 355 lqKQGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 425 KEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEY----VAKRLVVDHkql 500
Cdd:PRK06018 432 SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYmdgkIAKWWMPDD--- 508
|
490 500
....*....|....*....|....*.
gi 24648260 501 hcgVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:PRK06018 509 ---VAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
56-530 |
3.25e-24 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 107.04 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDG 135
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 136 kcfqrlSIIARILKSHVYTLKDHRLGMPRVEdllePTTAELyyvpetllLGGDHTVAILCTSGTTGLPKAVcISNSACLF 215
Cdd:PRK06060 111 ------ALRDRFQPSRVAEAAELMSEAARVA----PGGYEP--------MGGDALAYATYTSGTTGPPKAA-IHRHADPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 216 DFG--------FVTGQDVLLSFSTIDWSAGMFNML-FSCCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLL 286
Cdd:PRK06060 172 TFVdamcrkalRLTPEDTGLCSARMYFAYGLGNSVwFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 287 KTPTLNKQRlaSIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGG--VAANMGVAKPSSVGRIVPGVRVKILDE 364
Cdd:PRK06060 252 DSCSPDSFR--SLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQtfVSNRVDEWRLGTLGRVLPPYEIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 365 AGRSLGHGETGEILVHNGKVWNGYYANPNEskrMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQV 444
Cdd:PRK06060 330 DGTTAGPGVEGDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 445 IAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEmDIVEYVAKRLV-------VDHKqlhcgvFFLPE-LPKTGSG 516
Cdd:PRK06060 407 IIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDG-SVMRDLHRGLLnrlsafkVPHR------FAVVDrLPRTPNG 479
|
490
....*....|....
gi 24648260 517 KVLRQQARDQALGK 530
Cdd:PRK06060 480 KLVRGALRKQSPTK 493
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
196-520 |
4.47e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 106.13 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSA---------------------CLFDFGFVTGQdvllsfstidwSAGMFNMLfscCHGSTRIIT 254
Cdd:PRK04319 213 TSGSTGKPKGVLHVHNAmlqhyqtgkyvldlheddvywCTADPGWVTGT-----------SYGIFAPW---LNGATNVID 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 255 DRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLK--TPTLNKQRLASIRFV-SVGGgscyvanllKLQ-EFLITGQISYG- 329
Cdd:PRK04319 279 GGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLVKKYDLSSLRHIlSVGE---------PLNpEVVRWGMKVFGl 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 330 -----YALTECGG-VAAN---MGVaKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGkvW----NGYYANPnesK 396
Cdd:PRK04319 350 pihdnWWMTETGGiMIANypaMDI-KPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKG--WpsmmRGIWNNP---E 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 397 RMQDY--QGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVK 474
Cdd:PRK04319 424 KYESYfaGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAL 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24648260 475 IPGSRLTE---MDIVEYVAKRL--VVDHKQLHcgvfFLPELPKTGSGKVLR 520
Cdd:PRK04319 504 RPGYEPSEelkEEIRGFVKKGLgaHAAPREIE----FKDKLPKTRSGKIMR 550
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
56-458 |
1.93e-23 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 103.70 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCdG 135
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV-G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 136 KCFQRLSI-------IARILKSHVYTLKDHRlgmpRVEDLLEPTTAELyyvpETLLLGGDHTVAILCTSGTTGLPKAVCI 208
Cdd:cd05932 86 KLDDWKAMapgvpegLISISLPPPSAANCQY----QWDDLIAQHPPLE----ERPTRFPEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 209 SNSACLF-------DFGfVTGQDVLLSFSTIdwsAGMFNMLFscCHGSTRIITDRPYTPEYM---IQLVEKYKVTLLTVV 278
Cdd:cd05932 158 TFGSFAWaaqagieHIG-TEENDRMLSYLPL---AHVTERVF--VEGGSLYGGVLVAFAESLdtfVEDVQRARPTLFFSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 279 PQ-----QVASLLKTPTLNKQRLASIRFVS------------------VGGGSCYVANLLKLQEFLITGQISYGYALTE- 334
Cdd:cd05932 232 PRlwtkfQQGVQDKIPQQKLNLLLKIPVVNslvkrkvlkglgldqcrlAGCGSAPVPPALLEWYRSLGLNILEAYGMTEn 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 CGGVAANM-GVAKPSSVGRIVPGVRVKIldeagrslghGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYF 413
Cdd:cd05932 312 FAYSHLNYpGRDKIGTVGNAGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGEL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24648260 414 DNENYLHIVERKEDLLRFHGAQY-SPQEIEQVIAELPDVIEACVFG 458
Cdd:cd05932 382 DADGNLTITGRVKDIFKTSKGKYvAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
30-528 |
1.95e-23 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 104.11 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 30 IGKILFAFMRNHPNSICQISDteGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTpfhA 109
Cdd:PLN02860 9 ICQCLTRLATLRGNAVVTISG--NRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGG---I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 110 VSP----WQDEDTiKHLFSITRPKLIFCDGKC---FQRLSIIA-RILKSHVYTLKDHRLGMPRVEDLLEP--------TT 173
Cdd:PLN02860 84 VAPlnyrWSFEEA-KSAMLLVRPVMLVTDETCsswYEELQNDRlPSLMWQVFLESPSSSVFIFLNSFLTTemlkqralGT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 174 AELYYV--PETlllggdhtVAILC-TSGTTGLPKAVCISNSA----CLFDFGFV--TGQDVLLSFSTI----DWSAGMFN 240
Cdd:PLN02860 163 TELDYAwaPDD--------AVLICfTSGTTGRPKGVTISHSAlivqSLAKIAIVgyGEDDVYLHTAPLchigGLSSALAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 241 MLFSCCHgstriitdrPYTPEY----MIQLVEKYKVTLLTVVPQQVASLLKT--PTLNKQRLASIRFVSVGGGSCYVANL 314
Cdd:PLN02860 235 LMVGACH---------VLLPKFdakaALQAIKQHNVTSMITVPAMMADLISLtrKSMTWKVFPSVRKILNGGGSLSSRLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 315 LKLQEFLITGQISYGYALTE-CGGV----------------AANMGVAKPSS--------VGRIVPGVRVKI-LDEAGRs 368
Cdd:PLN02860 306 PDAKKLFPNAKLFSAYGMTEaCSSLtfmtlhdptlespkqtLQTVNQTKSSSvhqpqgvcVGKPAPHVELKIgLDESSR- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 369 lghgeTGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAEL 448
Cdd:PLN02860 385 -----VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 449 PDVieacvfglwnevdgdpAAAAVVKIPGSRLTEMDI---------------VEYVAKRLVVDHKQL--HCGV-----FF 506
Cdd:PLN02860 460 PGV----------------ASVVVVGVPDSRLTEMVVacvrlrdgwiwsdneKENAKKNLTLSSETLrhHCREknlsrFK 523
|
570 580 590
....*....|....*....|....*....|
gi 24648260 507 LPEL--------PKTGSGKVLRQQARDQAL 528
Cdd:PLN02860 524 IPKLfvqwrkpfPLTTTGKIRRDEVRREVL 553
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
18-535 |
2.78e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 103.28 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 18 PRPASFFDadcsigkILFAFMRNHPNSICQISdtEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVV 97
Cdd:PRK06164 7 PRADTLAS-------LLDAHARARPDAVALID--EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 98 LGCLLNGTPFHAVSPWQDEDTIKHLFSITRPK-LIFCDGkcFQRL---SIIARILKSHVYTLK-------------DHRL 160
Cdd:PRK06164 78 LACARLGATVIAVNTRYRSHEVAHILGRGRARwLVVWPG--FKGIdfaAILAAVPPDALPPLRaiavvddaadatpAPAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 161 GMPRVEDLLEPTTAelyyVPETLLLGGDHTVAILC--TSGTTGLPKAVCISNS-------ACLFDFGFVTGqDVLLSFST 231
Cdd:PRK06164 156 GARVQLFALPDPAP----PAAAGERAADPDAGALLftTSGTTSGPKLVLHRQAtllrharAIARAYGYDPG-AVLLAALP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 232 IDWSAGmFNMLFSCCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTpTLNKQRLASIR---FVSVGGGS 308
Cdd:PRK06164 231 FCGVFG-FSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDT-AGERADFPSARlfgFASFAPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 309 CYVANLLKLQEFLITGQisYG----YALTECGGVAAnmgvakPSSV-----GRIV-PGVRVKILD-EAGRSLGHGETGEI 377
Cdd:PRK06164 309 GELAALARARGVPLTGL--YGssevQALVALQPATD------PVSVrieggGRPAsPEARVRARDpQDGALLPDGESGEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 378 LVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVF 457
Cdd:PRK06164 381 EIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 458 GLwnEVDGDPAAAA-VVKIPGSRLTEMDIVEYVAKRLVvdHKQLHCGVFFLPELPKTGSG---KVLRQQARDQALgkKWA 533
Cdd:PRK06164 461 GA--TRDGKTVPVAfVIPTDGASPDEAGLMAACREALA--GFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQ--ARL 534
|
..
gi 24648260 534 DH 535
Cdd:PRK06164 535 AA 536
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
178-521 |
4.45e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 103.28 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 178 YVPetllLGGDHTVAILCTSGTTGLPKAVCISNSACL----FDFGFVTGQD---VLLSFSTIDWSAgmFNMLF--SCCHG 248
Cdd:PTZ00237 248 YVP----VESSHPLYILYTSGTTGNSKAVVRSNGPHLvglkYYWRSIIEKDiptVVFSHSSIGWVS--FHGFLygSLSLG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 249 STRI-----ITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKT-PTLNKQR----LASIRFVSVGGG------SCYVA 312
Cdd:PTZ00237 322 NTFVmfeggIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdPEATIIRskydLSNLKEIWCGGEvieesiPEYIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 313 NLLKLQEFLITGQISYGYALTECGGVaanmgVAKP-SSVGRIVPGVRVKILDEAGRSLGHGETGEI---LVHNGKVWNGY 388
Cdd:PTZ00237 402 NKLKIKSSRGYGQTEIGITYLYCYGH-----INIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVafkLPMPPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 389 YANPNESKRM-QDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGD- 466
Cdd:PTZ00237 477 YKNDEKFKQLfSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNv 556
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24648260 467 PAAAAVVKIPGS--------------RLTEMDIVEYVAKRLVVdhkqlhcgvfFLPELPKTGSGKVLRQ 521
Cdd:PTZ00237 557 PIGLLVLKQDQSnqsidlnklkneinNIITQDIESLAVLRKII----------IVNQLPKTKTGKIPRQ 615
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
193-519 |
5.45e-23 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 102.66 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVCISNS----------ACLFDFGfvtGQDVLLSFSTIDWSAGMFNMLFS--CCHGSTRIITDRPY-- 258
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGgylvyaattmKYVFDYG---PGDIYWCTADVGWVTGHSYLLYGplACGATTLLYEGVPNwp 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVPQQVASLLK--TPTLNKQRLASIRFVS-----------------VGGGSCYVANLlklqe 319
Cdd:cd17634 314 TPARMWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSSLRILGsvgepinpeayewywkkIGKEKCPVVDT----- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 320 fliTGQISYGyaltecGGVAANMGVAKPSSVG---RIVPGVRVKILDEAGRSLGHGETGEILVhnGKVWNG----YYANP 392
Cdd:cd17634 389 ---WWQTETG------GFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVI--TDPWPGqtrtLFGDH 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 393 NEskRMQDY----QGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPA 468
Cdd:cd17634 458 ER--FEQTYfstfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAP 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 469 AAAVV----KIPGSRLTEmDIVEYVAKRL--VVDHKQLHcgvfFLPELPKTGSGKVL 519
Cdd:cd17634 536 YAYVVlnhgVEPSPELYA-ELRNWVRKEIgpLATPDVVH----WVDSLPKTRSGKIM 587
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
172-458 |
1.16e-22 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 100.90 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 172 TTAELYYV-----PETLLL--GGDHTVAILCTSGTTGLPKAVCISNSACLFDF----GFVTGQ--DVLLSFSTIdW---- 234
Cdd:cd17640 65 SVEELLYIlnhseSVALVVenDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIrslsDIVPPQpgDRFLSILPI-Whsye 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 235 -SAGMFnmLFSCchGSTRIITdrpyTPEYMIQLVEKYKVTLLTVVPQQVASL-------LKTPTLNKQRLA-------SI 299
Cdd:cd17640 144 rSAEYF--IFAC--GCSQAYT----SIRTLKDDLKRVKPHYIVSVPRLWESLysgiqkqVSKSSPIKQFLFlfflsggIF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 300 RFVSVGGGSC--YVANLlklqeFLITG-QISYGYALTECGGVAANMGVAKP--SSVGRIVPGVRVKILDEAGRS-LGHGE 373
Cdd:cd17640 216 KFGISGGGALppHVDTF-----FEAIGiEVLNGYGLTETSPVVSARRLKCNvrGSVGRPLPGTEIKIVDPEGNVvLPPGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 374 TGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKED--LLRfHGAQYSPQEIEQVIAELPDV 451
Cdd:cd17640 291 KGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFI 369
|
....*..
gi 24648260 452 IEACVFG 458
Cdd:cd17640 370 EQIMVVG 376
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
56-458 |
2.13e-22 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 100.75 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQ--DDVVGIVGTNTTYLMPVVLGCllNGTPFHAVsPWQD---EDTIKHLFSITRPKL 130
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELAC--YAYSLVTV-PLYDtlgPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 131 IFCDgKCFQrlsiiarilkshVYTLKD-HRLGMPRVEDLLEPTtaelyyvPETLllggdhtvAILC-TSGTTGLPKAVCI 208
Cdd:cd05927 83 VFCD-AGVK------------VYSLEEfEKLGKKNKVPPPPPK-------PEDL--------ATICyTSGTTGNPKGVML 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 209 ------SNSACLFDFGFVTG----QDVLLSFSTIdwsAGMF---NMLFSCCHGS--------TRIITDRpytpeymiqlV 267
Cdd:cd05927 135 thgnivSNVAGVFKILEILNkinpTDVYISYLPL---AHIFervVEALFLYHGAkigfysgdIRLLLDD----------I 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 268 EKYKVTLLTVVP-------------QQVASLLKTPTLN-----------------------------KQRLAS-IRFVSV 304
Cdd:cd05927 202 KALKPTVFPGVPrvlnriydkifnkVQAKGPLKRKLFNfalnyklaelrsgvvraspfwdklvfnkiKQALGGnVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 305 GGGSCYVANLLKLQEFLITgQISYGYALTEC--GGVAANMGVAKPSSVGRIVPGVRVKILD--EAG-RSLGHGETGEILV 379
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGC-PVLEGYGQTECtaGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 380 HNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRF-HGAQYSPQEIEQVIAELPDVIEACVFG 458
Cdd:cd05927 361 RGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
349-526 |
2.58e-22 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 100.39 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 349 SVGRIVPGVRVKILDEAG-RSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQ------GWFHTGDMGYFdNENYLHI 421
Cdd:cd05931 356 SCGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALaatdegGWLRTGDLGFL-HDGELYI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 422 VERKEDLLRFHGAQYSPQEIEQVIAELPDVIE---ACVFGlwneVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL---VV 495
Cdd:cd05931 435 TGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFS----VPDDGEERLVVVAEVERGADPADLAAIAAAIraaVA 510
|
170 180 190
....*....|....*....|....*....|....
gi 24648260 496 DHKQLH-CGVFFLP--ELPKTGSGKVLRQQARDQ 526
Cdd:cd05931 511 REHGVApADVVLVRpgSIPRTSSGKIQRRACRAA 544
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
141-525 |
3.14e-22 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 99.31 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 141 LSIIArILKSH-VYTLKDHRLGMPRVEDLLEPTTAelyyvpeTLLL---GGDHTVAILCTSGTTGLPKAVCISNSACL-- 214
Cdd:cd17653 62 VAILA-ILKAGaAYVPLDAKLPSARIQAILRTSGA-------TLLLttdSPDDLAYIIFTSGSTGIPKGVMVPHRGVLny 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 215 -----FDFGFVTGQDVLLSFS-TIDWSAGMfnmLFSC-CHGSTRIITDRPYTPEYMIQlvekyKVTLLTVVPqqvaSLLK 287
Cdd:cd17653 134 vsqppARLDVGPGSRVAQVLSiAFDACIGE---IFSTlCNGGTLVLADPSDPFAHVAR-----TVDALMSTP----SILS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 288 TptLNKQRLASIRFVSVGGGSCyVANLLKLQEFLITGQISYGYALTECGGVAANMGVAKPSSVGRIVPGVRVKILDEAGR 367
Cdd:cd17653 202 T--LSPQDFPNLKTIFLGGEAV-PPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 368 SLGHGETGEILVHNGKVWNGYYANPNESKR----MQDYQGW--FHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEI 441
Cdd:cd17653 279 PVPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 442 EQVIAELPdvieacvfglwNEVDGdpAAAAVVkipGSRL----TEMDI-VEYVAKRLVVDHKQLHCGVFF--LPELPKTG 514
Cdd:cd17653 359 EEVVLQSQ-----------PEVTQ--AAAIVV---NGRLvafvTPETVdVDGLRSELAKHLPSYAVPDRIiaLDSFPLTA 422
|
410
....*....|.
gi 24648260 515 SGKVLRQQARD 525
Cdd:cd17653 423 NGKVDRKALRE 433
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
188-479 |
7.17e-22 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 99.12 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVAILCTSGTTGLPKAVCISNS-------AClFDFGFVTGQDVLLSFSTiDWSAGMFN--MLFSCCHGSTRIITDRPY 258
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHAnllanqrAC-LKFFSPKEDDVMMSFLP-PFHAYGFNscTLFPLLSGVPVVFAYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGG----SCYvANLLKLQEFLITGQisyGYALTE 334
Cdd:PRK06334 261 YPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDafkdSLY-QEALKTFPHIQLRQ---GYGTTE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 CGGVAANMGVAKP---SSVGRIVPGVRVKILDEAGR-SLGHGETGEILVHNGKVWNGYYAN-PNESKRMQDYQGWFHTGD 409
Cdd:PRK06334 337 CSPVITINTVNSPkheSCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEdFGQGFVELGGETWYVTGD 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 410 MGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAElpdvieacVFGLWNEVDGDPaaAAVVKIPGSR 479
Cdd:PRK06334 417 LGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME--------GFGQNAADHAGP--LVVCGLPGEK 476
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
65-532 |
8.23e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 99.01 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 65 AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDgkcfqrLSII 144
Cdd:PRK07008 49 AKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD------LTFL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 145 ARI--LKSHVYTLKdHRLGMPRVEDLLEPTTAELYYvpETLLLGGD----------HTVAILC-TSGTTGLPKAVCISN- 210
Cdd:PRK07008 123 PLVdaLAPQCPNVK-GWVAMTDAAHLPAGSTPLLCY--ETLVGAQDgdydwprfdeNQASSLCyTSGTTGNPKGALYSHr 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 211 -------SACLFDFGFVTGQDVLLS----FSTIDWSagmfnMLFSCCHGSTRIITDRPYTP-EYMIQLVEKYKVTLLTVV 278
Cdd:PRK07008 200 stvlhayGAALPDAMGLSARDAVLPvvpmFHVNAWG-----LPYSAPLTGAKLVLPGPDLDgKSLYELIEAERVTFSAGV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 279 PQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITgQISYGYALTE-------CGGVAANMGVAKPSSV- 350
Cdd:PRK07008 275 PTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGV-EVIHAWGMTEmsplgtlCKLKWKHSQLPLDEQRk 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 351 -----GRIVPGVRVKILDEAGRSLGH-GET-GEILVHNGKVWNGYYANpnESKRMQDyqGWFHTGDMGYFDNENYLHIVE 423
Cdd:PRK07008 354 llekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRG--DASPLVD--GWFPTGDVATIDADGFMQITD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 424 RKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEvdgDPaAAAVVKIPGSRLTEMDIVEY----VAKRLVV 495
Cdd:PRK07008 430 RSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkWDE---RP-LLVVVKRPGAEVTREELLAFyegkVAKWWIP 505
|
490 500 510
....*....|....*....|....*....|....*..
gi 24648260 496 DHkqlhcgVFFLPELPKTGSGKVLRQQARDQALGKKW 532
Cdd:PRK07008 506 DD------VVFVDAIPHTATGKLQKLKLREQFRDYVL 536
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
52-520 |
1.79e-21 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 97.05 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPwqdedtikhlfsiTRPKli 131
Cdd:cd17649 9 GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDP-------------EYPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 132 fcdgkcfQRLSiiarilkshvYTLKDHRLGMprvedLLEPTTAELYYVpetlllggdhtvaiLCTSGTTGLPKAVCISNS 211
Cdd:cd17649 74 -------ERLR----------YMLEDSGAGL-----LLTHHPRQLAYV--------------IYTSGSTGTPKGVAVSHG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 212 A----CLFDFGF--VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRP--YTPEYMIQLVEKYKVTLLTVVP---Q 280
Cdd:cd17649 118 PlaahCQATAERygLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPaylQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 281 QVASLLKTPTlnKQRLASIRFVSVGG---GSCYVANLLKLQEFLITGqisygYALTE---------CGGVAANMGVAKPs 348
Cdd:cd17649 198 QLAEEADRTG--DGRPPSLRLYIFGGealSPELLRRWLKAPVRLFNA-----YGPTEatvtplvwkCEAGAARAGASMP- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 349 sVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPN-------ESKRMQDYQGWFHTGDMG-YFDNENYlH 420
Cdd:cd17649 270 -IGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPEltaerfvPDPFGAPGSRLYRTGDLArWRDDGVI-E 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 421 IVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwNEVDGDPAAAAVVKIPGSRLTEMD--IVEYVAKRLvVDHK 498
Cdd:cd17649 348 YLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELRaqLRTALRASL-PDYM 425
|
490 500
....*....|....*....|..
gi 24648260 499 QLHcGVFFLPELPKTGSGKVLR 520
Cdd:cd17649 426 VPA-HLVFLARLPLTPNGKLDR 446
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
52-520 |
3.06e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 96.59 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLI 131
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 132 FCDGKCFQRLSiiarilkshvytlkdhrlGMPRVEDLLEPTTAELYYVPETLLLGgDHTVAILCTSGTTGLPKAVCIS-- 209
Cdd:cd12116 89 LTDDALPDRLP------------------AGLPVLLLALAAAAAAPAAPRTPVSP-DDLAYVIYTSGSTGRPKGVVVShr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 210 NSACLF-----DFGfVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYT--PEYMIQLVEKYKVTLLTVVPQQV 282
Cdd:cd12116 150 NLVNFLhsmreRLG-LGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQrdPEALARLIEAHSITVMQATPATW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 283 ASLLKTptlNKQRLASIRFVSvgGGSCYVANLLklQEFLITGQISYG-YALTEC---GGVAANMGVAKPSSVGRIVPGVR 358
Cdd:cd12116 229 RMLLDA---GWQGRAGLTALC--GGEALPPDLA--ARLLSRVGSLWNlYGPTETtiwSTAARVTAAAGPIPIGRPLANTQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 359 VKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNE-SKRMQD--YQG----WFHTGDMGYFDNENYLHIVERKEDLLRF 431
Cdd:cd12116 302 VYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALtAERFVPdpFAGpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 432 HGAQYSPQEIEQVIAELPDVIEACVFgLWNEvDGDPAAAAVVKIP-GSRLTEMDIVEYVAKRL----VVDHkqlhcgVFF 506
Cdd:cd12116 382 RGHRIELGEIEAALAAHPGVAQAAVV-VRED-GGDRRLVAYVVLKaGAAPDAAALRAHLRATLpaymVPSA------FVR 453
|
490
....*....|....
gi 24648260 507 LPELPKTGSGKVLR 520
Cdd:cd12116 454 LDALPLTANGKLDR 467
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
67-475 |
5.15e-21 |
|
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: 96.72 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNT-----TYLMPVVLGCLlngtpfhAVSPWQD--EDTIKHLFSITRPKLIFCDG--KC 137
Cdd:cd17641 23 AFALGLLALGVGRGDVVAILGDNRpewvwAELAAQAIGAL-------SLGIYQDsmAEEVAYLLNYTGARVVIAEDeeQV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 138 FQRLSIIARI--LKSHVYTlkDHRlGM-----PRV---EDLLEPTTAELYYVP---ETLLLGGD-HTVAILC-TSGTTGL 202
Cdd:cd17641 96 DKLLEIADRIpsVRYVIYC--DPR-GMrkyddPRLisfEDVVALGRALDRRDPglyEREVAAGKgEDVAVLCtTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 203 PKAVCISN------SACLFDFGFVTGQDVLLSFSTIDWsagMFNMLFSCCHG-STRIITDRPYTPEYMIQLVEKYKVTLL 275
Cdd:cd17641 173 PKLAMLSHgnflghCAAYLAADPLGPGDEYVSVLPLPW---IGEQMYSVGQAlVCGFIVNFPEEPETMMEDLREIGPTFV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 276 TVVPQ-------QVASLLKTPTLNKQRLASI---------------RFVSVGGGSCY-VANLL---KLQEFL-------- 321
Cdd:cd17641 250 LLPPRvwegiaaDVRARMMDATPFKRFMFELgmklglraldrgkrgRPVSLWLRLASwLADALlfrPLRDRLgfsrlrsa 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 322 ITGQISYG-----------------YALTECGG--VAANMGVAKPSSVGRIVPGVRVKIldeagrslghGETGEILVHNG 382
Cdd:cd17641 330 ATGGAALGpdtfrffhaigvplkqlYGQTELAGayTVHRDGDVDPDTVGVPFPGTEVRI----------DEVGEILVRSP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 383 KVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRF-HGAQYSPQEIEQVIAELPDVIEACVFGlwn 461
Cdd:cd17641 400 GVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVVLG--- 476
|
490
....*....|....
gi 24648260 462 evDGDPAAAAVVKI 475
Cdd:cd17641 477 --AGRPYLTAFICI 488
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
53-525 |
8.78e-21 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 95.11 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 53 GTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIF 132
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 CDgkcfqrlsiiarilkshvytlkdhrlgmprvedlleptTAELYYvpetlllggdhtvailcTSGTTGLPKAVCISNSA 212
Cdd:cd05940 81 VD--------------------------------------AALYIY-----------------TSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 213 CLFDFGFVTG------QDVLLSFSTIDWSAGMFNMLFSCC-HGSTRIITDRpYTPEYMIQLVEKYKVTLLTVVPQQVASL 285
Cdd:cd05940 106 AWRGGAFFAGsggalpSDVLYTCLPLYHSTALIVGWSACLaSGATLVIRKK-FSASNFWDDIRKYQATIFQYIGELCRYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 286 LKTPTLNKQRLASIRFVSVGG--GSCYVanllKLQEFLITGQISYGYALTECGGVAANMGvAKPSSVGRIVPGVR----- 358
Cdd:cd05940 185 LNQPPKPTERKHKVRMIFGNGlrPDIWE----EFKERFGVPRIAEFYAATEGNSGFINFF-GKPGAIGRNPSLLRkvapl 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 359 --VK--------ILDEAGR--SLGHGETGEILVHNGKVWN--GYyANPNES--KRMQDY--QG--WFHTGDMGYFDNENY 418
Cdd:cd05940 260 alVKydlesgepIRDAEGRciKVPRGEPGLLISRINPLEPfdGY-TDPAATekKILRDVfkKGdaWFNTGDLMRLDGEGF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 419 LHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwnEV---DGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVV 495
Cdd:cd05940 339 WYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGV--QVpgtDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPG 416
|
490 500 510
....*....|....*....|....*....|....
gi 24648260 496 DHKQLHcgVFFLPELPKTGSGK----VLRQQARD 525
Cdd:cd05940 417 YARPLF--LRLQPEMEITGTFKqqkvDLRNEGFD 448
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
180-521 |
1.22e-20 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 94.63 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 180 PETLLLGGDHTVAILCTSGTTGLPKAV-----CISN-SACLFDFGFVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRII 253
Cdd:cd17652 85 PALLLTTPDNLAYVIYTSGSTGRPKGVvvthrGLANlAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 254 TDRPYT--PEYMIQLVEKYKVTLLTVVPQQVASLlktPTLNkqrLASIRFVSVGGGSCyVANLLKlqEFLITGQISYGYA 331
Cdd:cd17652 165 APAEELlpGEPLADLLREHRITHVTLPPAALAAL---PPDD---LPDLRTLVVAGEAC-PAELVD--RWAPGRRMINAYG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 332 LTECGgVAANMGVAKPSS----VGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYY-----------ANP--NE 394
Cdd:cd17652 236 PTETT-VCATMAGPLPGGgvppIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLnrpgltaerfvADPfgAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 395 SKRMqdyqgwFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVfGLWNEVDGDPAAAA-VV 473
Cdd:cd17652 315 GSRM------YRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVV-VVRDDRPGDKRLVAyVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24648260 474 KIPGSRLTEMDIVEYVAKRL----VVDHkqlhcgVFFLPELPKTGSGKVLRQ 521
Cdd:cd17652 388 PAPGAAPTAAELRAHLAERLpgymVPAA------FVVLDALPLTPNGKLDRR 433
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
41-521 |
1.44e-20 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 94.72 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 41 HPNSICQISDteGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIK 120
Cdd:cd17651 8 TPDAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 121 HLFSITRPKLIFCDgkcfQRLSiiarilkshvytlkdHRLGMPRVEDLL--EPTTAELYYVPETLLLGGDHTVAILCTSG 198
Cdd:cd17651 86 FMLADAGPVLVLTH----PALA---------------GELAVELVAVTLldQPGAAAGADAEPDPALDADDLAYVIYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 199 TTGLPKAVCISnSACLFDFgfVTGQDVL---------LSFSTIDWSAGMFNMLFSCCHGST-RIITDRPYT-PEYMIQLV 267
Cdd:cd17651 147 STGRPKGVVMP-HRSLANL--VAWQARAsslgpgartLQFAGLGFDVSVQEIFSTLCAGATlVLPPEEVRTdPPALAAWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 268 EKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLklQEFLIT---GQISYGYALTE-----CGGVA 339
Cdd:cd17651 224 DEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDL--REFCAGlpgLRLHNHYGPTEthvvtALSLP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 340 ANMGVA-KPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPN------------ESKRMqdyqgwFH 406
Cdd:cd17651 302 GDPAAWpAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPEltaerfvpdpfvPGARM------YR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 407 TGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwNEVDGDPAAAA-VVKIPGSRLTEMDI 485
Cdd:cd17651 376 TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAR-EDRPGEKRLVAyVVGDPEAPVDAAEL 454
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24648260 486 VEYVAKRL----VVDHkqlhcgVFFLPELPKTGSGKVLRQ 521
Cdd:cd17651 455 RAALATHLpeymVPSA------FVLLDALPLTPNGKLDRR 488
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
164-520 |
1.45e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 94.31 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 164 RVEDLLEPTTAELyyvpetLLLGGDHTVAILCTSGTTGLPKAVCIS--NSACLFDF-GFVTGQD----VLLSFS-TIDWS 235
Cdd:cd12115 87 RLRFILEDAQARL------VLTDPDDLAYVIYTSGSTGRPKGVAIEhrNAAAFLQWaAAAFSAEelagVLASTSiCFDLS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 236 agMFNMLFSCCHGSTRIITDrpyTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNkqrlASIRFVSVGGGSCYVANLL 315
Cdd:cd12115 161 --VFELFGPLATGGKVVLAD---NVLALPDLPAAAEVTLINTVPSAAAELLRHDALP----ASVRVVNLAGEPLPRDLVQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 316 KLQEFLITGQISYGYALTE----CGGVAANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYAN 391
Cdd:cd12115 232 RLYARLQVERVVNLYGPSEdttySTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 392 PNES------------KRMqdYQgwfhTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL 459
Cdd:cd12115 312 PGLTaerflpdpfgpgARL--YR----TGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAI 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24648260 460 WNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLvvDHKQLHCGVFFLPELPKTGSGKVLR 520
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRL--PAYMVPSRFVRLDALPLTPNGKIDR 444
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
51-520 |
1.51e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 95.08 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 51 TEGT-ALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTN--TTYLmpVVLGCLLNGtpfhAVSPWQDED----TIKHLF 123
Cdd:PRK05857 36 CDGTsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNgpETYL--SVLACAKLG----AIAVMADGNlpiaAIERFC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 124 SITRPKLIfcdgkcfqrlsIIARILKSHVYTLKDHRLGMPRVEDLLEPTTAELYYVPET------LLLGGDHTVAILCTS 197
Cdd:PRK05857 110 QITDPAAA-----------LVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAaslagnADQGSEDPLAMIFTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 198 GTTGLPKAVCISNSAclfdfgFVTGQDVLLS--FSTIDWSA--------------GMFNMLFSCCHGSTrIITDRPYTPE 261
Cdd:PRK05857 179 GTTGEPKAVLLANRT------FFAVPDILQKegLNWVTWVVgettysplpathigGLWWILTCLMHGGL-CVTGGENTTS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 262 YMiQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLI-TGQIsygYALTECGGVAA 340
Cdd:PRK05857 252 LL-EILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEATGVrTAQV---YGLSETGCTAL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 341 -----NMGVAK--PSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHnGKVWN-------GYYANPNESKRMQdYQGWFH 406
Cdd:PRK05857 328 clptdDGSIVKieAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSASF-GTLWIkspanmlGYWNNPERTAEVL-IDGWVN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 407 TGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwnevdGDPAAAAVVKIPGSRLTEMDIV 486
Cdd:PRK05857 406 TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEI-----PDEEFGALVGLAVVASAELDES 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24648260 487 EYVA-KRLVVDHKQLH-------CGVFFLPELPKTGSGKVLR 520
Cdd:PRK05857 481 AARAlKHTIAARFRREsepmarpSTIVIVTDIPRTQSGKVMR 522
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
351-524 |
2.41e-20 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 94.69 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 351 GRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPnESKRMQDYQGWFHTGDMGYFdNENYLHIVERKEDLLR 430
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLII 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 431 FHGAQYSPQEIEQVIAELPDVI--EACVFGLwnEVDGDPAAAAVVKipgSRLTEMD----IVEYVAKRLVVDHkQLHCGV 504
Cdd:PRK09192 466 INGRNIWPQDIEWIAEQEPELRsgDAAAFSI--AQENGEKIVLLVQ---CRISDEErrgqLIHALAALVRSEF-GVEAAV 539
|
170 180
....*....|....*....|..
gi 24648260 505 FFLP--ELPKTGSGKVLRQQAR 524
Cdd:PRK09192 540 ELVPphSLPRTSSGKLSRAKAK 561
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
161-451 |
5.89e-20 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 93.04 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 161 GMPRVEDLLEPTTAELYYVPEtllLGGDHTVAILCTSGTTGLPKAVCISNSacLF---------DFGFVTGQDVLLSFSt 231
Cdd:PRK09274 150 GGTTLATLLRDGAAAPFPMAD---LAPDDMAAILFTSGSTGTPKGVVYTHG--MFeaqiealreDYGIEPGEIDLPTFP- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 232 idwsagMFnMLFSCCHGSTRIITD----RPYT--PEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVG 305
Cdd:PRK09274 224 ------LF-ALFGPALGMTSVIPDmdptRPATvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 306 GGSCYVANLLKLQEFLI-TGQISYGYALTECggvaanMGVAKPSS------------------VGRIVPGVRVKILD--- 363
Cdd:PRK09274 297 GAPVPIAVIERFRAMLPpDAEILTPYGATEA------LPISSIESreilfatraatdngagicVGRPVDGVEVRIIAisd 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 364 ------EAGRSLGHGETGEILVHNGKVWNGYYANPNESK--RMQDYQG--WFHTGDMGYFDNENYLHIVERKEDLLRFHG 433
Cdd:PRK09274 371 apipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRlaKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAG 450
|
330
....*....|....*...
gi 24648260 434 AQYSPQEIEQVIAELPDV 451
Cdd:PRK09274 451 GTLYTIPCERIFNTHPGV 468
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
17-526 |
1.24e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.26 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 17 GPRPASFFDAdcsigkilfAFMRNhPNSICQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPV 96
Cdd:PRK05852 15 GPRIADLVEV---------AATRL-PEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 97 VLGCLLNG---TPFHAVSPWQDEdTIKHLFSITRPKLIFCDGKCFQRLSIiARILKSHVYTLKDHRLGMPRVEDLLEPTT 173
Cdd:PRK05852 85 LLAASRADlvvVPLDPALPIAEQ-RVRSQAAGARVVLIDADGPHDRAEPT-TRWWPLTVNVGGDSGPSGGTLSVHLDAAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 174 AELYYVPETLLLGGDHTVaILCTSGTTGLPKAV-----CISNSACLFDFGFVTG-QDVLLSFSTIDWSAGMFNMLFSC-C 246
Cdd:PRK05852 163 EPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVpwthaNIASSVRAIITGYRLSpRDATVAVMPLYHGHGLIAALLATlA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 247 HGSTRIITDR-PYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRL--ASIRFVSVGGGSCYVANLLKLQ-EFLI 322
Cdd:PRK05852 242 SGGAVLLPARgRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQtEFAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 323 TGQISYGyaLTECGGVAANMGV----------AKPSSVGRIVpGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANP 392
Cdd:PRK05852 322 PVVCAFG--MTEATHQVTTTQIegigqtenpvVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 393 -NESKRMQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAA 471
Cdd:PRK05852 399 tITAANFTD--GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAV 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648260 472 VVKIPGSRLTEMDIVEYVAKRLvvdhkqlhcGVFFLP-------ELPKTGSGKVLRQQARDQ 526
Cdd:PRK05852 477 IVPRESAPPTAEELVQFCRERL---------AAFEIPasfqeasGLPHTAKGSLDRRAVAEQ 529
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
34-524 |
2.02e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 91.60 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 34 LFAFMRNHPNSICQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNG---TPFHAV 110
Cdd:PRK07768 8 MYANARTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGaslTMLHQP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 111 SPWQD-----EDTIKHLFSITRPKLIFcdGKCFQRLsiiarilkshVYTLKDHRLGMPRVEDLLEPTTAElyyVPETlll 185
Cdd:PRK07768 88 TPRTDlavwaEDTLRVIGMIGAKAVVV--GEPFLAA----------APVLEEKGIRVLTVADLLAADPID---PVET--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 gGDHTVAIL-CTSGTTGLPKAVCIS------NSACLFD-FGFVTGQDVLLSFSTIDWSAGMFNMLFS--CCHGSTRIITD 255
Cdd:PRK07768 150 -GEDDLALMqLTSGSTGSPKAVQIThgnlyaNAEAMFVaAEFDVETDVMVSWLPLFHDMGMVGFLTVpmYFGAELVKVTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 256 RPY--TPEYMIQLVEKYKVTLlTVVPQQVASLL-----KTPTLNKQRLASIRFVSVGGGSCYVANLlklQEFLITGQ--- 325
Cdd:PRK07768 229 MDFlrDPLLWAELISKYRGTM-TAAPNFAYALLarrlrRQAKPGAFDLSSLRFALNGAEPIDPADV---EDLLDAGArfg 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 326 -------ISYGYALT-------ECGG----------VAANMGVAKPS---------SVGRIVPGVRVKILDEAGRSLGHG 372
Cdd:PRK07768 305 lrpeailPAYGMAEAtlavsfsPCGAglvvdevdadLLAALRRAVPAtkgntrrlaTLGPPLPGLEVRVVDEDGQVLPPR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 373 ETGEILVHnGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVI 452
Cdd:PRK07768 385 GVGVIELR-GESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 453 EACV-------------FGLWNEVDGDPAAAAVVKIpgsrltEMDIVEYVAKRLVVDHKQLHcgvfFLP--ELPKTGSGK 517
Cdd:PRK07768 464 PGNAvavrldaghsregFAVAVESNAFEDPAEVRRI------RHQVAHEVVAEVGVRPRNVV----VLGpgSIPKTPSGK 533
|
....*..
gi 24648260 518 VLRQQAR 524
Cdd:PRK07768 534 LRRANAA 540
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
196-527 |
2.49e-19 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 90.32 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNS-------ACLFDFGFVTGqDVLLSFSTIDWSAGMFNMLFSCCH-GSTRIITDRP-YTPEYMIQL 266
Cdd:cd05974 93 TSGTTSKPKLVEHTHRsypvghlSTMYWIGLKPG-DVHWNISSPGWAKHAWSCFFAPWNaGATVFLFNYArFDAKRVLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 267 VEKYKVTLLtVVPQQVASLLKTPTLNKQRLAsIRFVsVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVAANM--GV 344
Cdd:cd05974 172 LVRYGVTTL-CAPPTVWRMLIQQDLASFDVK-LREV-VGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSpgQP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 345 AKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKV--WNGYYANPNE-SKRMQDyqGWFHTGDMGYFDNENYLHI 421
Cdd:cd05974 249 VKAGSMGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPVglMKGYAGDPDKtAHAMRG--GYYRTGDIAMRDEDGYLTY 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 422 VERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPG---SRLTEMDIVEYVAKRLvVDHK 498
Cdd:cd05974 327 VGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEIFRFSRERL-APYK 405
|
330 340
....*....|....*....|....*....
gi 24648260 499 QLHCGVFflPELPKTGSGKVLRQQARDQA 527
Cdd:cd05974 406 RIRRLEF--AELPKTISGKIRRVELRRRE 432
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
56-433 |
5.74e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 90.49 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPW-----QDEDTIKHLFSITRPKL 130
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAyslmsHDHAKLKHLFDLVKPRV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 131 IFC-DGKCFQRLSIIARILKS---HVYTLKDHRLGMPRVEDLLEPTTAELYYVPETLllgGDHTVA-ILCTSGTTGLPKA 205
Cdd:PRK12582 161 VFAqSGAPFARALAALDLLDVtvvHVTGPGEGIASIAFADLAATPPTAAVAAAIAAI---TPDTVAkYLFTSGSTGMPKA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 206 V-------C--ISNSACLFDFGFVTGQDVLLsfstiDW------SAG--MFNMLFSccHGSTRIITD-RPyTP---EYMI 264
Cdd:PRK12582 238 VintqrmmCanIAMQEQLRPREPDPPPPVSL-----DWmpwnhtMGGnaNFNGLLW--GGGTLYIDDgKP-LPgmfEETI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 265 QLVEKYKVTLLTVVPQQVASLL----KTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLI--TGQ---ISYGYALTEC 335
Cdd:PRK12582 310 RNLREISPTVYGNVPAGYAMLAeameKDDALRRSFFKNLRLMAYGGATLSDDLYERMQALAVrtTGHripFYTGYGATET 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 336 GGVAANMGVA--KPSSVGRIVPGVRVKILDEagrslghGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYF 413
Cdd:PRK12582 390 APTTTGTHWDteRVGLIGLPLPGVELKLAPV-------GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARF 462
|
410 420
....*....|....*....|
gi 24648260 414 DNENylhiveRKEDLLRFHG 433
Cdd:PRK12582 463 VDPD------DPEKGLIFDG 476
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
188-533 |
5.94e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 88.56 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVA-ILCTSGTTGLPKAVCISNSAcLFDFGFVT-------GQDVL-LSFSTIdwsAGMFNMLFSCCHGSTRIITDRP- 257
Cdd:PRK07824 34 DDDVAlVVATSGTTGTPKGAMLTAAA-LTASADAThdrlggpGQWLLaLPAHHI---AGLQVLVRSVIAGSEPVELDVSa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 258 -YTPEYMIQLVEKYKV--TLLTVVPQQVASLLKTPTlNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTe 334
Cdd:PRK07824 110 gFDPTALPRAVAELGGgrRYTSLVPMQLAKALDDPA-ATAALAELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSET- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 CGGVAANmgvakpssvGRIVPGVRVKILDeagrslGHGETGEILVHNGkvwngyYANPNESKRMQDyQGWFHTGDMGYFD 414
Cdd:PRK07824 188 SGGCVYD---------GVPLDGVRVRVED------GRIALGGPTLAKG------YRNPVDPDPFAE-PGWFRTDDLGALD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 415 NeNYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLV 494
Cdd:PRK07824 246 D-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLD 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24648260 495 VDH--KQLHcgvfFLPELPKTGSGKVLRqqardQALGKKWA 533
Cdd:PRK07824 325 RTAapRELH----VVDELPRRGIGKVDR-----RALVRRFA 356
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
193-529 |
1.29e-18 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 89.16 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVCISNS----------------------ACLFDFGFVTGQdvllsfstidwSAGMFNMLfscCHGST 250
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGgyllyaattfkyvfdyhpddiyWCTADIGWITGH-----------SYIVYGPL---ANGAT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 251 RIItdrpY--TPEY-----MIQLVEKYKVTLLTVVPQQVASLLKTPT--LNKQRLASIRFVS-----------------V 304
Cdd:cd05966 302 TVM----FegTPTYpdpgrYWDIVEKHKVTIFYTAPTAIRALMKFGDewVKKHDLSSLRVLGsvgepinpeawmwyyevI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 305 GGGSCyvanllklqeflitgQISYGYALTECGG-VAANMGVA---KPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVH 380
Cdd:cd05966 378 GKERC---------------PIVDTWWQTETGGiMITPLPGAtplKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 381 NGkvWNGY----YANPN--ESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEA 454
Cdd:cd05966 443 RP--WPGMartiYGDHEryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEA 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 455 CVFGLWNEVDGDPAAAAVV---KIPGSRLTEMDIVEYVAKRL----VVDHkqlhcgVFFLPELPKTGSGKVLRQQARDQA 527
Cdd:cd05966 521 AVVGRPHDIKGEAIYAFVTlkdGEEPSDELRKELRKHVRKEIgpiaTPDK------IQFVPGLPKTRSGKIMRRILRKIA 594
|
..
gi 24648260 528 LG 529
Cdd:cd05966 595 AG 596
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
52-521 |
1.75e-18 |
|
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: 88.00 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSP-WQDEdtikhlfsitrpkl 130
Cdd:cd17645 20 RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPdYPGE-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 131 ifcdgkcfqrlsiiarilkshvytlkdhrlgmpRVEDLLEPTTAELyyvpetLLLGGDHTVAILCTSGTTGLPKAVCISN 210
Cdd:cd17645 86 ---------------------------------RIAYMLADSSAKI------LLTNPDDLAYVIYTSGSTGLPKGVMIEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 211 SAcLFDFGF-------VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITD--RPYTPEYMIQLVEKYKVTLlTVVPQQ 281
Cdd:cd17645 127 HN-LVNLCEwhrpyfgVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPseRRLDLDALNDYFNQEGITI-SFLPTG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 282 VASllKTPTLNKQrlaSIRFVSVGGGscyvanllKLQEFLITG-QISYGYALTECGGVAANMGVAKPS---SVGRIVPGV 357
Cdd:cd17645 205 AAE--QFMQLDNQ---SLRVLLTGGD--------KLKKIERKGyKLVNNYGPTENTVVATSFEIDKPYaniPIGKPIDNT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 358 RVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNES------------KRMqdyqgwFHTGDMGYFDNENYLHIVERK 425
Cdd:cd17645 272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTaekfivhpfvpgERM------YRTGDLAKFLPDGNIEFLGRL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 426 EDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwNEVDGDPAAAAVVKIPgsrlTEMDIvEYVAKRLVVDHKQLHCGVF 505
Cdd:cd17645 346 DQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK-EDADGRKYLVAYVTAP----EEIPH-EELREWLKNDLPDYMIPTY 419
|
490
....*....|....*...
gi 24648260 506 F--LPELPKTGSGKVLRQ 521
Cdd:cd17645 420 FvhLKALPLTANGKVDRK 437
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
20-521 |
2.70e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.06 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 20 PASFFDADCsIGKILFAFMRNHPNSICQISDTEgtALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLG 99
Cdd:PRK12467 505 PATEYAPDC-VHQLIEAQARQHPERPALVFGEQ--VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 100 CLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSIIARIlkshvytlkdHRLGMPRVEDLLEPTTAELYYV 179
Cdd:PRK12467 582 VLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGL----------RSLCLDEPADLLCGYSGHNPEV 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 180 PetllLGGDHTVAILCTSGTTGLPKAVCISNSACLFDFGFV------TGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRII 253
Cdd:PRK12467 652 A----LDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIaerlqlAADDSMLMVSTFAFDLGVTELFGALASGATLHL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 254 TDRPYT--PEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRlaSIRFVSVGGGSCYVANLLKLQEFLITGQISYGYA 331
Cdd:PRK12467 728 LPPDCArdAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR--PQRALVCGGEALQVDLLARVRALGPGARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 332 LTE---------CGGVAANMGvakPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPN-ESKRM--- 398
Cdd:PRK12467 806 PTEttvgvstyeLSDEERDFG---NVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPAlTAERFvpd 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 399 ---QDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGlwneVDGDPAA---AAV 472
Cdd:PRK12467 883 pfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA----QPGDAGLqlvAYL 958
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24648260 473 VKIPGSRLTE----MDIVEYVAKRLVVDHkQLHCGVFFLPELPKTGSGKVLRQ 521
Cdd:PRK12467 959 VPAAVADGAEhqatRDELKAQLRQVLPDY-MVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
275-527 |
1.58e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.05 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 275 LTVVPQQVASLLktpTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGyaLTEcggVAANMGVAKPS------ 348
Cdd:PRK07445 211 LSLVPTQLQRLL---QLRPQWLAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYG--MTE---TASQIATLKPDdflagn 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 349 -SVGRIVPGVRVKILDeagrslghGETGEILVHNGKVWNGYYanPNeskrMQDYQGWFHTGDMGYFDNENYLHIVERKED 427
Cdd:PRK07445 283 nSSGQVLPHAQITIPA--------NQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 428 LLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----WNEVdgdpAAAAVVKIPGSrLTEMDIVEYVAKRLV-VDH-KQLH 501
Cdd:PRK07445 349 KIITGGENVYPAEVEAAILATGLVQDVCVLGLpdphWGEV----VTAIYVPKDPS-ISLEELKTAIKDQLSpFKQpKHWI 423
|
250 260
....*....|....*....|....*.
gi 24648260 502 CgvffLPELPKTGSGKVLRQQARDQA 527
Cdd:PRK07445 424 P----VPQLPRNPQGKINRQQLQQIA 445
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-517 |
2.03e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 83.97 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVC--------ISNSACLFDFG-FVTGQDVL----------------LSFSTIDWSA-GMFNMlfscc 246
Cdd:cd05924 8 ILYTGGTTGMPKGVMwrqedifrMLMGGADFGTGeFTPSEDAHkaaaaaagtvmfpappLMHGTGSWTAfGGLLG----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 247 hGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASllktPTLNKQR------LASIRFVSVGGGSCYVANLLKLQEF 320
Cdd:cd05924 83 -GQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMAR----PLIDALRdagpydLSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 321 LITGQISYGYALTECGGVAANMGVAKPSSVG-RIVPGVRVKILDEAGRSL--GHGETGEIlVHNGKVWNGYYANPNESKR 397
Cdd:cd05924 158 VPNITLVDAFGSSETGFTGSGHSAGSGPETGpFTRANPDTVVLDDDGRVVppGSGGVGWI-ARRGHIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 398 M---QDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVK 474
Cdd:cd05924 237 TfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24648260 475 IPGSRLTEMDIVEYVAKRLVvdHKQLHCGVFFLPELPKTGSGK 517
Cdd:cd05924 317 REGAGVDLEELREHCRTRIA--RYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
56-413 |
2.19e-17 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 85.32 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPW-----QDEDTIKHLFSITRPKL 130
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAyslvsQDFGKLRHVLELLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 131 IFC-DGKCFQRlsIIARILKSH--VYTLKDHRLGMPRV--EDLLEptTAELYYVPETLL-LGGDHTVAILCTSGTTGLPK 204
Cdd:PRK08180 150 VFAdDGAAFAR--ALAAVVPADveVVAVRGAVPGRAATpfAALLA--TPPTAAVDAAHAaVGPDTIAKFLFTSGSTGLPK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 205 AV-------CiSNSACL---FDFgFVTGQDVLLSFstIDWS---AGMFNMLFSCCHGSTRIITD-RPyTPEYMIQLVEKY 270
Cdd:PRK08180 226 AVinthrmlC-ANQQMLaqtFPF-LAEEPPVLVDW--LPWNhtfGGNHNLGIVLYNGGTLYIDDgKP-TPGGFDETLRNL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 271 KV---TLLTVVP----QQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLI--TGQ---ISYGYALTECGGV 338
Cdd:PRK08180 301 REispTVYFNVPkgweMLVPALERDAALRRRFFSRLKLLFYAGAALSQDVWDRLDRVAEatCGErirMMTGLGMTETAPS 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 339 AANMG--VAKPSSVGRIVPGVRVKILDEAGRSlghgetgEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYF 413
Cdd:PRK08180 381 ATFTTgpLSRAGNIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
53-534 |
3.69e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.78 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 53 GTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRpklif 132
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSG----- 3154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 cdgkcfqrlsiiARILKSHVYTLKDHRLGMPRVedLLEPTTAELYYVPETLLLGGDHTVAILCTSGTTGLPKAVCISNSA 212
Cdd:PRK12316 3155 ------------AQLLLSQSHLRLPLAQGVQVL--DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA 3220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 213 -CLFDFGFV-----TGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPY--TPEYMIQLVEKYKVTLLTVVPQQVAS 284
Cdd:PRK12316 3221 lSNHLCWMQqayglGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDwrDPALLVELINSEGVDVLHAYPSMLQA 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 285 LLKTPtlNKQRLASIRFVsVGGGSCYVANLlkLQEFLITGQISYGYALTECGGVAANMGVAKPSS----VGRIVPGVRVK 360
Cdd:PRK12316 3301 FLEEE--DAHRCTSLKRI-VCGGEALPADL--QQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKdavpIGRPIANRACY 3375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 361 ILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKR------MQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGA 434
Cdd:PRK12316 3376 ILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAErfvpdpFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGF 3455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 435 QYSPQEIEQVIAELPDVIEACVFglwnEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL----VVDHkqlhcgVFFLPEL 510
Cdd:PRK12316 3456 RIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLKASLpeymVPAH------LLFLERM 3525
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24648260 511 PKTGSGKVLR-----------QQA-------RDQALGKKWAD 534
Cdd:PRK12316 3526 PLTPNGKLDRkalprpdaallQQDyvapvneLERRLAAIWAD 3567
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
32-456 |
3.96e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 84.18 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 32 KILFAFMRNHPNSICQisDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVS 111
Cdd:PRK04813 6 ETIEEFAQTQPDFPAY--DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 112 PWQDEDTIKHLFSITRPKLIFC-DGKCFQRLSIiarilksHVYTLKDhrlgmprVEDLLEPTTAelyyVPETLLLGGDHT 190
Cdd:PRK04813 84 VSSPAERIEMIIEVAKPSLIIAtEELPLEILGI-------PVITLDE-------LKDIFATGNP----YDFDHAVKGDDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 191 VAILCTSGTTGLPKAVCISnSACL--F------DFGFVTGQDVL----LSF--STIDW-----SAGMFNMLfscchgsTR 251
Cdd:PRK04813 146 YYIIFTSGTTGKPKGVQIS-HDNLvsFtnwmleDFALPEGPQFLnqapYSFdlSVMDLyptlaSGGTLVAL-------PK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 252 IITDRPytpeymIQLVE---KYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISY 328
Cdd:PRK04813 218 DMTANF------KQLFEtlpQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 329 GYALTEcGGVAANmGVA---------KPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANP------- 392
Cdd:PRK04813 292 TYGPTE-ATVAVT-SIEitdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPektaeaf 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648260 393 NESKRMQDYqgwfHTGDMGYFDNeNYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACV 456
Cdd:PRK04813 370 FTFDGQPAY----HTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV 428
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
66-524 |
4.79e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 84.02 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 66 IRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCF----QRL 141
Cdd:cd05915 35 RRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLplveAIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 142 SIIARILKSHVYTLKdhrlgMPRVEDLLepTTAELYYVPETLLLGGDhTVAILCTSGTTGLPKAVCISNSACLFDfgfVT 221
Cdd:cd05915 115 GELKTVQHFVVMDEK-----APEGYLAY--EEALGEEADPVRVPERA-ACGMAYTTGTTGLPKGVVYSHRALVLH---SL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 222 GQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEYM-IQLVEKYKVTLLTVVPQQVASLLKTP----------- 289
Cdd:cd05915 184 AASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVlPGPRLDPASLVELFDGEGVTFTAGVPtvwlaladyle 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 290 TLNKQRLASIRFVSvgGGSCYVANLLKLQEfLITGQISYGYALTECGGVAA---------------NMGVAKPSSVGRIV 354
Cdd:cd05915 264 STGHRLKTLRRLVV--GGSAAPRSLIARFE-RMGVEVRQGYGLTETSPVVVqnfvkshleslseeeKLTLKAKTGLPIPL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 355 PGVRVkiLDEAGRSLGH-GETGEILVHNGK-VWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFH 432
Cdd:cd05915 341 VRLRV--ADEEGRPVPKdGKALGEVQLKGPwITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 433 GAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDpAAAAVVKIPGSRLTEMDIVEYvAKRLVVDHKQLHCGVFFLPELPK 512
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE-RPLAVVVPRGEKPTPEELNEH-LLKAGFAKWQLPDAYVFAEEIPR 496
|
490
....*....|..
gi 24648260 513 TGSGKVLRQQAR 524
Cdd:cd05915 497 TSAGKFLKRALR 508
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
25-493 |
6.90e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.77 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 25 DADCSIGKILFAFMRNHPNSICQISdtEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGC---- 100
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLF--EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLaklg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 101 ----LLNGTpfhavspwQDEDTIKHLFSITRPKLIFCDGKCFQRLSII------ARILKSHVYTLKDHRLGMPRVEDLLE 170
Cdd:PRK08279 112 avvaLLNTQ--------QRGAVLAHSLNLVDAKHLIVGEELVEAFEEAradlarPPRLWVAGGDTLDDPEGYEDLAAAAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 171 --PTTAElyyvPETLLLGGDHTVAILCTSGTTGLPKAVCISNSACL---FDFGFVTG---QDVLLSFSTIDWSAGmfnml 242
Cdd:PRK08279 184 gaPTTNP----ASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLkamGGFGGLLRltpDDVLYCCLPLYHNTG----- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 243 FSCCHGST-----RIITDRPYT-----PEymiqlVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRfvsvgggsCYVA 312
Cdd:PRK08279 255 GTVAWSSVlaagaTLALRRKFSasrfwDD-----VRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLR--------LMIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 313 NLLK-------LQEFLItGQISYGYALTEcggvaANMGVA----KPSSVGRiVPGVR------VK--------ILDEAGR 367
Cdd:PRK08279 322 NGLRpdiwdefQQRFGI-PRILEFYAASE-----GNVGFInvfnFDGTVGR-VPLWLahpyaiVKydvdtgepVRDADGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 368 SL--GHGETGEILvhnGKVWNGY----YANP--NESKRMQDY--QG--WFHTGDMGYFDNENYLHIVERKEDLLRFHGAQ 435
Cdd:PRK08279 395 CIkvKPGEVGLLI---GRITDRGpfdgYTDPeaSEKKILRDVfkKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGEN 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24648260 436 YSPQEIEQVIAELPDVIEACVFGLwnEV---DGDPAAAAVVKIPGSRLTEMDIVEYVAKRL 493
Cdd:PRK08279 472 VATTEVENALSGFPGVEEAVVYGV--EVpgtDGRAGMAAIVLADGAEFDLAALAAHLYERL 530
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
440-517 |
1.51e-16 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 74.12 E-value: 1.51e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24648260 440 EIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLvVDHKQLHcGVFFLPELPKTGSGK 517
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREEL-GPYAVPK-EVVFVDELPKTRSGK 76
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
189-523 |
5.08e-16 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 81.15 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 189 HTVAILCTSGTTGLPK---------AVCISNSACLFdFGFVTGqDVLLSFSTIDWSAGmfnmlfsccH----------GS 249
Cdd:PRK10524 234 EPSYILYTSGTTGKPKgvqrdtggyAVALATSMDTI-FGGKAG-ETFFCASDIGWVVG---------HsyivyapllaGM 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 250 TRIITD-RPYTPEYMI--QLVEKYKVTLLTVVPQQVASLLKTPT--LNKQRLASIRFVSVGGGScyvanllkLQEflITG 324
Cdd:PRK10524 303 ATIMYEgLPTRPDAGIwwRIVEKYKVNRMFSAPTAIRVLKKQDPalLRKHDLSSLRALFLAGEP--------LDE--PTA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 325 Q-ISYG--------YALTECGG--VAANMGVA----KPSSVGRIVPGVRVKILDEA-GRSLGHGETGeILVHNG------ 382
Cdd:PRK10524 373 SwISEAlgvpvidnYWQTETGWpiLAIARGVEdrptRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKG-VLVIEGplppgc 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 383 --KVWNgyyanpNESKRMQDYqgWFH-------TGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIE 453
Cdd:PRK10524 452 mqTVWG------DDDRFVKTY--WSLfgrqvysTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 454 ACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRL--VVDhKQLhcG-------VFFLPELPKTGSGKVLRQ--Q 522
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEKEImaLVD-SQL--GavarparVWFVSALPKTRSGKLLRRaiQ 600
|
.
gi 24648260 523 A 523
Cdd:PRK10524 601 A 601
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
42-520 |
6.43e-16 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 80.20 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 42 PNSICQISDTEgtALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPwqdedtikh 121
Cdd:cd17650 1 PDAIAVSDATR--QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDP--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 122 lfsitrpklifcdgkcfqrlsiiarilkshvytlkdhrlGMP--RVEDLLEPTTAELyyvpetLLLGGDHTVAILCTSGT 199
Cdd:cd17650 70 ---------------------------------------DYPaeRLQYMLEDSGAKL------LLTQPEDLAYVIYTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 200 TGLPKAVCIS-----NSACLFD--FGFVTGQDVLLSFSTI--DWSAGMFnmLFSCCHGSTRIIT--DRPYTPEYMIQLVE 268
Cdd:cd17650 105 TGKPKGVMVEhrnvaHAAHAWRreYELDSFPVRLLQMASFsfDVFAGDF--ARSLLNGGTLVICpdEVKLDPAALYDLIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 269 KYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKL-QEFLITGQISYGYALTECG-------GVAA 340
Cdd:cd17650 183 KSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLaARFGQGMRIINSYGVTEATidstyyeEGRD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 341 NMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESK------------RMqdyqgwFHTG 408
Cdd:cd17650 263 PLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAerfvenpfapgeRM------YRTG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 409 DMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVfgLWNEVDGDPAAAAVVKIPGSRLTEMDIVEY 488
Cdd:cd17650 337 DLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV--AVREDKGGEARLCAYVVAAATLNTAELRAF 414
|
490 500 510
....*....|....*....|....*....|....
gi 24648260 489 VAKRLvvdhKQLHCGVFFLP--ELPKTGSGKVLR 520
Cdd:cd17650 415 LAKEL----PSYMIPSYYVQldALPLTPNGKVDR 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
56-521 |
7.56e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.54 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 56 LTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDG 135
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 136 KCFQRLSIIARILkshvytlkdhRLGMPRVEDLLE-PTTAelyyvPETLLlGGDHTVAILCTSGTTGLPKAVCISNSAcL 214
Cdd:PRK12316 2109 HLLERLPLPAGVA----------RLPLDRDAEWADyPDTA-----PAVQL-AGENLAYVIYTSGSTGLPKGVAVSHGA-L 2171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 215 FDFGFVTGQ-------DVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRP-YTPEYMIQLVEKYKVTLLTVVPQQVASLL 286
Cdd:PRK12316 2172 VAHCQAAGEryelspaDCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDElWDPEQLYDEMERHGVTILDFPPVYLQQLA 2251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 287 KTPTLNKQRLAsIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTE---------CGGVAANMGVAKPssVGRIVPGV 357
Cdd:PRK12316 2252 EHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEavvtpllwkCRPQDPCGAAYVP--IGRALGNR 2328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 358 RVKILDEAGRSLGHGETGEILVHNGKVWNGYYANP-------------NESKRMqdyqgwFHTGDMGYFDNENYLHIVER 424
Cdd:PRK12316 2329 RAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPgltaerfvpdpfsASGERL------YRTGDLARYRADGVVEYLGR 2402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 425 KEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDHKQLHcgV 504
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAH--W 2479
|
490
....*....|....*..
gi 24648260 505 FFLPELPKTGSGKVLRQ 521
Cdd:PRK12316 2480 VVLERLPLNPNGKLDRK 2496
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
196-525 |
1.16e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 79.61 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAV----------CISNsaclfdfgfvtgqdvllsfsTIDWSAGMFNM------LFSC---CH-------GS 249
Cdd:PRK08162 190 TSGTTGNPKGVvyhhrgaylnALSN--------------------ILAWGMPKHPVylwtlpMFHCngwCFpwtvaarAG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 250 TRIITdRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLItgQISYG 329
Cdd:PRK08162 250 TNVCL-RKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGF--DLTHV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 330 YALTECGGVA---------------------ANMGVAKPSsvgriVPGVRVkiLD-EAGRSLGH-GET-GEILVHNGKVW 385
Cdd:PRK08162 327 YGLTETYGPAtvcawqpewdalplderaqlkARQGVRYPL-----QEGVTV--LDpDTMQPVPAdGETiGEIMFRGNIVM 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 386 NGYYANPNESKR-MQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGL----W 460
Cdd:PRK08162 400 KGYLKNPKATEEaFAG--GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKpdpkW 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24648260 461 NEVdgdPAAAAVVKiPGSRLTEMDIVEyvakrlvvdHKQLHCGVFFLP------ELPKTGSGK----VLRQQARD 525
Cdd:PRK08162 478 GEV---PCAFVELK-DGASATEEEIIA---------HCREHLAGFKVPkavvfgELPKTSTGKiqkfVLREQAKS 539
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
188-526 |
2.27e-15 |
|
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: 78.68 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVAILCTSGTTGLPKAVCISNSACLFD-FGFVTGQDVLLSFSTIDWSAGMFNMLFSCCHGS------------TRIIT 254
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNmFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLApliagmnqylmpTRLFI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 255 DRPYTpeYMIQlVEKYKVTLLTVvP----QQVASLLKTPTLNKQRLASIRFVSVGGGSCyvanLLKLQEFLITGQISYGY 330
Cdd:cd05908 186 RRPIL--WLKK-ASEHKATIVSS-PnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPI----DYELCHEFLDHMSKYGL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 331 ---ALTECGGVA-ANMGVAKPS-----------------------------------SVGRIVPGVRVKILDEAGRSLGH 371
Cdd:cd05908 258 krnAILPVYGLAeASVGASLPKaqspfktitlgrrhvthgepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 372 GETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENyLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDV 451
Cdd:cd05908 338 GYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGR-LVITGREKDIIFVNGQNVYPHDIERIAEELEGV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 452 ieacvfglwnevdgDPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDH---------------KQLHCG-VFFLPELPKTGS 515
Cdd:cd05908 417 --------------ELGRVVACGVNNSNTRNEEIFCFIEHRKSEDDfyplgkkikkhlnkrGGWQINeVLPIRRIPKTTS 482
|
410
....*....|.
gi 24648260 516 GKVLRQQARDQ 526
Cdd:cd05908 483 GKVKRYELAQR 493
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
34-413 |
2.82e-15 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 78.63 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 34 LFAFMRNHPNSICqISDTEG----TALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHA 109
Cdd:cd05921 1 LAHWARQAPDRTW-LAEREGnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 110 VSPW-----QDEDTIKHLFSITRPKLIFC-DGKCFQRlsIIARILKSH-----VYTLKDHRLGMPRVEDLLEPTTAElyy 178
Cdd:cd05921 80 VSPAyslmsQDLAKLKHLFELLKPGLVFAqDAAPFAR--ALAAIFPLGtplvvSRNAVAGRGAISFAELAATPPTAA--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 179 VPETLLLGGDHTVA-ILCTSGTTGLPKAV-------CISNSACLFDFGFVTGQDVLLsfstIDW------SAGMFNMLFS 244
Cdd:cd05921 155 VDAAFAAVGPDTVAkFLFTSGSTGLPKAVintqrmlCANQAMLEQTYPFFGEEPPVL----VDWlpwnhtFGGNHNFNLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 245 CCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTV---VPQQ----VASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKL 317
Cdd:cd05921 231 LYNGGTLYIDDGKPMPGGFEETLRNLREISPTVyfnVPAGwemlVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 318 QEFLI--TGQ---ISYGYALTECGGVAANMG--VAKPSSVGRIVPGVRVKILDEAGRSlghgetgEILVHNGKVWNGYYA 390
Cdd:cd05921 311 QALAVatVGEripMMAGLGATETAPTATFTHwpTERSGLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWR 383
|
410 420
....*....|....*....|...
gi 24648260 391 NPNESKRMQDYQGWFHTGDMGYF 413
Cdd:cd05921 384 QPELTAQAFDEEGFYCLGDAAKL 406
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
24-521 |
2.97e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.62 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 24 FDADCSIGKILFAFMRNHPNSICQISDTEgtALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLN 103
Cdd:PRK12316 4547 YPATRCVHQLVAERARMTPDAVAVVFDEE--KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKA 4624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 104 GTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSIIARIlkshvytlkdHRLGMPRVEDLLE-PTTAelyyvPEt 182
Cdd:PRK12316 4625 GGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGL----------ASLALDRDEDWEGfPAHD-----PA- 4688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 183 LLLGGDHTVAILCTSGTTGLPKAVCISNSAcLFDFGFVTGQ-------DVLLSFSTIDWSAGMFNMLFSCCHGSTRIITD 255
Cdd:PRK12316 4689 VRLHPDNLAYVIYTSGSTGRPKGVAVSHGS-LVNHLHATGEryeltpdDRVLQFMSFSFDGSHEGLYHPLINGASVVIRD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 256 RPYT-PEYMIQLVEKYKVTLLTVVPQQVASLLKTPTlNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTE 334
Cdd:PRK12316 4768 DSLWdPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 CGGV-----AANMGVAKPSSV--GRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPN-ESKRMQ----DYQ 402
Cdd:PRK12316 4847 TTVTvllwkARDGDACGAAYMpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPAlTAERFVpdpfGAP 4926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 403 G--WFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGlwneVDGD----------PAAA 470
Cdd:PRK12316 4927 GgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA----QEGAvgkqlvgyvvPQDP 5002
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24648260 471 AVVKIPGSRLTEMDIVEYVAKRLVVDHK-QLHcgVFFLPELPKTGSGKVLRQ 521
Cdd:PRK12316 5003 ALADADEAQAELRDELKAALRERLPEYMvPAH--LVFLARMPLTPNGKLDRK 5052
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
38-525 |
3.81e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 78.29 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 38 MRNHPNSICQI--------SDTEGTALTNGEA--ITFA---IRIAQQLKAM----GLKQDDVVGIVGTNTTYLMPVVLGC 100
Cdd:PRK05620 5 MQDVPLSLTRIleygstvhGDTTVTTWGGAEQeqTTFAaigARAAALAHALhdelGITGDQRVGSMMYNCAEHLEVLFAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 101 LLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLsiiARILKS-----HVYTLKDHRLGMPRVEDllePTTAE 175
Cdd:PRK05620 85 ACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQL---GEILKEcpcvrAVVFIGPSDADSAAAHM---PEGIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 176 LYYVpETLLLG----------GDHTVAILCTS-GTTGLPKAVCISNSAcLFDFGfvtgqdvlLSFSTIDWSAGMFNMLFS 244
Cdd:PRK05620 159 VYSY-EALLDGrstvydwpelDETTAAAICYStGTTGAPKGVVYSHRS-LYLQS--------LSLRTTDSLAVTHGESFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 245 CC----H-------------GSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVgGG 307
Cdd:PRK05620 229 CCvpiyHvlswgvplaafmsGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYV-GG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 308 SCYVANLLKLQEFLITGQISYGYALTECGGVAAnmgVAKPS-------------SVGRIVPGVRVKILDEaGRSLGHGE- 373
Cdd:PRK05620 308 SAVPPILIKAWEERYGVDVVHVWGMTETSPVGT---VARPPsgvsgearwayrvSQGRFPASLEYRIVND-GQVMESTDr 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 374 -TGEILVHNGKVWNGYYANPNE-----SKRMQDYQ-----------GWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQY 436
Cdd:PRK05620 384 nEGEIQVRGNWVTASYYHSPTEegggaASTFRGEDvedandrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 437 SPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEmDIVEYVAKRL--VVDHKQLHCGVFFLPELPKTG 514
Cdd:PRK05620 464 YSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR-ETAERLRDQLrdRLPNWMLPEYWTFVDEIDKTS 542
|
570
....*....|....*
gi 24648260 515 SGKV----LRQQARD 525
Cdd:PRK05620 543 VGKFdkkdLRQHLAD 557
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-521 |
1.87e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.92 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEaITF--------AIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLF 123
Cdd:PRK12316 526 EAPALAFGE-ETLdyaelnrrANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 124 SITRPKLIFCDGKCFQRLSIIARIlkshvytlkdHRLGMPRVEDLLEPTTAElyyVPETLLLGgDHTVAILCTSGTTGLP 203
Cdd:PRK12316 605 EDSGVQLLLSQSHLGRKLPLAAGV----------QVLDLDRPAAWLEGYSEE---NPGTELNP-ENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 204 KAVCISNSA-------CLFDFGFVTGQDVL----LSFSTIDWsagmfnMLFSCCHGSTRIITDRP---YTPEYMIQLVEK 269
Cdd:PRK12316 671 KGAGNRHRAlsnrlcwMQQAYGLGVGDTVLqktpFSFDVSVW------EFFWPLMSGARLVVAAPgdhRDPAKLVELINR 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 270 YKVTLLTVVPQQVASLLKTPTLnkQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTE-----CGGVAANMGV 344
Cdd:PRK12316 745 EGVDTLHFVPSMLQAFLQDEDV--ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEaaidvTHWTCVEEGG 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 345 AKPsSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANP------------NESKRMqdyqgwFHTGDMGY 412
Cdd:PRK12316 823 DSV-PIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPgltaerfvpspfVAGERM------YRTGDLAR 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 413 FDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGlwneVDGDPAAAAVV-KIPGSRLTEmDIVEYVAK 491
Cdd:PRK12316 896 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVlESEGGDWRE-ALKAHLAA 970
|
490 500 510
....*....|....*....|....*....|....
gi 24648260 492 RL----VVDHkqlhcgVFFLPELPKTGSGKVLRQ 521
Cdd:PRK12316 971 SLpeymVPAQ------WLALERLPLTPNGKLDRK 998
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
265-527 |
1.91e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 75.80 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 265 QLVEKYKVTLLTVVPQQVASLLKTPTL--NKQRLASIRFVSVGGGscyvanllKLQEFL---ITGQIsyGYALTECGGVA 339
Cdd:PRK10946 266 PLIEKHQVNVTALVPPAVSLWLQAIAEggSRAQLASLKLLQVGGA--------RLSETLarrIPAEL--GCQLQQVFGMA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 340 ---ANMGVAKPSSV------GR-IVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGD 409
Cdd:PRK10946 336 eglVNYTRLDDSDErifttqGRpMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 410 MGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVV-----KIPGSR--LTE 482
Cdd:PRK10946 416 LVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVvkeplKAVQLRrfLRE 495
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 24648260 483 MDIVEYvakrlvvdhkQLHCGVFFLPELPKTGSGKVLRQQARDQA 527
Cdd:PRK10946 496 QGIAEF----------KLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-459 |
4.85e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 74.42 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVAILCTSGTTGLPKAVCISNS-------ACLFDFGFVTGQDVLLSFSTIdwsaGMFNMLFscchGSTRIITD----R 256
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGtfaaqidALRQLYGIRPGEVDLATFPLF----ALFGPAL----GLTSVIPDmdptR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 257 PYT--PEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLI-TGQISYGYALT 333
Cdd:cd05910 157 PARadPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSdEAEILTPYGAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 334 ECGGVAANMGVAKPSS------------VGRIVPGVRVKIL--DEAG-------RSLGHGETGEILVHNGKVWNGYYANP 392
Cdd:cd05910 237 EALPVSSIGSRELLATttaatsggagtcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTPTYVNRP 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648260 393 NESK----RMQDYQGWFHTGDMGYFDNENYLHIVERKEDLL-RFHGAQYSPQeIEQVIAELPDVIEACVFGL 459
Cdd:cd05910 317 VATAlakiDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRViTTGGTLYTEP-VERVFNTHPGVRRSALVGV 387
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
330-520 |
9.68e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.15 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 330 YALTECGGVAANMGVAKPSSVGRIVPGVRVkildEAGRslGHGETGEILVHNGKvwngyyanpNEskrmqdyqgwFHTGD 409
Cdd:PRK08308 243 YGCSEAGCVSICPDMKSHLDLGNPLPHVSV----SAGS--DENAPEEIVVKMGD---------KE----------IFTKD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 410 MGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKipGSRLTEMDIVEYV 489
Cdd:PRK08308 298 LGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIS--HEEIDPVQLREWC 375
|
170 180 190
....*....|....*....|....*....|.
gi 24648260 490 AKRLVVdHKQLHCGVfFLPELPKTGSGKVLR 520
Cdd:PRK08308 376 IQHLAP-YQVPHEIE-SVTEIPKNANGKVSR 404
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
166-424 |
9.96e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 73.86 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 166 EDLLEPTTAELYYVPETLLLGGDHTVAILCTSGTTGLPKAV----------CISNSACLFD-FGFVTGQDVLLSFSTIdw 234
Cdd:PTZ00216 242 TDVVAKGHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVmhthgsltagILALEDRLNDlIGPPEEDETYCSYLPL-- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 235 sAGMF-----NMLFS----CCHGSTRIITD---RPYTpeymiQLVEkYKVTLLTVVPQ--------------QVASL--- 285
Cdd:PTZ00216 320 -AHIMefgvtNIFLArgalIGFGSPRTLTDtfaRPHG-----DLTE-FRPVFLIGVPRifdtikkaveaklpPVGSLkrr 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 286 ------------LK----TPTLNKQRLASIR---------FVSvGGGSCYVANllklQEFL--ITGQISYGYALTE---C 335
Cdd:PTZ00216 393 vfdhayqsrlraLKegkdTPYWNEKVFSAPRavlggrvraMLS-GGGPLSAAT----QEFVnvVFGMVIQGWGLTEtvcC 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 336 GGVAaNMGVAKPSSVGRIVPGVRVKILDEAGRSlgHGET----GEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMG 411
Cdd:PTZ00216 468 GGIQ-RTGDLEPNAVGQLLKGVEMKLLDTEEYK--HTDTpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVG 544
|
330
....*....|...
gi 24648260 412 YFDNENYLHIVER 424
Cdd:PTZ00216 545 SIAANGTLRIIGR 557
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
164-518 |
1.01e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 73.20 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 164 RVEDLLEPTTAELyyvpetLLLGGDHTVAILCTSGTTGLPKAVCIS--------NSACLFDFGFVTGQDVLLSFSTIDWS 235
Cdd:cd17648 76 RIQFILEDTGARV------VITNSTDLAYAIYTSGTTGKPKGVLVEhgsvvnlrTSLSERYFGRDNGDEAVLFFSNYVFD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 236 AGMFNMLFSCCHGSTRIITDRP--YTPEYMIQLVEKYKVTLLTVVPqqvaSLLKTPTLNkqRLASIRFVSVGGGSCYVAN 313
Cdd:cd17648 150 FFVEQMTLALLNGQKLVVPPDEmrFDPDRFYAYINREKVTYLSGTP----SVLQQYDLA--RLPHLKRVDAAGEEFTAPV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 314 LLKL-QEFliTGQISYGYALTECgGVAANMGVAKPS-----SVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNG 387
Cdd:cd17648 224 FEKLrSRF--AGLIINAYGPTET-TVTNHKRFFPGDqrfdkSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 388 YY-----------ANP---NESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIE 453
Cdd:cd17648 301 YLnrpeltaerflPNPfqtEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRE 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648260 454 ACVFGLWNEVDGDPAAAA-----VVKIPGSrLTEMDIVEYVAKRL---VVDhKQLHcgvfFLPELPKTGSGKV 518
Cdd:cd17648 381 CAVVAKEDASQAQSRIQKylvgyYLPEPGH-VPESDLLSFLRAKLpryMVP-ARLV----RLEGIPVTINGKL 447
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
48-517 |
1.66e-13 |
|
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: 73.07 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 48 ISDTEGTA--LTNGEAITFAIRIAQQLKAMGLKQDD-VVGIVgTNTTYlmpVVLGCLLN---GTPFHAVSPwqDEDTIKH 121
Cdd:cd05943 89 YAAEDGERteVTWAELRRRVARLAAALRALGVKPGDrVAGYL-PNIPE---AVVAMLATasiGAIWSSCSP--DFGVPGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 122 L--FSITRPKLIF-CD-----GKCFQRLSIIARILKS--------HV-YTLKDHRLGMP------RVEDLL-EPTTAELY 177
Cdd:cd05943 163 LdrFGQIEPKVLFaVDaytynGKRHDVREKVAELVKGlpsllavvVVpYTVAAGQPDLSkiakalTLEDFLaTGAAGELE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 178 YVPetllLGGDHTVAILCTSGTTGLPKavCISNSA--------------ClfDFGFvtgQDVLLSFSTIDWSagMFNMLF 243
Cdd:cd05943 243 FEP----LPFDHPLYILYSSGTTGLPK--CIVHGAggtllqhlkehilhC--DLRP---GDRLFYYTTCGWM--MWNWLV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 244 S-CCHGSTRIITDRP---YTPEYMIQLVEKYKVTLLTVVPQQVASLLK---TPTLNkQRLASIRFV-SVGG-----GSCY 310
Cdd:cd05943 310 SgLAVGATIVLYDGSpfyPDTNALWDLADEEGITVFGTSAKYLDALEKaglKPAET-HDLSSLRTIlSTGSplkpeSFDY 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 311 VANllKLQEFLITGQISYGyalTECGGVAANMGVAKPSSVGRI---VPGVRVKILDEAGRSLgHGETGEILVHNG----- 382
Cdd:cd05943 389 VYD--HIKPDVLLASISGG---TDIISCFVGGNPLLPVYRGEIqcrGLGMAVEAFDEEGKPV-WGEKGELVCTKPfpsmp 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 383 -KVWNgyyaNPNESKRMQDY----QG-WFHtGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACV 456
Cdd:cd05943 463 vGFWN----DPDGSRYRAAYfakyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLV 537
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648260 457 FGLWNEVDGDPAAAAVVKIPGSRLTEmDIVEYVAKRLVVDHKQLHC--GVFFLPELPKTGSGK 517
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELDD-ELRKRIRSTIRSALSPRHVpaKIIAVPDIPRTLSGK 599
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
137-527 |
3.98e-13 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 71.42 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 137 CFQR-----LSIIArILKS-HVYTLKDHRLGMPRVEDLLEPTTAELyyvpeTLLLGGDHTVAILCTSGTTGLPKAVCISN 210
Cdd:cd05918 55 CFEKskwavVAMLA-VLKAgGAFVPLDPSHPLQRLQEILQDTGAKV-----VLTSSPSDAAYVIFTSGSTGKPKGVVIEH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 211 SA---CLFDFG---FVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIIT---DRPYTPEYMIQlveKYKVTLLTVVPQq 281
Cdd:cd05918 129 RAlstSALAHGralGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPseeDRLNDLAGFIN---RLRVTWAFLTPS- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 282 VASLLktptlNKQRLASIRFVSVGGGSCY--VANLLKLQEFLITGqisYGyaLTEC---GGVAANMGVAKPSSVGRIVpG 356
Cdd:cd05918 205 VARLL-----DPEDVPSLRTLVLGGEALTqsDVDTWADRVRLINA---YG--PAECtiaATVSPVVPSTDPRNIGRPL-G 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 357 VRVKILDEA--GRSLGHGETGEILVHNGKVWNGYYANPNESK---------RMQDYQGW----FHTGDMGYFDNENYLHI 421
Cdd:cd05918 274 ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAaafiedpawLKQEGSGRgrrlYRTGDLVRYNPDGSLEY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 422 VERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAA--AAVVKIPGSRLTEMDIVEYVAK-----RLV 494
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlVAFVVLDGSSSGSGDGDSLFLEpsdefRAL 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 24648260 495 VDHKQLHC----------GVFF-LPELPKTGSGKVLRQQARDQA 527
Cdd:cd05918 434 VAELRSKLrqrlpsymvpSVFLpLSHLPLTASGKIDRRALRELA 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
375-527 |
7.92e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.03 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 375 GEILVHNGKVWNGYYANPNESKrmQDYQ-GWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIE 453
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKANE--EAFAnGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLE 480
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24648260 454 ACVFGLWNEVDGDPAAAAVVKIPGS-----RLTEMDIVEYVAKRLvvDHKQLHCGVFFLPeLPKTGSGKVLRQQARDQA 527
Cdd:PLN02479 481 ASVVARPDERWGESPCAFVTLKPGVdksdeAALAEDIMKFCRERL--PAYWVPKSVVFGP-LPKTATGKIQKHVLRAKA 556
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
169-521 |
2.00e-12 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 69.39 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 169 LEPT--TAELYYVPE----TLLLGGDHTVA-ILCTSGTTGLPKAVCISNSACL-FDFG-----FVTGQDVLLSFSTIDWS 235
Cdd:cd17644 80 LDPNypQERLTYILEdaqiSVLLTQPENLAyVIYTSGSTGKPKGVMIEHQSLVnLSHGlikeyGITSSDRVLQFASIAFD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 236 AGMFNMLFSCCHGSTRIItdRP----YTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRL-ASIRFVSVGGGSCY 310
Cdd:cd17644 160 VAAEEIYVTLLSGATLVL--RPeemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 311 VANLLKLQEflITG---QISYGYALTECGGVAANMGVAKPSS-------VGRIVPGVRVKILDEAGRSLGHGETGEILVH 380
Cdd:cd17644 238 PELVRQWQK--NVGnfiQLINVYGPTEATIAATVCRLTQLTErnitsvpIGRPIANTQVYILDENLQPVPVGVPGELHIG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 381 NGKVWNGYYANP--------NESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVI 452
Cdd:cd17644 316 GVGLARGYLNRPeltaekfiSHPFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVK 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 453 EACVFGLWNEVDGDPAAAAVV-KIPGSRLTEmDIVEYVAKRLvVDHkQLHCGVFFLPELPKTGSGKVLRQ 521
Cdd:cd17644 396 TAVVIVREDQPGNKRLVAYIVpHYEESPSTV-ELRQFLKAKL-PDY-MIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
350-526 |
1.55e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 66.71 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 350 VGRIVPGVRVKIL-DEAGRSLGHGETGEILVHNGKVWNGYYANPNeskrmQDYQGWFHTGDMGYF-DNEnyLHIVERKED 427
Cdd:PRK05851 347 LGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYLvDGG--LVVCGRAKE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 428 LLRFHGAQYSPQEIEQVIAELPDVIEACVFGL-WNEVDGDPAAAAVVKIPGSRltemdivEYVAKRLVVDHKQLHCG--- 503
Cdd:PRK05851 420 LITVAGRNIFPTEIERVAAQVRGVREGAVVAVgTGEGSARPGLVIAAEFRGPD-------EAGARSEVVQRVASECGvvp 492
|
170 180
....*....|....*....|....*..
gi 24648260 504 --VFFLP--ELPKTGSGKVLRQQARDQ 526
Cdd:PRK05851 493 sdVVFVApgSLPRTSSGKLRRLAVKRS 519
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
293-458 |
2.00e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 66.76 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 293 KQRLAS-IRFVSVGGGSCYvanlLKLQEFLITGQISY---GYALTE-CGGVAanmgVAKP---SSVGRI-VPGV----RV 359
Cdd:PLN02430 378 KAKLGGrLRLLISGGAPLS----TEIEEFLRVTSCAFvvqGYGLTEtLGPTT----LGFPdemCMLGTVgAPAVynelRL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 360 KILDEAGRS-LGHGETGEILVHNGKVWNGYYANP---NESkrMQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQ 435
Cdd:PLN02430 450 EEVPEMGYDpLGEPPRGEICVRGKCLFSGYYKNPeltEEV--MKD--GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGE 525
|
170 180
....*....|....*....|....
gi 24648260 436 YSPQE-IEQVIAELPDVIEACVFG 458
Cdd:PLN02430 526 YVALEyLENVYGQNPIVEDIWVYG 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
187-534 |
2.14e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 187 GDHTVAILCTSGTTGLPKAVCISNSA-----CLFDFGF-VTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITD-RPYT 259
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGAlanhlCWIAEAYeLDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDnDLWD 3315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 260 PEYMIQLVEKYKVTLLTVVPQQVASLLKTPtlNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTE----- 334
Cdd:PRK12467 3316 PEELWQAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEavvtv 3393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 335 ----CGGVAANMGVAKPssVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNES-------------KR 397
Cdd:PRK12467 3394 tlwkCGGDAVCEAPYAP--IGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaerfvadpfsgsgGR 3471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 398 MqdyqgwFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPG 477
Cdd:PRK12467 3472 L------YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQ 3545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 478 SRLTE---MDIVEYVAKRLVVDHkqlhcgVFFLPELPKTGSGKVLR-----------------QQARDQALGKKWAD 534
Cdd:PRK12467 3546 GDWREtlrDHLAASLPDYMVPAQ------LLVLAAMPLGPNGKVDRkalpdpdakgsreyvapRSEVEQQLAAIWAD 3616
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
68-520 |
2.71e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 66.61 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 68 IAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFcdgkcfqrlsiiari 147
Cdd:PRK10252 496 LANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLI--------------- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 148 lkshvyTLKDHRLGMPRVEDLLEPTTAELYYVPETLLLGG---DHTVAILCTSGTTGLPKAVCISNSACL-------FDF 217
Cdd:PRK10252 561 ------TTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLsqpHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwmqNHY 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 218 GFvTGQDVLLSFS--TIDWSAGMFNMLFSCchGSTRIIT--DRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPT--L 291
Cdd:PRK10252 635 PL-TADDVVLQKTpcSFDVSVWEFFWPFIA--GAKLVMAepEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTpeG 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 292 NKQRLASIR--FVSvggGSCYVANLLKLQEFLITGQISYGYALTEC---------GGVAANMGVAKPSSVGRIVPGVRVK 360
Cdd:PRK10252 712 ARQSCASLRqvFCS---GEALPADLCREWQQLTGAPLHNLYGPTEAavdvswypaFGEELAAVRGSSVPIGYPVWNTGLR 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 361 ILDEAGRSLGHGETGEILVHNGKVWNGYYANPN------------ESKRMqdyqgwFHTGDMGYFDNENYLHIVERKEDL 428
Cdd:PRK10252 789 ILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDltasrfiadpfaPGERM------YRTGDVARWLDDGAVEYLGRSDDQ 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 429 LRFHGAQYSPQEIEQVIAELPDV----IEACVFGLWNEVDGDPA--AAAVVKIPGSRLTEMDIVEYVAKRLvVDHKqlhC 502
Cdd:PRK10252 863 LKIRGQRIELGEIDRAMQALPDVeqavTHACVINQAAATGGDARqlVGYLVSQSGLPLDTSALQAQLRERL-PPHM---V 938
|
490 500
....*....|....*....|
gi 24648260 503 GVFF--LPELPKTGSGKVLR 520
Cdd:PRK10252 939 PVVLlqLDQLPLSANGKLDR 958
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
325-535 |
3.36e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 65.92 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 325 QISYGYALTecggVAANMGVAKPS-SVGRIVPGVRVKILDE-AGRSLGHGETGEILVHNGKVWNGYYANPNESK-----R 397
Cdd:PRK12476 382 QLGAGRAVR----VAADAPNAVAHvSCGQVARSQWAVIVDPdTGAELPDGEVGEIWLHGDNIGRGYWGRPEETErtfgaK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 398 MQ-------------DYQGWFHTGDMG-YFDNEnyLHIVERKEDLLRFHGAQYSPQEIEQVIAEL-PDVIEACVFGLwnE 462
Cdd:PRK12476 458 LQsrlaegshadgaaDDGTWLRTGDLGvYLDGE--LYITGRIADLIVIDGRNHYPQDIEATVAEAsPMVRRGYVTAF--T 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 463 VDGDPAAAAVV---KIPG-SRLTEMDIVEyvAKRLVVDHKqlH----CGVFFLPE--LPKTGSGKVLRQQARDQALGKKW 532
Cdd:PRK12476 534 VPAEDNERLVIvaeRAAGtSRADPAPAID--AIRAAVSRR--HglavADVRLVPAgaIPRTTSGKLARRACRAQYLDGRL 609
|
...
gi 24648260 533 ADH 535
Cdd:PRK12476 610 GVH 612
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
52-522 |
3.61e-11 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 65.43 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 52 EGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLI 131
Cdd:cd17655 19 EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 132 FCDGKcfqrlSIIARILKSHVYTLKDHRLGMPRVEDLLEPTTAelyyvpetlllggDHTVAILCTSGTTGLPKAVCI--- 208
Cdd:cd17655 99 LTQSH-----LQPPIAFIGLIDLLDEDTIYHEESENLEPVSKS-------------DDLAYVIYTSGSTGKPKGVMIehr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 209 --SNSACLFDFGFVTGQ--DVLLsFSTIDWSAGMFNMLFSCCHGSTRII----TDRPYTPeyMIQLVEKYKVTLLTVVPq 280
Cdd:cd17655 161 gvVNLVEWANKVIYQGEhlRVAL-FASISFDASVTEIFASLLSGNTLYIvrkeTVLDGQA--LTQYIRQNRITIIDLTP- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 281 qvASLLKTPTLNKQRLASIRFVSVGGGSC---YVANLLKLqeFLITGQISYGYALTECgGVAANMGVAKPS-------SV 350
Cdd:cd17655 237 --AHLKLLDAADDSEGLSLKHLIVGGEALsteLAKKIIEL--FGTNPTITNAYGPTET-TVDASIYQYEPEtdqqvsvPI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 351 GRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANP---NE---------SKRMqdyqgwFHTGDMGYFDNENY 418
Cdd:cd17655 312 GKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPeltAEkfvddpfvpGERM------YRTGDLARWLPDGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 419 LHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEvDGDPAAAAVVkIPGSRLTEMDIVEYVAKRLvvdhK 498
Cdd:cd17655 386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDE-QGQNYLCAYI-VSEKELPVAQLREFLAREL----P 459
|
490 500
....*....|....*....|....*.
gi 24648260 499 QLHCGVFF--LPELPKTGSGKVLRQQ 522
Cdd:cd17655 460 DYMIPSYFikLDEIPLTPNGKVDRKA 485
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
171-527 |
6.74e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 64.92 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 171 PTTAELYYVpetlllGGDHTVAILCTSGTTGLPKAVCISN------SACLFDFGF-VTGQDVLLSFSTIDWSAGMFNMLF 243
Cdd:PLN02654 264 PTKCEVEWV------DAEDPLFLLYTSGSTGKPKGVLHTTggymvyTATTFKYAFdYKPTDVYWCTADCGWITGHSYVTY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 244 S-CCHGSTRIITDRpyTPEY-----MIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLA--SIR--------------- 300
Cdd:PLN02654 338 GpMLNGATVLVFEG--APNYpdsgrCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRvlgsvgepinpsawr 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 301 --FVSVGGGSCYVANLLKLQEfliTGqisyGYALTECGGVAANmgvaKPSSVGRIVPGVRVKILDEAGRSLgHGE-TGEI 377
Cdd:PLN02654 416 wfFNVVGDSRCPISDTWWQTE---TG----GFMITPLPGAWPQ----KPGSATFPFFGVQPVIVDEKGKEI-EGEcSGYL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 378 LVHngKVWNGYYAN------PNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDV 451
Cdd:PLN02654 484 CVK--KSWPGAFRTlygdheRYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQC 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 452 IEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMdiveyVAKRLVVDHKQlHCGVFFLPE-------LPKTGSGKVLRQQAR 524
Cdd:PLN02654 562 AEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE-----LRKSLILTVRN-QIGAFAAPDkihwapgLPKTRSGKIMRRILR 635
|
...
gi 24648260 525 DQA 527
Cdd:PLN02654 636 KIA 638
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
319-458 |
7.68e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 64.74 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 319 EFL---ITGQISYGYALTECGGVAANMGVAKPSS--VGRIVPGVRVKILDEAGRSLGHGET----GEILVHNGKVWNGYY 389
Cdd:PLN02736 394 EFLricFGGRVLEGYGMTETSCVISGMDEGDNLSghVGSPNPACEVKLVDVPEMNYTSEDQpyprGEICVRGPIIFKGYY 473
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 390 ANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQY-SPQEIEQVIAELPDVIEACVFG 458
Cdd:PLN02736 474 KDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYiAPEKIENVYAKCKFVAQCFVYG 543
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
53-525 |
9.01e-11 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 63.98 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 53 GTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTpfhaVSPWQDedtikhlFSITRPKLIF 132
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGV----ETALIN-------SNLRLESLLH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 133 CdgkcfqrlsIIARILKSHVYTLKDhrlgmprveDLLEPTTAELYYVPetlllGGDHTvAILC---TSGTTGLPKAVCIS 209
Cdd:cd05939 70 C---------ITVSKAKALIFNLLD---------PLLTQSSTEPPSQD-----DVNFR-DKLFyiyTSGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 210 NS-----ACLFDFGF-VTGQDVLLSFSTIDWSAGMFNMLFSC-CHGSTRIITDRPYTPEYMIQLVeKYKVTLLTVVPQQV 282
Cdd:cd05939 126 HSryyriAAGAYYAFgMRPEDVVYDCLPLYHSAGGIMGVGQAlLHGSTVVIRKKFSASNFWDDCV-KYNCTIVQYIGEIC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 283 ASLLKTPTLNKQRLASIRFVsvgggscyVANLLK-------LQEFLITgQISYGYALTECGGVAANMG--VAKPSSVGRI 353
Cdd:cd05939 205 RYLLAQPPSEEEQKHNVRLA--------VGNGLRpqiweqfVRRFGIP-QIGEFYGATEGNSSLVNIDnhVGACGFNSRI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 354 VPG---VRVKILDEAGRSL-----GH------GETGEILvhnGKV--------WNGyYANPNES--KRMQDY----QGWF 405
Cdd:cd05939 276 LPSvypIRLIKVDEDTGELirdsdGLcipcqpGEPGLLV---GKIiqndplrrFDG-YVNEGATnkKIARDVfkkgDSAF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 406 HTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLW-NEVDGDPAAAAVVkipgSRLTEMD 484
Cdd:cd05939 352 LSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvPGVEGRAGMAAIV----DPERKVD 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24648260 485 iVEYVAKRLVVDHKQLHCGVF--FLPELPKTGSGKV----LRQQARD 525
Cdd:cd05939 428 -LDRFSAVLAKSLPPYARPQFirLLPEVDKTGTFKLqktdLQKEGYD 473
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
67-527 |
9.98e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 64.14 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCL--------LNgtpFHAVspwqdEDTIKHLFSITRPKLIFcdgkcF 138
Cdd:PRK07798 40 RLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFkaravpvnVN---YRYV-----EDELRYLLDDSDAVALV-----Y 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 139 QR--LSIIARILKS--HVYTLKdhrlgmpRVED---LLEPTTAELYyvpETLLLGGDHT----------VAILCTSGTTG 201
Cdd:PRK07798 107 ERefAPRVAEVLPRlpKLRTLV-------VVEDgsgNDLLPGAVDY---EDALAAGSPErdfgerspddLYLLYTGGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 202 LPKAVC---------------------ISNSACLFDFGFVTGQDVLLSFSTIDWSAGM---FNMLFScchGSTRIITDRP 257
Cdd:PRK07798 177 MPKGVMwrqedifrvllggrdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQwaaFAALFS---GQTVVLLPDV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 258 -YTPEYMIQLVEKYKVTLLTVVPQQVAS-LLKTptLNKQR---LASIRFVSVGGG--SCYVANllKLQEFLITGQISYGY 330
Cdd:PRK07798 254 rFDADEVWRTIEREKVNVITIVGDAMARpLLDA--LEARGpydLSSLFAIASGGAlfSPSVKE--ALLELLPNVVLTDSI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 331 ALTECG--GVAANMGVAKPSSVGRIVPGVRVKILDEAGRSL--GHGETGeILVHNGKVWNGYYANPNESK---RMQDYQG 403
Cdd:PRK07798 330 GSSETGfgGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVepGSGEIG-WIARRGHIPLGYYKDPEKTAetfPTIDGVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 404 WFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEM 483
Cdd:PRK07798 409 YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24648260 484 DIVEYVAKRLVvdhkqlhcG------VFFLPELPKTGSGKVLRQQARDQA 527
Cdd:PRK07798 489 ELRAHCRSSLA--------GykvpraIWFVDEVQRSPAGKADYRWAKEQA 530
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
167-524 |
1.16e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.80 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 167 DLLEPTTAELYYVPEtllLGGDHTVAILCTSGTTGLPKAVCISN-----SACLFDFGF---VTGQDVLLS----FSTIDW 234
Cdd:PRK05691 148 DTLDPALAEAWQEPA---LQPDDIAFLQYTSGSTALPKGVQVSHgnlvaNEQLIRHGFgidLNPDDVIVSwlplYHDMGL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 235 SAGMFNMLFS---CCHGSTRIITDRPYT---------------PEYMIQL----VEKYKVTLLTVVPQQVASLLKTP--- 289
Cdd:PRK05691 225 IGGLLQPIFSgvpCVLMSPAYFLERPLRwleaiseyggtisggPDFAYRLcserVSESALERLDLSRWRVAYSGSEPirq 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 290 -TLNK--QRLASIRFVSVGGGSCYvaNLLKLQEFLITGQISYGYALTECGGVAANMGVAKPS------SVGRIVPGVRVK 360
Cdd:PRK05691 305 dSLERfaEKFAACGFDPDSFFASY--GLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGtgsvlmSCGRSQPGHAVL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 361 ILDEA-GRSLGHGETGEILVHNGKVWNGYYANPNESKRM---QDYQGWFHTGDMGyFDNENYLHIVERKEDLLRFHGAQY 436
Cdd:PRK05691 383 IVDPQsLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 437 SPQEIEQVIAELPDVIE---ACVFGLwnEVDGDPAAAAVVKIPGS--RLTEMDIVEYVAKRLVVDHKQLHCGVFFLPE-- 509
Cdd:PRK05691 462 YPQDIEKTVEREVEVVRkgrVAAFAV--NHQGEEGIGIAAEISRSvqKILPPQALIKSIRQAVAEACQEAPSVVLLLNpg 539
|
410
....*....|....*.
gi 24648260 510 -LPKTGSGKVLRQQAR 524
Cdd:PRK05691 540 aLPKTSSGKLQRSACR 555
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
168-539 |
1.33e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 63.96 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 168 LLEPTTAELYYVPETLLLggdhtvaILCTSGTTGLPKAVCISNSA---------CLFDFgfvTGQDVLLS----FSTIDW 234
Cdd:PRK08043 352 LLMPRLAQVKQQPEDAAL-------ILFTSGSEGHPKGVVHSHKSllanveqikTIADF---TPNDRFMSalplFHSFGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 235 SAGMFNMLFScchGSTRIITDRPYtpeymiqlveKYKVTLLTVVPQQVASLLKTPTL--NKQRLAS------IRFVsvgg 306
Cdd:PRK08043 422 TVGLFTPLLT---GAEVFLYPSPL----------HYRIVPELVYDRNCTVLFGTSTFlgNYARFANpydfarLRYV---- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 307 gscyVANLLKLQE---------FLItgQISYGYALTECGGVAA-NMGVA-KPSSVGRIVPGVRVKILDEAGRSLGhgetG 375
Cdd:PRK08043 485 ----VAGAEKLQEstkqlwqdkFGL--RILEGYGVTECAPVVSiNVPMAaKPGTVGRILPGMDARLLSVPGIEQG----G 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 376 EILVHNGKVWNGYY--ANPN-------ESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIA 446
Cdd:PRK08043 555 RLQLKGPNIMNGYLrvEKPGvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 447 EL-PDVIEACVFglwnEVDGDPAAAAVVKIPGSRLTEmDIVEYVAKRLVVDHKQLHCGVFFLPELPKTGSGKVlrqqarD 525
Cdd:PRK08043 635 GVsPDKQHATAI----KSDASKGEALVLFTTDSELTR-EKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKP------D 703
|
410
....*....|....
gi 24648260 526 QALGKKWADHGNGH 539
Cdd:PRK08043 704 FVTLKSMVDEPEQH 717
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
196-458 |
3.18e-10 |
|
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: 62.76 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSACLFDFGFVT----------GQDVLLSF---STIdwSAGMFNMLFSCCHGS------------T 250
Cdd:cd05933 158 TSGTTGMPKGVMLSHDNITWTAKAASqhmdlrpatvGQESVVSYlplSHI--AAQILDIWLPIKVGGqvyfaqpdalkgT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 251 RIITDRPYTPEYMI---QLVEKYKVTLLTVVPQ------QVASLLKTPTLnKQRLASIRFVSVGGGSCYVANLL---KLQ 318
Cdd:cd05933 236 LVKTLREVRPTAFMgvpRVWEKIQEKMKAVGAKsgtlkrKIASWAKGVGL-ETNLKLMGGESPSPLFYRLAKKLvfkKVR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 319 EFL--------ITG-----------------QISYGYALTECGG--VAANMGVAKPSSVGRIVPGVRVKILDEagRSLGH 371
Cdd:cd05933 315 KALgldrcqkfFTGaapisretlefflslniPIMELYGMSETSGphTISNPQAYRLLSCGKALPGCKTKIHNP--DADGI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 372 GEtgeILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVER-KEDLLRFHGAQYSPQEIEQVI-AELP 449
Cdd:cd05933 393 GE---ICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRiKELIITAGGENVPPVPIEDAVkKELP 469
|
....*....
gi 24648260 450 DVIEACVFG 458
Cdd:cd05933 470 IISNAMLIG 478
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
182-458 |
1.23e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 60.52 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 182 TLLLGGDHTVAILC-TSGTTGLPKAVCISNSACL-----FDFGFVTgQDVLLSFSTIDW--SAGMFNMLFSCCHGSTRII 253
Cdd:cd05937 80 RFVIVDPDDPAILIyTSGTTGLPKAAAISWRRTLvtsnlLSHDLNL-KNGDRTYTCMPLyhGTAAFLGACNCLMSGGTLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 254 TDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANllKLQEFLITGQISYGYALT 333
Cdd:cd05937 159 LSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWE--RFRERFNVPEIGEFYAAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 334 EcgGVAA----NMGVAKPSSVGRIVPGVR---------VKILDEAGRSL-----------GHGETGEILV----HNGKVW 385
Cdd:cd05937 237 E--GVFAltnhNVGDFGAGAIGHHGLIRRwkfenqvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGrvpfKNREAF 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24648260 386 NGYYANPN--ESKRMQDY--QG--WFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFG 458
Cdd:cd05937 315 QGYLHNEDatESKLVRDVfrKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
67-520 |
1.75e-09 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 60.18 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSIIar 146
Cdd:cd17656 25 QLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRHLKSKLSFN-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 147 ilKSHVytlkdhrlgMPRVEDLLEPTTAELYYVPETlllggDHTVAILCTSGTTGLPKAVCIS--NSACLFDF-----GF 219
Cdd:cd17656 103 --KSTI---------LLEDPSISQEDTSNIDYINNS-----DDLLYIIYTSGTTGKPKGVQLEhkNMVNLLHFerektNI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 220 VTGQDVLlSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEY--MIQLVEKY---KVTLLTVVPQQVASLLKTptlnKQ 294
Cdd:cd17656 167 NFSDKVL-QFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVeqLFDLVKRHnieVVFLPVAFLKFIFSEREF----IN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 295 RLAS-IRFVSVGGGSCYVANLLklQEFLITGQISYG--YALTECGGVAA---NMGVAKPS--SVGRIVPGVRVKILDEAG 366
Cdd:cd17656 242 RFPTcVKHIITAGEQLVITNEF--KEMLHEHNVHLHnhYGPSETHVVTTytiNPEAEIPElpPIGKPISNTWIYILDQEQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 367 RSLGHGETGEILVHNGKVWNGYYANP------------NESKRMqdyqgwFHTGDMGYFDNENYLHIVERKEDLLRFHGA 434
Cdd:cd17656 320 QLQPQGIVGELYISGASVARGYLNRQeltaekffpdpfDPNERM------YRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 435 QYSPQEIEQVIAELPDVIEACVFgLWNEVDGDPAAAAVVkIPGSRLTEMDIVEYVAKRLvvdhKQLHCGVFFLP--ELPK 512
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVL-DKADDKGEKYLCAYF-VMEQELNISQLREYLAKQL----PEYMIPSFFVPldQLPL 467
|
....*...
gi 24648260 513 TGSGKVLR 520
Cdd:cd17656 468 TPNGKVDR 475
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
193-518 |
2.55e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 59.41 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAV-----CISN---SAC-LFDfgfVTGQDVLL--SFSTIDWSAGMFNMLFSccHGSTRIITDRPYTPE 261
Cdd:cd17654 123 VIHTSGTTGTPKIVavphkCILPniqHFRsLFN---ITSEDILFltSPLTFDPSVVEIFLSLS--SGATLLIVPTSVKVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 262 YMI---QLVEKYKVTLL----TVVPQQVASLLKTPTLNkqRLASIRFVSVGGGSCYVANLLK--LQEFLITgQISYGYAL 332
Cdd:cd17654 198 PSKladILFKRHRITVLqatpTLFRRFGSQSIKSTVLS--ATSSLRVLALGGEPFPSLVILSswRGKGNRT-RIFNIYGI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 333 TE--CGGVAANMGVAK-PSSVGRIVPGVRVKILDEAGRSlGHGEtgeilVHNGKVWNGYYanpneskrMQDYQG-----W 404
Cdd:cd17654 275 TEvsCWALAYKVPEEDsPVQLGSPLLGTVIEVRDQNGSE-GTGQ-----VFLGGLNRVCI--------LDDEVTvpkgtM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 405 FHTGDMGYFdNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELpDVIEACVFGLWNEvdgDPAAAAVVKIPGSRLTEmd 484
Cdd:cd17654 341 RATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC-LGVESCAVTLSDQ---QRLIAFIVGESSSSRIH-- 413
|
330 340 350
....*....|....*....|....*....|....
gi 24648260 485 ivEYVAKRLVVDHKQLHCGVfFLPELPKTGSGKV 518
Cdd:cd17654 414 --KELQLTLLSSHAIPDTFV-QIDKLPLTSHGKV 444
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
196-456 |
3.97e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 58.73 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNSA---------CLFDFG-----------F-VTGQDVLlsfstidW-------------SAGMFNM 241
Cdd:PRK09029 143 TSGSTGLPKAAVHTAQAhlasaegvlSLMPFTaqdswllslplFhVSGQGIV-------WrwlyagatlvvrdKQPLEQA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 242 LFSCCHGStriitdrpytpeymiqlvekykvtlltVVPQQVASLLKtptlNKQRLASIRFVSVGGGSCYVANLLKLQEFL 321
Cdd:PRK09029 216 LAGCTHAS---------------------------LVPTQLWRLLD----NRSEPLSLKAVLLGGAAIPVELTEQAEQQG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 322 ITgqiSY-GYALTEcggvAANMGVAKP----SSVGRIVPGVRVKILDeagrslghgetGEILVHNGKVWNGYYANpNESK 396
Cdd:PRK09029 265 IR---CWcGYGLTE----MASTVCAKRadglAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQ-GQLV 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648260 397 RMQDYQGWFHTGDMGYFDNENyLHIVERKeDLLRFHGA---QysPQEIEQVIAELPDVIEACV 456
Cdd:PRK09029 326 PLVNDEGWFATRDRGEWQNGE-LTILGRL-DNLFFSGGegiQ--PEEIERVINQHPLVQQVFV 384
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
359-448 |
7.48e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 58.42 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 359 VKILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMqdYQG-------------WFHTGDMGY-FDNEnyLHIVE 423
Cdd:PRK05850 381 VRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERT--FGAtlvdpspgtpegpWLRTGDLGFiSEGE--LFIVG 456
|
90 100
....*....|....*....|....*
gi 24648260 424 RKEDLLRFHGAQYSPQEIEQVIAEL 448
Cdd:PRK05850 457 RIKDLLIVDGRNHYPDDIEATIQEI 481
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
329-458 |
1.62e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 57.34 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 329 GYALTE-CGGVAANM--GVAKPSSVGRIVPGVRVK---ILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQdYQ 402
Cdd:PLN02614 417 GYGLTEsCAGTFVSLpdELDMLGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVL-ID 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 403 GWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQE-IEQVIAELPDVIEACVFG 458
Cdd:PLN02614 496 GWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVEnIENIYGEVQAVDSVWVYG 552
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
193-529 |
1.77e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 57.07 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 193 ILCTSGTTGLPKAVcISNSA-----------------------CLFDFGFVTGQdvllsfstidwSAGMFNMLfscCHGS 249
Cdd:PRK00174 250 ILYTSGSTGKPKGV-LHTTGgylvyaamtmkyvfdykdgdvywCTADVGWVTGH-----------SYIVYGPL---ANGA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 250 TRIItdrpY--TPEY-----MIQLVEKYKVTLLTVVPQQVASLLKTPT--LNKQRLASIR-----------------FVS 303
Cdd:PRK00174 315 TTLM----FegVPNYpdpgrFWEVIDKHKVTIFYTAPTAIRALMKEGDehPKKYDLSSLRllgsvgepinpeawewyYKV 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 304 VGGGSCyvanllklqeflitgQISYGYALTECGGVaanM-----GV--AKPSSVGRIVPGVRVKILDEAGRSLGHGETGe 376
Cdd:PRK00174 391 VGGERC---------------PIVDTWWQTETGGI---MitplpGAtpLKPGSATRPLPGIQPAVVDEEGNPLEGGEGG- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 377 ILVHNgKVWNGY----YANPnesKRMQD-----YQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAE 447
Cdd:PRK00174 452 NLVIK-DPWPGMmrtiYGDH---ERFVKtyfstFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 448 LPDVIEACVFGLWNEVDGDPAAAAVV---KIPGSRLTEMDIVEYVAKRL----VVDHkqlhcgVFFLPELPKTGSGKVLR 520
Cdd:PRK00174 528 HPKVAEAAVVGRPDDIKGQGIYAFVTlkgGEEPSDELRKELRNWVRKEIgpiaKPDV------IQFAPGLPKTRSGKIMR 601
|
....*....
gi 24648260 521 QQARDQALG 529
Cdd:PRK00174 602 RILRKIAEG 610
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
326-451 |
2.34e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 56.66 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 326 ISYGYALTE-CGGvaANMGVAKPSSVGRI---VPGVRVKILD-EAGrslGHGET------GEILVHNGKVWNGYYANpnE 394
Cdd:PLN02387 448 IGQGYGLTEtCAG--ATFSEWDDTSVGRVgppLPCCYVKLVSwEEG---GYLISdkpmprGEIVIGGPSVTLGYFKN--Q 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648260 395 SKRMQDYQ------GWFHTGDMGYFDNENYLHIVERKEDLLRF-HGAQYSPQEIEQVIAELPDV 451
Cdd:PLN02387 521 EKTDEVYKvdergmRWFYTGDIGQFHPDGCLEIIDRKKDIVKLqHGEYVSLGKVEAALSVSPYV 584
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
317-458 |
5.87e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 55.62 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 317 LQEFL-IT--GQISYGYALTE-CGGVAANMGVAKP--SSVGRIVPGV--RVKILDEAG-RSLGHGETGEILVHNGKVWNG 387
Cdd:PLN02861 399 VEEFLrVTscSVLSQGYGLTEsCGGCFTSIANVFSmvGTVGVPMTTIeaRLESVPEMGyDALSDVPRGEICLRGNTLFSG 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648260 388 YYANPNESKRMQdYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQE-IEQVIAELPDVIEACVFG 458
Cdd:PLN02861 479 YHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVEnLENTYSRCPLIASIWVYG 549
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
67-519 |
9.62e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 54.80 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 67 RIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPK-LIFCD-----GKCFQR 140
Cdd:PRK03584 126 ALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKvLIAVDgyrygGKAFDR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 141 LSIIARILKS--------HVYTLKDHRLGMPRV-----EDLLEP-TTAELYYVPetllLGGDHTVAILCTSGTTGLPKav 206
Cdd:PRK03584 206 RAKVAELRAAlpslehvvVVPYLGPAAAAAALPgallwEDFLAPaEAAELEFEP----VPFDHPLWILYSSGTTGLPK-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 207 CISNSA--------------ClfDFGfvtGQDVLLSFSTIDWSagMFNMLFSCCH-GSTRIITD----RPyTPEYMIQLV 267
Cdd:PRK03584 280 CIVHGHggillehlkelglhC--DLG---PGDRFFWYTTCGWM--MWNWLVSGLLvGATLVLYDgspfYP-DPNVLWDLA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 268 EKYKVTLLTVVPQQVASLLKtptlnkqrlASIRFvsvggGSCYvaNLLKLQEFLITG------QISYGYAltecgGVAAN 341
Cdd:PRK03584 352 AEEGVTVFGTSAKYLDACEK---------AGLVP-----GETH--DLSALRTIGSTGsplppeGFDWVYE-----HVKAD 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 342 MGVAKPSS--------VG--RIVP-----------GVRVKILDEAGRSLGhGETGEILVHNG------KVWNgyyaNPnE 394
Cdd:PRK03584 411 VWLASISGgtdicscfVGgnPLLPvyrgeiqcrglGMAVEAWDEDGRPVV-GEVGELVCTKPfpsmplGFWN----DP-D 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 395 SKRMQD-----YQG-WFHtGDmgyfdnenYLHIVERkeDLLRFHG---AQYSPQ-------EIEQVIAELPDVIEACVFG 458
Cdd:PRK03584 485 GSRYRDayfdtFPGvWRH-GD--------WIEITEH--GGVVIYGrsdATLNRGgvrigtaEIYRQVEALPEVLDSLVIG 553
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 459 LwnEVDGDPAAAA--VVKIPGSRLTE-------MDIVEYVAKRLVVDHkqlhcgVFFLPELPKTGSGKVL 519
Cdd:PRK03584 554 Q--EWPDGDVRMPlfVVLAEGVTLDDalrarirTTIRTNLSPRHVPDK------IIAVPDIPRTLSGKKV 615
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
196-493 |
1.45e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 54.22 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 196 TSGTTGLPKAVCISNS---ACLFDFGF--VTGQDVLLSFSTIDWSAGMFNMLFSCCH-GSTrIITDRPYTPEYMIQLVEK 269
Cdd:cd05938 152 TSGTTGLPKAARISHLrvlQCSGFLSLcgVTADDVIYITLPLYHSSGFLLGIGGCIElGAT-CVLKPKFSASQFWDDCRK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 270 YKVTLLTVVPQQVASLLKTPTLNKQRLASIRfVSVGGGscYVANLLK--LQEFlitG--QISYGYALTEcggvaANMG-- 343
Cdd:cd05938 231 HNVTVIQYIGELLRYLCNQPQSPNDRDHKVR-LAIGNG--LRADVWRefLRRF---GpiRIREFYGSTE-----GNIGff 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 344 --VAKPSSVGR-------IVPGVRVK--------ILDEAGRSL--GHGETGEIL--VHNGKVWNGYYANPNES--KRMQD 400
Cdd:cd05938 300 nyTGKIGAVGRvsylyklLFPFELIKfdvekeepVRDAQGFCIpvAKGEPGLLVakITQQSPFLGYAGDKEQTekKLLRD 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 401 Y--QG--WFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwnEV---DGDPAAAAVV 473
Cdd:cd05938 380 VfkKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV--TVpghEGRIGMAAVK 457
|
330 340
....*....|....*....|
gi 24648260 474 KIPGSRLTEMDIVEYVAKRL 493
Cdd:cd05938 458 LKPGHEFDGKKLYQHVREYL 477
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
187-530 |
2.66e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.82 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 187 GDHTVAILCTSGTTGLPKAVCISNSACLFDFGFVTgqdvllsfSTIDWSAG--MFNML--FSCcHGstriitdrpYTPEY 262
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVA--------ARIDFSPEdkVFNALpvFHS-FG---------LTGGL 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 263 MIQLVEKYKVTL------LTVVPQQV----ASLL-KTPT-LNK-QRLA------SIRFVSVGggscyvANLLK------- 316
Cdd:PRK06814 854 VLPLLSGVKVFLypsplhYRIIPELIydtnATILfGTDTfLNGyARYAhpydfrSLRYVFAG------AEKVKeetrqtw 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 317 LQEFLItgQISYGYALTECGGV-AANMGVA-KPSSVGRIVPGVRVKILDEAGRSLGhgetGEILVHNGKVWNGYY--ANP 392
Cdd:PRK06814 928 MEKFGI--RILEGYGVTETAPViALNTPMHnKAGTVGRLLPGIEYRLEPVPGIDEG----GRLFVRGPNVMLGYLraENP 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 393 NESKRMQDyqGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAEL-PDvieacvfglwnevdgdpAAAA 471
Cdd:PRK06814 1002 GVLEPPAD--GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPD-----------------ALHA 1062
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 472 VVKIP----GSRL---------TEMDIVEYVAKR----LVVDHKQLHcgvffLPELPKTGSGKV----LRQQARDQALGK 530
Cdd:PRK06814 1063 AVSIPdarkGERIillttasdaTRAAFLAHAKAAgaseLMVPAEIIT-----IDEIPLLGTGKIdyvaVTKLAEEAAAKP 1137
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
361-524 |
5.88e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 52.42 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 361 ILD-EAGRSLGHGETGEILVHNGKVWNGYYANPNESKRM-----------------QDYQGWFHTGDMG-YFDNEnyLHI 421
Cdd:PRK07769 404 IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATfqnilksrlseshaegaPDDALWVRTGDYGvYFDGE--LYI 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 422 VERKEDLLRFHGAQYSPQEIE------------------QVIA-ELPD-VIEACVFGLWNEVDGDPAAAAVV--KIPGSR 479
Cdd:PRK07769 482 TGRVKDLVIIDGRNHYPQDLEytaqeatkalrtgyvaafSVPAnQLPQvVFDDSHAGLKFDPEDTSEQLVIVaeRAPGAH 561
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24648260 480 LTEMD-IVEYVAKRLVVDHKQLHCGVFFLP--ELPKTGSGKVLRQQAR 524
Cdd:PRK07769 562 KLDPQpIADDIRAAIAVRHGVTVRDVLLVPagSIPRTSSGKIARRACR 609
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
180-456 |
1.20e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.71 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 180 PETLLLGGDHTVAILCTSGTTGLPKAVCISNSAC------LFDFGFVTGQDVLL-----SFSTIDWSAgmFNMLFSCChg 248
Cdd:PRK05691 1265 APGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALaerlqwMQATYALDDSDVLMqkapiSFDVSVWEC--FWPLITGC-- 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 249 stRIITDRP---YTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLnkQRLASIRFVSVGGGSCYVANLLKLQEFLITGQ 325
Cdd:PRK05691 1341 --RLVLAGPgehRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA--AACTSLRRLFSGGEALPAELRNRVLQRLPQVQ 1416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 326 ISYGYALTEcggVAANM---------GVAKPssVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNES- 395
Cdd:PRK05691 1417 LHNRYGPTE---TAINVthwqcqaedGERSP--IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTa 1491
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 396 KRM------QDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACV 456
Cdd:PRK05691 1492 ERFvpdplgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAV 1558
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
65-526 |
2.99e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 50.08 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 65 AIRIAQQLKAMGLKQDDVVGI-----VGTNTTYLMPVVLGCLLNGTPFHAVSPwqdedTIKHLFSITRPKLIFC------ 133
Cdd:PLN03052 218 VSRVANALDALGFEKGDAIAIdmpmnVHAVIIYLAIILAGCVVVSIADSFAPS-----EIATRLKISKAKAIFTqdvivr 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 134 DGKCFQRLS--IIARILKSHVYTLKDHRLGMP-RVEDL--------LEPTTAELYYVPetLLLGGDHTVAILCTSGTTGL 202
Cdd:PLN03052 293 GGKSIPLYSrvVEAKAPKAIVLPADGKSVRVKlREGDMswddflarANGLRRPDEYKA--VEQPVEAFTNILFSSGTTGE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 203 PKAV---------CISNSACLFDfgfVTGQDVLLSFSTIDWSAGMFnMLFSCC---------HGStriitdrPYTPEYMi 264
Cdd:PLN03052 371 PKAIpwtqltplrAAADAWAHLD---IRKGDIVCWPTNLGWMMGPW-LVYASLlngatlalyNGS-------PLGRGFA- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 265 QLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLqefliTGQISYGYALTECGG------- 337
Cdd:PLN03052 439 KFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFGSTGEASSVDDYLWL-----MSRAGYKPIIEYCGGtelgggf 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 338 VAANMgvAKPSSVGRI-VP--GVRVKILDEAGRSLGHGE--TGEILVH-----------NGKVWNGYYanpnesKRMQDY 401
Cdd:PLN03052 514 VTGSL--LQPQAFAAFsTPamGCKLFILDDSGNPYPDDApcTGELALFplmfgasstllNADHYKVYF------KGMPVF 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 402 QGWF---HtGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPD-VIEACVFGLwNEVDGDP---AAAAVVK 474
Cdd:PLN03052 586 NGKIlrrH-GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAADEsVLETAAIGV-PPPGGGPeqlVIAAVLK 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24648260 475 IPGSRLTEMDIVEYVAKRLVvdHKQLH-----CGVFFLPELPKTGSGKVLRQQARDQ 526
Cdd:PLN03052 664 DPPGSNPDLNELKKIFNSAI--QKKLNplfkvSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
188-521 |
1.70e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 188 DHTVAILCTSGTTGLPKAVCISN-------SACLFDFGfVTGQDVLLSFSTIDWSAGMFNMLFSCCHGStRIITDR--PY 258
Cdd:PRK05691 2333 QHQAYLIYTSGSTGKPKGVVVSHgeiamhcQAVIERFG-MRADDCELHFYSINFDAASERLLVPLLCGA-RVVLRAqgQW 2410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 TPEYMIQLVEKYKVTLLTVVP---QQVASLLKTptlnKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTEC 335
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPsygSQLAQWLAG----QGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTET 2486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 336 ggVAANMGVAKPSS---------VGRIVpGVRVK-ILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKR-------M 398
Cdd:PRK05691 2487 --VVMPLACLAPEQleegaasvpIGRVV-GARVAyILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAErfvadpfA 2563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 399 QDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLwnevdGDPAAAAVVKIPGS 478
Cdd:PRK05691 2564 ADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-----DTPSGKQLAGYLVS 2638
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24648260 479 RLTEMDIVEYVAKRLVV-DHKQLHCGVFFLP-------ELPKTGSGKVLRQ 521
Cdd:PRK05691 2639 AVAGQDDEAQAALREALkAHLKQQLPDYMVPahlilldSLPLTANGKLDRR 2689
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
248-515 |
5.15e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 46.25 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 248 GSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIR-FVsvggGSCYVANLLK-LQEFLITGQ 325
Cdd:PRK07868 671 GGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRlFI----GSGMPTGLWErVVEAFAPAH 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 326 ISYGYALTECGGVAANMGVAKPSSVGRIVPG---VRV--------KIL-DEAG--RSLGHGETGEILVH-------NGKV 384
Cdd:PRK07868 747 VVEFFATTDGQAVLANVSGAKIGSKGRPLPGagrVELaaydpehdLILeDDRGfvRRAEVNEVGVLLARargpidpTASV 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 385 WNGYYAnPNESkrmqdyqgWFHTGDMGYFDNENYLHIVERKEDLLRF-HGAQYSpQEIEQVIAELPDVIEACVFGLwnEV 463
Cdd:PRK07868 827 KRGVFA-PADT--------WISTEYLFRRDDDGDYWLVDRRGSVIRTaRGPVYT-EPVTDALGRIGGVDLAVTYGV--EV 894
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24648260 464 DGDP-AAAAVVKIPGSRLTEMDIVEYVAKRLVVDHKQLhcgVFFLPELPKTGS 515
Cdd:PRK07868 895 GGRQlAVAAVTLRPGAAITAADLTEALASLPVGLGPDI---VHVVPEIPLSAT 944
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
186-458 |
5.88e-05 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 45.91 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 186 GGDHTVAILCTSGTTGLPK-AVCISNSACLFDFGFVTGQD------VLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPY 258
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKgAMYTERLVATFWLKVSSIQDirppasITLNFMPMSHIAGRISLYGTLARGGTAYFAAASD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 259 tpeyMIQLVEKY---KVTLLTVVPQ-----------QVASLLKTP----TLNKQRLASIRFVSVGG-------GSCYVAN 313
Cdd:cd17632 301 ----MSTLFDDLalvRPTELFLVPRvcdmlfqryqaELDRRSVAGadaeTLAERVKAELRERVLGGrllaavcGSAPLSA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 314 LLK-LQEFLITGQISYGYALTECGGVAANMGVAKPssvgrivPGVRVKILDEAgrSLGHGET------GEILVHNGKVWN 386
Cdd:cd17632 377 EMKaFMESLLDLDLHDGYGSTEAGAVILDGVIVRP-------PVLDYKLVDVP--ELGYFRTdrphprGELLVKTDTLFP 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648260 387 GYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSP-QEIEQVIAELPDVIEACVFG 458
Cdd:cd17632 448 GYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTvARLEAVFAASPLVRQIFVYG 520
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
350-457 |
2.29e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 40.79 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648260 350 VGRIVPGVRVKILDEAGRSL-GHGETGEILVHNGKVWNGYYANPNESKRMQDY------------QGWFHTGDMGYF--- 413
Cdd:cd05905 363 SGKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFLLDGETNDTFKVfpstrlstgitnNSYARTGLLGFLrpt 442
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24648260 414 -------DNENYLHIVERKEDLLRFHGAQYSPQEIEQ-VIAELPDVIEACVF 457
Cdd:cd05905 443 kctdlnvEEHDLLFVVGSIDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAVF 494
|
|
| |
