|
Name |
Accession |
Description |
Interval |
E-value |
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
132-445 |
2.30e-73 |
|
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: 233.72 E-value: 2.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHDF-TLLQKKYSVARSVK-----RVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRTPNRV 205
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrNLLAAAAALAASGGltegdVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSQSK 285
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAP-GIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 286 SnDSLWIKLSD-----KNIESRVVD-----------GMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVEVDGD-YI 345
Cdd:cd04433 160 P-DDDARKPGSvgrpvPGVEVRIVDpdggelppgeiGELVVRGPSVMKGYWNNPeatAAVDEDGWYRTGDLGRLDEDgYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 346 KILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYK 425
Cdd:cd04433 239 YIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--EELRAHVRERLAPYK 316
|
330 340
....*....|....*....|
gi 1264249082 426 IPQKVVLTTKKMHTERFKKD 445
Cdd:cd04433 317 VPRRVVFVDALPRTASGKID 336
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3-432 |
1.74e-63 |
|
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: 211.59 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 3 IDFLFERFEMNKECEAIVWEDKTYTYEWFLNQIKIYTRELNEH--RKMDytIVSLEADYSPYSIAMFLALIELGCTVVPi 80
Cdd:COG0318 2 ADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALgvGPGD--RVALLLPNSPEFVVAFLAALRAGAVVVP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 81 LNSLVDSKKKEYyeIVELENViKVergsfeIINIqrdyiqnelllqlkklkhpgLVLFSSGTTGSSKAIVHDFTLLqkkY 160
Cdd:COG0318 79 LNPRLTAEELAY--ILEDSGA-RA------LVTA--------------------LILYTSGTTGRPKGVMLTHRNL---L 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 161 SVARSVKRVIPF-----ML----FDHIGG-VNTLFQIISSSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLILS 230
Cdd:COG0318 127 ANAAAIAAALGLtpgdvVLvalpLFHVFGlTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 231 EVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSQSKSNDSLWIKLSD----KNIESRVVD- 305
Cdd:COG0318 207 PEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVgrplPGVEVRIVDe 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 306 ----------GMLQIKSMSTMIGYINAP----SPFtQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENV 370
Cdd:COG0318 286 dgrelppgevGEIVVRGPNVMKGYWNDPeataEAF-RDGWLRTGDLGRLDEDgYLYIVGRKKDMIISGGENVYPAEVEEV 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264249082 371 IQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVVL 432
Cdd:COG0318 365 LAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA--EELRAFLRERLARYKVPRRVEF 424
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
60-430 |
1.23e-47 |
|
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: 170.05 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 60 SPYSIAMFLALIELGCTVVPiLNSLV----------DSKKKEYYEIVELENVIKVERGSFEIINIQRDYIqnelllqlkk 129
Cdd:cd05936 59 CPQFPIAYFGALKAGAVVVP-LNPLYtprelehilnDSGAKALIVAVSFTDLLAAGAPLGERVALTPEDV---------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 130 lkhpGLVLFSSGTTGSSKA--IVHdFTLLQKKYSVARSVK-------RVIPFMLFDHIGG--VNtLFQIISSSGCLVIID 198
Cdd:cd05936 128 ----AVLQYTSGTTGVPKGamLTH-RNLVANALQIKAWLEdllegddVVLAALPLFHVFGltVA-LLLPLALGATIVLIP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 199 DRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSE-- 276
Cdd:cd05936 202 RFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTEts 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 --------YGVLYSQSksndslwIKLSDKNIESRVVD-----------GMLQIKSMSTMIGYINAP----SPFTqDGWLM 333
Cdd:cd05936 281 pvvavnplDGPRKPGS-------IGIPLPGTEVKIVDddgeelppgevGELWVRGPQVMKGYWNRPeetaEAFV-DGWLR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKR 412
Cdd:cd05936 353 TGDIGYMDEDgYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE--EE 430
|
410
....*....|....*...
gi 1264249082 413 LREFCKDKLPLYKIPQKV 430
Cdd:cd05936 431 IIAFCREQLAGYKVPRQV 448
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
133-431 |
5.07e-44 |
|
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: 159.70 E-value: 5.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVH-DFTLLQKKYS--VARSVKR----VIPFMLFdHIGGVNT-LFQIISSSGCLVIIDDRTPNR 204
Cdd:cd17631 100 LALLMYTSGTTGRPKGAMLtHRNLLWNAVNalAALDLGPddvlLVVAPLF-HIGGLGVfTLPTLLRGGTVVILRKFDPET 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIfpHVKITQMYGLSEYGVLYSQS 284
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSNDSLwiklsDK---------NIESRVVD-----------GMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVEVD 341
Cdd:cd17631 257 SPEDHR-----RKlgsagrpvfFVEVRIVDpdgrevppgevGEIVVRGPHVMAGYWNRPeatAAAFRDGWFHTGDLGRLD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 342 GD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDK 420
Cdd:cd17631 332 EDgYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDE--DELIAHCRER 409
|
330
....*....|.
gi 1264249082 421 LPLYKIPQKVV 431
Cdd:cd17631 410 LARYKIPKSVE 420
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
135-425 |
1.38e-43 |
|
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: 159.30 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 135 LVLFSSGTTG-------SSKAIVHDFTLLQKKYSVARSVKRVIPFML-FDHIGGVNTLfqIISS-SGCLVIIDDRT-PNR 204
Cdd:cd05911 150 AILYSSGTTGlpkgvclSHRNLIANLSQVQTFLYGNDGSNDVILGFLpLYHIYGLFTT--LASLlNGATVIIMPKFdSEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVLYSQS 284
Cdd:cd05911 228 FLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVN 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSNDSLWI---KLSdKNIESRVVD------------GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-Y 344
Cdd:cd05911 308 PDGDDKPGsvgRLL-PNVEAKIVDddgkdslgpnepGEICVRGPQVMKGYYNNPeatkETFDEDGWLHTGDIGYFDEDgY 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 345 IKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLY 424
Cdd:cd05911 387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE--KEVKDYVAKKVASY 464
|
.
gi 1264249082 425 K 425
Cdd:cd05911 465 K 465
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
137-430 |
5.39e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 147.26 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 137 LFSSGTTGSSKAIVH---DFTLLQKkySVARSVK-----RVIPFM-LFdHIGGVNTLFQIISSSGCLVIIDDRTPNRVCN 207
Cdd:PRK06187 173 LYTSGTTGHPKGVVLshrNLFLHSL--AVCAWLKlsrddVYLVIVpMF-HVHAWGLPYLALMAGAKQVIPRRFDPENLLD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 208 MIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSQSKSN 287
Cdd:PRK06187 250 LIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETSPVVSVLPPE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 288 DSL---WIKLSD-----KNIESRVVD-------------GMLQIKSMSTMIGYINAPSP---FTQDGWLMTGDMVEVDGD 343
Cdd:PRK06187 329 DQLpgqWTKRRSagrplPGVEARIVDddgdelppdggevGEIIVRGPWLMQGYWNRPEAtaeTIDGGWLHTGDVGYIDED 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 344 -YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLP 422
Cdd:PRK06187 409 gYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA--KELRAFLRGRLA 486
|
....*...
gi 1264249082 423 LYKIPQKV 430
Cdd:PRK06187 487 KFKLPKRI 494
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
17-430 |
7.28e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 144.28 E-value: 7.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 17 EAIVWEDKTYTYEWFLNQIKIYTRELNEH--RKMDYtiVSLEADYSPYSIAMFLALIELGCTVVPIlNS----------L 84
Cdd:PRK07656 22 EAYVFGDQRLTYAELNARVRRAAAALAALgiGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPL-NTrytadeaayiL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 85 VDSKKK----------EYYEIVE----LENVIKVERGSFEIINIQRDYIQNELLLQLKKLKHPGL-------VLFSSGTT 143
Cdd:PRK07656 99 ARGDAKalfvlglflgVDYSATTrlpaLEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVdpddvadILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 144 GSSKAIV--HdftllQKKYSVARSV---------KRVI---P-FMLFDHIGGVNTLFQiisSSGCLVIIDDRTPNRVCNM 208
Cdd:PRK07656 179 GRPKGAMltH-----RQLLSNAADWaeylgltegDRYLaanPfFHVFGYKAGVNAPLM---RGATILPLPVFDPDEVFRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 209 IEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVLYSQSKSND 288
Cdd:PRK07656 251 IETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTTFNRLDD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 289 SL-----WIKLSDKNIESRVVD-----------GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKI 347
Cdd:PRK07656 331 DRktvagTIGTAIAGVENKIVNelgeevpvgevGELLVRGPNVMKGYYDDPeataAAIDADGWLHTGDLGRLDEEgYLYI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 348 LGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIP 427
Cdd:PRK07656 411 VDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE--EELIAYCREHLAKYKVP 488
|
...
gi 1264249082 428 QKV 430
Cdd:PRK07656 489 RSI 491
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
18-432 |
7.79e-38 |
|
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: 142.81 E-value: 7.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 18 AIVWEDKTYTYEWFLNQIKIYTRELNEHRK-MDYTIVSLEADYSPYSIAMFLALIELGCTVVPILNSlvdskkkeyYEIV 96
Cdd:cd05941 4 AIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPS---------YPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 97 ELENVIKvERGSFEIINiqrdyiqnelllqlkklkhPGLVLFSSGTTGSSKAIVH-------DFTLLQK--KYSVARSVK 167
Cdd:cd05941 75 ELEYVIT-DSEPSLVLD-------------------PALILYTSGTTGRPKGVVLthanlaaNVRALVDawRWTEDDVLL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 168 RVIPfmLFdHIGG-VNTLFQIISSSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLI--------LSEVYKKYNL 238
Cdd:cd05941 135 HVLP--LH-HVHGlVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLqyyeahftDPQFARAAAA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 239 NSLQTISYGSEVMPEATLSKINEIFPHVkITQMYGLSEYGVLYSQSKSNDSL--WIKLSDKNIESRVVD----------- 305
Cdd:cd05941 212 ERLRLMVSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMALSNPLDGERRpgTVGMPLPGVQARIVDeetgeplprge 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 306 -GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKS-EIINIGGEKVFPAEVENVIQLMDGVE 378
Cdd:cd05941 291 vGEIQVRGPSVFKEYWNKPeatkEEFTDDGWFKTGDLGVVDEDgYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVS 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1264249082 379 EVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKrLREFCKDKLPLYKIPQKVVL 432
Cdd:cd05941 371 ECAVIGVPDPDWGERVVAVVVLRAGAAALSLEE-LKEWAKQRLAPYKRPRRLIL 423
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
11-433 |
1.56e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 139.91 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 11 EMNKECEAIVWEDKTYTY-EWFlNQIKIYTRELNEHRKMDYTIVSLEADYSPYsIAMFLALIELGCTVVPILNSLVDSKK 89
Cdd:PRK07638 12 SLQPNKIAIKENDRVLTYkDWF-ESVCKVANWLNEKESKNKTIAILLENRIEF-LQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 90 KEYYEIVELENVIKVERGSFEIINIQRDYIQ----NELLLQLKKLKHPGLVL--------FSSGTTGSSKAI-------V 150
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLPDEEGRVIEidewKRMIEKYLPTYAPIENVqnapfymgFTSGSTGKPKAFlraqqswL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 151 HDFTLLQKKYSVARSVKRVIPFMLFDHI---GGVNTLFQiissSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLL 227
Cdd:PRK07638 170 HSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTLYV----GQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 228 ILSEVYKKynlNSLQTISYGSEVMPEATlSKINEIFPHVKITQMYGLSEYGVLySQSKSNDSLWIKLSD----KNIESRV 303
Cdd:PRK07638 246 YKENRVIE---NKMKIISSGAKWEAEAK-EKIKNIFPYAKLYEFYGASELSFV-TALVDEESERRPNSVgrpfHNVQVRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 304 VD-----------GMLQIKSMSTMIGYIN---APSPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVE 368
Cdd:PRK07638 321 CNeageevqkgeiGTVYVKSPQFFMGYIIggvLARELNADGWMTVRDVGYEDEEgFIYIVGREKNMILFGGINIFPEEIE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264249082 369 NVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNesvsefRKRLREFCKDKLPLYKIPQKVVLT 433
Cdd:PRK07638 401 SVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSAT------KQQLKSFCLQRLSSFKIPKEWHFV 459
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
64-433 |
3.08e-36 |
|
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: 139.37 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 64 IAMFLALIELGCTVVPI---------------------------LNSLVDSKKKEYYEIVEL--ENVIKVERGSFEIINI 114
Cdd:cd05926 53 VVAFLAAARAGAVVAPLnpaykkaefefyladlgsklvltpkgeLGPASRAASKLGLAILELalDVGVLIRAPSAESLSN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 115 QRDYIQNELLLQLKKLKHPGLVLFSSGTTGSSKA-------IVHDFTLLQKKYSVARSVKRVIPFMLFdHIGG-VNTLFQ 186
Cdd:cd05926 133 LLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGvplthrnLAASATNITNTYKLTPDDRTLVVMPLF-HVHGlVASLLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 187 IISSSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYN-LNSLQTISYGSEVMPEATLSKINEIFpH 265
Cdd:cd05926 212 TLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATF-G 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 266 VKITQMYGLSEYGvlySQSKSND-----------------SLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAP----S 324
Cdd:cd05926 291 APVLEAYGMTEAA---HQMTSNPlppgprkpgsvgkpvgvEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPeanaE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 325 PFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN 403
Cdd:cd05926 368 AAFKDGWFRTGDLGYLDADgYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG 447
|
410 420 430
....*....|....*....|....*....|
gi 1264249082 404 ESVSEfrKRLREFCKDKLPLYKIPQKVVLT 433
Cdd:cd05926 448 ASVTE--EELRAFCRKHLAAFKVPKKVYFV 475
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
132-431 |
3.32e-36 |
|
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: 135.61 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAI-------VHDFTLLQKKYSVARSVKRVIPFMLfDHIGGVNTLFQIISSSGCLVIIDDRTPNR 204
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYyrserswIESFVCNEDLFNISGEDAILAPGPL-SHSLFLYGAISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLILSEVykkyNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYG-VLYSq 283
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQALARTLE----PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSfITYN- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 284 skSNDSLWIKLSD----KNIESRVVD------GMLQIKSMSTMIGYINAPSpFTQDGWLMTGDMVEVDGD-YIKILGRKS 352
Cdd:cd17633 155 --FNQESRPPNSVgrpfPNVEIEIRNadggeiGKIFVKSEMVFSGYVRGGF-SNPDGWMSVGDIGYVDEEgYLYLVGRES 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264249082 353 EIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVklsTNESVSefRKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd17633 232 DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLT--YKQLKRFLKQKLSRYEIPKKII 305
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
27-429 |
4.33e-34 |
|
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: 132.57 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 27 TYEWFLNQIKIYTRELNEHRKMDYTIVSLEADYSPYSIAMFLALIELGCTVVPILNSLVDSKKKEYYEIVELENVI---K 103
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLtdsL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 104 VERGSFEIINIQRDYIQNELLLQLKKLKH---PGLVLFSSGTTGSSKAIVHDFtllQKKYSVARSVKRVIPFMLFD---- 176
Cdd:TIGR01923 81 LEEKDFQADSLDRIEAAGRYETSLSASFNmdqIATLMFTSGTTGKPKAVPHTF---RNHYASAVGSKENLGFTEDDnwll 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 177 -----HIGGVNTLFQIISSSGCLVIIDDRtpNRVCNMIEKHQVQALPASPTFINLLiLSEVYKKYNLnslQTISYGSEVM 251
Cdd:TIGR01923 158 slplyHISGLSILFRWLIEGATLRIVDKF--NQLLEMIANERVTHISLVPTQLNRL-LDEGGHNENL---RKILLGGSAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 252 PeATLSK--INEIFPhvkITQMYGLSEygvLYSQS--KSNDSLWIK------LSDKNIESRVVD----GMLQIKSMSTMI 317
Cdd:TIGR01923 232 P-APLIEeaQQYGLP---IYLSYGMTE---TCSQVttATPEMLHARpdvgrpLAGREIKIKVDNkeghGEIMVKGANLMK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 318 GYIN---APSPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQM 393
Cdd:TIGR01923 305 GYLYqgeLTPAFEQQGWFNTGDIGELDGEgFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQV 384
|
410 420 430
....*....|....*....|....*....|....*.
gi 1264249082 394 VKAVVKLSTNESVSEfrkrLREFCKDKLPLYKIPQK 429
Cdd:TIGR01923 385 PVAYIVSESDISQAK----LIAYLTEKLAKYKVPIA 416
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
195-433 |
2.42e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 128.90 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 195 VIIDDRTPNRVCNMIEKHQVQALPASPT-FINLLiLSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYG 273
Cdd:PRK08316 242 VILDAPDPELILRTIEAERITSFFAPPTvWISLL-RHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 274 LSEYGVLYSQSKSNDSLwIKLSDK-----NIESRVVD-----------GMLQIKSMSTMIGYINAP----SPFtQDGWLM 333
Cdd:PRK08316 321 QTEIAPLATVLGPEEHL-RRPGSAgrpvlNVETRVVDddgndvapgevGEIVHRSPQLMLGYWDDPektaEAF-RGGWFH 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKR 412
Cdd:PRK08316 399 SGDLGVMDEEgYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE--DE 476
|
250 260
....*....|....*....|.
gi 1264249082 413 LREFCKDKLPLYKIPQKVVLT 433
Cdd:PRK08316 477 LIAHCRARLAGFKVPKRVIFV 497
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
133-431 |
2.53e-32 |
|
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: 128.40 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHD---------FTLLQKKYSVARSvKRVIPFMLFDHIGGVNTLFQI-ISSSGCLVIIDDRTP 202
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVIPqraaesrvlFMSTQAGLRHGRH-NVVLGLMPLYHVIGFFAVLVAaLALDGTYVVVEEFDP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKiTQMYGLSE-YGVLY 281
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK-VNIYGTTEaMNSLY 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 282 SQSKSNDS------------LWIKLSDKNIESRVVDGMLQIKSMS--TMIGYINAPSPFT---QDGWLMTGDMVEVDGD- 343
Cdd:cd05923 310 MRDARTGTemrpgffsevriVRIGGSPDEALANGEEGELIVAAAAdaAFTGYLNQPEATAkklQDGWYRTGDVGYVDPSg 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 344 YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNeSVSEfrKRLREFCKD-KLP 422
Cdd:cd05923 390 DVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSA--DELDQFCRAsELA 466
|
....*....
gi 1264249082 423 LYKIPQKVV 431
Cdd:cd05923 467 DFKRPRRYF 475
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
138-431 |
5.38e-32 |
|
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: 124.70 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKA--IVHdFTLLQKKYSVARSVKR------VIPFMLFdH-----IGGVNTLfqiisSSGCLVIIDDRT--P 202
Cdd:cd05917 9 FTSGTTGSPKGatLTH-HNIVNNGYFIGERLGLteqdrlCIPVPLF-HcfgsvLGVLACL-----THGATMVFPSPSfdP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPT-FINLLILSEvYKKYNLNSLQT-ISYGSEVmPEATLSKINEIFPHVKITQMYGLSEYGVL 280
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTmFIAELEHPD-FDKFDLSSLRTgIMAGAPC-PPELMKRVIEVMNMKDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 YSQSKSNDSLWIKLSD-----KNIESRVVD------------GMLQIKSMSTMIGYINAPS----PFTQDGWLMTGDMVE 339
Cdd:cd05917 160 STQTRTDDSIEKRVNTvgrimPHTEAKIVDpeggivppvgvpGELCIRGYSVMKGYWNDPEktaeAIDGDGWLHTGDLAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 340 VDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCK 418
Cdd:cd05917 240 MDEDgYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE--EDIKAYCK 317
|
330
....*....|...
gi 1264249082 419 DKLPLYKIPQKVV 431
Cdd:cd05917 318 GKIAHYKVPRYVF 330
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
25-431 |
5.16e-31 |
|
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: 123.23 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 25 TYTYEWFLNQIKIYTRELNEHRKMDYTIVSLEADYSPYSIAMFLALIELGCTVVPILNSLvdSKKKEYYEIVELEnvIKV 104
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRL--TPNELAFQLKDSD--VKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 105 ErgsfEIINIqrdyiqnelllqlkklkhpglvLFSSGTTGSSKAIVHDFtllQKKYSVARSVKR----------VIPFML 174
Cdd:cd05912 77 D----DIATI----------------------MYTSGTTGKPKGVQQTF---GNHWWSAIGSALnlglteddnwLCALPL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 175 FdHIGGVNTLF-QIISssGCLVIIDDR-TPNRVCNMIEKHQVQALPASPTFINLLIlsEVYKKYNLNSLQTISYGSEVMP 252
Cdd:cd05912 128 F-HISGLSILMrSVIY--GMTVYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILLGGGPAP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 253 EATLSKINEI-FPhvkITQMYGLSEygvLYSQS---KSNDSLwIKLSD-----KNIESRVVD--------GMLQIKSMST 315
Cdd:cd05912 203 KPLLEQCKEKgIP---VYQSYGMTE---TCSQIvtlSPEDAL-NKIGSagkplFPVELKIEDdgqppyevGEILLKGPNV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 316 MIGYINAPSP---FTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITG 391
Cdd:cd05912 276 TKGYLNRPDAteeSFENGWFKTGDIGYLDEEgFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWG 355
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1264249082 392 QMVKAVVKLSTNESVSEfrkrLREFCKDKLPLYKIPQKVV 431
Cdd:cd05912 356 QVPVAFVVSERPISEEE----LIAYCSEKLAKYKVPKKIY 391
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
136-428 |
9.75e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 124.50 E-value: 9.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSK-AIVHDFTLLQKKYSVARSV------KRVIPFMLFDHIGGVNTLFQIISSSGCLVI-IDDRTPNRVCN 207
Cdd:PRK12583 206 IQYTSGTTGFPKgATLSHHNILNNGYFVAESLgltehdRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 208 MIEKHQVQALPASPT-FINLLILSEvYKKYNLNSLQT-ISYGSEVMPEATLSKINEI-FPHVKITqmYGLSEYGVLYSQS 284
Cdd:PRK12583 286 AVEEERCTALYGVPTmFIAELDHPQ-RGNFDLSSLRTgIMAGAPCPIEVMRRVMDEMhMAEVQIA--YGMTETSPVSLQT 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSNDSLWIKLSD-----KNIESRVVD-----------GMLQIKSMSTMIGYINAPSP----FTQDGWLMTGDMVEVDGD- 343
Cdd:PRK12583 363 TAADDLERRVETvgrtqPHLEVKVVDpdgatvprgeiGELCTRGYSVMKGYWNNPEAtaesIDEDGWMHTGDLATMDEQg 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 344 YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPL 423
Cdd:PRK12583 443 YVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASE--EELREFCKARIAH 520
|
....*
gi 1264249082 424 YKIPQ 428
Cdd:PRK12583 521 FKVPR 525
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
132-431 |
1.39e-30 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 124.07 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHDF--TLLQkkysVARSVKRV--------------IPFMlFDHIGGVntLFQIISssGCLV 195
Cdd:COG0365 185 DPLFILYTSGTTGKPKGVVHTHggYLVH----AATTAKYVldlkpgdvfwctadIGWA-TGHSYIV--YGPLLN--GATV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 196 IIDDRTPN-----RVCNMIEKHQVQALPASPTFINLLILS--EVYKKYNLNSLQTIsyGS--EVMPEATLSKINEIFpHV 266
Cdd:COG0365 256 VLYEGRPDfpdpgRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLL--GSagEPLNPEVWEWWYEAV-GV 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 267 KITQMYGLSEygvlysqsksndSLWIKLSdkN-----------------IESRVVD-----------GMLQIK----SMs 314
Cdd:COG0365 333 PIVDGWGQTE------------TGGIFIS--NlpglpvkpgsmgkpvpgYDVAVVDedgnpvppgeeGELVIKgpwpGM- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 315 tMIGYINAPSPF------TQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKN 387
Cdd:COG0365 398 -FRGYWNDPERYretyfgRFPGWYRTGDGARRDEDgYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPD 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1264249082 388 AITGQMVKAVVKLSTNESVS-EFRKRLREFCKDKLPLYKIPQKVV 431
Cdd:COG0365 477 EIRGQVVKAFVVLKPGVEPSdELAKELQAHVREELGPYAYPREIE 521
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-445 |
2.02e-30 |
|
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: 120.95 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 134 GLVLFSSGTTGSSKAIV---HDFTLLQK-------------KYSVARSVKR-------VIPFMlfdHIGGVNTLFQIISS 190
Cdd:cd05924 6 LYILYTGGTTGMPKGVMwrqEDIFRMLMggadfgtgeftpsEDAHKAAAAAagtvmfpAPPLM---HGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 191 SGCLVIIDDR-TPNRVCNMIEKHQVQALP------ASPtfinLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIF 263
Cdd:cd05924 83 GQTVVLPDDRfDPEEVWRTIEKHKVTSMTivgdamARP----LIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 264 PHVKITQMYGLSEYGVL---YSQSKSNDS--------LWIKLSDkniESRVV----DGMLQIKSMSTM-IGYINAPSP-- 325
Cdd:cd05924 159 PNITLVDAFGSSETGFTgsgHSAGSGPETgpftranpDTVVLDD---DGRVVppgsGGVGWIARRGHIpLGYYGDEAKta 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 326 ---FTQDG--WLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVK 399
Cdd:cd05924 236 etfPEVDGvrYAVPGDRATVEADgTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQ 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1264249082 400 LSTNESVSEfrKRLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKD 445
Cdd:cd05924 316 LREGAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
133-435 |
1.11e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 120.74 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHD-----FTLLQKKYSV-ARSVKRVIPFMLFDHIGGVNTL-FQIISSSGCLVIIDDRTPNRV 205
Cdd:PRK06839 151 SFIICYTSGTTGKPKGAVLTqenmfWNALNNTFAIdLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVPRKFEPTKA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEifPHVKITQMYGLSEY-------- 277
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID--RGFLFGQGFGMTETsptvfmls 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 278 --------GVLYSQSKSNDSLWIKLSDKNIESRVVdGMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVEVDGD-YI 345
Cdd:PRK06839 309 eedarrkvGSIGKPVLFCDYELIDENKNKVEVGEV-GELLIRGPNVMKEYWNRPdatEETIQDGWLCTGDLARVDEDgFV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 346 KILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYK 425
Cdd:PRK06839 388 YIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE--KDVIEHCRLFLAKYK 465
|
330
....*....|
gi 1264249082 426 IPQKVVLTTK 435
Cdd:PRK06839 466 IPKEIVFLKE 475
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
133-427 |
1.24e-29 |
|
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: 117.82 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHdfTLLQKKYSvARSVKRVIPFMLFD---------HIGGVNTLFQIISSSGCLVIIDDRTPN 203
Cdd:cd17630 2 LATVILTSGSTGTPKAVVH--TAANLLAS-AAGLHSRLGFGGGDswllslplyHVGGLAILVRSLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVcnmiekhqvQALPASPTFINLL------ILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIfpHVKITQMYGLSEY 277
Cdd:cd17630 79 AE---------DLAPPGVTHVSLVptqlqrLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 278 GvlySQSKSNDSLWIKLSD-----KNIESRVV-DGMLQIKSMSTMIGYINA--PSPFTQDGWLMTGDMVEVDGD-YIKIL 348
Cdd:cd17630 148 A---SQVATKRPDGFGRGGvgvllPGRELRIVeDGEIWVGGASLAMGYLRGqlVPEFNEDGWFTTKDLGELHADgRLTVL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264249082 349 GRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrkrLREFCKDKLPLYKIP 427
Cdd:cd17630 225 GRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAE----LRAWLKDKLARFKLP 299
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
136-430 |
1.74e-29 |
|
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: 117.60 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIV--HDFTLlqkkySVARSVKRVIPFMLFDHIGGVNTLFQIIS-SSGCLV-IIDDRT--------PN 203
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQTL-----RAAAAWADCADLTEDDRYLIINPFFHTFGyKAGIVAcLLTGATvvpvavfdVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVLYSQ 283
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 284 SKSNDSLWIKLSD----KNIESRVVD-GMLQIKSMSTMIGYINAPSPFTQ----DGWLMTGDMVEVD-GDYIKILGRKSE 353
Cdd:cd17638 160 RPGDDAETVATTCgracPGFEVRIADdGEVLVRGYNVMQGYLDDPEATAEaidaDGWLHTGDVGELDeRGYLRITDRLKD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264249082 354 IINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKV 430
Cdd:cd17638 240 MYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTE--EDVIAWCRERLANYKVPRFV 314
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
60-358 |
1.80e-29 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 118.95 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 60 SPYSIAMFLALIELGCTVVP------------ILNS------LVDS--------KKKEYYEIVELENVIKVERGSFEIIN 113
Cdd:pfam00501 56 SPEWVVAFLACLKAGAVYVPlnprlpaeelayILEDsgakvlITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 114 IQRDYIQNELLLQLKKLK--HPGLVLFSSGTTGSSKAIVHD------FTLLQKKYS----VARSVKRVIPFMLFDHIGGV 181
Cdd:pfam00501 136 PEEAKPADVPPPPPPPPDpdDLAYIIYTSGTTGKPKGVMLThrnlvaNVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 182 NT-LFQIISSSGCLVIID---DRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLS 257
Cdd:pfam00501 216 SLgLLGPLLAGATVVLPPgfpALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 258 KINEIFPHVkITQMYGLSEYGVLYSQSKSNDSLWIKLSD-----KNIESRVVD------------GMLQIKSMSTMIGYI 320
Cdd:pfam00501 296 RFRELFGGA-LVNGYGLTETTGVVTTPLPLDEDLRSLGSvgrplPGTEVKIVDdetgepvppgepGELCVRGPGVMKGYL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1264249082 321 NAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIG 358
Cdd:pfam00501 375 NDPeltaEAFDEDGWYRTGDLGRRDEDgYLEIVGRKKDQIKLG 417
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
137-408 |
4.39e-28 |
|
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: 116.18 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 137 LFSSGTTGSSKAIV-------------HDFTLLQKKYSVarsvkRVIPFMLFDHIGGVNTLFQIISSSG-CLVIIDDRTP 202
Cdd:cd05904 164 LYSSGTTGRSKGVMlthrnliamvaqfVAGEGSNSDSED-----VFLCVLPMFHIYGLSSFALGLLRLGaTVVVMPRFDL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEY-GVLY 281
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEStGVVA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 282 S-------QSKSNDSLWIKlsdKNIESRVVD------------GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMV 338
Cdd:cd05904 319 McfapekdRAKYGSVGRLV---PNVEAKIVDpetgeslppnqtGELWIRGPSIMKGYLNNPeataATIDKEGWLHTGDLC 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264249082 339 EVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSE 408
Cdd:cd05904 396 YIDEDgYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE 466
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
132-431 |
1.15e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 115.41 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHD-FTLLQkkySVARSVKRV---------IPFMLFdHIGGVNTlFQIISSSGCLVIIDDR- 200
Cdd:PRK07788 208 PGGIVILTSGTTGTPKGAPRPePSPLA---PLAGLLSRVpfragettlLPAPMF-HATGWAH-LTLAMALGSTVVLRRRf 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 201 TPNRVCNMIEKHQVQALPASPTFIN--LLILSEVYKKYNLNSLQTI-SYGSEVMPE---ATLSKINEIfphvkITQMYGL 274
Cdd:PRK07788 283 DPEATLEDIAKHKATALVVVPVMLSriLDLGPEVLAKYDTSSLKIIfVSGSALSPElatRALEAFGPV-----LYNLYGS 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 275 SEygVLYSQSKSNDSLW--------------IKLSDKN---IESRVVdGMLQIKSMSTMIGYINAPSPFTQDGWLMTGDM 337
Cdd:PRK07788 358 TE--VAFATIATPEDLAeapgtvgrppkgvtVKILDENgneVPRGVV-GRIFVGNGFPFEGYTDGRDKQIIDGLLSSGDV 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 338 VEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREF 416
Cdd:PRK07788 435 GYFDEDgLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE--DAIKDY 512
|
330
....*....|....*
gi 1264249082 417 CKDKLPLYKIPQKVV 431
Cdd:PRK07788 513 VRDNLARYKVPRDVV 527
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
18-432 |
8.09e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 112.36 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 18 AIVWEDKTYTYEWFLNQIKIYTRELNEHRKMDYTIVSLEADYSPYSIAMFLALIELGCTVVpILNS----------LVDS 87
Cdd:PRK03640 20 AIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAV-LLNTrlsreellwqLDDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 88 KKK------EYYEIVELENVIKVE---RGSFEIINIQRDYIQNELLLqlkklkhpglVLFSSGTTGSSKAIVHDFtllQK 158
Cdd:PRK03640 99 EVKclitddDFEAKLIPGISVKFAelmNGPKEEAEIQEEFDLDEVAT----------IMYTSGTTGKPKGVIQTY---GN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 159 KYSVARSV----------KRVIPFMLFdHIGGVNTLF-QIISssGCLVIIDDR-TPNRVCNMIEKHQVQALPASPTFINL 226
Cdd:PRK03640 166 HWWSAVGSalnlglteddCWLAAVPIF-HISGLSILMrSVIY--GMRVVLVEKfDAEKINKLLQTGGVTIISVVSTMLQR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 227 LIlsEVYKK--YNlNSLQTISYGSEVMPEATLSKINEifPHVKITQMYGLSEYGvlySQS---KSNDSL----------- 290
Cdd:PRK03640 243 LL--ERLGEgtYP-SSFRCMLLGGGPAPKPLLEQCKE--KGIPVYQSYGMTETA---SQIvtlSPEDALtklgsagkplf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 291 --WIKLSDKNIESRVVD-GMLQIKSMSTMIGYINAPSPFTQ---DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVF 363
Cdd:PRK03640 315 pcELKIEKDGVVVPPFEeGEIVVKGPNVTKGYLNREDATREtfqDGWFKTGDIGYLDEEgFLYVLDRRSDLIISGGENIY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264249082 364 PAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrkrLREFCKDKLPLYKIPQKVVL 432
Cdd:PRK03640 395 PAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEE----LRHFCEEKLAKYKVPKRFYF 459
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
133-439 |
3.01e-26 |
|
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: 110.28 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFTLLQKKYSVARSVKRVIPFMLFDHIGG----VNTLFQIISS--SGCLVIIDDR--TPNR 204
Cdd:cd05969 91 PTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADpgwvTGTVYGIWAPwlNGVTNVVYEGrfDAES 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLILSEVY--KKYNLNSLQTI-SYGSEVMPEATLSKINEIfpHVKITQMYGLSEYGvly 281
Cdd:cd05969 171 WYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIhSVGEPLNPEAIRWGMEVF--GVPIHDTWWQTETG--- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 282 SQSKSN-DSLWIKLSD-----KNIESRVVD-----------GMLQIKS--MSTMIGYINAPSPFTQ---DGWLMTGDMVE 339
Cdd:cd05969 246 SIMIANyPCMPIKPGSmgkplPGVKAAVVDengnelppgtkGILALKPgwPSMFRGIWNDEERYKNsfiDGWYLTGDLAY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 340 VDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN-ESVSEFRKRLREFC 417
Cdd:cd05969 326 RDEDgYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfEPSDELKEEIINFV 405
|
330 340
....*....|....*....|..
gi 1264249082 418 KDKLPLYKIPQKVVLTTKKMHT 439
Cdd:cd05969 406 RQKLGAHVAPREIEFVDNLPKT 427
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
134-433 |
6.47e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 110.36 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 134 GLVLFSSGTTGSSKAIV---HDF-------------TLLQKKYSVARSVKR--------VIPFMlfdHIGGVNTLFQIIS 189
Cdd:PRK07798 166 LYLLYTGGTTGMPKGVMwrqEDIfrvllggrdfatgEPIEDEEELAKRAAAgpgmrrfpAPPLM---HGAGQWAAFAALF 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 190 SSGCLVIIDDRT--PNRVCNMIEKHQVQALP------ASPtfinLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINE 261
Cdd:PRK07798 243 SGQTVVLLPDVRfdADEVWRTIEREKVNVITivgdamARP----LLDALEARGPYDLSSLFAIASGGALFSPSVKEALLE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 262 IFPHVKITQMYGLSEYGVLYSQSKSNDSLWIKLSDKNIESR--VVD-------------GMLQiKSMSTMIGYINAPSP- 325
Cdd:PRK07798 319 LLPNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRtvVLDedgnpvepgsgeiGWIA-RRGHIPLGYYKDPEKt 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 326 ----FTQDG--WLMTGDM--VEVDGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAV 397
Cdd:PRK07798 398 aetfPTIDGvrYAIPGDRarVEADGT-ITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAV 476
|
330 340 350
....*....|....*....|....*....|....*.
gi 1264249082 398 VKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVVLT 433
Cdd:PRK07798 477 VQLREGARPDL--AELRAHCRSSLAGYKVPRAIWFV 510
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
18-431 |
8.59e-26 |
|
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: 108.87 E-value: 8.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 18 AIVWEDKTYTYEWFLNQIKIYTRELNEHRKMDYTIVSLEADYSPYSIAMFLALIELGCTVVPILNSlvdskkkeyYEIVE 97
Cdd:cd05945 9 AVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS---------SPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 98 LENVIKVERGSFeIINIQRD--YIqnelllqlkklkhpglvLFSSGTTGSSKAIVHDFTLLQKKYSVARSVKRVIP---F 172
Cdd:cd05945 80 IREILDAAKPAL-LIADGDDnaYI-----------------IFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPgdvF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 173 M-----LFDHigGVNTLFQIISSSGCLVIIDD---RTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTI 244
Cdd:cd05945 142 LnqapfSFDL--SVMDLYPALASGATLVPVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 245 SYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVLYSQ-------SKSNDSLWIKLSDKNIESRVVD-----------G 306
Cdd:cd05945 220 LFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYievtpevLDGYDRLPIGYAKPGAKLVILDedgrpvppgekG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 307 MLQIKSMSTMIGYINAPSP-----FTQDG--WLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVE 378
Cdd:cd05945 300 ELVISGPSVSKGYLNNPEKtaaafFPDEGqrAYRTGDLVRLEADgLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1264249082 379 EVAVVGEKNAITGQMVKAVVKLSTNESvSEFRKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd05945 380 EAVVVPKYKGEKVTELIAFVVPKPGAE-AGLTKAIKAELAERLPPYMIPRRFV 431
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
133-430 |
1.41e-25 |
|
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: 108.19 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFTLLQKKYSVARSVKRVIPFMLFDHIG----GVNTLFQIIS--SSGCLVIIDDR---TPN 203
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIAdpgwAKGAWSSFFGpwLLGATVFVYEGprfDAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVCNMIEKHQVQALPASPTFINLLIlSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYsq 283
Cdd:cd05972 163 RILELLERYGVTSFCGPPTAYRMLI-KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTV-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 284 sksNDSLWIKLSDKNI-------ESRVVD-----------GMLQIKSM--STMIGYINAP---SPFTQDGWLMTGDMVEV 340
Cdd:cd05972 239 ---GNFPDMPVKPGSMgrptpgyDVAIIDddgrelppgeeGDIAIKLPppGLFLGYVGDPektEASIRGDYYLTGDRAYR 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 341 DGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKL-STNESVSEFRKRLREFCK 418
Cdd:cd05972 316 DEDgYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLtSGYEPSEELAEELQGHVK 395
|
330
....*....|..
gi 1264249082 419 DKLPLYKIPQKV 430
Cdd:cd05972 396 KVLAPYKYPREI 407
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
132-447 |
3.76e-25 |
|
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: 107.92 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLF---SSGTTGSSKAI--VHDFTLlqkkYSVARSVKR-----------VIP----FMLfdhigGVNTLFQIISSS 191
Cdd:COG1021 182 DPDDVAFfqlSGGTTGLPKLIprTHDDYL----YSVRASAEIcgldadtvylaALPaahnFPL-----SSPGVLGVLYAG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 192 GCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPhVKITQM 271
Cdd:COG1021 253 GTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-CTLQQV 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 272 YGLSEYGVLYSqsKSNDSLWIKLS---------DkniESRVVD-----------GMLQIKSMSTMIGYINAP----SPFT 327
Cdd:COG1021 332 FGMAEGLVNYT--RLDDPEEVILTtqgrpispdD---EVRIVDedgnpvppgevGELLTRGPYTIRGYYRAPehnaRAFT 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 328 QDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVkLSTNESV 406
Cdd:COG1021 407 PDGFYRTGDLVRRTPDgYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV-VPRGEPL 485
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1264249082 407 SefRKRLREFCKDK-LPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:COG1021 486 T--LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKK 525
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
65-432 |
4.70e-25 |
|
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: 106.70 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 65 AMFLALIELGCTVVPILNSLVDSkkkeyyeivELENVIKveRGSFEIINIQRDYIQNELLLQLKKlkhPGLVLFSSGTTG 144
Cdd:cd05903 41 VLYLACLRIGAVTNPILPFFREH---------ELAFILR--RAKAKVFVVPERFRQFDPAAMPDA---VALLLFTSGTTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 145 SSKAIVHDFTllqkkySVARSVKRVIPFMLFD------------HIGGVNTLFQIISSSGCLVIIDDR-TPNRVCNMIEK 211
Cdd:cd05903 107 EPKGVMHSHN------TLSASIRQYAERLGLGpgdvflvaspmaHQTGFVYGFTLPLLLGAPVVLQDIwDPDKALALMRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 212 HQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSQSKSNDSLW 291
Cdd:cd05903 181 HGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 292 IKLSDKN----IESRVVD-----------GMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVEVD-GDYIKILGRKS 352
Cdd:cd05903 260 RLYTDGRplpgVEIKVVDdtgatlapgveGELLSRGPSVFLGYLDRPdltADAAPEGWFRTGDLARLDeDGYLRITGRSK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 353 EIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSeFRKRLREFCKDKLPLYKIPQKVVL 432
Cdd:cd05903 340 DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLT-FDELVAYLDRQGVAKQYWPERLVH 418
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
174-434 |
1.59e-24 |
|
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: 103.50 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 174 LFdHIGGVNTLFQIISSSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISyGSEvMPE 253
Cdd:cd17637 50 LF-HIAGLNLALATFHAGGANVVMEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL-GLD-APE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 254 aTLSKINEIFPhVKITQMYGLSEYGVLYSQSKSND--------SLW--IKLSDKN-IESRV-VDGMLQIKSMSTMIGYIN 321
Cdd:cd17637 127 -TIQRFEETTG-ATFWSLYGQTETSGLVTLSPYRErpgsagrpGPLvrVRIVDDNdRPVPAgETGEIVVRGPLVFQGYWN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 322 AP--SPFT-QDGWLMTGDMVEVDGD-YIKILGRKSE--IINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVK 395
Cdd:cd17637 205 LPelTAYTfRNGWHHTGDLGRFDEDgYLWYAGRKPEkeLIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIK 284
|
250 260 270
....*....|....*....|....*....|....*....
gi 1264249082 396 AVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVVLTT 434
Cdd:cd17637 285 AVCVLKPGATLTA--DELIEFVGSRIARYKKPRYVVFVE 321
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
133-431 |
1.75e-24 |
|
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: 105.91 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVH---DFTLLQKKYsvARSVKRVIP----F---MLFDHIGGVNTLFQIISSSGCLVIIDDR-T 201
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHlhaDIYWTAELY--ARNVLGIREddvcFsaaKLFFAYGLGNSLTFPLSVGATTVLMPERpT 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 PNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFP-------------HVKI 268
Cdd:cd05959 243 PAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGldildgigstemlHIFL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 269 TQMYGLSEYGvlySQSKSNDSLWIKLSDKNiESRVVD---GMLQIKSMSTMIGYINAP----SPFtQDGWLMTGDMVEVD 341
Cdd:cd05959 323 SNRPGRVRYG---TTGKPVPGYEVELRDED-GGDVADgepGELYVRGPSSATMYWNNRdktrDTF-QGEWTRTGDKYVRD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 342 GD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSE-FRKRLREFCKD 419
Cdd:cd05959 398 DDgFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEaLEEELKEFVKD 477
|
330
....*....|..
gi 1264249082 420 KLPLYKIPQKVV 431
Cdd:cd05959 478 RLAPYKYPRWIV 489
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
138-430 |
2.14e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 105.66 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSK-AIVHDFTLLQKKYSVARSVK-----RV-IPFMLFDHIGGVNTLFQIISSSGCLVIIDDR-TPNRVCNMI 209
Cdd:PRK08315 206 YTSGTTGFPKgATLTHRNILNNGYFIGEAMKlteedRLcIPVPLYHCFGMVLGNLACVTHGATMVYPGEGfDPLATLAAV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 210 EKHQVQALPASPT-FINLLILSEvYKKYNLNSLQT-ISYGS----EVMPEAtlskINEIfpHVK-ITQMYGLSEYGVLYS 282
Cdd:PRK08315 286 EEERCTALYGVPTmFIAELDHPD-FARFDLSSLRTgIMAGSpcpiEVMKRV----IDKM--HMSeVTIAYGMTETSPVST 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 283 QSKSNDSLwiklsDK----------NIESRVVD------------GMLQIKSMSTMIGYINAPSP----FTQDGWLMTGD 336
Cdd:PRK08315 359 QTRTDDPL-----EKrvttvgralpHLEVKIVDpetgetvprgeqGELCTRGYSVMKGYWNDPEKtaeaIDADGWMHTGD 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 337 MVEVDGD-YIKILGR-KSEIINiGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLR 414
Cdd:PRK08315 434 LAVMDEEgYVNIVGRiKDMIIR-GGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE--EDVR 510
|
330
....*....|....*.
gi 1264249082 415 EFCKDKLPLYKIPQKV 430
Cdd:PRK08315 511 DFCRGKIAHYKIPRYI 526
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
133-434 |
2.52e-24 |
|
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: 103.11 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFTLL----------QKKYSVARSVKRVIPFmlfDHIGGVNTLFQIISSSGCLVIIDDRTP 202
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFfavpdilqkeGLNWVVGDVTYLPLPA---THIGGLWWILTCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NR-VCNMIEKHQVQALPASPTFINLLILseVYKKYN--LNSLQTISYGSEVMPEATlSKINEIFPHVKITQMYGLSEYGV 279
Cdd:cd17635 80 YKsLFKILTTNAVTTTCLVPTLLSKLVS--ELKSANatVPSLRLIGYGGSRAIAAD-VRFIEATGLTNTAQVYGLSETGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 280 LYSQSKSNDS--------------LWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAPSPFTQ---DGWLMTGDMVEV-D 341
Cdd:cd17635 157 ALCLPTDDDSieinavgrpypgvdVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEvliDGWVNTGDLGERrE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 342 GDYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKrLREFCKDKL 421
Cdd:cd17635 237 DGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRA-LKHTIRREL 315
|
330
....*....|...
gi 1264249082 422 PLYKIPQKVVLTT 434
Cdd:cd17635 316 EPYARPSTIVIVT 328
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
133-447 |
2.71e-24 |
|
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: 105.10 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAI--VHDftllQKKYSVARSVK-----------RVIP----FMLfdHIGGVntlFQIISSSGCLV 195
Cdd:cd05920 141 VALFLLSGGTTGTPKLIprTHN----DYAYNVRASAEvcgldqdtvylAVLPaahnFPL--ACPGV---LGTLLAGGRVV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 196 IIDDRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLS 275
Cdd:cd05920 212 LAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 276 EYGVLYSQSKSNDSLWIKLSDKNI----ESRVVD-----------GMLQIKSMSTMIGYINAPS----PFTQDGWLMTGD 336
Cdd:cd05920 291 EGLLNYTRLDDPDEVIIHTQGRPMspddEIRVVDeegnpvppgeeGELLTRGPYTIRGYYRAPEhnarAFTPDGFYRTGD 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 337 MVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNE-SVSEFRKRLR 414
Cdd:cd05920 371 LVRRTPDgYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPpSAAQLRRFLR 450
|
330 340 350
....*....|....*....|....*....|...
gi 1264249082 415 EFckdKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:cd05920 451 ER---GLAAYKLPDRIEFVDSLPLTAVGKIDKK 480
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
136-432 |
7.88e-24 |
|
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: 103.38 E-value: 7.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSK-------AIVHDFTLLQKKYSVARSVkRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRT---PNRV 205
Cdd:cd05930 98 VIYTSGSTGKPKgvmvehrGLVNLLLWMQEAYPLTPGD-RVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVrkdPEAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTFINLLIlsEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE------YGV 279
Cdd:cd05930 177 ADLLAEEGITVLHLTPSLLRLLL--QELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEatvdatYYR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 280 LYSQSKSNDSLWIKLSDKNIESRVVDGMLQ-----------IKSMSTMIGYINAPS---------PFTQDGWLM-TGDMV 338
Cdd:cd05930 255 VPPDDEEDGRVPIGRPIPNTRVYVLDENLRpvppgvpgelyIGGAGLARGYLNRPEltaerfvpnPFGPGERMYrTGDLV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 339 --EVDGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREF 416
Cdd:cd05930 335 rwLPDGN-LEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDE--EELRAH 411
|
330
....*....|....*.
gi 1264249082 417 CKDKLPLYKIPQKVVL 432
Cdd:cd05930 412 LAERLPDYMVPSAFVV 427
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
134-428 |
8.53e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 103.96 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 134 GLVLFSSGTTGSSKAIV--------HDFTLLQKKYSVARSVKRVIPFMLFDHIGGVNTLFQIISSSGC-LVIIDDRTPNR 204
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMlthknlvsNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYkMVLIPKFDMKM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPeatlSKINEIFPHV---KITQMYGLSEYgvly 281
Cdd:PRK06710 289 VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLP----VEVQEKFETVtggKLVEGYGLTES---- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 282 SQSKSNDSLWIKLSDKNI-------ESRVVD------------GMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVE 339
Cdd:PRK06710 361 SPVTHSNFLWEKRVPGSIgvpwpdtEAMIMSletgealppgeiGEIVVKGPQIMKGYWNKPeetAAVLQDGWLHTGDVGY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 340 VDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCK 418
Cdd:PRK06710 441 MDEDgFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSE--EELNQFAR 518
|
330
....*....|
gi 1264249082 419 DKLPLYKIPQ 428
Cdd:PRK06710 519 KYLAAYKVPK 528
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
138-430 |
1.38e-23 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 103.21 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKA--IVHD---FTLLQKK---YSVARSVKR--VIPFMLFdHIGG--VNTLFQIISSSGCLVIIDDRTPNRV 205
Cdd:PRK08974 213 YTGGTTGVAKGamLTHRnmlANLEQAKaayGPLLHPGKElvVTALPLY-HIFAltVNCLLFIELGGQNLLITNPRDIPGF 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIfPHVKITQMYGLSEYGVL----- 280
Cdd:PRK08974 292 VKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKL-TGQYLLEGYGLTECSPLvsvnp 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 YSQSKSNDSlwIKLSDKNIESRVVD-----------GMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVEVDGD-YI 345
Cdd:PRK08974 371 YDLDYYSGS--IGLPVPSTEIKLVDddgnevppgepGELWVKGPQVMLGYWQRPeatDEVIKDGWLATGDIAVMDEEgFL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 346 KILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKA-VVKlsTNESVSefRKRLREFCKDKLPLY 424
Cdd:PRK08974 449 RIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIfVVK--KDPSLT--EEELITHCRRHLTGY 524
|
....*.
gi 1264249082 425 KIPQKV 430
Cdd:PRK08974 525 KVPKLV 530
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
133-431 |
3.18e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 102.39 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIV--H---DFTLLQKKYSV------ARSVKRVIPfmLFdHIGGVnTLFQIISSS--GCLVIIDD 199
Cdd:PRK05605 221 VALILYTSGTTGKPKGAQltHrnlFANAAQGKAWVpglgdgPERVLAALP--MF-HAYGL-TLCLTLAVSigGELVLLPA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 200 RTPNRVCNMIEKHQVQALPASPTFINLLIlsEVYKKYNLnSLQTISY---GSEVMPEATLSKInEIFPHVKITQMYGLSE 276
Cdd:PRK05605 297 PDIDLILDAMKKHPPTWLPGVPPLYEKIA--EAAEERGV-DLSGVRNafsGAMALPVSTVELW-EKLTGGLLVEGYGLTE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 YGVLYSQSKSNDS-----LWIKLSDKNIesRVVD-------------GMLQIKSMSTMIGYINAP---SPFTQDGWLMTG 335
Cdd:PRK05605 373 TSPIIVGNPMSDDrrpgyVGVPFPDTEV--RIVDpedpdetmpdgeeGELLVRGPQVFKGYWNRPeetAKSFLDGWFRTG 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 336 DMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLR 414
Cdd:PRK05605 451 DVVVMEEDgFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDP--EGLR 528
|
330
....*....|....*..
gi 1264249082 415 EFCKDKLPLYKIPQKVV 431
Cdd:PRK05605 529 AYCREHLTRYKVPRRFY 545
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
137-434 |
1.64e-22 |
|
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: 99.46 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 137 LFSSGTTGSSKAIVHDFT-------LLQKKYSVARSVKRV--IPFMLFDHIGGVNTLFQIISSSGCLVIIDDRTPNRVCN 207
Cdd:cd05919 97 LYSSGTTGPPKGVMHAHRdpllfadAMAREALGLTPGDRVfsSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 208 MIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSqSKSN 287
Cdd:cd05919 177 TLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGHIFL-SNRP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 288 DSLWIKLSDKNI---ESRVVD-----------GMLQIKSMSTMIGYINAPS---PFTQDGWLMTGDMVEVDGD-YIKILG 349
Cdd:cd05919 255 GAWRLGSTGRPVpgyEIRLVDeeghtippgeeGDLLVRGPSAAVGYWNNPEksrATFNGGWYRTGDKFCRDADgWYTHAG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 350 RKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSE-FRKRLREFCKDKLPLYKIPQ 428
Cdd:cd05919 335 RADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEsLARDIHRHLLERLSAHKVPR 414
|
....*.
gi 1264249082 429 KVVLTT 434
Cdd:cd05919 415 RIAFVD 420
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
138-448 |
2.18e-22 |
|
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: 99.63 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIV--------HDFTLLQKKySVARSVKRVI-PFMLFDHIGGVNTLFQIISSSGCLVIIDDR-TPNRVCN 207
Cdd:cd12119 170 YTSGTTGNPKGVVyshrslvlHAMAALLTD-GLGLSESDVVlPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYlDPASLAE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 208 MIEKHQVQALPASPTFINLLiLSEV-YKKYNLNSLQTISYGSEVMPEATLSKINEIfpHVKITQMYGLSEYGVLYSQSKS 286
Cdd:cd12119 249 LIEREGVTFAAGVPTVWQGL-LDHLeANGRDLSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHAWGMTETSPLGTVARP 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 287 NDSlWIKLSDKN--------------IESRVVD-------------GMLQIKSMSTMIGYINAPSP---FTQDGWLMTGD 336
Cdd:cd12119 326 PSE-HSNLSEDEqlalrakqgrpvpgVELRIVDddgrelpwdgkavGELQVRGPWVTKSYYKNDEEseaLTEDGWLRTGD 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 337 MVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLRE 415
Cdd:cd12119 405 VATIDEDgYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA--EELLE 482
|
330 340 350
....*....|....*....|....*....|...
gi 1264249082 416 FCKDKLPLYKIPQKVVLTTKKMHTERFKKDKKV 448
Cdd:cd12119 483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKA 515
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
133-430 |
2.98e-22 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 98.66 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFTLLqkkysVARSVKRVIPFMLFDH-------------IGGVNTLFQIISSSGCLVIIDD 199
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAHRVL-----LGHLPGVQFPFNLFPRdgdlywtpadwawIGGLLDVLLPSLYFGVPVLAHR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 200 RT---PNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSE 276
Cdd:cd05971 165 MTkfdPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 YGVLYSqsksNDSLWIKLSDKNIES-------RVVD-----------GMLQIK--SMSTMIGYINAPS----PFTQDgWL 332
Cdd:cd05971 244 CNLVIG----NCSALFPIKPGSMGKpipghrvAIVDdngtplppgevGEIAVElpDPVAFLGYWNNPSatekKMAGD-WL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 333 MTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRK 411
Cdd:cd05971 319 LTGDLGRKDSDgYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
330 340
....*....|....*....|
gi 1264249082 412 R-LREFCKDKLPLYKIPQKV 430
Cdd:cd05971 399 ReIQELVKTRLAAHEYPREI 418
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
53-430 |
7.89e-22 |
|
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: 97.16 E-value: 7.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 53 VSLEADYSPYSIAMFLALIELGCTVVPIlNSLVDSKkkeyyeivELENVIKVERGSFEIINIQRDYIqnelllqlkklkh 132
Cdd:cd05935 29 VGICLQNSPQYVIAYFAIWRANAVVVPI-NPMLKER--------ELEYILNDSGAKVAVVGSELDDL------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 pGLVLFSSGTTGSSKAIVHD-----FTLLQKKYSVARSVKRVI-PFMLFDHIGG-VNTLFQIISSSGCLVIIDDRTPNRV 205
Cdd:cd05935 87 -ALIPYTSGTTGLPKGCMHThfsaaANALQSAVWTGLTPSDVIlACLPLFHVTGfVGSLNTAVYVGGTYVLMARWDRETA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPhVKITQMYGLSEygvLYSQSK 285
Cdd:cd05935 166 LELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTE---TMSQTH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 286 SNDSLWIKLS-----DKNIESRVVD------------GMLQIKSMSTMIGYINAPSP----FTQDG---WLMTGDMVEVD 341
Cdd:cd05935 242 TNPPLRPKLQclgip*FGVDARVIDietgrelppnevGEIVVRGPQIFKGYWNRPEEteesFIEIKgrrFFRTGDLGYMD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 342 GD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLStnesvSEFRKRLRE----- 415
Cdd:cd05935 322 EEgYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLR-----PEYRGKVTEediie 396
|
410
....*....|....*
gi 1264249082 416 FCKDKLPLYKIPQKV 430
Cdd:cd05935 397 WAREQMAAYKYPREV 411
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
141-448 |
9.23e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 97.75 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 141 GTTGSSKAIVHDF----TLLQKKYSvARSVKRVIPFML---FDHIGG---VNTLFQiissSGCLVIIDDRTPNRVCNMIE 210
Cdd:PRK06188 178 GTTGKPKGVMGTHrsiaTMAQIQLA-EWEWPADPRFLMctpLSHAGGaffLPTLLR----GGTVIVLAKFDPAEVLRAIE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 211 KHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVkITQMYGLSE--YGVLYSQSKSND 288
Cdd:PRK06188 253 EQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTEapMVITYLRKRDHD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 289 -------------SLW--IKLSDKNieSRVVD----GMLQIKSMSTMIGYINAPSPFTQ---DGWLMTGDMVEVDGD-YI 345
Cdd:PRK06188 332 pddpkrltscgrpTPGlrVALLDED--GREVAqgevGEICVRGPLVMDGYWNRPEETAEafrDGWLHTGDVAREDEDgFY 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 346 KILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYK 425
Cdd:PRK06188 410 YIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA--AELQAHVKERKGSVH 487
|
330 340
....*....|....*....|...
gi 1264249082 426 IPQKVVLTTKKMHTERFKKDKKV 448
Cdd:PRK06188 488 APKQVDFVDSLPLTALGKPDKKA 510
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
138-431 |
1.47e-21 |
|
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: 96.98 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIV--HDFTLLQKKYSVARSVKRVIPFMLFD----HIGGVNTLFQIISSSGCLVIIDDRTPNRVCNMIEK 211
Cdd:cd12118 140 YTSGTTGRPKGVVyhHRGAYLNALANILEWEMKQHPVYLWTlpmfHCNGWCFPWTVAAVGGTNVCLRKVDAKAIYDLIEK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 212 HQVQALPASPTFINLLIlsevykKYNLNSLQTISYGSEVM------PEATLSKINEIFPHVkiTQMYGLSE-YGVLYSQS 284
Cdd:cd12118 220 HKVTHFCGAPTVLNMLA------NAPPSDARPLPHRVHVMtagappPAAVLAKMEELGFDV--THVYGLTEtYGPATVCA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSNDslWIKLSDKN---IESR------------VVD--------------GMLQIKSMSTMIGYINAP---SPFTQDGWL 332
Cdd:cd12118 292 WKPE--WDELPTEErarLKARqgvryvgleevdVLDpetmkpvprdgktiGEIVFRGNIVMKGYLKNPeatAEAFRGGWF 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 333 MTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrK 411
Cdd:cd12118 370 HSGDLAVIHPDgYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE--E 447
|
330 340
....*....|....*....|
gi 1264249082 412 RLREFCKDKLPLYKIPQKVV 431
Cdd:cd12118 448 EIIAFCREHLAGFMVPKTVV 467
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-427 |
2.59e-21 |
|
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: 95.44 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 53 VSLEADYSPYSIAMFLALIELGCTVVPILNSLVDSkkkeyyeivELENVIKVERGSFEIINiqrdyiqnelllqlkklkh 132
Cdd:cd05934 31 VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGD---------ELAYIIDHSGAQLVVVD------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIV--HDFTLLQKKYSVARSVKR-------VIPfmLFdHIGGV-NTLFQIISSSGCLVIIDDRTP 202
Cdd:cd05934 83 PASILYTSGTTGPPKGVVitHANLTFAGYYSARRFGLGeddvyltVLP--LF-HINAQaVSVLAALSVGATLVLLPRFSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTIsYGSEVmPEATLSKINEIFpHVKITQMYGLSEYGVLYS 282
Cdd:cd05934 160 SRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAA-YGAPN-PPELHEEFEERF-GVRLLEGYGMTETIVGVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 283 QSKSNDSLW--IKLSDKNIESRVVD-----------GMLQIKSM---STMIGYINAPSPFTQ---DGWLMTGDMVEVDGD 343
Cdd:cd05934 237 GPRDEPRRPgsIGRPAPGYEVRIVDddgqelpagepGELVIRGLrgwGFFKGYYNMPEATAEamrNGWFHTGDLGYRDAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 344 -YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLP 422
Cdd:cd05934 317 gFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDP--EELFAFCEGQLA 394
|
....*
gi 1264249082 423 LYKIP 427
Cdd:cd05934 395 YFKVP 399
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
135-435 |
4.53e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 95.64 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 135 LVLFSSGTTGSSK--AIVHDFTLLQKKYSVArsvkrVIPFMLFD---------HIGGVNTLFQIISSSGCLVIIDDRTPN 203
Cdd:PLN02860 176 LICFTSGTTGRPKgvTISHSALIVQSLAKIA-----IVGYGEDDvylhtaplcHIGGLSSALAMLMVGACHVLLPKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVCNMIEKHQVQALPASPTFINLLI----LSEVYKKYNlnSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE--- 276
Cdd:PLN02860 251 AALQAIKQHNVTSMITVPAMMADLIsltrKSMTWKVFP--SVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacs 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 ---YGVLY--SQSKSNDSLWIKLSDKN-----------------IESRVV------DGMLQIKSMSTMIGY----INAPS 324
Cdd:PLN02860 329 sltFMTLHdpTLESPKQTLQTVNQTKSssvhqpqgvcvgkpaphVELKIGldessrVGRILTRGPHVMLGYwgqnSETAS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 325 PFTQDGWLMTGDMVEVDG-DYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKL--- 400
Cdd:PLN02860 409 VLSNDGWLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLrdg 488
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1264249082 401 ---STNESVSEFRKR------LREFCKDK-LPLYKIPQKVVLTTK 435
Cdd:PLN02860 489 wiwSDNEKENAKKNLtlssetLRHHCREKnLSRFKIPKLFVQWRK 533
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
134-446 |
1.32e-20 |
|
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: 93.70 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 134 GLVLFSSGTTGSSKAIVH---DFTLLQKKYSV----ARSVKRVI--PFMLFDHIGGVNTLFQIISSSGClVIIDDRTPNR 204
Cdd:cd05958 100 CILAFTSGTTGAPKATMHfhrDPLASADRYAVnvlrLREDDRFVgsPPLAFTFGLGGVLLFPFGVGASG-VLLEEATPDL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSqS 284
Cdd:cd05958 179 LLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEMFHIFI-S 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSNDSLWIKLSDKNI---ESRVVD-----------GMLQIKSmSTMIGYINAPSPFT--QDGWLMTGDMVEVDGD-YIKI 347
Cdd:cd05958 257 ARPGDARPGATGKPVpgyEAKVVDdegnpvpdgtiGRLAVRG-PTGCRYLADKRQRTyvQGGWNITGDTYSRDPDgYFRH 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 348 LGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKR-LREFCKDKLPLYKI 426
Cdd:cd05958 336 QGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLAReLQDHAKAHIAPYKY 415
|
330 340
....*....|....*....|
gi 1264249082 427 PQKVVLTTKKMHTERFKKDK 446
Cdd:cd05958 416 PRAIEFVTELPRTATGKLQR 435
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
136-433 |
1.42e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.14 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIV--H-----------DFTLLQKKYSVARSVK-RVIPFMlfdHIGGVnTLFQI--ISSSGCLVIIDD 199
Cdd:PLN02574 203 IMYSSGTTGASKGVVltHrnliamvelfvRFEASQYEYPGSDNVYlAALPMF---HIYGL-SLFVVglLSLGSTIVVMRR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 200 RTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYN-LNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYG 278
Cdd:PLN02574 279 FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEvLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTEST 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 279 VL----YSQSKSNDSLWIKLSDKNIESRVVD------------GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMV 338
Cdd:PLN02574 359 AVgtrgFNTEKLSKYSSVGLLAPNMQAKVVDwstgcllppgncGELWIQGPGVMKGYLNNPkatqSTIDKDGWLRTGDIA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 339 EVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFC 417
Cdd:PLN02574 439 YFDEDgYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQ--EAVINYV 516
|
330
....*....|....*.
gi 1264249082 418 KDKLPLYKIPQKVVLT 433
Cdd:PLN02574 517 AKQVAPYKKVRKVVFV 532
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
137-430 |
5.22e-20 |
|
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: 92.06 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 137 LFSSGTTGSSKAI--------VHDFTllqkkysvarsvkRVIPFMLFDHIGGVNTL--------------FQIISSSGCL 194
Cdd:cd05929 131 LYSGGTTGRPKGIkrglpggpPDNDT-------------LMAAALGFGPGADSVYLspaplyhaapfrwsMTALFMGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 195 VIIDDRTPNRVCNMIEKHQVQALPASPT-FINLLILSE-VYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVkitqmy 272
Cdd:cd05929 198 VLMEKFDPEEFLRLIERYRVTFAQFVPTmFVRLLKLPEaVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI------ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 273 gLSEYgvlYSQSKSNDSLWIK----LSDKNIESRVVDGMLQI-----KSMST-MIG--YINAPSPFT------------- 327
Cdd:cd05929 272 -IWEY---YGGTEGQGLTIINgeewLTHPGSVGRAVLGKVHIldedgNEVPPgEIGevYFANGPGFEytndpektaaarn 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 328 QDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESV 406
Cdd:cd05929 348 EGGWSTLGDVGYLDEDgYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADA 427
|
330 340
....*....|....*....|....*
gi 1264249082 407 SE-FRKRLREFCKDKLPLYKIPQKV 430
Cdd:cd05929 428 GTaLAEELIAFLRDRLSRYKCPRSI 452
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
138-430 |
5.86e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 92.33 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIVHDFTLLQkkYSVARSVK-----------RVIPFMlfdHIGG-VNTLFQIISSSGCLVII---DDRTP 202
Cdd:PRK08314 197 YTSGTTGVPKGCMHTHRTVM--ANAVGSVLwsnstpesvvlAVLPLF---HVTGmVHSMNAPIYAGATVVLMprwDREAA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRvcnMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGvlyS 282
Cdd:PRK08314 272 AR---LIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELT-GLDYVEGYGLTETM---A 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 283 QSKSNDSLWIKLS-----DKNIESRVVD------------GMLQIKSMSTMIGYINAP-----SPFTQDG--WLMTGDMV 338
Cdd:PRK08314 345 QTHSNPPDRPKLQclgipTFGVDARVIDpetleelppgevGEIVVHGPQVFKGYWNRPeataeAFIEIDGkrFFRTGDLG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 339 EVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKRLREFC 417
Cdd:PRK08314 425 RMDEEgYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIIAWA 504
|
330
....*....|...
gi 1264249082 418 KDKLPLYKIPQKV 430
Cdd:PRK08314 505 REHMAAYKYPRIV 517
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
138-425 |
3.65e-19 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 90.04 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIvhdftLLQKKYSVAR---SVKRVIPFML----------FDHIGGVNTL-FQIISSSGCLVIIDDRTPN 203
Cdd:PLN02330 191 FSSGTTGISKGV-----MLTHRNLVANlcsSLFSVGPEMIgqvvtlglipFFHIYGITGIcCATLRNKGKVVVMSRFELR 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEAT--LSKINEIFPHVKITQMYGLSEYGVL- 280
Cdd:PLN02330 266 TFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPelLTAFEAKFPGVQVQEAYGLTEHSCIt 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 ---------YSQSKSNDSLWIKlsdKNIESRVVD------------GMLQIKSMSTMIGYIN----APSPFTQDGWLMTG 335
Cdd:PLN02330 346 lthgdpekgHGIAKKNSVGFIL---PNLEVKFIDpdtgrslpkntpGELCVRSQCVMQGYYNnkeeTDRTIDEDGWLHTG 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 336 DM--VEVDGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLstNESVSEFRKRL 413
Cdd:PLN02330 423 DIgyIDDDGD-IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVI--NPKAKESEEDI 499
|
330
....*....|..
gi 1264249082 414 REFCKDKLPLYK 425
Cdd:PLN02330 500 LNFVAANVAHYK 511
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
23-447 |
5.88e-19 |
|
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: 88.68 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 23 DKTYTYEWFLNQIKIYTRELNEHRKMDYTIVSLEADYSPYSIAMFLALIELGCTVVPILNSLVDSKKKEyyeivelenvI 102
Cdd:cd17654 14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLT----------V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 103 KVERGSFEIIniQRDYIQNELLLQLKKLKHPGL--------VLFSSGTTGSSK-------AIVHDFTLLQKKYSVARSVK 167
Cdd:cd17654 84 MKKCHVSYLL--QNKELDNAPLSFTPEHRHFNIrtdeclayVIHTSGTTGTPKivavphkCILPNIQHFRSLFNITSEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 168 RVI-PFMLFDHigGVNTLFQIISSSGCLVIIddRTPNRVC------NMIEKHQVQALPASPTFINLLiLSEVYKKYNLN- 239
Cdd:cd17654 162 LFLtSPLTFDP--SVVEIFLSLSSGATLLIV--PTSVKVLpskladILFKRHRITVLQATPTLFRRF-GSQSIKSTVLSa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 240 --SLQTISYGSEVMPEAT-LSKINEIFPHVKITQMYGLSEYGV--LYSQSKSNDS---LWIKLSDKNIESR-----VVDG 306
Cdd:cd17654 237 tsSLRVLALGGEPFPSLViLSSWRGKGNRTRIFNIYGITEVSCwaLAYKVPEEDSpvqLGSPLLGTVIEVRdqngsEGTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 307 MLQIKSMStMIGYINAP--SPFTQdgWLMTGDMVEVDGDYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVG 384
Cdd:cd17654 317 QVFLGGLN-RVCILDDEvtVPKGT--MRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264249082 385 EKNaitgQMVkaVVKLSTNESVSEFRKRLRefcKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:cd17654 394 SDQ----QRL--IAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKS 447
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
133-415 |
8.20e-19 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 88.54 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVH-DFTLLQKKYSVARSVK-----RVIPFMLFDHIGGVN-TLFQIISSSGCLVIIDDRT-PNR 204
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLsHKNLLANVEQITAIFDpnpedVVFGALPFFHSFGLTgCLWLPLLSGIKVVFHPNPLdYKK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINllILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSQS 284
Cdd:cd05909 229 IPELIYDKKATILLGTPTFLR--GYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISVN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSN---------------DSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAPSP---FTQDGWLMTGDMVEVDGD-YI 345
Cdd:cd05909 306 TPQspnkegtvgrplpgmEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELtsfAFGDGWYDTGDIGKIDGEgFL 385
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264249082 346 KILGRKSEIINIGGEKVFPAEVENVIQLMDGVE-EVAVVGEKNAITGQMVKAVVkLSTNESVSEFRKRLRE 415
Cdd:cd05909 386 TITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLT-TTTDTDPSSLNDILKN 455
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
133-432 |
1.32e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 88.30 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFTLLQKK---------YSVARSVKRV-IPFMlfdHIGGVNTLFQIISSSGCLVI--IDDR 200
Cdd:PRK07786 176 PALIMYTSGTTGRPKGAVLTHANLTGQamtclrtngADINSDVGFVgVPLF---HIAGIGSMLPGLLLGAPTVIypLGAF 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 201 TPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLnSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVL 280
Cdd:PRK07786 253 DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPV 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 YSQSKSNDSLWiKLSD-----KNIESRVVD-----------GMLQIKSMSTMIGYINAPSPfTQD----GWLMTGDMVEV 340
Cdd:PRK07786 332 TCMLLGEDAIR-KLGSvgkviPTVAARVVDenmndvpvgevGEIVYRAPTLMSGYWNNPEA-TAEafagGWFHSGDLVRQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 341 DGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFrKRLREFCKD 419
Cdd:PRK07786 410 DEEgYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTL-EDLAEFLTD 488
|
330
....*....|...
gi 1264249082 420 KLPLYKIPQKVVL 432
Cdd:PRK07786 489 RLARYKHPKALEI 501
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
299-431 |
3.37e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 86.85 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 299 IESRVVD------------GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEK 361
Cdd:PRK07514 330 VSLRVTDpetgaelppgeiGMIEVKGPNVFKGYWRMPektaEEFRADGFFITGDLGKIDERgYVHIVGRGKDLIISGGYN 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 362 VFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVV 431
Cdd:PRK07514 410 VYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE--AAILAALKGRLARFKQPKRVF 477
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
306-430 |
3.41e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 87.13 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 306 GMLQIKSMSTMIGYINAPSP----FTQDGWLMTGD--MVEVDGdYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEE 379
Cdd:PRK05677 405 GELCVKGPQVMKGYWQRPEAtdeiLDSDGWLKTGDiaLIQEDG-YMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1264249082 380 VAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKV 430
Cdd:PRK05677 484 CAAIGVPDEKSGEAIKVFVVVKPGETLTK--EQVMEHMRANLTGYKVPKAV 532
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
318-447 |
3.80e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 86.86 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 318 GYINAP----SPFTqDGWLMTGDM--VEVDGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITG 391
Cdd:PRK05852 393 GYLGDPtitaANFT-DGWLRTGDLgsLSAAGD-LSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYG 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1264249082 392 QMVKAVVklSTNESVSEFRKRLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:PRK05852 471 EAVAAVI--VPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
133-444 |
4.53e-18 |
|
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: 86.40 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFT-----LLQKKY-----------SVARS--VKRVipfmlFDHIGGvntlfQIISssGCL 194
Cdd:cd05970 187 ILLVYFSSGTTGMPKMVEHDFTyplghIVTAKYwqnvregglhlTVADTgwGKAV-----WGKIYG-----QWIA--GAA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 195 VIIDDR---TPNRVCNMIEKHQVQALPASPTFINLLIlSEVYKKYNLNSLQTISYGSEVMPEATLSKINEiFPHVKITQM 271
Cdd:cd05970 255 VFVYDYdkfDPKALLEKLSKYGVTTFCAPPTIYRFLI-REDLSRYDLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 272 YGLSEYGVLY-----------SQSKSNDSLWIKLSDKN-----------IESRVVDGmlqiKSMSTMIGYINAP---SPF 326
Cdd:cd05970 333 FGQTETTLTIatfpwmepkpgSMGKPAPGYEIDLIDREgrsceageegeIVIRTSKG----KPVGLFGGYYKDAektAEV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 327 TQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLS-TNE 404
Cdd:cd05970 409 WHDGYYHTGDAAWMDEDgYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAkGYE 488
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1264249082 405 SVSEFRKRLREFCKDKLPLYKIPQKV--VLTTKKMHTERFKK 444
Cdd:cd05970 489 PSEELKKELQDHVKKVTAPYKYPRIVefVDELPKTISGKIRR 530
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
134-434 |
7.48e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 85.73 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 134 GLVLFSSGTTGSSKAIVHDFTLLQKKYSVARSVKrvipFMLFDHIGGVNTLF----------------QIISSSGCLVII 197
Cdd:PRK08276 143 ADMLYSSGTTGRPKGIKRPLPGLDPDEAPGMMLA----LLGFGMYGGPDSVYlspaplyhtaplrfgmSALALGGTVVVM 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 198 DDRTPNRVCNMIEKHQVQALPASPT-FINLLILSE-VYKKYNLNSLQTISYGSEVMPeatlskineifPHVKiTQM---Y 272
Cdd:PRK08276 219 EKFDAEEALALIERYRVTHSQLVPTmFVRMLKLPEeVRARYDVSSLRVAIHAAAPCP-----------VEVK-RAMidwW 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 273 G--LSEYgvlYSQSKSNDSLWIKLSD---------KNIES--RVVD-----------GMLQIKSMSTMIGYINAP----S 324
Cdd:PRK08276 287 GpiIHEY---YASSEGGGVTVITSEDwlahpgsvgKAVLGevRILDedgnelppgeiGTVYFEMDGYPFEYHNDPektaA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 325 PFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN 403
Cdd:PRK08276 364 ARNPHGWVTVGDVGYLDEDgYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADG 443
|
330 340 350
....*....|....*....|....*....|..
gi 1264249082 404 -ESVSEFRKRLREFCKDKLPLYKIPQKVVLTT 434
Cdd:PRK08276 444 aDAGDALAAELIAWLRGRLAHYKCPRSIDFED 475
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
22-447 |
1.43e-17 |
|
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: 84.80 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 22 EDKTYTYEWFLNQIKiYTRELNEHRKMDYT-IVSLEADYSPYSIAMFLALIELGCTVVPILNSlvdskkkeyYEIVELEN 100
Cdd:cd05914 4 GGEPLTYKDLADNIA-KFALLLKINGVGTGdRVALMGENRPEWGIAFFAIWTYGAIAVPILAE---------FTADEVHH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 101 VIKVERGSFEIINIQRDYiqnelllqlkklkhpGLVLFSSGTTGSSKAIVHDFTLLQKKYSVARSVK------RVIPFML 174
Cdd:cd05914 74 ILNHSEAKAIFVSDEDDV---------------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVllgkgdKILSILP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 175 FDHIGGVNTLFQIISSSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTfinLLILSEVYKKYNLNSLQT----------- 243
Cdd:cd05914 139 LHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGVPV---PLVIEKIFKMDIIPKLTLkkfkfklakki 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 244 ------------------------ISYGSEVMPEAT--LSKINeiFPhvkITQMYGLSEYG-----------VLYSQSKS 286
Cdd:cd05914 216 nnrkirklafkkvheafggnikefVIGGAKINPDVEefLRTIG--FP---YTIGYGMTETApiisysppnriRLGSAGKV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 287 NDSLWIKLSDKNIESRvvDGMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVD-GDYIKILGRKSEIINIG-GE 360
Cdd:cd05914 291 IDGVEVRIDSPDPATG--EGEIIVRGPNVMKGYYKNPeataEAFDKDGWFHTGDLGKIDaEGYLYIRGRKKEMIVLSsGK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 361 KVFPAEVENVIQLMDGV-EEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKRLREFCKDKL----PLYKIPQKVvlttk 435
Cdd:cd05914 369 NIYPEEIEAKINNMPFVlESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVnqkvPNYKKISKV----- 443
|
490
....*....|..
gi 1264249082 436 KMHTERFKKDKK 447
Cdd:cd05914 444 KIVKEEFEKTPK 455
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
209-430 |
1.61e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 84.69 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 209 IEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIfPHVKITQMYGLSEYG-VL----YSQ 283
Cdd:PRK07059 297 LKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEM-TGCPITEGYGLSETSpVAtcnpVDA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 284 SKSNDSLWIKLSDKNIESRVVDGM---------LQIKSMSTMIGYINAPSP----FTQDGWLMTGDMVEVDGD-YIKILG 349
Cdd:PRK07059 376 TEFSGTIGLPLPSTEVSIRDDDGNdlplgepgeICIRGPQVMAGYWNRPDEtakvMTADGFFRTGDVGVMDERgYTKIVD 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 350 RKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKA-VVKlsTNESVSEfrKRLREFCKDKLPLYKIPQ 428
Cdd:PRK07059 456 RKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLfVVK--KDPALTE--EDVKAFCKERLTNYKRPK 531
|
..
gi 1264249082 429 KV 430
Cdd:PRK07059 532 FV 533
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
305-386 |
2.59e-17 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 84.38 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 305 DGMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEII-NIGGEKVFPAEVENVIQLMDGVE 378
Cdd:COG1022 414 DGEILVRGPNVMKGYYKNPeataEAFDADGWLHTGDIGELDEDgFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIE 493
|
....*...
gi 1264249082 379 EVAVVGEK 386
Cdd:COG1022 494 QAVVVGDG 501
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
133-433 |
3.28e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 83.70 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIV----------HDFTLLQKkySVARSVKRVIPFMlFDHIGGVNTLFQIISSSGCLVIIDDRTP 202
Cdd:PRK09088 137 VSLILFTSGTSGQPKGVMlsernlqqtaHNFGVLGR--VDAHSSFLCDAPM-FHIIGLITSVRPVLAVGGSILVSNGFEP 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEK------HQV------QALPASPTFinllilsevyKKYNLNSLQTISYGSEvmPEATLSKINEIFPHVKITQ 270
Cdd:PRK09088 214 KRTLGRLGDpalgitHYFcvpqmaQAFRAQPGF----------DAAALRHLTALFTGGA--PHAAEDILGWLDDGIPMVD 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 271 MYGLSEYGVLYSQSKSNDSLWIK-----LSDKNIESRVVD-----------GMLQIKSMSTMIGYINAPSP----FTQDG 330
Cdd:PRK09088 282 GFGMSEAGTVFGMSVDCDVIRAKagaagIPTPTVQTRVVDdqgndcpagvpGELLLRGPNLSPGYWRRPQAtaraFTGDG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 331 WLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVklSTNESVSEF 409
Cdd:PRK09088 362 WFRTGDIARRDADgFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAI--VPADGAPLD 439
|
330 340
....*....|....*....|....
gi 1264249082 410 RKRLREFCKDKLPLYKIPQKVVLT 433
Cdd:PRK09088 440 LERIRSHLSTRLAKYKVPKHLRLV 463
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
136-432 |
8.62e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 82.63 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIVHDFTLLQKK-------YSVARSVKRVIPFMLFdHIG-----GVNTLFQiissSGCLVIIDDRTPN 203
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWKsidhviaLGLTASERLLVVGPLY-HVGafdlpGIAVLWV----GGTLRIHREFDPE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEY---GVL 280
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETcsgDTL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 YSQSKSND---SLWIKLSDKNIESRVVDGMLQIKSMSTMI---------GYINAPSPFTQ---DGWLMTGDMVEVDGD-Y 344
Cdd:PRK06145 309 MEAGREIEkigSTGRALAHVEIRIADGAGRWLPPNMKGEIcmrgpkvtkGYWKDPEKTAEafyGDWFRSGDVGYLDEEgF 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 345 IKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSefRKRLREFCKDKLPLY 424
Cdd:PRK06145 389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT--LEALDRHCRQRLASF 466
|
....*...
gi 1264249082 425 KIPQKVVL 432
Cdd:PRK06145 467 KVPRQLKV 474
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
304-428 |
9.06e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 82.40 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 304 VDGMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEE 379
Cdd:PRK06178 413 AEGEIVVRTPSLLKGYWNKPeatAEALRDGWLHTGDIGKIDEQgFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG 492
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1264249082 380 VAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQ 428
Cdd:PRK06178 493 SAVVGRPDPDKGQVPVAFVQLKPGADLTA--AALQAWCRENMAVYKVPE 539
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
174-431 |
1.23e-16 |
|
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: 80.42 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 174 LFdHIGGVNTLFQIISSSGCLVIIDDRTPNRVCNMIEKHQVQ-ALPASPTFINLLILSEVyKKYNLNSLQTISYGSEVMP 252
Cdd:cd17636 50 LF-HIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNAD-GLYDLSSLRSSPAAPEWND 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 253 EATLSkineifphvkiTQMYGLSEYGvlYSQSK-SNDSLWIKLSDKNIES----------RVVD-----------GMLQI 310
Cdd:cd17636 128 MATVD-----------TSPWGRKPGG--YGQTEvMGLATFAALGGGAIGGagrpsplvqvRILDedgrevpdgevGEIVA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 311 KSMSTMIGYINAP---SPFTQDGWLMTGDM--VEVDGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGE 385
Cdd:cd17636 195 RGPTVMAGYWNRPevnARRTRGGWHHTNDLgrREPDGS-LSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1264249082 386 KNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd17636 274 PDPRWAQSVKAIVVLKPGASVTE--AELIEHCRARIASYKKPKSVE 317
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
305-386 |
1.42e-16 |
|
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: 81.49 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 305 DGMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKSE-IINIGGEKVFPAEVENVIQLMDGVE 378
Cdd:cd05907 278 DGEILVRGPNVMLGYYKNPeataEALDADGWLHTGDLGEIDEDgFLHITGRKKDlIITSGGKNISPEPIENALKASPLIS 357
|
....*...
gi 1264249082 379 EVAVVGEK 386
Cdd:cd05907 358 QAVVIGDG 365
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
134-430 |
1.50e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 81.66 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 134 GLVLFSSGTTGSSKAIVHD------------FTLLQKKYSVARSVKRVIPFMLFdHIGGVNTLFQIISSSGCLVIIDDRT 201
Cdd:PRK13391 157 TDMLYSSGTTGRPKGIKRPlpeqppdtplplTAFLQRLWGFRSDMVYLSPAPLY-HSAPQRAVMLVIRLGGTVIVMEHFD 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 PNRVCNMIEKHQVQALPASPT-FINLLIL-SEVYKKYNLNSLQTISYGSEVMPeatlskineifPHVK----------IT 269
Cdd:PRK13391 236 AEQYLALIEEYGVTHTQLVPTmFSRMLKLpEEVRDKYDLSSLEVAIHAAAPCP-----------PQVKeqmidwwgpiIH 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 270 QMYGLSEyGVLYSQSKSNDslWikLSDKNIESRVVDGMLQI--KSMS---------------TMIGYINAP-----SPFT 327
Cdd:PRK13391 305 EYYAATE-GLGFTACDSEE--W--LAHPGTVGRAMFGDLHIldDDGAelppgepgtiwfeggRPFEYLNDPaktaeARHP 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 328 QDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKL-STNES 405
Cdd:PRK13391 380 DGTWSTVGDIGYVDEDgYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPvDGVDP 459
|
330 340
....*....|....*....|....*
gi 1264249082 406 VSEFRKRLREFCKDKLPLYKIPQKV 430
Cdd:PRK13391 460 GPALAAELIAFCRQRLSRQKCPRSI 484
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
291-430 |
2.26e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 81.19 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 291 WIKLSDKNIESRVVD-------------GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKS 352
Cdd:PRK07787 294 WVGLPLAGVETRLVDedggpvphdgetvGELQVRGPTLFDGYLNRPdataAAFTADGWFRTGDVAVVDPDgMHRIVGRES 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264249082 353 -EIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrkrLREFCKDKLPLYKIPQKV 430
Cdd:PRK07787 374 tDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADE----LIDFVAQQLSVHKRPREV 448
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
64-431 |
2.36e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 80.47 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 64 IAMFLALIELGCTVVPILNSlvdSKKKEYYEIVELENVIKVERGSFEIINIQRDYIQNELllqlkklkhPGLVLFSSGTT 143
Cdd:PRK08308 46 ITLVFFLKEKGASVLPIHPD---TPKEAAIRMAKRAGCHGLLYGESDFTKLEAVNYLAEE---------PSLLQYSSGTT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 144 GSSKAIVHDFTLLQKK---YSVARSVKRV-IPFML--FDH----IGGVntlFQIISSSGCLVIIDDRTPNRVCNMIEKHQ 213
Cdd:PRK08308 114 GEPKLIRRSWTEIDREieaYNEALNCEQDeTPIVAcpVTHsyglICGV---LAALTRGSKPVIITNKNPKFALNILRNTP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 214 VQALPASPTFINLLIlSEVYKKYNLNSLQTisYGSeVMPEATLSKINEIFPHVkiTQMYGLSEYGV--LYSQSKSNDSLW 291
Cdd:PRK08308 191 QHILYAVPLMLHILG-RLLPGTFQFHAVMT--SGT-PLPEAWFYKLRERTTYM--MQQYGCSEAGCvsICPDMKSHLDLG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 292 IKLSDkniesrvvdgmLQIKSMSTMigyiNAPSPF---TQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEV 367
Cdd:PRK08308 265 NPLPH-----------VSVSAGSDE----NAPEEIvvkMGDKEIFTKDLGYKSERgTLHFMGRMDDVINVSGLNVYPIEV 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264249082 368 ENVIQLMDGVEEVAVVGEKNAITGQMVKAvvKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVV 431
Cdd:PRK08308 330 EDVMLRLPGVQEAVVYRGKDPVAGERVKA--KVISHEEIDP--VQLREWCIQHLAPYQVPHEIE 389
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
138-422 |
2.51e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.18 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIVhdftLLQKKY--SVARSVKRVIPFMLF---DHIGGVNTLFQIISSSGCL----------VIIDDRTP 202
Cdd:PLN02246 186 YSSGTTGLPKGVM----LTHKGLvtSVAQQVDGENPNLYFhsdDVILCVLPMFHIYSLNSVLlcglrvgaaiLIMPKFEI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSevmpeATLSK-----INEIFPHVKITQMYGLSEY 277
Cdd:PLN02246 262 GALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGA-----APLGKeledaFRAKLPNAVLGQGYGMTEA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 278 GVLYSQSK--SNDSLWIKLSD-----KNIESRVVD------------GMLQIKSMSTMIGYINAP----SPFTQDGWLMT 334
Cdd:PLN02246 337 GPVLAMCLafAKEPFPVKSGScgtvvRNAELKIVDpetgaslprnqpGEICIRGPQIMKGYLNDPeataNTIDKDGWLHT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 335 GDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSE----- 408
Cdd:PLN02246 417 GDIGYIDDDdELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEdeikq 496
|
330 340
....*....|....*....|..
gi 1264249082 409 -------FRKRLRE-FCKDKLP 422
Cdd:PLN02246 497 fvakqvvFYKRIHKvFFVDSIP 518
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
85-432 |
3.60e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.83 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 85 VDSKKKEYYEIVELENVIKveRGSFEIINIQRDY-IQNElllqlkklkHPGLVL-FSSGTTGSSKAIV--HDFTLLQKKY 160
Cdd:PLN03102 149 IDFPKRPSSEELDYECLIQ--RGEPTPSLVARMFrIQDE---------HDPISLnYTSGTTADPKGVVisHRGAYLSTLS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 161 SVARSVKRVIPFMLFD----HIGGVNTLFQIISSSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKY 236
Cdd:PLN03102 218 AIIGWEMGTCPVYLWTlpmfHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 237 NLNSLQTISYGSEVMPEATLSKINEIFPHVkiTQMYGLSEYG--VLYSQSKSNdslWIKLSD------------------ 296
Cdd:PLN03102 298 PRSGPVHVLTGGSPPPAALVKKVQRLGFQV--MHAYGLTEATgpVLFCEWQDE---WNRLPEnqqmelkarqgvsilgla 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 297 -------KNIESRVVDGM----LQIKSMSTMIGYINAPSPFTQ---DGWLMTGDM--VEVDGdYIKILGRKSEIINIGGE 360
Cdd:PLN03102 373 dvdvknkETQESVPRDGKtmgeIVIKGSSIMKGYLKNPKATSEafkHGWLNTGDVgvIHPDG-HVEIKDRSKDIIISGGE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 361 KVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFR--------KRLREFCKDKLPLYKIPQKVVL 432
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRvdklvtreRDLIEYCRENLPHFMCPRKVVF 531
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
135-432 |
3.85e-16 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 80.48 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 135 LVLFSSGTTGSSKAIVHDF-TLLQKKYSVARSVK----RVIpFML--FDHIGG-VNTLFQIISSSGCLVIIDDRTPNRVC 206
Cdd:PRK13295 201 QLIYTSGTTGEPKGVMHTAnTLMANIVPYAERLGlgadDVI-LMAspMAHQTGfMYGLMMPVMLGATAVLQDIWDPARAA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 207 NMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSQSKS 286
Cdd:PRK13295 280 ELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTENGAVTLTKLD 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 287 NDSLWIKLSD----KNIESRVVD-----------GMLQIKSMSTMIGYINAPSPFTQD--GWLMTGDMVEVDGD-YIKIL 348
Cdd:PRK13295 359 DPDERASTTDgcplPGVEVRVVDadgaplpagqiGRLQVRGCSNFGGYLKRPQLNGTDadGWFDTGDLARIDADgYIRIS 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 349 GRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSeFRKrLREFCKD-KLPLYKIP 427
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLD-FEE-MVEFLKAqKVAKQYIP 516
|
....*
gi 1264249082 428 QKVVL 432
Cdd:PRK13295 517 ERLVV 521
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
135-431 |
3.87e-16 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 80.57 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 135 LVLFSSGTTGSSKAIVHDFTllqKKYSVARSVKRVIPFM----------LFdHIGGVNTLfQIISSSGCLVIIDDR-TPN 203
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTPWRaeeptvivapMF-HAWGFSQL-VLAASLACTIVTRRRfDPE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVCNMIEKHQVQALPASPTFINLL--ILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVkITQMYGLSEYGVLY 281
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVMFDRImdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 282 SQSKSNDSLWIKLSDK---NIESRVVD-----------GMLQIKSMSTMIGYINAPSPFTQDGWLMTGDMVEVDGD-YIK 346
Cdd:PRK13382 354 TATPADLRAAPDTAGRpaeGTEIRILDqdfrevptgevGTIFVRNDTQFDGYTSGSTKDFHDGFMASGDVGYLDENgRLF 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 347 ILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLstNESVSEFRKRLREFCKDKLPLYKI 426
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL--KPGASATPETLKQHVRDNLANYKV 511
|
....*
gi 1264249082 427 PQKVV 431
Cdd:PRK13382 512 PRDIV 516
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
305-427 |
5.07e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 79.65 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 305 DGMLQIKSMSTMIGYInaPSPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVV 383
Cdd:PRK07445 301 TGNITIQAQSLALGYY--PQILDSQGIFETDDLGYLDAQgYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVL 378
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1264249082 384 GEKNAITGQMVKAV-VKLSTNESVSEFRKRLrefcKDKLPLYKIP 427
Cdd:PRK07445 379 GLPDPHWGEVVTAIyVPKDPSISLEELKTAI----KDQLSPFKQP 419
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
136-431 |
5.30e-16 |
|
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: 79.75 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAI-------VHDFTLLQKKYSVARSVKRVIPFM---LFDHIggVNTLFQIISSSGCLVIIDDR---TP 202
Cdd:cd17648 99 AIYTSGTTGKPKGVlvehgsvVNLRTSLSERYFGRDNGDEAVLFFsnyVFDFF--VEQMTLALLNGQKLVVPPDEmrfDP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLILSevykkyNLNSLQTISYGSEVMPEATLSKINEIFPHvKITQMYGLSEYGV--- 279
Cdd:cd17648 177 DRFYAYINREKVTYLSGTPSVLQQYDLA------RLPHLKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVtnh 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 280 --LYS-QSKSNDSL--------WIKLSD--KNIESRVVdGMLQIKSMSTMIGYINAP---------SPFTQDGWLM---- 333
Cdd:cd17648 250 krFFPgDQRFDKSLgrpvrntkCYVLNDamKRVPVGAV-GELYLGGDGVARGYLNRPeltaerflpNPFQTEQERArgrn 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 -----TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQ--MVKAVVK--LSTN 403
Cdd:cd17648 329 arlykTGDLVRWLPSgELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVGyyLPEP 408
|
330 340
....*....|....*....|....*...
gi 1264249082 404 ESVSEfrKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd17648 409 GHVPE--SDLLSFLRAKLPRYMVPARLV 434
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
192-430 |
5.82e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 80.03 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 192 GCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLI--LSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKIT 269
Cdd:PRK10946 251 GTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLqaIAEGGSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 270 QMYGLSEYGVLY------------SQSK---SNDSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAP----SPFTQDG 330
Cdd:PRK10946 330 QVFGMAEGLVNYtrlddsderiftTQGRpmsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPqhnaSAFDANG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 331 WLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVV-------GEKNA---ITGQMVKAVVk 399
Cdd:PRK10946 410 FYCSGDLVSIDPDgYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVsmedelmGEKSCaflVVKEPLKAVQ- 488
|
250 260 270
....*....|....*....|....*....|.
gi 1264249082 400 lstnesvseFRKRLREfckDKLPLYKIPQKV 430
Cdd:PRK10946 489 ---------LRRFLRE---QGIAEFKLPDRV 507
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
135-408 |
8.26e-16 |
|
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: 79.49 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 135 LVLFSSGTTGSSKAIVHDFTLLQKKYSVAR------------SVKRVIPFMlfdHIGGVNTLFQIISSSGCLVIIDDRTP 202
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTHKNIVARFSHARdpifgnqiipdtAILTVIPFH---HGFGMFTTLGYLICGFRVVLMYKFEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE--YGVL 280
Cdd:cd17642 265 ELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEttSAIL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 YSQSKSNDSLWIKLSDKNIESRVVD------------GMLQIKSMSTMIGYINAPSP----FTQDGWLMTGDMVEVDGD- 343
Cdd:cd17642 345 ITPEGDDKPGAVGKVVPFFYAKVVDldtgktlgpnerGELCVKGPMIMKGYVNNPEAtkalIDKDGWLHSGDIAYYDEDg 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264249082 344 YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSE 408
Cdd:cd17642 425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTE 489
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
136-435 |
8.74e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 79.41 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIV--HDFTLLQKKYSVARS--VKRVIPFML--------FDHigGVNTLFQIISSSgclVIIDDRTPN 203
Cdd:PRK06087 192 VLFTSGTEGLPKGVMltHNNILASERAYCARLnlTWQDVFMMPaplghatgFLH--GVTAPFLIGARS---VLLDIFTPD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 204 RVCNMIEKHQVQ-ALPASPTFINLLILSEvYKKYNLNSLQTISYGSEVMPEATLSKINEifPHVKITQMYGLSEyGVLYS 282
Cdd:PRK06087 267 ACLALLEQQRCTcMLGATPFIYDLLNLLE-KQPADLSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTE-SSPHA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 283 QSKSNDSL-----WIKLSDKNIESRVVDGMLQI-----------KSMSTMIGYINAPS----PFTQDGWLMTGDMVEVDG 342
Cdd:PRK06087 343 VVNLDDPLsrfmhTDGYAAAGVEIKVVDEARKTlppgcegeeasRGPNVFMGYLDEPEltarALDEEGWYYSGDLCRMDE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 343 D-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKRLREFCKDKL 421
Cdd:PRK06087 423 AgYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSRKRV 502
|
330
....*....|....
gi 1264249082 422 PLYKIPQKVVLTTK 435
Cdd:PRK06087 503 AKYKYPEHIVVIDK 516
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
133-378 |
1.25e-15 |
|
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: 78.86 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDF-TLLqkkySVARSVKRVIPF---------MLFDHIGGVNT--LFQIISssGC------- 193
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHrNIL----ARSAGKIQHNGLtpqdvflnwVPLDHVGGLVElhLRAVYL--GCqqvhvpt 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 194 -LVIIDdrtPNRVCNMIEKHQVqALPASPTFINLLILSEVYK----KYNLNSLQTISYGSEVMPEATLSKINEIF----- 263
Cdd:cd05906 243 eEILAD---PLRWLDLIDRYRV-TITWAPNFAFALLNDLLEEiedgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLepygl 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 264 PHVKITQMYGLSEY--GVLYSQSKSNDslwiKLSDKN-----------IESRVVD-----------GMLQIKSMSTMIGY 319
Cdd:cd05906 319 PPDAIRPAFGMTETcsGVIYSRSFPTY----DHSQALefvslgrpipgVSMRIVDdegqllpegevGRLQVRGPVVTKGY 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264249082 320 INAP----SPFTQDGWLMTGDMVEVDGDYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVE 378
Cdd:cd05906 395 YNNPeanaEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-432 |
1.35e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 78.64 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIV--HdFTLLQKKYSVA-----RSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDD-RTPNR 204
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRlsH-QNLLANARSIAeylgiTADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDgVLDDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLiLSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVLYS-- 282
Cdd:cd05922 198 FWEDLREHGATGLAGVPSTYAML-TRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTyl 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 283 -------------QSKSNDSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAPS----PFTQDGWLMTGDMVEVDGD-Y 344
Cdd:cd05922 277 pperilekpgsigLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPyrrkEGRGGGVLHTGDLARRDEDgF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 345 IKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAItGQMVKAVVKLSTNESVSEFRKRLREfckdKLPLY 424
Cdd:cd05922 357 LFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDVLRSLAE----RLPPY 431
|
....*...
gi 1264249082 425 KIPQKVVL 432
Cdd:cd05922 432 KVPATVRV 439
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
306-432 |
1.76e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 78.71 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 306 GMLQIKSMSTMIGYINAPSPFTQ----DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEV 380
Cdd:PRK12492 413 GELCIKGPQVMKGYWQQPEATAEaldaEGWFKTGDIAVIDPDgFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANC 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1264249082 381 AVVGEKNAITGQMVKA-VVKLSTNESVSEfrkrLREFCKDKLPLYKIPQKVVL 432
Cdd:PRK12492 493 AAIGVPDERSGEAVKLfVVARDPGLSVEE----LKAYCKENFTGYKVPKHIVL 541
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
306-430 |
1.88e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 78.38 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 306 GMLQIKSMSTMIGYINAPSPFTQ----DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEV 380
Cdd:PRK08751 409 GELCIKGPQVMKGYWKRPEETAKvmdaDGWLHTGDIARMDEQgFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEV 488
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1264249082 381 AVVGEKNAITGQMVKAV-VKLSTNESVSEfrkrLREFCKDKLPLYKIPQKV 430
Cdd:PRK08751 489 AAVGVPDEKSGEIVKVViVKKDPALTAED----VKAHARANLTGYKQPRII 535
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
223-385 |
4.18e-15 |
|
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: 77.12 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 223 FINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIfpHVKITQMYGLSE---YGVLySQSKSNDSLWIKLSDKNI 299
Cdd:cd05932 259 VVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYRSL--GLNILEAYGMTEnfaYSHL-NYPGRDKIGTVGNAGPGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 300 ESRVV-DGMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIG-GEKVFPAEVENVIQ 372
Cdd:cd05932 336 EVRISeDGEILVRSPALMMGYYKDPeataEAFTADGFLRTGDKGELDADgNLTITGRVKDIFKTSkGKYVAPAPIENKLA 415
|
170
....*....|...
gi 1264249082 373 LMDGVEEVAVVGE 385
Cdd:cd05932 416 EHDRVEMVCVIGS 428
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
134-430 |
4.73e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 134 GLVLFSSGTTGSSKAIVHDFTllqkkysvARSVKRviPFmlfDHIGGVNTLFQIISSSGCL---VIIDDRTPNRVCNM-- 208
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQPDLP--------GRDVDA--PG---DPIVAIARAFYDISESDIYyssAPIYHAAPLRWCSMvh 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 209 --------------------IEKHQVQALPASPT-FINLLIL-SEVYKKYNLNSLQTISYGSEVMP-EATLSKINEIFPh 265
Cdd:PRK13390 218 alggtvvlakrfdaqatlghVERYRITVTQMVPTmFVRLLKLdADVRTRYDVSSLRAVIHAAAPCPvDVKHAMIDWLGP- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 266 vKITQMYGLSE-YGVLYSQSKSndslWikLSDKNIESRVVDGMLQI----------KSMSTM--------IGYINAPS-- 324
Cdd:PRK13390 297 -IVYEYYSSTEaHGMTFIDSPD----W--LAHPGSVGRSVLGDLHIcdddgnelpaGRIGTVyferdrlpFRYLNDPEkt 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 325 --------PFtqdgWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVK 395
Cdd:PRK13390 370 aaaqhpahPF----WTTVGDLGSVDEDgYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVK 445
|
330 340 350
....*....|....*....|....*....|....*.
gi 1264249082 396 AVVKLSTN-ESVSEFRKRLREFCKDKLPLYKIPQKV 430
Cdd:PRK13390 446 AVIQLVEGiRGSDELARELIDYTRSRIAHYKAPRSV 481
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
302-430 |
6.64e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.85 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 302 RVVDGMLQIKSMSTMIGYINAPS--PFTQDGWLMTGDMVEVDGDYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEE 379
Cdd:PRK07824 204 RVEDGRIALGGPTLAKGYRNPVDpdPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVAD 283
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1264249082 380 VAVVGEKNAITGQMVKAVVklSTNESVSEFRKRLREFCKDKLPLYKIPQKV 430
Cdd:PRK07824 284 CAVFGLPDDRLGQRVVAAV--VGDGGPAPTLEALRAHVARTLDRTAAPREL 332
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
6-427 |
1.26e-14 |
|
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: 75.83 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 6 LF-ERFEMNKECEAIVWEDKTYTYewflnqikiytRELNEHR------------KMDyTIVSLEADYSPYSIAMFLALIE 72
Cdd:cd17655 2 LFeEQAEKTPDHTAVVFEDQTLTY-----------RELNERAnqlartlrekgvGPD-TIVGIMAERSLEMIVGILGILK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 73 LGCTVVPILNS---------LVDSKKKEyyeIVELENVIKVERGSFEIINIQRDYIQNELLLQLKKLKHPG---LVLFSS 140
Cdd:cd17655 70 AGGAYLPIDPDypeeriqyiLEDSGADI---LLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDdlaYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 141 GTTGSSK-------AIVHDFTLLQKKYSVARSVkRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRTPNRV---CNMIE 210
Cdd:cd17655 147 GSTGKPKgvmiehrGVVNLVEWANKVIYQGEHL-RVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqalTQYIR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 211 KHQVQALPASPTFINLLilsEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPH-VKITQMYGLSEYGV-----LYSQS 284
Cdd:cd17655 226 QNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVdasiyQYEPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 K------------SNDSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAPS---------PFTQDGWLM-TGDMVEV-- 340
Cdd:cd17655 303 TdqqvsvpigkplGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPEltaekfvddPFVPGERMYrTGDLARWlp 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 341 DGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrkrLREFCKDK 420
Cdd:cd17655 383 DGN-IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQ----LREFLARE 457
|
....*..
gi 1264249082 421 LPLYKIP 427
Cdd:cd17655 458 LPDYMIP 464
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
141-422 |
1.69e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 74.44 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 141 GTTGSSKAIVHDFT---------LLQKKYSVARSVKRVIPfmLFdHIGG-VNTLFQIISSSGCLVIIDD---RTPNRVCN 207
Cdd:cd05944 12 GTTGTPKLAQHTHSnevynawmlALNSLFDPDDVLLCGLP--LF-HVNGsVVTLLTPLASGAHVVLAGPagyRNPGLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 208 ---MIEKHQVQALPASPTFINLLIlsEVYKKYNLNSLQTISYGSEVMPEATLSKInEIFPHVKITQMYGLSEYGVLYSQS 284
Cdd:cd05944 89 fwkLVERYRITSLSTVPTVYAALL--QVPVNADISSLRFAMSGAAPLPVELRARF-EDATGLPVVEGYGLTEATCLVAVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSND-----SLWIKLSDKNIESRVVDG--MLQIKSMSTMIGYINAPSP---------------FTQDGWLMTGDMVEVDG 342
Cdd:cd05944 166 PPDGpkrpgSVGLRLPYARVRIKVLDGvgRLLRDCAPDEVGEICVAGPgvfggylytegnknaFVADGWLNTGDLGRLDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 343 D-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKL 421
Cdd:cd05944 246 DgYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE--EELLAWARDHV 323
|
.
gi 1264249082 422 P 422
Cdd:cd05944 324 P 324
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
174-422 |
2.05e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 75.38 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 174 LFdHIGGV-NTLFQIISSSGCLVIIDD---RTPNRVCN---MIEKHQVQALPASPTFINLLILSEVyKKYNLNSLQTISY 246
Cdd:PRK07529 263 LF-HVNALlVTGLAPLARGAHVVLATPqgyRGPGVIANfwkIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALC 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 247 GSEVMPEATLSKINEifpH--VKITQMYGLSE----------YGVL----------YSQSKSndslwIKLSDKNIESR-- 302
Cdd:PRK07529 341 GAAPLPVEVFRRFEA---AtgVRIVEGYGLTEatcvssvnppDGERrigsvglrlpYQRVRV-----VILDDAGRYLRdc 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 303 VVD--GMLQIKSMSTMIGYINAP---SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDG 376
Cdd:PRK07529 413 AVDevGVLCIAGPNVFSGYLEAAhnkGLWLEDGWLNTGDLGRIDADgYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPA 492
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1264249082 377 VEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLP 422
Cdd:PRK07529 493 VALAAAVGRPDAHAGELPVAYVQLKPGASATE--AELLAFARDHIA 536
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
322-445 |
2.14e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 75.20 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 322 APSPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKL 400
Cdd:PRK05620 422 ANDRFTADGWLRTGDVGSVTRDgFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVL 501
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1264249082 401 S-----TNESVSEFRKRLRefckDKLPLYKIPQ--KVVLTTKKMHTERF-KKD 445
Cdd:PRK05620 502 ApgiepTRETAERLRDQLR----DRLPNWMLPEywTFVDEIDKTSVGKFdKKD 550
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-447 |
2.64e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.76 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIVHDFTLL-------QKKYSVaRSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDD--RTPNRVC 206
Cdd:PRK12316 2151 VIYTSGSTGLPKGVAVSHGALvahcqaaGERYEL-SPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDelWDPEQLY 2229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 207 NMIEKHQVQALPASPTFINLLIlSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE---------- 276
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQLA-EHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEavvtpllwkc 2308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 --------YGVLYSQSKSNDSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAPS---------PFTQDGWLM--TGDM 337
Cdd:PRK12316 2309 rpqdpcgaAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGltaerfvpdPFSASGERLyrTGDL 2388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 338 VE--VDG--DYikiLGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNEsvsEFRKRL 413
Cdd:PRK12316 2389 ARyrADGvvEY---LGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAE---DLLAEL 2462
|
330 340 350
....*....|....*....|....*....|....
gi 1264249082 414 REFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:PRK12316 2463 RAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRK 2496
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-447 |
3.35e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.38 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSK-------AIVHDFTLLQKKYSVARSvKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRT--PNRVC 206
Cdd:PRK12316 4699 VIYTSGSTGRPKgvavshgSLVNHLHATGERYELTPD-DRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLwdPERLY 4777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 207 NMIEKHQVQALPASPTFINLLiLSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVLYSQSKS 286
Cdd:PRK12316 4778 AEIHEHRVTVLVFPPVYLQQL-AEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKA 4856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 287 NDSLWIKLSD-------KNIESRVVDGMLQ-----------IKSMSTMIGYIN---------APSPFTQDGWLM--TGDM 337
Cdd:PRK12316 4857 RDGDACGAAYmpigtplGNRSGYVLDGQLNplpvgvagelyLGGEGVARGYLErpaltaerfVPDPFGAPGGRLyrTGDL 4936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 338 VEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVK-----LSTNESVSEFRK 411
Cdd:PRK12316 4937 ARYRADgVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPqdpalADADEAQAELRD 5016
|
330 340 350
....*....|....*....|....*....|....*.
gi 1264249082 412 RLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:PRK12316 5017 ELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
132-431 |
6.28e-14 |
|
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: 73.56 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSK--AIVHD--FTLLQ--KKYSVARSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDD---RTP 202
Cdd:cd17649 95 QLAYVIYTSGSTGTPKgvAVSHGplAAHCQatAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDelwASA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLIL------SEVYKkynlnSLQTISYGSEVMPEATLSKINEIfpHVKITQMYGLSE 276
Cdd:cd17649 175 DELAEMVRELGVTVLDLPPAYLQQLAEeadrtgDGRPP-----SLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 YGV---LYSQSKSNDSLWIKL---------------SDKNIESRVVDGMLQIKSMSTMIGYINAPS---------PFTQD 329
Cdd:cd17649 248 ATVtplVWKCEAGAARAGASMpigrplggrsayildADLNPVPVGVTGELYIGGEGLARGYLGRPEltaerfvpdPFGAP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 330 G--WLMTGDMVE--VDGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVkAVVKLSTNES 405
Cdd:cd17649 328 GsrLYRTGDLARwrDDGV-IEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAAAA 405
|
330 340
....*....|....*....|....*.
gi 1264249082 406 VSEFRKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd17649 406 QPELRAQLRTALRASLPDYMVPAHLV 431
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
133-421 |
6.79e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 73.78 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAI--VHDFTLLQkkYSVARSVKRVIPfmlfDHI-------GGVN-TLFQIISS--SGCLVIID-- 198
Cdd:PRK04319 207 GAILHYTSGSTGKPKGVlhVHNAMLQH--YQTGKYVLDLHE----DDVywctadpGWVTgTSYGIFAPwlNGATNVIDgg 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 199 DRTPNRVCNMIEKHQVQALPASPTFINLLIL--SEVYKKYNLNSLQTI-SYGSEVMPEAtlskineifphVKITQ-MYGL 274
Cdd:PRK04319 281 RFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLVKKYDLSSLRHIlSVGEPLNPEV-----------VRWGMkVFGL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 275 --------SEYG-VLYSQSKSNDslwIKLSD-----KNIESRVVD-----------GMLQIK----SMstMIGYINAPSP 325
Cdd:PRK04319 350 pihdnwwmTETGgIMIANYPAMD---IKPGSmgkplPGIEAAIVDdqgnelppnrmGNLAIKkgwpSM--MRGIWNNPEK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 326 FTQ---DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENViqLMD--GVEEVAVVGEKNAITGQMVKAVVK 399
Cdd:PRK04319 425 YESyfaGDWYVSGDSAYMDEDgYFWFQGRVDDVIKTSGERVGPFEVESK--LMEhpAVAEAGVIGKPDPVRGEIIKAFVA 502
|
330 340
....*....|....*....|...
gi 1264249082 400 LSTN-ESVSEFRKRLREFCKDKL 421
Cdd:PRK04319 503 LRPGyEPSEELKEEIRGFVKKGL 525
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
133-430 |
2.11e-13 |
|
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: 71.78 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFTLLQKKYSVARSVKRVIPFMLFDHI---GGVNTLFQIISS---SGCLVIIDDR--TPNR 204
Cdd:cd05973 90 PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAadpGWAYGLYYAITGplaLGHPTILLEGgfSVES 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 205 VCNMIEKHQVQALPASPTFINLLILSEVYKKYNLN-SLQTISYGSE-VMPE------ATLSkineifphVKITQMYGLSE 276
Cdd:cd05973 170 TWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEpLTPEvirwfdAALG--------VPIHDHYGQTE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 YGVLYSQSKSND---------------SLWIKLSDKNIESRVVDGMLQI----KSMSTMIGYINAPSPFTQDGWLMTGDM 337
Cdd:cd05973 242 LGMVLANHHALEhpvhagsagrampgwRVAVLDDDGDELGPGEPGRLAIdianSPLMWFRGYQLPDTPAIDGGYYLTGDT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 338 VEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN-ESVSEFRKRLRE 415
Cdd:cd05973 322 VEFDPDgSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGhEGTPALADELQL 401
|
330
....*....|....*
gi 1264249082 416 FCKDKLPLYKIPQKV 430
Cdd:cd05973 402 HVKKRLSAHAYPRTI 416
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
193-434 |
2.34e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 193 CLVIIDdrtPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKynlnslQTISYGSEVM------PEATLSKINEIfpHV 266
Cdd:PRK08162 253 CLRKVD---PKLIFDLIREHGVTHYCGAPIVLSALINAPAEWR------AGIDHPVHAMvagaapPAAVIAKMEEI--GF 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 267 KITQMYGLSE-YG---VLYSQSKsndslWIKLSDKN---IESR------------VVD--------------GMLQIKSM 313
Cdd:PRK08162 322 DLTHVYGLTEtYGpatVCAWQPE-----WDALPLDEraqLKARqgvryplqegvtVLDpdtmqpvpadgetiGEIMFRGN 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 314 STMIGYINAPSPfTQ----DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNA 388
Cdd:PRK08162 397 IVMKGYLKNPKA-TEeafaGGWFHTGDLAVLHPDgYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1264249082 389 ITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVVLTT 434
Cdd:PRK08162 476 KWGEVPCAFVELKDGASATE--EEIIAHCREHLAGFKVPKAVVFGE 519
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
306-447 |
2.83e-13 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 71.64 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 306 GMLQIKSM---STMIGYINAPSP----FTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGV 377
Cdd:PRK08008 367 GEICIKGVpgkTIFKEYYLDPKAtakvLEADGWLHTGDTGYVDEEgFFYFVDRRCNMIKRGGENVSCVELENIIATHPKI 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 378 EEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:PRK08008 447 QDIVVVGIKDSIRDEAIKAFVVLNEGETLSE--EEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKK 514
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
3-431 |
3.52e-13 |
|
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: 71.31 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 3 IDFLFE-RFEMNKECEAIVWEDKTYTYEWF---LNQIKIYTREL---NEhrkmdyTIVSLEADYSPYSIAMFLALIELGC 75
Cdd:cd17644 2 IHQLFEeQVERTPDAVAVVFEDQQLTYEELntkANQLAHYLQSLgvkSE------SLVGICVERSLEMIIGLLAILKAGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 76 TVVPIlnslvdskKKEYYEivelenvikvERGSfeiiniqrdYIQNELLLQLKKLKHPGL--VLFSSGTTGSSK------ 147
Cdd:cd17644 76 AYVPL--------DPNYPQ----------ERLT---------YILEDAQISVLLTQPENLayVIYTSGSTGKPKgvmieh 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 148 -AIVHDFTLLQKKYSVARSvKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDD---RTPNRVCNMIEKHQVQALPASPTF 223
Cdd:cd17644 129 qSLVNLSHGLIKEYGITSS-DRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 224 INLLILSEVYKKYNL-NSLQTISYGSE-VMPE--ATLSKIneIFPHVKITQMYGLSE-------YGVLYSQSKSNDSLWI 292
Cdd:cd17644 208 WHLLVLELLLSTIDLpSSLRLVIVGGEaVQPElvRQWQKN--VGNFIQLINVYGPTEatiaatvCRLTQLTERNITSVPI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 293 KLSDKNIESRVVD-----------GMLQIKSMSTMIGYINAPS---------PFTQ---DGWLMTGDMVEV--DGDyIKI 347
Cdd:cd17644 286 GRPIANTQVYILDenlqpvpvgvpGELHIGGVGLARGYLNRPEltaekfishPFNSsesERLYKTGDLARYlpDGN-IEY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 348 LGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAiTG--QMVKAVVKLSTNE-SVSEfrkrLREFCKDKLPLY 424
Cdd:cd17644 365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQ-PGnkRLVAYIVPHYEESpSTVE----LRQFLKAKLPDY 439
|
....*..
gi 1264249082 425 KIPQKVV 431
Cdd:cd17644 440 MIPSAFV 446
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
133-433 |
3.84e-13 |
|
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: 71.45 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDftllQKKYSVA-----RSVKRVIP---FMLFDHIGGVNTLFQIISS---SGCLVIIDDRT 201
Cdd:cd17634 234 PLFILYTSGTTGKPKGVLHT----TGGYLVYaattmKYVFDYGPgdiYWCTADVGWVTGHSYLLYGplaCGATTLLYEGV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 PN-----RVCNMIEKHQVQALPASPTFINLLILS--EVYKKYNLNSLQTI-SYGSEVMPEATLSKINEIF----PHVK-- 267
Cdd:cd17634 310 PNwptpaRMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILgSVGEPINPEAYEWYWKKIGkekcPVVDtw 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 268 ---------ITQMYGLSEygvLYSQSKSNDSLWIKLSDKNIESRVVDGMLQIKSMSTM------IGYINAPSPFTQ---- 328
Cdd:cd17634 390 wqtetggfmITPLPGAIE---LKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpwpgqtRTLFGDHERFEQtyfs 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 329 --DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNES 405
Cdd:cd17634 467 tfKGMYFSGDGARRDEDgYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE 546
|
330 340
....*....|....*....|....*....
gi 1264249082 406 VS-EFRKRLREFCKDKLPLYKIPQKVVLT 433
Cdd:cd17634 547 PSpELYAELRNWVRKEIGPLATPDVVHWV 575
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
138-437 |
7.41e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 70.46 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIVhdFTLLQKKYSVARSVKRVIPFML----------FDHIGGVNTLFQIISSSGCLVIIDDR-TPNRVC 206
Cdd:PRK07470 170 FTSGTTGRPKAAV--LTHGQMAFVITNHLADLMPGTTeqdaslvvapLSHGAGIHQLCQVARGAATVLLPSERfDPAEVW 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 207 NMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEA----TLSKINEIfphvkITQMYGLSEY----G 278
Cdd:PRK07470 248 ALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRAdqkrALAKLGKV-----LVQYFGLGEVtgniT 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 279 VLYSQSKSNDS-------------LWIKLSDKNIESRVVD----GMLQIKSMSTMIGYINAPSP----FtQDGWLMTGDM 337
Cdd:PRK07470 323 VLPPALHDAEDgpdarigtcgferTGMEVQIQDDEGRELPpgetGEICVIGPAVFAGYYNNPEAnakaF-RDGWFRTGDL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 338 VEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREF 416
Cdd:PRK07470 402 GHLDARgFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE--AELLAW 479
|
330 340 350
....*....|....*....|....*....|..
gi 1264249082 417 CKDKLPLYKIPQKVVL-----------TTKKM 437
Cdd:PRK07470 480 LDGKVARYKLPKRFFFwdalpksgygkITKKM 511
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
138-449 |
7.70e-13 |
|
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: 70.15 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIVHDFtllQKKYSVARSV-------KRVIPFML----FDHIGGVNTLFQIISSSGCLVIIDDRTPNRVC 206
Cdd:cd05915 160 YTTGTTGLPKGVVYSH---RALVLHSLAAslvdgtaLSEKDVVLpvvpMFHVNAWCLPYAATLVGAKQVLPGPRLDPASL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 207 -NMIEKHQVQALPASPTFINLLI-LSEVYKKYNLNSLQTISYGSEvmPEATLSKINEIfPHVKITQMYGLSE-YGV---- 279
Cdd:cd05915 237 vELFDGEGVTFTAGVPTVWLALAdYLESTGHRLKTLRRLVVGGSA--APRSLIARFER-MGVEVRQGYGLTEtSPVvvqn 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 280 ----LYSQSKSNDSLWIKLSDK-NIESRVVDGM----------------LQIKSMSTMIGYIN----APSPFTQDGWLMT 334
Cdd:cd05915 314 fvksHLESLSEEEKLTLKAKTGlPIPLVRLRVAdeegrpvpkdgkalgeVQLKGPWITGGYYGneeaTRSALTPDGFFRT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 335 GDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrkRL 413
Cdd:cd05915 394 GDIAVWDEEgYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPE---EL 470
|
330 340 350
....*....|....*....|....*....|....*..
gi 1264249082 414 REFCKDKLPLYK-IPQKVVLTTKKMHTERFKKDKKVF 449
Cdd:cd05915 471 NEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
133-411 |
2.60e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 68.50 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVhdftLLQKKYSVARSVKRVIPFMLFD--------------HIGGvntLFQIISS--SGCLVI 196
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVL----LANRTFFAVPDILQKEGLNWVTwvvgettysplpatHIGG---LWWILTClmHGGLCV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 197 IDDRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEifPHVKITQMYGLSE 276
Cdd:PRK05857 244 TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEA--TGVRTAQVYGLSE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 YGV----LYSQSKSNDSL------------WIKLSDKN--------IESRVVDGMLQIKSMSTMIGYINAPSPFTQ---D 329
Cdd:PRK05857 322 TGCtalcLPTDDGSIVKIeagavgrpypgvDVYLAATDgigptapgAGPSASFGTLWIKSPANMLGYWNNPERTAEvliD 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 330 GWLMTGDMVEVDGD---YIKilGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESV 406
Cdd:PRK05857 402 GWVNTGDLLERREDgffYIK--GRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDE 479
|
....*
gi 1264249082 407 SEFRK 411
Cdd:PRK05857 480 SAARA 484
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
133-430 |
3.48e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 68.19 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHD-FTLLQKK---------YSVARSVKRVIPFMLFdHIGGVNTLFQIISSSGCLVIIDDRTP 202
Cdd:PRK12406 154 PQSMIYTSGTTGHPKGVRRAaPTPEQAAaaeqmraliYGLKPGIRALLTGPLY-HSAPNAYGLRAGRLGGVLVLQPRFDP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPT-FINLLIL-SEVYKKYNLNSLQTISYGSEVMPeatlskineifPHVK----------ITQ 270
Cdd:PRK12406 233 EELLQLIERHRITHMHMVPTmFIRLLKLpEEVRAKYDVSSLRHVIHAAAPCP-----------ADVKramiewwgpvIYE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 271 MYGLSEYGVLySQSKSNDSL-------------WIKLSDKN-----------IESRVvDGMlqiksmsTMIGYINAP--- 323
Cdd:PRK12406 302 YYGSTESGAV-TFATSEDALshpgtvgkaapgaELRFVDEDgrplpqgeigeIYSRI-AGN-------PDFTYHNKPekr 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 324 SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLST 402
Cdd:PRK12406 373 AEIDRGGFITSGDVGYLDADgYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQP 452
|
330 340
....*....|....*....|....*...
gi 1264249082 403 NESVSEfrKRLREFCKDKLPLYKIPQKV 430
Cdd:PRK12406 453 GATLDE--ADIRAQLKARLAGYKVPKHI 478
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
107-443 |
4.35e-12 |
|
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: 67.90 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 107 GSFEIINI-QRDYIQNELLLQLKKLKHPGLVLFSSGTTGSSKAIVH-DFTLLQKKYSVARSVK-----RVIPFMLFDH-- 177
Cdd:cd05908 81 KLNKVWNTlKNPYLITEEEVLCELADELAFIQFSSGSTGDPKGVMLtHENLVHNMFAILNSTEwktkdRILSWMPLTHdm 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 178 ----------IGGVNTLFQIISssgcLVIiddRTPNRVCNMIEKHQVQALpASPTFINLLILS----EVYKKYNLNSLQT 243
Cdd:cd05908 161 gliafhlaplIAGMNQYLMPTR----LFI---RRPILWLKKASEHKATIV-SSPNFGYKYFLKtlkpEKANDWDLSSIRM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 244 ISYGSE-VMPEATLSKINEIFPH-VKITQM---YGLSEYGVLYSQSKSNDSLW--------------IKLSDK------- 297
Cdd:cd05908 233 ILNGAEpIDYELCHEFLDHMSKYgLKRNAIlpvYGLAEASVGASLPKAQSPFKtitlgrrhvthgepEPEVDKkdseclt 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 298 ---------NIESRVVD-----------GMLQIKSMSTMIGYINAPSP----FTQDGWLMTGDMVEVDGDYIKILGRKSE 353
Cdd:cd05908 313 fvevgkpidETDIRICDednkilpdgyiGHIQIRGKNVTPGYYNNPEAtakvFTDDGWLKTGDLGFIRNGRLVITGREKD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 354 IINIGGEKVFPAEVENVIQLMDGVE--EVAVVGEKNAITGQ---MVKAVVKLSTNESVS---EFRKRLREF----CKDKL 421
Cdd:cd05908 393 IIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTRNeeiFCFIEHRKSEDDFYPlgkKIKKHLNKRggwqINEVL 472
|
410 420
....*....|....*....|..
gi 1264249082 422 PLYKIPQkvvltTKKMHTERFK 443
Cdd:cd05908 473 PIRRIPK-----TTSGKVKRYE 489
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
133-430 |
4.45e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 67.85 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFS-SGTTGSSKAIVHD-FTLLQKKYSVARSV-----KRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRTPNRV 205
Cdd:PRK06164 182 AGALLFTtSGTTSGPKLVLHRqATLLRHARAIARAYgydpgAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAART 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTFINLlILSEVYKKYNLNSLQTISYGS------EVMPEATlskiNEIFPhvkITQMYGLSEYGV 279
Cdd:PRK06164 262 ARALRRHRVTHTFGNDEMLRR-ILDTAGERADFPSARLFGFASfapalgELAALAR----ARGVP---LTGLYGSSEVQA 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 280 LYSQSKSNDSLWIK------LSDKNIESRVVD------------GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDM 337
Cdd:PRK06164 334 LVALQPATDPVSVRiegggrPASPEARVRARDpqdgallpdgesGEIEIRAPSLMRGYLDNPdataRALTDDGYFRTGDL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 338 --VEVDGDYIkILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKnaITGQMVK-AVVKLSTNESVSEfrKRLR 414
Cdd:PRK06164 414 gyTRGDGQFV-YQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT--RDGKTVPvAFVIPTDGASPDE--AGLM 488
|
330
....*....|....*.
gi 1264249082 415 EFCKDKLPLYKIPQKV 430
Cdd:PRK06164 489 AACREALAGFKVPARV 504
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
366-443 |
4.68e-12 |
|
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: 61.41 E-value: 4.68e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264249082 366 EVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLstNESVSEFRKRLREFCKDKLPLYKIPQKVVLTTKKMHTERFK 443
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVL--KPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
138-435 |
6.51e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 67.75 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIVHD----FTLLQkkySVARSVKRVIPF--------MLFDHiGGVNTLFQIISSSGCLVIIDDRTPNRV 205
Cdd:PRK06060 152 YTSGTTGPPKAAIHRhadpLTFVD---AMCRKALRLTPEdtglcsarMYFAY-GLGNSVWFPLATGGSAVINSAPVTPEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIE-KHQVQALPASPTFINLLIlsEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSEYGVLYSQS 284
Cdd:PRK06060 228 AAILSaRFGPSVLYGVPNFFARVI--DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 285 KSND----SLWIKLSDKNIesRVV-----------DGMLQIKSMSTMIGYINAPSPFTQD-GWLMTGDMVEVDGD-YIKI 347
Cdd:PRK06060 306 RVDEwrlgTLGRVLPPYEI--RVVapdgttagpgvEGDLWVRGPAIAKGYWNRPDSPVANeGWLDTRDRVCIDSDgWVTY 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 348 LGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKR-LREFCKDKLPLYKI 426
Cdd:PRK06060 384 RCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRdLHRGLLNRLSAFKV 463
|
....*....
gi 1264249082 427 PQKVVLTTK 435
Cdd:PRK06060 464 PHRFAVVDR 472
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
136-382 |
7.07e-12 |
|
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: 66.91 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIV--HD----FTLLQKKYSVARSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRTPNRVCN-- 207
Cdd:TIGR01733 125 VIYTSGSTGRPKGVVvtHRslvnLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAAll 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 208 --MIEKHQVQALPASPTFINLLILSEVYKkynLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE-------YG 278
Cdd:TIGR01733 205 aaLIAEHPVTVLNLTPSLLALLAAALPPA---LASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTEttvwstaTL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 279 VLYSQSKSNDSLWIKLSDKNIESRVVDGMLQ-----------IKSMSTMIGYINAP---------SPF-TQDGWLM--TG 335
Cdd:TIGR01733 282 VDPDDAPRESPVPIGRPLANTRLYVLDDDLRpvpvgvvgelyIGGPGVARGYLNRPeltaerfvpDPFaGGDGARLyrTG 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1264249082 336 DMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAV 382
Cdd:TIGR01733 362 DLVRYLPDgNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
136-431 |
1.84e-11 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 65.64 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIV--HD----FTLLQKKYSVARSVKRVIPF-------MLFDHIGgvnTLfqiiSSSGCLVII-DDRT 201
Cdd:cd05918 111 VIFTSGSTGKPKGVVieHRalstSALAHGRALGLTSESRVLQFasytfdvSILEIFT---TL----AAGGCLCIPsEEDR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 PNRVCNMIEKHQVQALPASPTFINLLILSEVykkynlNSLQTISYGSEVMPEATlskINEIFPHVKITQMYGLSE---YG 278
Cdd:cd05918 184 LNDLAGFINRLRVTWAFLTPSVARLLDPEDV------PSLRTLVLGGEALTQSD---VDTWADRVRLINAYGPAEctiAA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 279 VLYSQSKSND----------SLWIkLSDKNIESRVVDGM---LQIKSMSTMIGYINAP----SPFTQD-GWLM------- 333
Cdd:cd05918 255 TVSPVVPSTDprnigrplgaTCWV-VDPDNHDRLVPIGAvgeLLIEGPILARGYLNDPektaAAFIEDpAWLKqegsgrg 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 -----TGDMV--EVDGDyIKILGRKSEIINIGGEKVFPAEVENVI-QLMDGVEEVAV--VGEKNAITGQMVKAVVKLSTN 403
Cdd:cd05918 334 rrlyrTGDLVryNPDGS-LEYVGRKDTQVKIRGQRVELGEIEHHLrQSLPGAKEVVVevVKPKDGSSSPQLVAFVVLDGS 412
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1264249082 404 ESV------------SEFR---KRLREFCKDKLPLYKIPQKVV 431
Cdd:cd05918 413 SSGsgdgdslflepsDEFRalvAELRSKLRQRLPSYMVPSVFL 455
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
6-432 |
1.92e-11 |
|
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: 65.69 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 6 LFERF-EMNKECEAIVWEDKTYTYewflnqikiytRELNEH--RKMDY---------TIVSLEADYSPYSIAMFLALIEL 73
Cdd:cd12117 2 LFEEQaARTPDAVAVVYGDRSLTY-----------AELNERanRLARRlraagvgpgDVVGVLAERSPELVVALLAVLKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 74 GCTVVPI--------LNSLV-DSKKKeyyeIV---ELENVIKVERGSFEIINIQRDYIQNELLLQLKKLKHPGLVLFSSG 141
Cdd:cd12117 71 GAAYVPLdpelpaerLAFMLaDAGAK----VLltdRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 142 TTGSSK--AIVHdftllqkkYSVARSVK--RVIPF-----ML------FDhiggVNTlFQI---ISSSGCLVIIDDRT-- 201
Cdd:cd12117 147 STGRPKgvAVTH--------RGVVRLVKntNYVTLgpddrVLqtsplaFD----AST-FEIwgaLLNGARLVLAPKGTll 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 -PNRVCNMIEKHQVQALPASPTFINLLILSEVYKkynLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE---- 276
Cdd:cd12117 214 dPDALGALIAEEGVTVLWLTAALFNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnttf 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 --YGVLYSQSKSNDSLWIKLSDKNIESRVVD-----------GMLQIKSMSTMIGYIN---------APSPFTQDGWLM- 333
Cdd:cd12117 291 ttSHVVTELDEVAGSIPIGRPIANTRVYVLDedgrpvppgvpGELYVGGDGLALGYLNrpaltaerfVADPFGPGERLYr 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAV-VGEKNAITGQMVKAVV---KLSTNEsvse 408
Cdd:cd12117 371 TGDLARWLPDgRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLVAYVVaegALDAAE---- 446
|
490 500
....*....|....*....|....
gi 1264249082 409 frkrLREFCKDKLPLYKIPQKVVL 432
Cdd:cd12117 447 ----LRAFLRERLPAYMVPAAFVV 466
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
132-415 |
2.10e-11 |
|
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: 65.80 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHDftllQKKYSVARSVKrvipfmlFDHIGGVNT--LFQIISSSGCLV----II-------- 197
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRD----NGGHAVALNWS-------MRNIYGIKPgdVWWAASDVGWVVghsyIVygpllhga 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 198 --------DDRTPN-----RVcnmIEKHQVQALPASPTFINLL----ILSEVYKKYNLNSLQTISYGSEVMPEATLSKIN 260
Cdd:cd05967 300 ttvlyegkPVGTPDpgafwRV---IEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 261 EIFpHVKITQMYGLSEYGVLYSQSKSN-DSLWIKLSDKNI-----ESRVVD-----------GMLQIK---SMSTMIGYI 320
Cdd:cd05967 377 NTL-GVPVIDHWWQTETGWPITANPVGlEPLPIKAGSPGKpvpgyQVQVLDedgepvgpnelGNIVIKlplPPGCLLTLW 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 321 NAPSPFTQ------DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQM 393
Cdd:cd05967 456 KNDERFKKlylskfPGYYDTGDAGYKDEDgYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQV 535
|
330 340
....*....|....*....|....*...
gi 1264249082 394 V------KAVVKLSTNESVSEFRKRLRE 415
Cdd:cd05967 536 PlglvvlKEGVKITAEELEKELVALVRE 563
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
132-447 |
3.68e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSK-------AIVHDFTLLQKKYS--VARSVKRVIPFMlFDhiGGVNTLFQIISSSGCLVII---DD 199
Cdd:PRK12316 656 NLAYVIYTSGSTGKPKgagnrhrALSNRLCWMQQAYGlgVGDTVLQKTPFS-FD--VSVWEFFWPLMSGARLVVAapgDH 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 200 RTPNRVCNMIEKHQVQALPASPTFINLLILSEvyKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE--Y 277
Cdd:PRK12316 733 RDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEaaI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 278 GVLYSQ--SKSNDSLWIKLSDKNIESRVVDGMLQ-----------IKSMSTMIGYIN---------APSPFTqDGWLM-- 333
Cdd:PRK12316 811 DVTHWTcvEEGGDSVPIGRPIANLACYILDANLEpvpvgvlgelyLAGRGLARGYHGrpgltaerfVPSPFV-AGERMyr 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVgeknAITGQMVKAVVKLsTNESVSeFRKR 412
Cdd:PRK12316 890 TGDLARYRADgVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVL-ESEGGD-WREA 963
|
330 340 350
....*....|....*....|....*....|....*
gi 1264249082 413 LREFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:PRK12316 964 LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRK 998
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
33-427 |
4.41e-11 |
|
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: 64.41 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 33 NQIKIYTRELNEHRKmdyTIVSLEADYSPYSIAMFLALIELGCTVVPIlnslvdskkKEYYEIVELENVIkvERGSFEII 112
Cdd:cd17650 23 NQLARTLRGLGVAPG---SVVGVCADRSLDAIVGLLAVLKAGGAYVPI---------DPDYPAERLQYML--EDSGAKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 113 NIQRDyiqnelllqlkklkHPGLVLFSSGTTGSSKAIV-------HDFTLLQKKYSVARSVKRV--IPFMLFDHIGGvnT 183
Cdd:cd17650 89 LTQPE--------------DLAYVIYTSGTTGKPKGVMvehrnvaHAAHAWRREYELDSFPVRLlqMASFSFDVFAG--D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 184 LFQIISSSGCLVIIDDRT---PNRVCNMIEKHQVQALPASPTFInLLILSEVYK-KYNLNSLQTISYGSEVMPE---ATL 256
Cdd:cd17650 153 FARSLLNGGTLVICPDEVkldPAALYDLILKSRITLMESTPALI-RPVMAYVYRnGLDLSAMRLLIVGSDGCKAqdfKTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 257 SKinEIFPHVKITQMYGLSEYGV---LYSQSKS---------------NDSLWIKLSDKNIESRVVDGMLQIKSMSTMIG 318
Cdd:cd17650 232 AA--RFGQGMRIINSYGVTEATIdstYYEEGRDplgdsanvpigrplpNTAMYVLDERLQPQPVGVAGELYIGGAGVARG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 319 YINAP---------SPFTQDGWLM-TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKN 387
Cdd:cd17650 310 YLNRPeltaerfveNPFAPGERMYrTGDLARWRADgNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRED 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1264249082 388 AiTGQ-----MVKAVVKLSTNEsvsefrkrLREFCKDKLPLYKIP 427
Cdd:cd17650 390 K-GGEarlcaYVVAAATLNTAE--------LRAFLAKELPSYMIP 425
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
133-430 |
6.33e-11 |
|
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: 64.41 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PGLVLFSSGTTGSSKAIVHDFTLLQKKYSV-ARSVKRVIPFMLFDHIGGVNTLFQIISS------SGCLVIIDDRT---P 202
Cdd:cd05928 176 PMAIYFTSGTTGSPKMAEHSHSSLGLGLKVnGRYWLDLTASDIMWNTSDTGWIKSAWSSlfepwiQGACVFVHHLPrfdP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 NRVCNMIEKHQVQALPASPTFINLLILSEVyKKYNLNSLQTISYGSEVMPEATLSKINEIfPHVKITQMYGLSEYGVLYS 282
Cdd:cd05928 256 LVILKTLSSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGYGQTETGLICA 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 283 QSKS----------------------NDSLWIKLSDKNIESRVvdgmLQIKSMSTMIGYINAP----SPFTQDGWLmTGD 336
Cdd:cd05928 334 NFKGmkikpgsmgkasppydvqiiddNGNVLPPGTEGDIGIRV----KPIRPFGLFSGYVDNPektaATIRGDFYL-TGD 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 337 MVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVS---EFRKR 412
Cdd:cd05928 409 RGIMDEDgYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHdpeQLTKE 488
|
330
....*....|....*...
gi 1264249082 413 LREFCKDKLPLYKIPQKV 430
Cdd:cd05928 489 LQQHVKSVTAPYKYPRKV 506
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
306-383 |
6.48e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.40 E-value: 6.48e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264249082 306 GMLQIKSMSTMIGYINAPsPFTQDGWLMTGDMVEVDGDYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVV 383
Cdd:PRK05851 373 GEIEIRGASMMSGYLGQA-PIDPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
132-435 |
6.87e-11 |
|
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: 64.12 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHDfT---LLQkkysVARSVKRVipfmlFDH-----------IGGVNTLFQIIS---SSGCL 194
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHT-TggyLLY----AATTFKYV-----FDYhpddiywctadIGWITGHSYIVYgplANGAT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 195 VIIDDRTPN-----RVCNMIEKHQVQALPASPTFINLLIL--SEVYKKYNLNSLQTI-SYGSEVMPEATL---SKI-NEI 262
Cdd:cd05966 302 TVMFEGTPTypdpgRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLgSVGEPINPEAWMwyyEVIgKER 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 263 FPHVK-----------ITQMYGLSE----------YGVlysqsksndSLWIKLSDKNIESRVVDGMLQIKS-----MSTM 316
Cdd:cd05966 382 CPIVDtwwqtetggimITPLPGATPlkpgsatrpfFGI---------EPAILDEEGNEVEGEVEGYLVIKRpwpgmARTI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 317 IG----YINAP-SPFTqdGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAIT 390
Cdd:cd05966 453 YGdherYEDTYfSKFP--GYYFTGDGARRDEDgYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1264249082 391 GQMVKAVVKLSTNESVS-EFRKRLREFCKDKLPLYKIPQKVVLTTK 435
Cdd:cd05966 531 GEAIYAFVTLKDGEEPSdELRKELRKHVRKEIGPIATPDKIQFVPG 576
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
316-431 |
1.08e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 63.71 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 316 MIGYINAPSPFT---QDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITG 391
Cdd:PLN02479 413 MKGYLKNPKANEeafANGWFHSGDLGVKHPDgYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWG 492
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1264249082 392 QMVKAVVKLSTNESVSEFRKRLRE---FCKDKLPLYKIPQKVV 431
Cdd:PLN02479 493 ESPCAFVTLKPGVDKSDEAALAEDimkFCRERLPAYWVPKSVV 535
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
300-427 |
2.54e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 62.20 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 300 ESRVVDGMLQIKSMSTMIGYI--NAPSPFT-QDGWLMTGDMVEVDGDYIKILGRkseIINI---GGEKVFPAEVENVIQL 373
Cdd:PRK09029 299 EVKLVDGEIWLRGASLALGYWrqGQLVPLVnDEGWFATRDRGEWQNGELTILGR---LDNLffsGGEGIQPEEIERVINQ 375
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1264249082 374 MDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrkrLREFCKDKLPLYKIP 427
Cdd:PRK09029 376 HPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVN----LAEWLQDKLARFQQP 425
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
220-419 |
6.98e-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: 61.22 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 220 SPTFINL---LILSEVYKKYNLNSLQTISYGSEVMPEATLskinEIF--PHVKITQMYGLSE------------YGvLYS 282
Cdd:cd05933 298 SPLFYRLakkLVFKKVRKALGLDRCQKFFTGAAPISRETL----EFFlsLNIPIMELYGMSEtsgphtisnpqaYR-LLS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 283 QSKSNDSLWIKLSDKNIESrvvDGMLQIKSMSTMIGYINAPSPFTQ----DGWLMTGDMVEVDGD-YIKILGRKSE-IIN 356
Cdd:cd05933 373 CGKALPGCKTKIHNPDADG---IGEICFWGRHVFMGYLNMEDKTEEaideDGWLHSGDLGKLDEDgFLYITGRIKElIIT 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264249082 357 IGGEKVFPAEVENVI-QLMDGVEEVAVVGEKNAITGQMV--KAVVKLSTNESVSEFRKRLREFCKD 419
Cdd:cd05933 450 AGGENVPPVPIEDAVkKELPIISNAMLIGDKRKFLSMLLtlKCEVNPETGEPLDELTEEAIEFCRK 515
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
191-431 |
1.00e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 191 SGCLVII----DDRTPNRVCNMIEKHQVQALPASPTFINLLIlsEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHV 266
Cdd:PRK05691 1338 TGCRLVLagpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI--DEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQV 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 267 KITQMYGLSEYG--VLYSQSKSNDSLW--IKLSDKNIESRVVDGMLQ-----------IKSMSTMIGYINAPS------- 324
Cdd:PRK05691 1416 QLHNRYGPTETAinVTHWQCQAEDGERspIGRPLGNVLCRVLDAELNllppgvagelcIGGAGLARGYLGRPAltaerfv 1495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 325 --PFTQDGWLM--TGDMV--EVDGdYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVV 398
Cdd:PRK05691 1496 pdPLGEDGARLyrTGDRArwNADG-ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYT 1574
|
250 260 270
....*....|....*....|....*....|...
gi 1264249082 399 KLSTNESVSEfrkRLREFCKDKLPLYKIPQKVV 431
Cdd:PRK05691 1575 GEAGQEAEAE---RLKAALAAELPEYMVPAQLI 1604
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
60-431 |
1.20e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 60.29 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 60 SPYSIAMFLALIELGCTVVPILNSLVDSKKKEYYEIVELENVIKVERGSFEIINIQRdYIQNELLLQLKKLKHPGL---- 135
Cdd:PRK04813 62 SPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPV-ITLDELKDIFATGNPYDFdhav 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 -------VLFSSGTTGSSKA--IVHD----FT---------------LLQKKYSVARSVKRVIPfmlfdhiggvnTLFqi 187
Cdd:PRK04813 141 kgddnyyIIFTSGTTGKPKGvqISHDnlvsFTnwmledfalpegpqfLNQAPYSFDLSVMDLYP-----------TLA-- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 188 isSSGCLVIID-DRT--PNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFP 264
Cdd:PRK04813 208 --SGGTLVALPkDMTanFKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 265 HVKITQMYGLSEYGVLYSQ------------------SKSNDSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAPSP- 325
Cdd:PRK04813 286 SATIYNTYGPTEATVAVTSieitdemldqykrlpigyAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKt 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 326 ----FTQDGW--LMTGDMVEVDGDYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVK 399
Cdd:PRK04813 366 aeafFTFDGQpaYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVV 445
|
410 420 430
....*....|....*....|....*....|....
gi 1264249082 400 LSTNESVSEFR--KRLREFCKDKLPLYKIPQKVV 431
Cdd:PRK04813 446 PKEEDFEREFEltKAIKKELKERLMEYMIPRKFI 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
132-431 |
5.37e-09 |
|
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: 58.06 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSK-------AIVHDFTLLQKKYSVARSvKRVI---PFMlFDHigGVNTLFQIISSSGCLVIID--- 198
Cdd:cd17646 139 NLAYVIYTSGSTGRPKgvmvthaGIVNRLLWMQDEYPLGPG-DRVLqktPLS-FDV--SVWELFWPLVAGARLVVARpgg 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 199 DRTPNRVCNMIEKHQVQALPASP----TFINLLILSEvykkynLNSLQTISYGSEVMPEATLSKINEIfPHVKITQMYGL 274
Cdd:cd17646 215 HRDPAYLAALIREHGVTTCHFVPsmlrVFLAEPAAGS------CASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 275 SE--YGVLYSQSKSND---SLWIKLSDKNIESRVVDGMLQ-----------IKSMSTMIGYINAPS---------PFTQD 329
Cdd:cd17646 288 TEaaIDVTHWPVRGPAetpSVPIGRPVPNTRLYVLDDALRpvpvgvpgelyLGGVQLARGYLGRPAltaerfvpdPFGPG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 330 GWLM-TGDMVEV--DGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITG-QMVKAVVKLSTNES 405
Cdd:cd17646 368 SRMYrTGDLARWrpDGA-LEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAaRLVGYVVPAAGAAG 446
|
330 340
....*....|....*....|....*.
gi 1264249082 406 VSEfrKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd17646 447 PDT--AALRAHLAERLPEYMVPAAFV 470
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
318-434 |
1.42e-08 |
|
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: 56.53 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 318 GYINAPS---------PFTQDG--WLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGE 385
Cdd:cd12116 330 GYLGRPAltaerfvpdPFAGPGsrLYRTGDLVRRRADgRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVR 409
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1264249082 386 KNAITGQMVkAVVKLSTNESVSEfrKRLREFCKDKLPLYKIPQKVVLTT 434
Cdd:cd12116 410 EDGGDRRLV-AYVVLKAGAAPDA--AALRAHLRATLPAYMVPSAFVRLD 455
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
192-447 |
1.56e-08 |
|
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: 57.17 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 192 GCLVIIDD---RTPNRVCNMIEKHQVQALPASPTFINLLIlseVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKI 268
Cdd:COG1020 684 ATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 269 TQMYGLSEYGVlysqsksnDSLWIKLSDKNIES--------------RVVDGMLQ-----------IKSMSTMIGYINAP 323
Cdd:COG1020 761 VNLYGPTETTV--------DSTYYEVTPPDADGgsvpigrpiantrvYVLDAHLQpvpvgvpgelyIGGAGLARGYLNRP 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 324 ---------SPFTQDGWLM--TGDMVEV--DGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAIT 390
Cdd:COG1020 833 eltaerfvaDPFGFPGARLyrTGDLARWlpDGN-LEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPG 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1264249082 391 GQMVKAVVKLSTNESVSEFRKRLREfcKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:COG1020 912 DKRLVAYVVPEAGAAAAAALLRLAL--ALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
136-415 |
1.64e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 57.24 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIV--HDFTLlqkkySVARSVKRVIPFMLFDHIGG-----------VNTLFQIISssGCLVI-----I 197
Cdd:PRK08633 787 IIFSSGSEGEPKGVMlsHHNIL-----SNIEQISDVFNLRNDDVILSslpffhsfgltVTLWLPLLE--GIKVVyhpdpT 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 198 DDRTpnrVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFpHVKITQMYGLSEY 277
Cdd:PRK08633 860 DALG---IAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKF-GIRILEGYGATET 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 278 GVLYSQSKSN---DSLWIKLSDKN---------IESRVVD------------GMLQIKSMSTMIGYINAPSP-------F 326
Cdd:PRK08633 936 SPVASVNLPDvlaADFKRQTGSKEgsvgmplpgVAVRIVDpetfeelppgedGLILIGGPQVMKGYLGDPEKtaevikdI 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 327 TQDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQ--LMDGVEEVAVVGEKNAITGQMVkAVVKLSTN 403
Cdd:PRK08633 1016 DGIGWYVTGDKGHLDEDgFLTITDRYSRFAKIGGEMVPLGAVEEELAkaLGGEEVVFAVTAVPDEKKGEKL-VVLHTCGA 1094
|
330
....*....|..
gi 1264249082 404 ESVSEFRKRLRE 415
Cdd:PRK08633 1095 EDVEELKRAIKE 1106
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
299-430 |
1.71e-08 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 56.69 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 299 IESRVVD-----------GMLQIKS---MSTMIGYINAPSPFTQ---DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGE 360
Cdd:PRK06155 352 FEARVVDehdqelpdgepGELLLRAdepFAFATGYFGMPEKTVEawrNLWFHTGDRVVRDADgWFRFVDRIKDAIRRRGE 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 361 KVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVsEFRKrLREFCKDKLPLYKIPQKV 430
Cdd:PRK06155 432 NISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTAL-EPVA-LVRHCEPRLAYFAVPRYV 499
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
132-414 |
1.88e-08 |
|
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: 56.51 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHDF--TLLQKKYSVA-----RSVKRVIPF-----MLFDhiggvntlFQIIS-SSGCLVIID 198
Cdd:cd05943 250 HPLYILYSSGTTGLPKCIVHGAggTLLQHLKEHIlhcdlRPGDRLFYYttcgwMMWN--------WLVSGlAVGATIVLY 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 199 D-----RTPNRVCNMIEKHQVQALPASPTFInlLILSEVYKK----YNLNSLQTI-SYGSEVMPEATLSKINEIFPHVKI 268
Cdd:cd05943 322 DgspfyPDTNALWDLADEEGITVFGTSAKYL--DALEKAGLKpaetHDLSSLRTIlSTGSPLKPESFDYVYDHIKPDVLL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 269 TQMYGLSEYGVLYSQSKSNDSLWI-KLSDKN----IES------RVVD--GMLQIKS-MSTM-IGYINAP--SPFtQDGW 331
Cdd:cd05943 400 ASISGGTDIISCFVGGNPLLPVYRgEIQCRGlgmaVEAfdeegkPVWGekGELVCTKpFPSMpVGFWNDPdgSRY-RAAY 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 332 LMTGDMVEVDGDYIK--------ILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN 403
Cdd:cd05943 479 FAKYPGVWAHGDWIEitprggvvILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG 558
|
330
....*....|..
gi 1264249082 404 ESVS-EFRKRLR 414
Cdd:cd05943 559 VELDdELRKRIR 570
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
329-449 |
2.01e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 56.29 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 329 DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEK-NAITGQMVKAVVKLSTNESV 406
Cdd:cd05937 337 DIYFRTGDLLRQDADgRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvPGHDGRAGCAAITLEESSAV 416
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1264249082 407 -SEFRK-RLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKKVF 449
Cdd:cd05937 417 pTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
132-281 |
2.08e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 56.29 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHD--FTLLQKKYSVARSVKRVIPFMLFDH--IGGV---NTLFQIISSSGCLV------IID 198
Cdd:PTZ00237 255 HPLYILYTSGTTGNSKAVVRSngPHLVGLKYYWRSIIEKDIPTVVFSHssIGWVsfhGFLYGSLSLGNTFVmfeggiIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 199 DRTPNRVCNMIEKHQVQALPASPTFINLLI-----LSEVYKKYNLNSLQTISYGSEV----MPEATLSKINeifphVKIT 269
Cdd:PTZ00237 335 KHIEDDLWNTIEKHKVTHTLTLPKTIRYLIktdpeATIIRSKYDLSNLKEIWCGGEVieesIPEYIENKLK-----IKSS 409
|
170
....*....|..
gi 1264249082 270 QMYGLSEYGVLY 281
Cdd:PTZ00237 410 RGYGQTEIGITY 421
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-447 |
5.24e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.73 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 115 QRDYIQNELLLQLKKLKHPGLVLFSSGTTGSSKAIVHDFTLLQKKYSVARSV------KRVIPFMLFDHIGGVNTLFQII 188
Cdd:PRK12316 3180 GDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAyglgvgDRVLQFTTFSFDVFVEELFWPL 3259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 189 SSSGCLVIIDDR---TPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNlnSLQTISYGSEVMPEATLSKINEIFPh 265
Cdd:PRK12316 3260 MSGARVVLAGPEdwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT--SLKRIVCGGEALPADLQQQVFAGLP- 3336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 266 vkITQMYGLSEYGVLYSQSK---------------SNDSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYINAPS------ 324
Cdd:PRK12316 3337 --LYNLYGPTEATITVTHWQcveegkdavpigrpiANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGltaerf 3414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 325 ---PFTQDGWLM-TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVgeknAITGQMVKAVVK 399
Cdd:PRK12316 3415 vpdPFVPGERLYrTGDLARYRADgVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVV 3490
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1264249082 400 LSTNESvsEFRKRLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:PRK12316 3491 PEDEAG--DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRK 3536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
18-431 |
8.74e-08 |
|
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: 54.24 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 18 AIVWEDKTYTYewflnqikiytRELNE------HRKMDY-----TIVSLEADYSPYSIAMFLALIELGCTVVPIlnslvd 86
Cdd:cd17643 5 AVVDEDRRLTY-----------GELDAranrlaRTLRAEgvgpgDRVALALPRSAELIVALLAILKAGGAYVPI------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 87 skkkeyyeivELENviKVERGSFeiinIQRDyiqNELLLQLKKLKHPGLVLFSSGTTGSSKAIV--HDftllqkkySVAR 164
Cdd:cd17643 68 ----------DPAY--PVERIAF----ILAD---SGPSLLLTDPDDLAYVIYTSGSTGRPKGVVvsHA--------NVLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 165 ---SVKRVIPF------MLFDHIG---GVNTLFQIISSSGCLVIIDD---RTPNRVCNMIEKHQVQALPASPTFINLLIL 229
Cdd:cd17643 121 lfaATQRWFGFneddvwTLFHSYAfdfSVWEIWGALLHGGRLVVVPYevaRSPEDFARLLRDEGVTVLNQTPSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 230 SEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVK--ITQMYGLSEYGV-----------LYSQSKSN-----DSLW 291
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTVhvtfrpldaadLPAAAASPigrplPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 292 IKLSDKNIE--SRVVDGMLQIKSMSTMIGYINAP---------SPFTQDGWLM--TGDMV--EVDGDYiKILGRKSEIIN 356
Cdd:cd17643 281 VYVLDADGRpvPPGVVGELYVSGAGVARGYLGRPeltaerfvaNPFGGPGSRMyrTGDLArrLPDGEL-EYLGRADEQVK 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264249082 357 IGGEKVFPAEVENVIQLMDGVEEVAV-VGEKNAITGQMVKAVVklsTNESVSEFRKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd17643 360 IRGFRIELGEIEAALATHPSVRDAAViVREDEPGDTRLVAYVV---ADDGAAADIAELRALLKELLPDYMVPARYV 432
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
133-434 |
1.31e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 53.85 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 133 PG-LVLFSSGTTGSSK----------AIVHDFTLLQKkySVARSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRT 201
Cdd:PRK13383 175 PGrIVLLTSGTTGKPKgvprapqlrsAVGVWVTILDR--TRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFD 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 PNRVCNMIEKHQVQALPASPTFI-NLLILSEVYKKYN-LNSLQTISYGSEVMPEATLSKINEIFPHVkITQMYGLSEYGV 279
Cdd:PRK13383 253 AEAALAQASLHRADAFTAVPVVLaRILELPPRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 280 LYSQSKSNDSLW------------IKLSDKN---IESRVVdGMLQIKSMSTMIGYINAPSPFTQDGWLMTGDMVEVD-GD 343
Cdd:PRK13383 332 GALATPADLRDApetvgkpvagcpVRILDRNnrpVGPRVT-GRIFVGGELAGTRYTDGGGKAVVDGMTSTGDMGYLDnAG 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 344 YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfrKRLREFCKDKLPL 423
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDA--AQLRDYLKDRVSR 488
|
330
....*....|.
gi 1264249082 424 YKIPQKVVLTT 434
Cdd:PRK13383 489 FEQPRDINIVS 499
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
299-375 |
2.93e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 299 IESRVVD-------GMLQIKSMSTMIGYINAPSPFT----QDGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAE 366
Cdd:PRK06814 968 IEYRLEPvpgidegGRLFVRGPNVMLGYLRAENPGVleppADGWYDTGDIVTIDEEgFITIKGRAKRFAKIAGEMISLAA 1047
|
....*....
gi 1264249082 367 VENVIQLMD 375
Cdd:PRK06814 1048 VEELAAELW 1056
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
329-421 |
3.19e-07 |
|
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: 52.49 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 329 DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVS 407
Cdd:cd05968 470 DNVWVHGDFAYYDEEgYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPT 549
|
90
....*....|....*
gi 1264249082 408 E-FRKRLREFCKDKL 421
Cdd:cd05968 550 EaLAEELMERVADEL 564
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
341-414 |
4.65e-07 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 52.26 E-value: 4.65e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264249082 341 DGdYIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEFRKRLR 414
Cdd:PRK10524 486 DG-YYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLA 558
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
334-415 |
5.58e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 52.07 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVS-EFRK 411
Cdd:PRK00174 487 TGDGARRDEDgYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdELRK 566
|
....
gi 1264249082 412 RLRE 415
Cdd:PRK00174 567 ELRN 570
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
132-431 |
8.12e-07 |
|
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: 51.16 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSK--AIVHD--FTLLQ---KKYSVA--RSVKRVIPfMLFDHigGVNTLFQIISSSGCLVIIDDrtp 202
Cdd:cd12115 106 DLAYVIYTSGSTGRPKgvAIEHRnaAAFLQwaaAAFSAEelAGVLASTS-ICFDL--SVFELFGPLATGGKVVLADN--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 203 nrvcnmiekhqVQALPASP-----TFIN--------LLILSEVYKkynlnSLQTISYGSEVMPEATLSKINEIFPHVKIT 269
Cdd:cd12115 180 -----------VLALPDLPaaaevTLINtvpsaaaeLLRHDALPA-----SVRVVNLAGEPLPRDLVQRLYARLQVERVV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 270 QMYGLSE------YGVLYSQSKSNDSL-------WIKLSDKNIESRV--VDGMLQIKSMSTMIGYINAPS---------P 325
Cdd:cd12115 244 NLYGPSEdttystVAPVPPGASGEVSIgrplantQAYVLDRALQPVPlgVPGELYIGGAGVARGYLGRPGltaerflpdP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 326 FTQDGWLM-TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN 403
Cdd:cd12115 324 FGPGARLYrTGDLVRWRPDgLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG 403
|
330 340
....*....|....*....|....*...
gi 1264249082 404 ESVSefRKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd12115 404 AAGL--VEDLRRHLGTRLPAYMVPSRFV 429
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
52-431 |
8.87e-07 |
|
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: 50.94 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 52 IVSLEADYSPYSIAMFLAliELGCTVVPILNSLVDSKKKEYYEIVELENVIKVERGSfeiiNIqrDYIQNELllqlkklk 131
Cdd:cd17656 65 FVPIDPEYPEERRIYIML--DSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTS----NI--DYINNSD-------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAI------VHDFTLLQKKYSVARSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVIIDDRTPNRV 205
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVqlehknMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 ---CNMIEKHQVQALPASPTFINLLI-LSEVYKKYNLNSLQTISYGSEVMPEATLSKIneIFPH-VKITQMYGLSEYGVL 280
Cdd:cd17656 209 eqlFDLVKRHNIEVVFLPVAFLKFIFsEREFINRFPTCVKHIITAGEQLVITNEFKEM--LHEHnVHLHNHYGPSETHVV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 YS----------------QSKSNDSLWIKLSDKNIESRVVDGMLQIKSMSTMIGYIN---------APSPFTQDGWLM-T 334
Cdd:cd17656 287 TTytinpeaeipelppigKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNrqeltaekfFPDPFDPNERMYrT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 335 GDMVEV--DGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKA----VVKLSTNEsvse 408
Cdd:cd17656 367 GDLARYlpDGN-IEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyfvmEQELNISQ---- 441
|
410 420
....*....|....*....|...
gi 1264249082 409 frkrLREFCKDKLPLYKIPQKVV 431
Cdd:cd17656 442 ----LREYLAKQLPEYMIPSFFV 460
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
136-431 |
1.04e-06 |
|
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: 50.73 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 136 VLFSSGTTGSSKAIV--HDFTL-----LQKKYSVaRSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVIID---DRTPNRV 205
Cdd:cd12114 131 VIFTSGSTGTPKGVMisHRAALntildINRRFAV-GPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDearRRDPAHW 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSEVMPEATLSKINEIFPHVKITQMYGLSE--------- 276
Cdd:cd12114 210 AELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEasiwsiyhp 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 277 ------------YGV-LYSQSksndslwiklsdknieSRVVD-----------GMLQIKSMSTMIGYINAP----SPFTQ 328
Cdd:cd12114 290 idevppdwrsipYGRpLANQR----------------YRVLDprgrdcpdwvpGELWIGGRGVALGYLGDPeltaARFVT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 329 DG----WLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVklSTN 403
Cdd:cd12114 354 HPdgerLYRTGDLGRYRPDgTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVV--PDN 431
|
330 340
....*....|....*....|....*...
gi 1264249082 404 ESVSEFRKRLREFCKDKLPLYKIPQKVV 431
Cdd:cd12114 432 DGTPIAPDALRAFLAQTLPAYMIPSRVI 459
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
132-432 |
1.90e-06 |
|
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: 49.94 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIV------HDFTLLQKKYSVARSVKRVIPF--MLFDhiGGVNTLFQIISSSGCLVIIDDRT-- 201
Cdd:cd17652 94 NLAYVIYTSGSTGRPKGVVvthrglANLAAAQIAAFDVGPGSRVLQFasPSFD--ASVWELLMALLAGATLVLAPAEEll 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 -PNRVCNMIEKHQVQALPASPTFinLLILSEVykkyNLNSLQTISYGSEVMPeATLSKinEIFPHVKITQMYGLSEYGVL 280
Cdd:cd17652 172 pGEPLADLLREHRITHVTLPPAA--LAALPPD----DLPDLRTLVVAGEACP-AELVD--RWAPGRRMINAYGPTETTVC 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 YSQSKS---NDSLWIKLSDKNIESRVVD-----------GMLQIKSMSTMIGYINAPS---------PFTQDGWLM--TG 335
Cdd:cd17652 243 ATMAGPlpgGGVPPIGRPVPGTRVYVLDarlrpvppgvpGELYIAGAGLARGYLNRPGltaerfvadPFGAPGSRMyrTG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 336 DMV--EVDGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEE-VAVVGEKNAITGQMVK-AVVKLSTNESVSEfrk 411
Cdd:cd17652 323 DLArwRADGQ-LEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEaVVVVRDDRPGDKRLVAyVVPAPGAAPTAAE--- 398
|
330 340
....*....|....*....|.
gi 1264249082 412 rLREFCKDKLPLYKIPQKVVL 432
Cdd:cd17652 399 -LRAHLAERLPGYMVPAAFVV 418
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
299-388 |
2.03e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 49.99 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 299 IESRVVD-----------GMLQIKSMSTMIGYINAPSPF-TQD--GWLMTGDM-VEVDGDYIKILGRKSEIINIGGEKVF 363
Cdd:PRK07768 369 LEVRVVDedgqvlpprgvGVIELRGESVTPGYLTMDGFIpAQDadGWLDTGDLgYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1264249082 364 PAEVENVIQLMDGV----------------EEVAVVGEKNA 388
Cdd:PRK07768 449 PTDIERAAARVEGVrpgnavavrldaghsrEGFAVAVESNA 489
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
292-385 |
2.44e-06 |
|
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: 49.66 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 292 IKLSDknIESRVV-----DGMLQIKSMSTMIGYINAPSP----FTQDGWLMTGDMVEV--DGDyIKILGR-KSEIINIGG 359
Cdd:cd17640 275 IKIVD--PEGNVVlppgeKGIVWVRGPQVMKGYYKNPEAtskvLDSDGWFNTGDLGWLtcGGE-LVLTGRaKDTIVLSNG 351
|
90 100
....*....|....*....|....*.
gi 1264249082 360 EKVFPAEVENVIQLMDGVEEVAVVGE 385
Cdd:cd17640 352 ENVEPQPIEEALMRSPFIEQIMVVGQ 377
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
325-430 |
2.45e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 49.90 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 325 PFTqdGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN 403
Cdd:PLN02654 510 PFA--GYYFSGDGCSRDKDgYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEG 587
|
90 100
....*....|....*....|....*...
gi 1264249082 404 ESVS-EFRKRLREFCKDKLPLYKIPQKV 430
Cdd:PLN02654 588 VPYSeELRKSLILTVRNQIGAFAAPDKI 615
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
132-432 |
4.55e-06 |
|
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: 48.88 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIV--H----DFTLLQKKYSVARSVKRVIPFML--FDhiGGVNTLFQIISSSGCLVIIDDRT-- 201
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVmpHrslaNLVAWQARASSLGPGARTLQFAGlgFD--VSVQEIFSTLCAGATLVLPPEEVrt 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 202 -PNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGSE-VMPEATLSKINEIFPHVKITQMYGLSEYGV 279
Cdd:cd17651 215 dPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEqLVLTEDLREFCAGLPGLRLHNHYGPTETHV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 280 LYSQSKSND-SLW-----IKLSDKNIESRVVD-----------GMLQIKSMSTMIGYINAP---------SPFTQDGwLM 333
Cdd:cd17651 295 VTALSLPGDpAAWpapppIGRPIDNTRVYVLDaalrpvppgvpGELYIGGAGLARGYLNRPeltaerfvpDPFVPGA-RM 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 334 --TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSEfr 410
Cdd:cd17651 374 yrTGDLARWLPDgELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA-- 451
|
330 340
....*....|....*....|..
gi 1264249082 411 KRLREFCKDKLPLYKIPQKVVL 432
Cdd:cd17651 452 AELRAALATHLPEYMVPSAFVL 473
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
171-371 |
4.62e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.04 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 171 PFmlfdHIGGVN--TLFQIISSSGCLVIIDDRTPNRVCNMIEKHQVQALPASPTFINLLILSEVYKKYNLNSLQTISYGS 248
Cdd:PRK06334 233 PF----HAYGFNscTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 249 EVMPEATLSKINEIFPHVKITQMYGLSEYGVLYSQSKSN---------------DSLWIKLSDKNIESRVVDGMLQIKSM 313
Cdd:PRK06334 309 DAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITINTVNspkhescvgmpirgmDVLIVSEETKVPVSSGETGLVLTRGT 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264249082 314 STMIGYINApsPFTQ-------DGWLMTGDMVEVD--GD-YIKilGRKSEIINIGGEKVFPAEVENVI 371
Cdd:PRK06334 389 SLFSGYLGE--DFGQgfvelggETWYVTGDLGYVDrhGElFLK--GRLSRFVKIGAEMVSLEALESIL 452
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
329-450 |
5.37e-06 |
|
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: 48.50 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 329 DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITG---QMVKAVVKLSTNE 404
Cdd:cd05940 322 DAWFNTGDLMRLDGEgFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDgraGMAAIVLQPNEEF 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1264249082 405 SVSEFRKRLREfckdKLPLYKIPQKVVLTTKKMHTERFKKDKKVFM 450
Cdd:cd05940 402 DLSALAAHLEK----NLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
329-439 |
5.98e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 48.55 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 329 DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKN-AITGQMVKAVVKlstNESV 406
Cdd:PRK07008 408 DGWFPTGDVATIDADgFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHpKWDERPLLVVVK---RPGA 484
|
90 100 110
....*....|....*....|....*....|...
gi 1264249082 407 SEFRKRLREFCKDKLPLYKIPQKVVLTTKKMHT 439
Cdd:PRK07008 485 EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHT 517
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
169-432 |
6.85e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 48.22 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 169 VIPfmlfdhIGGVNTLFQIisssgclviiddrtpnrvcNMIEKHQVQALPASPTFinLLILSEVYKKYNLN----SLQTI 244
Cdd:COG1541 156 VIP------AGGGNTERQL-------------------RLMQDFGPTVLVGTPSY--LLYLAEVAEEEGIDprdlSLKKG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 245 SYGSEVMPEATLSKINEIFpHVKITQMYGLSEYGVLYSqsksndslwiklsdknIESRVVDGM-----LQIksmsTMIgy 319
Cdd:COG1541 209 IFGGEPWSEEMRKEIEERW-GIKAYDIYGLTEVGPGVA----------------YECEAQDGLhiwedHFL----VEI-- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 320 IN----APSPFTQDGWL---------M------TGDMVEVDGD----------YIKILGRKSEIINIGGEKVFPAEVENV 370
Cdd:COG1541 266 IDpetgEPVPEGEEGELvvttltkeaMpliryrTGDLTRLLPEpcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEV 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264249082 371 IQLMDGVEE--VAVVGEKNAitgqMVKAVVKLSTNESVS--EFRKRLREFCKDKLplyKIPQKVVL 432
Cdd:COG1541 346 LLRIPEVGPeyQIVVDREGG----LDELTVRVELAPGASleALAEAIAAALKAVL---GLRAEVEL 404
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
329-448 |
9.56e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 47.95 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 329 DGWLMTGDMVEVDGD-YIKILGRkseiinIG------GEKVFPAEVENVIQLMDGVEEVAVVG------EKNAitGqMvk 395
Cdd:PRK08279 438 DAWFNTGDLMRDDGFgHAQFVDR------LGdtfrwkGENVATTEVENALSGFPGVEEAVVYGvevpgtDGRA--G-M-- 506
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1264249082 396 AVVKLSTNEsvsEF-RKRLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKdKKV 448
Cdd:PRK08279 507 AAIVLADGA---EFdLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKY-RKV 556
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
318-447 |
1.13e-05 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 47.55 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 318 GYINAP---------SPF-TQDGWLMTGDMVEV--DGDyIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGE 385
Cdd:cd17645 301 GYLNRPeltaekfivHPFvPGERMYRTGDLAKFlpDGN-IEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264249082 386 KNAITGQMVKAVVKLSTNESVSEfrkrLREFCKDKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:cd17645 380 EDADGRKYLVAYVTAPEEIPHEE----LREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
306-385 |
4.48e-05 |
|
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: 45.67 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 306 GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGDMVEVDGD-YIKILGRKSEIINIG-GEKVFPAEVENVIQLMDGVEE 379
Cdd:cd05927 356 GEVCIRGPNVFSGYYKDPektaEALDEDGWLHTGDIGEWLPNgTLKIIDRKKNIFKLSqGEYVAPEKIENIYARSPFVAQ 435
|
....*.
gi 1264249082 380 VAVVGE 385
Cdd:cd05927 436 IFVYGD 441
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
132-254 |
5.39e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.56 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 132 HPGLVLFSSGTTGSSKAIVHDF--TLLQKKYSVA-----RSVKRVIPF-----MLFdhiggvNTLFQIISSSGCLVIIDD 199
Cdd:PRK03584 264 HPLWILYSSGTTGLPKCIVHGHggILLEHLKELGlhcdlGPGDRFFWYttcgwMMW------NWLVSGLLVGATLVLYDG 337
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264249082 200 ----RTPNRVCNMIEKHQVQALPASPTFINLLILSEVY--KKYNLNSLQTI-SYGSEVMPEA 254
Cdd:PRK03584 338 spfyPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVpgETHDLSALRTIgSTGSPLPPEG 399
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
302-415 |
6.46e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 45.38 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 302 RVVdGMLQIKSMSTMIGYINAPSpfTQ-----DGWLMTGDMVEVDGDYIKILGRKSEIINIGGEKVFPAEVENVIQLMDG 376
Cdd:PRK09192 409 RVV-GHICVRGPSLMSGYFRDEE--SQdvlaaDGWLDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPE 485
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1264249082 377 VE--EVAVVGEKNAiTGQMVKAVV--KLSTNESvsefRKRLRE 415
Cdd:PRK09192 486 LRsgDAAAFSIAQE-NGEKIVLLVqcRISDEER----RGQLIH 523
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
138-447 |
7.99e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 45.13 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 138 FSSGTTGSSKAIV--------HDFTLLQKKYSVARSVKRVIPFMLFDHIGGVNTLFQIISSSGCLVI----IDDRTpnrV 205
Cdd:PRK06018 184 YTSGTTGDPKGVLyshrsnvlHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgakLDGAS---V 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 206 CNMIEKHQVQALPASPTfINLLILSEVYK-KYNLNSLQTISYGSEVMPEATLSKIN----EIFPHVKITQMYGLSEYGVL 280
Cdd:PRK06018 261 YELLDTEKVTFTAGVPT-VWLMLLQYMEKeGLKLPHLKMVVCGGSAMPRSMIKAFEdmgvEVRHAWGMTEMSPLGTLAAL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 281 ---YSQSKSNDSLWIKLSDK----NIESRVVD-------------GMLQIKSMSTMIGYINA-PSPFTQDGWLMTGDMVE 339
Cdd:PRK06018 340 kppFSKLPGDARLDVLQKQGyppfGVEMKITDdagkelpwdgktfGRLKVRGPAVAAAYYRVdGEILDDDGFFDTGDVAT 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 340 VDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTNESVSefRKRLREFCK 418
Cdd:PRK06018 420 IDAYgYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETAT--REEILKYMD 497
|
330 340
....*....|....*....|....*....
gi 1264249082 419 DKLPLYKIPQKVVLTTKKMHTERFKKDKK 447
Cdd:PRK06018 498 GKIAKWWMPDDVAFVDAIPHTATGKILKT 526
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
266-384 |
9.93e-05 |
|
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: 44.72 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 266 VKITQMYGLSEYGVLYSQSKSND--SLWIKLSDKNIESRVVD-GMLQIKSMSTMIGYINAP----SPFTQDGWLMTGD-- 336
Cdd:cd17641 349 VPLKQLYGQTELAGAYTVHRDGDvdPDTVGVPFPGTEVRIDEvGEILVRSPGVFVGYYKNPeataEDFDEDGWLHTGDag 428
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1264249082 337 MVEVDGdYIKILGRKSEIINIG-GEKVFPAEVENVIQLMDGVEEVAVVG 384
Cdd:cd17641 429 YFKENG-HLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
323-432 |
1.49e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 323 PSPFTQDGWLM--TGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNA----ITGQMVK 395
Cdd:PRK05691 2559 ADPFAADGGRLyrTGDLVRLRADgLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPsgkqLAGYLVS 2638
|
90 100 110
....*....|....*....|....*....|....*..
gi 1264249082 396 AVVKLStNESVSEFRKRLREFCKDKLPLYKIPQKVVL 432
Cdd:PRK05691 2639 AVAGQD-DEAQAALREALKAHLKQQLPDYMVPAHLIL 2674
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
318-400 |
2.44e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 43.52 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 318 GYINAPSPFTQ---DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQM 393
Cdd:PRK07867 366 GYYNDPEADAErmrGGVYWSGDLAYRDADgYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQ 445
|
....*..
gi 1264249082 394 VKAVVKL 400
Cdd:PRK07867 446 VMAALVL 452
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-425 |
2.79e-04 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 42.94 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 65 AMFLALIELGCTVVPILNSLVDSKKKEyyeivelenviKVERGSFEIINIQRDYIQNElllqlkklkhPGLVLFSSGTTG 144
Cdd:cd05974 40 EAMLAAMKLGAVVIPATTLLTPDDLRD-----------RVDRGGAVYAAVDENTHADD----------PMLLYFTSGTTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 145 SSKAIVHDftllQKKYSVarsvkrvipfmlfdhiGGVNTLFQI----------ISSSG-----------------CLVII 197
Cdd:cd05974 99 KPKLVEHT----HRSYPV----------------GHLSTMYWIglkpgdvhwnISSPGwakhawscffapwnagaTVFLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 198 DDR--TPNRVCNMIEKHQVQALPASPTFINLLIlsevykKYNLNSLQT-----ISYGSEVMPEaTLSKINEIFpHVKITQ 270
Cdd:cd05974 159 NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLI------QQDLASFDVklrevVGAGEPLNPE-VIEQVRRAW-GLTIRD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 271 MYGLSEYGVLYSQS-----------KSNDSLWIKLSDKN----IESRVVDGMLQIKSMSTMIGYINAP---SPFTQDGWL 332
Cdd:cd05974 231 GYGQTETTALVGNSpgqpvkagsmgRPLPGYRVALLDPDgapaTEGEVALDLGDTRPVGLMKGYAGDPdktAHAMRGGYY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 333 MTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITGQMVKAVVKLSTN-ESVSEFR 410
Cdd:cd05974 311 RTGDIAMRDEDgYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyEPSPETA 390
|
410
....*....|....*
gi 1264249082 411 KRLREFCKDKLPLYK 425
Cdd:cd05974 391 LEIFRFSRERLAPYK 405
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
318-398 |
3.20e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 43.09 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 318 GYINAPSPFTQ---DGWLMTGDMVEVDGD-YIKILGRKSEIINIGGEKVFPAEVENVIQLMDGVEEVAVVGEKNAITG-Q 392
Cdd:PRK13388 365 GYYNNPEATAErmrHGMYWSGDLAYRDADgWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGdQ 444
|
....*.
gi 1264249082 393 MVKAVV 398
Cdd:PRK13388 445 VMAALV 450
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
300-372 |
3.20e-04 |
|
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: 43.00 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 300 ESRVVD------------GMLQIKSMSTMIGYINAPsPFTQ-----------DGWLMTGDM-VEVDGdYIKILGRKSEII 355
Cdd:cd05931 365 EVRIVDpetgrelpdgevGEIWVRGPSVASGYWGRP-EATAetfgalaatdeGGWLRTGDLgFLHDG-ELYITGRLKDLI 442
|
90
....*....|....*..
gi 1264249082 356 NIGGEKVFPAEVENVIQ 372
Cdd:cd05931 443 IVRGRNHYPQDIEATAE 459
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
318-433 |
2.50e-03 |
|
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: 40.28 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 318 GYINAPS----PFTQDGWLMTGDMVEVDGD-YIKILGRKSEII-NIGGEKVFPAEVENVI---QLMDGVeEVAVVGEKNA 388
Cdd:cd17639 343 GYYKNPEktkeAFDGDGWFHTGDIGEFHPDgTLKIIDRKKDLVkLQNGEYIALEKLESIYrsnPLVNNI-CVYADPDKSY 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264249082 389 ITGQMV---KAVVKLSTNESVSEfrKRLREFCKDK------------------LPLYKIPQKVVLT 433
Cdd:cd17639 422 PVAIVVpneKHLTKLAEKHGVIN--SEWEELCEDKklqkavlkslaetaraagLEKFEIPQGVVLL 485
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
328-443 |
5.96e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 39.03 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 328 QDGWLMTGDMVEVDGD-YIKILGRKSEIINIG-GEKVFPAEVENVIQLMDGVEEVAVVGEKnaiTGQMVKAVVKL---ST 402
Cdd:PLN02430 491 KDGWFHTGDIGEILPNgVLKIIDRKKNLIKLSqGEYVALEYLENVYGQNPIVEDIWVYGDS---FKSMLVAVVVPneeNT 567
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1264249082 403 NE--SVSEFRKRLREFCkdKLPLYKipqKVVLTTKKMHTERFK 443
Cdd:PLN02430 568 NKwaKDNGFTGSFEELC--SLPELK---EHILSELKSTAEKNK 605
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
335-432 |
6.52e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 38.91 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264249082 335 GDMVE-VDGDYIKILGRKSEIINIGGEKVFPAEVENVI-QLMDGVEEVAVVGEKNAITGQ---MVKAVVKLST--NESVS 407
Cdd:PLN03052 594 GDIFErTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPeqlVIAAVLKDPPgsNPDLN 673
|
90 100
....*....|....*....|....*.
gi 1264249082 408 EFRKRLREFCKDKL-PLYKIPQKVVL 432
Cdd:PLN03052 674 ELKKIFNSAIQKKLnPLFKVSAVVIV 699
|
|
| |
