|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
6-464 |
2.24e-147 |
|
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: 428.07 E-value: 2.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:COG0318 17 ALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGdhpvladlmpmldlddpiapaapitgsprpgddAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:COG0318 97 ARALVT---------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWG 244
Cdd:COG0318 144 VLVALPLFHVFGLtVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 245 ATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIACNPPEQ--SRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARS 321
Cdd:COG0318 224 GAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPgeRRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 322 ASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDG 400
Cdd:COG0318 303 PNVMKGYWnDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDE 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 401 VNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKELH 464
Cdd:COG0318 383 KWGERVVAFVVL-RPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
6-461 |
1.68e-116 |
|
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: 349.94 E-value: 1.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd05936 17 ALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDHPvLADLmpmldLDDPIAPAAPITgsPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDAL--RLTER 163
Cdd:cd05936 97 AKALIVAVS-FTDL-----LAAGAPLGERVA--LTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 164 DRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIM 242
Cdd:cd05936 169 DVVLAALPLFHVFGLtVALLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 243 WGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIACNPPEQSR-LDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQAR 320
Cdd:cd05936 249 SGGAPLPVEVAERFEELTGVPIVEGYGLTETsPVVAVNPLDGPRkPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 321 SASLMAGYLPA-AANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPD 399
Cdd:cd05936 328 GPQVMKGYWNRpEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPD 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576413765 400 GVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05936 408 PYSGEAVKAFVVLK-EGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
6-457 |
2.15e-116 |
|
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: 348.45 E-value: 2.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd17631 13 ALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAhavgdhpVLADlmpmldlddpiapaapitgsprpgDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd17631 93 AK-------VLFD------------------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWG 244
Cdd:cd17631 142 LLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 245 ATPVTVSIAETVTRRtGVRWVPAYGTTEL-PVIACNPPE--QSRLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARS 321
Cdd:cd17631 222 GAPMPERLLRALQAR-GVKFVQGYGMTETsPGVTFLSPEdhRRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 322 ASLMAGYL--PAAaNAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPD 399
Cdd:cd17631 300 PHVMAGYWnrPEA-TAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPD 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 576413765 400 GVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLR 457
Cdd:cd17631 379 EKWGEAVVAVVVP-RPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
10-456 |
3.90e-116 |
|
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: 349.59 E-value: 3.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHA 89
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 90 VGDHPVLADLMPMLD----------LDDPIAPAAPITGSPRPG-----------------DDAVLVFSSGTTGLPKAVRH 142
Cdd:cd05911 87 FTDPDGLEKVKEAAKelgpkdkiivLDDKPDGVLSIEDLLSPTlgeededlppplkdgkdDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 143 THASLDAAVRQWRDALRLTER--DRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPI 220
Cdd:cd05911 167 SHRNLIANLSQVQTFLYGNDGsnDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 221 AQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWV-PAYGTTEL-PVIACNPPEQSRLDSVGRPVAGVDV 298
Cdd:cd05911 247 AAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTETgGILTVNPDGDDKPGSVGRLLPNVEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 299 RIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAP 376
Cdd:cd05911 327 KIVDDDGKDSLGPNEPGEICVRGPQVMKGYYnnPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 377 AEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYKRL-SRVVFVPEIPRLPSGKV 455
Cdd:cd05911 407 AELEAVLLEHPGVADAAVIGIPDEVSGE-LPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLrGGVVFVDEIPKSASGKI 485
|
.
gi 576413765 456 L 456
Cdd:cd05911 486 L 486
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
123-456 |
3.83e-112 |
|
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: 334.25 E-value: 3.83e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRI 202
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 203 LRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL--PVIACNP 280
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 281 PE-QSRLDSVGRPVAGVDVRIVSLDTGEpVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLR 358
Cdd:cd04433 161 DDdARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWnNPEATAAVDEDGWYRTGDLGRLDEDGYLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 359 ITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRL 438
Cdd:cd04433 240 IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVL-RPGADLDAEELRAHVRERLAPYKVP 318
|
330
....*....|....*...
gi 576413765 439 SRVVFVPEIPRLPSGKVL 456
Cdd:cd04433 319 RRVVFVDALPRTASGKID 336
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
12-460 |
1.01e-104 |
|
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: 321.11 E-value: 1.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDH-------ALGLT 84
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKqvkdsgaKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 85 DPAHA------------VGDHPVLADLMPMLDLDDPIA--PAAPITgsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAA 150
Cdd:cd05904 111 TAELAeklaslalpvvlLDSAEFDSLSFSDLLFEADEAepPVVVIK----QDDVAALLYSSGTTGRSKGVMLTHRNLIAM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 151 VRQ--WRDALRLTERDRIQVATPPSHILGLLNILTA-LRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASH 227
Cdd:cd05904 187 VAQfvAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGlLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 228 PRLESYDLSSLRFIMWGATPVTVSIAETVTRR-TGVRWVPAYGTTEL-PVIACNPPE---QSRLDSVGRPVAGVDVRIVS 302
Cdd:cd05904 267 PIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTEStGVVAMCFAPekdRAKYGSVGRLVPNVEAKIVD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 303 LDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVE 380
Cdd:cd05904 347 PETGESLPPNQTGELWIRGPSIMKGYLnnPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 381 TVLHSHPAVKDCAVFGVPDGVNGEAVvaavatHA-----PGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKV 455
Cdd:cd05904 427 ALLLSHPEILDAAVIPYPDEEAGEVP------MAfvvrkPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKI 500
|
....*
gi 576413765 456 LRRVL 460
Cdd:cd05904 501 LRKEL 505
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
6-462 |
4.22e-101 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 312.12 E-value: 4.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--- 82
Cdd:PRK06187 24 AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNdae 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ----LTDPAHAvgdhPVLADLMPMLDL--------DDPIAPAAPITGS----------------PRPGDDAVLVFSSGTT 134
Cdd:PRK06187 104 drvvLVDSEFV----PLLAAILPQLPTvrtvivegDGPAAPLAPEVGEyeellaaasdtfdfpdIDENDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 135 GLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIE 214
Cdd:PRK06187 180 GHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPRRFDPENLLDLIETERVTFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 215 MAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIACNPPE------QSRLD 287
Cdd:PRK06187 260 FAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETsPVVSVLPPEdqlpgqWTKRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 288 SVGRPVAGVDVRIVSLDTGE-PVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKE 365
Cdd:PRK06187 340 SAGRPLPGVEARIVDDDGDElPPDGGEVGEIIVRGPWLMQGYWnRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 366 MIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVVFVP 445
Cdd:PRK06187 420 VIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK-PGATLDAKELRAFLRGRLAKFKLPKRIAFVD 498
|
490
....*....|....*..
gi 576413765 446 EIPRLPSGKVLRRVLKE 462
Cdd:PRK06187 499 ELPRTSVGKILKRVLRE 515
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
6-462 |
4.02e-98 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 304.13 E-value: 4.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDE--------- 76
Cdd:PRK07656 23 AYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEaayilargd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 77 ------VDHALGLTDPAHA----------VGDHPVLADLMPMLDLDDPIAPAAPITGSP--RPGDDAVLVFSSGTTGLPK 138
Cdd:PRK07656 103 akalfvLGLFLGVDYSATTrlpalehvviCETEEDDPHTEKMKTFTDFLAAGDPAERAPevDPDDVADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 139 AVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAV 217
Cdd:PRK07656 183 GAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYkAGVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 218 APIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWV-PAYGTTELPVIAC-NPPEQSRLD---SVGRP 292
Cdd:PRK07656 263 PTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVlTGYGLSEASGVTTfNRLDDDRKTvagTIGTA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 293 VAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVR 370
Cdd:PRK07656 343 IAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYddPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 371 GFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVvaavatHA-----PGNTGVAAELTARVAAQLAPYKRLSRVVFVP 445
Cdd:PRK07656 422 GFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG------KAyvvlkPGAELTEEELIAYCREHLAKYKVPRSIEFLD 495
|
490
....*....|....*..
gi 576413765 446 EIPRLPSGKVLRRVLKE 462
Cdd:PRK07656 496 ELPKNATGKVLKRALRE 512
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
6-462 |
2.24e-91 |
|
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: 284.57 E-value: 2.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIA-GERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLT 84
Cdd:cd05941 4 AIVDDGDSITYADLVARAARLANRLLALGKDLrGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 85 DPAHAVgdhpvladlmpmldlddpiapaapitgsprpgDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERD 164
Cdd:cd05941 84 EPSLVL--------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 165 RIQVATPPSHILGLLNILTA-LRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYD--------L 235
Cdd:cd05941 132 VLLHVLPLHHVHGLVNALLCpLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDpqfaraaaA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQSRLD-SVGRPVAGVDVRIVSLDTGEPVGPGDV 314
Cdd:cd05941 212 ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPgTVGMPLPGVQARIVDEETGEPLPRGEV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 315 GEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEM-IKVRGFQVAPAEVETVLHSHPAVKD 391
Cdd:cd05941 292 GEIQVRGPSVFKEYWnkPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDiIKSGGYKVSALEIERVLLAHPGVSE 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576413765 392 CAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05941 372 CAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
24-460 |
3.04e-85 |
|
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: 268.58 E-value: 3.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 24 DGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVgdhpVLADLmpml 103
Cdd:cd05935 12 KKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV----VGSEL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 104 dlddpiapaapitgsprpGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLN-IL 182
Cdd:cd05935 84 ------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGsLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 183 TALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGV 262
Cdd:cd05935 146 TAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 263 RWVPAYGTTE-LPVIACNPPEQSRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWR 339
Cdd:cd05935 226 RFVEGYGLTEtMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWnrPEETEESFIE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 340 DG---WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPG 416
Cdd:cd05935 306 IKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLR-PE 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 576413765 417 NTGVAAE--LTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd05935 385 YRGKVTEedIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
4-370 |
5.79e-84 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 264.56 E-value: 5.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 4 PAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGL 83
Cdd:pfam00501 12 TALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 84 TDPAHAVGDHPVLAD-------------LMPMLDLDDPI-----------APAAPITGSPRPGDD-AVLVFSSGTTGLPK 138
Cdd:pfam00501 92 SGAKVLITDDALKLEellealgklevvkLVLVLDRDPVLkeeplpeeakpADVPPPPPPPPDPDDlAYIIYTSGTTGKPK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 139 AVRHTHASLDAAVRQW----RDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRF---DVDRILRHIENDR 210
Cdd:pfam00501 172 GVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFpalDPAALLELIERYK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 211 ITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPP----EQSRL 286
Cdd:pfam00501 252 VTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLpldeDLRSL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 287 DSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLK 364
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLndPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKK 411
|
....*.
gi 576413765 365 EMIKVR 370
Cdd:pfam00501 412 DQIKLG 417
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
19-462 |
4.08e-83 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 266.08 E-value: 4.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 19 LDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEV--------------------- 77
Cdd:PLN02246 56 VELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIakqakasgakliitqscyvdk 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 78 --DHALGLTDPAHAVGDHP-VLADLMPMLDLDDPIAPAAPItgSPrpgDDAV-LVFSSGTTGLPKAVRHTHASLDAAVRQ 153
Cdd:PLN02246 136 lkGLAEDDGVTVVTIDDPPeGCLHFSELTQADENELPEVEI--SP---DDVVaLPYSSGTTGLPKGVMLTHKGLVTSVAQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 154 WRDA----LRLTERDRIQVATPPSHILGLLNI-LTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHP 228
Cdd:PLN02246 211 QVDGenpnLYFHSDDVILCVLPMFHIYSLNSVlLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 229 RLESYDLSSLRFIMWGATPVTVSIAETVTRRtgvrwVP------AYGTTEL-PVIACNP-----PEQSRLDSVGRPVAGV 296
Cdd:PLN02246 291 VVEKYDLSSIRMVLSGAAPLGKELEDAFRAK-----LPnavlgqGYGMTEAgPVLAMCLafakePFPVKSGSCGTVVRNA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 297 DVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQV 374
Cdd:PLN02246 366 ELKIVDPETGASLPRNQPGEICIRGPQIMKGYLndPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 375 APAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGK 454
Cdd:PLN02246 446 APAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVR-SNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGK 524
|
....*...
gi 576413765 455 VLRRVLKE 462
Cdd:PLN02246 525 ILRKDLRA 532
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
6-462 |
5.74e-82 |
|
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: 261.86 E-value: 5.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRR--VSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEV------ 77
Cdd:cd05926 5 ALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFefylad 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 78 -DHALGLTDPAHAVGD-----HPVLADLMPMLDLDDPI--------------APAAPITGSPRPGDDAVLVFSSGTTGLP 137
Cdd:cd05926 85 lGSKLVLTPKGELGPAsraasKLGLAILELALDVGVLIrapsaeslsnlladKKNAKSEGVPLPDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 138 KAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLL-NILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMA 216
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVaSLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 217 VAPIAQALASHPRLESYD-LSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIACNP--PEQSRLDSVGRP 292
Cdd:cd05926 245 VPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAaHQMTSNPlpPGPRKPGSVGKP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 293 VaGVDVRIVsLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVR 370
Cdd:cd05926 325 V-GVEVRIL-DEDGEILPPGVVGEICLRGPNVTRGYLnnPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 371 GFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRL 450
Cdd:cd05926 403 GEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGE-EVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKT 481
|
490
....*....|..
gi 576413765 451 PSGKVLRRVLKE 462
Cdd:cd05926 482 ATGKIQRRKVAE 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
5-462 |
8.51e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 262.97 E-value: 8.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 5 AALVIEDRRVSRHALDALSDGLGATLHHR-GVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHAlgL 83
Cdd:PRK08314 27 TAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY--V 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 84 TDP---------------AHAVGD----HPVLADLMPMLDLDDPIAP------AAPITGSPRPG---------------- 122
Cdd:PRK08314 105 TDSgarvaivgselapkvAPAVGNlrlrHVIVAQYSDYLPAEPEIAVpawlraEPPLQALAPGGvvawkealaaglappp 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 -----DD-AVLVFSSGTTGLPKAVRHTHASLDAAV---RQWRDalrLTERDRIQVATPPSHILGLLN-ILTALRVGTSVR 192
Cdd:PRK08314 185 htagpDDlAVLPYTSGTTGVPKGCMHTHRTVMANAvgsVLWSN---STPESVVLAVLPLFHVTGMVHsMNAPIYAGATVV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 193 LHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE 272
Cdd:PRK08314 262 LMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 273 lpVIA---CNPPEQSRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAA-ANAEVWRDG--WYR 344
Cdd:PRK08314 342 --TMAqthSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWnrPEAtAEAFIEIDGkrFFR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 345 TGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVA--AVATHAPGNTGvAA 422
Cdd:PRK08314 420 TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAvvVLRPEARGKTT-EE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 576413765 423 ELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK08314 499 EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQE 538
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
11-461 |
1.98e-81 |
|
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: 258.38 E-value: 1.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 11 DRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAV 90
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 91 GDhpvladlmpmldlddpiaPAApitgsprpgddavLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVAT 170
Cdd:cd05934 81 VD------------------PAS-------------ILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 171 PPSHILGLL-NILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMwgATPVT 249
Cdd:cd05934 130 PLFHINAQAvSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAY--GAPNP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 250 VSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQSRLD-SVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSA---SLM 325
Cdd:cd05934 208 PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPgSIGRPAPGYEVRIVD-DDGQELPAGEPGELVIRGLrgwGFF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 326 AGYL--PAAaNAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNG 403
Cdd:cd05934 287 KGYYnmPEA-TAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGE 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 576413765 404 EAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05934 366 DEVKAVVVLR-PGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
13-462 |
7.82e-80 |
|
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: 254.61 E-value: 7.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 13 RVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVgd 92
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 93 hpvladLMPMLDLDDPIApaapitgspRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPP 172
Cdd:cd05903 79 ------VPERFRQFDPAA---------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 173 SHILGLLN-ILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVS 251
Cdd:cd05903 144 AHQTGFVYgFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 252 IAETVTRRTGVRWVPAYGTTELPVIACN---PPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGY 328
Cdd:cd05903 224 LARRAAELLGAKVCSAYGSTECPGAVTSitpAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 329 LPAA-ANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVV 407
Cdd:cd05903 303 LDRPdLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERAC 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 576413765 408 AAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05903 383 AVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
6-465 |
9.58e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 256.78 E-value: 9.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--- 82
Cdd:PRK08316 29 ALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDhsg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ----LTDPAHA---------VGDHPVLADLMP--------MLDLDDPIAPAAPITGSPRPGDDAV--LVFSSGTTGLPKA 139
Cdd:PRK08316 109 arafLVDPALAptaeaalalLPVDTLILSLVLggreapggWLDFADWAEAGSVAEPDVELADDDLaqILYTSGTESLPKG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 140 VRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNIL-TALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVA 218
Cdd:PRK08316 189 AMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLgPYLYVGATNVILDAPDPELILRTIEAERITSFFAPP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 219 PIAQALASHPRLESYDLSSLRFIMWGAT--PVTVsIAETVTRRTGVRWVPAYGTTELPVIAC--NPPEQ-SRLDSVGRPV 293
Cdd:PRK08316 269 TVWISLLRHPDFDTRDLSSLRKGYYGASimPVEV-LKELRERLPGLRFYNCYGQTEIAPLATvlGPEEHlRRPGSAGRPV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 294 AGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYLPA-AANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGF 372
Cdd:PRK08316 348 LNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDpEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 373 QVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHApGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPS 452
Cdd:PRK08316 427 NVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA-GATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPS 505
|
490
....*....|...
gi 576413765 453 GKVLRRVLKELHG 465
Cdd:PRK08316 506 GKILKRELRERYA 518
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
5-463 |
1.31e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 249.64 E-value: 1.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 5 AALVIED-----RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWK------ 73
Cdd:COG0365 26 VALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGaealad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 74 -------------------------RDEVDHAL-GLTDPAH--AVGDHPVLADLMPMLDLDDPIA-PAAPITGSPRPGDD 124
Cdd:COG0365 106 riedaeakvlitadgglrggkvidlKEKVDEALeELPSLEHviVVGRTGADVPMEGDLDWDELLAaASAEFEPEPTDADD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 125 -AVLVFSSGTTGLPKAVRHTHAS----LDAAVRQWrdaLRLTERDRIQVATPPSHILGLLNILTA-LRVGTSVRLH---P 195
Cdd:COG0365 186 pLFILYTSGTTGKPKGVVHTHGGylvhAATTAKYV---LDLKPGDVFWCTADIGWATGHSYIVYGpLLNGATVVLYegrP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 196 RF-DVDRILRHIENDRITIeMAVAPIA-QALASHP--RLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTT 271
Cdd:COG0365 263 DFpDPGRLWELIEKYGVTV-FFTAPTAiRALMKAGdePLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 272 EL--PVIACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSA--SLMAGYL-PAAANAEVWRD---GWY 343
Cdd:COG0365 342 ETggIFISNLPGLPVKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPwpGMFRGYWnDPERYRETYFGrfpGWY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 344 RTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVA--AVATHAPGNTGVA 421
Cdd:COG0365 421 RTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAfvVLKPGVEPSDELA 500
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 576413765 422 AELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:COG0365 501 KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
26-463 |
2.38e-75 |
|
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: 245.90 E-value: 2.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDP----AHAVGDHPVLA---- 97
Cdd:cd17642 57 LAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPtivfCSKKGLQKVLNvqkk 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 98 --------------DLMPMLDLDDPIAPAAPITGSP---------RPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQW 154
Cdd:cd17642 137 lkiiktiiildskeDYKGYQCLYTFITQNLPPGFNEydfkppsfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 155 RDAL---RLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLE 231
Cdd:cd17642 217 RDPIfgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 232 SYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWV-PAYGTTE-LPVIACNPPEQSRLDSVGRPVAGVDVRIVSLDTGEPV 309
Cdd:cd17642 297 KYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTEtTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 310 GPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHP 387
Cdd:cd17642 377 GPNERGELCVKGPMIMKGYVnnPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHP 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 388 AVKDCAVFGVPDGVNGEAVVAAVATHApGNTGVAAELTARVAAQLAPYKRL-SRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:cd17642 457 KIFDAGVAGIPDEDAGELPAAVVVLEA-GKTMTEKEVMDYVASQVSTAKRLrGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
26-462 |
4.86e-72 |
|
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: 233.39 E-value: 4.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEvdhalgLTDPahavgdhpvLADLMPMLDl 105
Cdd:cd05912 14 LAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNE------LAFQ---------LKDSDVKLD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 106 ddpiapaapitgsprpgDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTAL 185
Cdd:cd05912 78 -----------------DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 186 RVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALAS-HPRLESYdlsSLRFIMWGATPVTVSIAETVTRRtGVRW 264
Cdd:cd05912 141 IYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEiLGEGYPN---NLRCILLGGGPAPKPLLEQCKEK-GIPV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 265 VPAYGTTE-LPVIACNPPEQS--RLDSVGRPVAGVDVRIVSldtgEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWRD 340
Cdd:cd05912 217 YQSYGMTEtCSQIVTLSPEDAlnKIGSAGKPLFPVELKIED----DGQPPYEVGEILLKGPNVTKGYLnRPDATEESFEN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 341 GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNtgv 420
Cdd:cd05912 293 GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS--- 369
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 576413765 421 AAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05912 370 EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
6-463 |
5.37e-72 |
|
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: 236.97 E-value: 5.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:COG1021 43 AVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 P-AHAVGD-----------------HP------VLADLMPMLDLDDPIA-PAAPITGSPRPGDDAVLVFSSGTTGLPKAV 140
Cdd:COG1021 123 AvAYIIPDrhrgfdyralarelqaeVPslrhvlVVGDAGEFTSLDALLAaPADLSEPRPDPDDVAFFQLSGGTTGLPKLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 141 RHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLN--ILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVA 218
Cdd:COG1021 203 PRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpgVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 219 PIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNP--PEQSRLDSVGRPVAGV 296
Cdd:COG1021 283 PLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLddPEEVILTTQGRPISPD 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 297 D-VRIVSlDTGEPVGPGDVGEIQARSASLMAGYLPA-AANAEVW-RDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQ 373
Cdd:COG1021 363 DeVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRApEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 374 VAPAEVETVLHSHPAVKDCAVFGVPDGVNGEavvaavATHA---PGNTGV-AAELTARVAAQ-LAPYKRLSRVVFVPEIP 448
Cdd:COG1021 442 IAAEEVENLLLAHPAVHDAAVVAMPDEYLGE------RSCAfvvPRGEPLtLAELRRFLRERgLAAFKLPDRLEFVDALP 515
|
490
....*....|....*
gi 576413765 449 RLPSGKVLRRVLKEL 463
Cdd:COG1021 516 LTAVGKIDKKALRAA 530
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
6-462 |
2.81e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 232.18 E-value: 2.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVS-RHALDALSDGLGAtLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDevDHALGLT 84
Cdd:PRK06188 30 ALVLGDTRLTyGQLADRISRYIQA-FEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD--DHAYVLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 85 D---------PAH-------------------AVGDHPVLADLmpmLDLDDPIAPAaPITGSPRPGDDAVLVFSSGTTGL 136
Cdd:PRK06188 107 DagistlivdPAPfveralallarvpslkhvlTLGPVPDGVDL---LAAAAKFGPA-PLVAAALPPDIAGLAYTGGTTGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 137 PKAVRHTHASLDA------AVRQWRDALRLTerdriqVATPPSHILGLLNILTALRVGTsVRLHPRFDVDRILRHIENDR 210
Cdd:PRK06188 183 PKGVMGTHRSIATmaqiqlAEWEWPADPRFL------MCTPLSHAGGAFFLPTLLRGGT-VIVLAKFDPAEVLRAIEEQR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 211 ITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVT-VSIAETVtRRTGVRWVPAYGTTELPVIAC-------NPPE 282
Cdd:PRK06188 256 ITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSpVRLAEAI-ERFGPIFAQYYGQTEAPMVITylrkrdhDPDD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 283 QSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGY--LPAAaNAEVWRDGWYRTGDVGWLDGNGWLRIT 360
Cdd:PRK06188 335 PKRLTSCGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMDGYwnRPEE-TAEAFRDGWLHTGDVAREDEDGFYYIV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 361 DRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSR 440
Cdd:PRK06188 413 DRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLR-PGAAVDAAELQAHVKERKGSVHAPKQ 491
|
490 500
....*....|....*....|..
gi 576413765 441 VVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK06188 492 VDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
6-464 |
6.17e-67 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 222.14 E-value: 6.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLI----SPA---WKRDEVD 78
Cdd:PRK03640 20 AIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLntrlSREellWQLDDAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 79 HALGLTDPAHA---VGDHPVLADLMPMLDLDDPIapaaPITGSPrpgDDAV--LVFSSGTTGLPKAVRHTHASldaavrQ 153
Cdd:PRK03640 100 VKCLITDDDFEaklIPGISVKFAELMNGPKEEAE----IQEEFD---LDEVatIMYTSGTTGKPKGVIQTYGN------H 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 154 WRDA------LRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASH 227
Cdd:PRK03640 167 WWSAvgsalnLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 228 PRLESYDlSSLRFIMWGATPVTVSIAETVTRRtGVRWVPAYGTTELPV-IACNPPEQS--RLDSVGRPVAGVDVRIVslD 304
Cdd:PRK03640 247 LGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETASqIVTLSPEDAltKLGSAGKPLFPCELKIE--K 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 305 TGEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVL 383
Cdd:PRK03640 323 DGVVVPPFEEGEIVVKGPNVTKGYLnREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 384 HSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNtgvAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK03640 403 LSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT---EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
.
gi 576413765 464 H 464
Cdd:PRK03640 480 V 480
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
14-461 |
3.69e-66 |
|
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: 218.75 E-value: 3.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 14 VSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVgdh 93
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 94 pvladlmpmLDLDDPiapaapitgsprpgddAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPS 173
Cdd:cd05972 78 ---------TDAEDP----------------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 174 HILGLLNILTA-LRVGTSVRLH--PRFDVDRILRHIENDRITIeMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTV 250
Cdd:cd05972 133 WAKGAWSSFFGpWLLGATVFVYegPRFDAERILELLERYGVTS-FCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 251 SIAETVTRRTGVRWVPAYGTTELPVIACNPPEQS-RLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSA--SLMAG 327
Cdd:cd05972 212 EVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPvKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPppGLFLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 328 YLPAAAN-AEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAV 406
Cdd:cd05972 291 YVGDPEKtEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVV 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 407 VA--AVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05972 371 KAfvVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
19-463 |
4.31e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 222.18 E-value: 4.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 19 LDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALglTDPAHAV-------- 90
Cdd:PRK05605 63 LGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPF--EDHGARVaivwdkva 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 91 -------GDHPV-------LADLMPM---LDLDDPIAPA----APITGS--------------------------PRPGD 123
Cdd:PRK05605 141 ptverlrRTTPLetivsvnMIAAMPLlqrLALRLPIPALrkarAALTGPapgtvpwetlvdaaiggdgsdvshprPTPDD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 124 DAVLVFSSGTTGLPKAVRHTHASLDAAVRQ---WRDALRlTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDV 199
Cdd:PRK05605 221 VALILYTSGTTGKPKGAQLTHRNLFANAAQgkaWVPGLG-DGPERVLAALPMFHAYGLtLCLTLAVSIGGELVLLPAPDI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 200 DRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIAC 278
Cdd:PRK05605 300 DLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETsPIIVG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 279 NP-PEQSRLDSVGRPVAGVDVRIVSLDT-GEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNG 355
Cdd:PRK05605 380 NPmSDDRRPGYVGVPFPDTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWnRPEETAKSFLDGWFRTGDVVVMEEDG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 356 WLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPY 435
Cdd:PRK05605 460 FIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSE-EVVAAVVLEPGAALDPEGLRAYCREHLTRY 538
|
490 500
....*....|....*....|....*...
gi 576413765 436 KRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK05605 539 KVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
3-455 |
1.14e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 218.37 E-value: 1.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK06178 48 QRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDPAHAVG------------------------------DHPVL----------------ADLMPMLDlDDPIAPAAPIt 116
Cdd:PRK06178 128 DAGAEVLLAldqlapvveqvraetslrhvivtsladvlpAEPTLplpdslraprlaaagaIDLLPALR-ACTAPVPLPP- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 117 gsPRPGDDAVLVFSSGTTGLPKAVRHTHASL-DAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLH 194
Cdd:PRK06178 206 --PALDALAALNYTGGTTGMPKGCEHTQRDMvYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGEnFGLLFPLFSGATLVLL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 195 PRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMwgatpvTVSIAETVTRRTGVRWVPAYGTTeLP 274
Cdd:PRK06178 284 ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVR------VVSFVKKLNPDYRQRWRALTGSV-LA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 275 VIACNPPEQSRLDS------------------VGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL-PAAANA 335
Cdd:PRK06178 357 EAAWGMTETHTCDTftagfqdddfdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWnKPEATA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 336 EVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAP 415
Cdd:PRK06178 437 EALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQ-VPVAFVQLKP 515
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 576413765 416 GNTGVAAELTARVAAQLAPYKrLSRVVFVPEIPRLPSGKV 455
Cdd:PRK06178 516 GADLTAAALQAWCRENMAVYK-VPEIRIVDALPMTATGKV 554
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
6-461 |
3.83e-64 |
|
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: 213.88 E-value: 3.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIA-GERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLT 84
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 85 DPAHAVGDHPVLADlmpmldlddpiapaapitgsprpGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQW-RDALRLTER 163
Cdd:cd05958 83 RITVALCAHALTAS-----------------------DDICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLRED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 164 DRIqVATPP-SHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRfi 241
Cdd:cd05958 140 DRF-VGSPPlAFTFGLgGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLR-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 242 mwgatpVTVSIAETVTRRTGVRWVPAYG---------TTELPVIACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPG 312
Cdd:cd05958 217 ------KCVSAGEALPAALHRAWKEATGipiidgigsTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 313 DVGEIQARSASLMAgYLPAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDC 392
Cdd:cd05958 290 TIGRLAVRGPTGCR-YLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEC 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576413765 393 AVFGVPD---GVNGEAVVAAVATHAPGNTgVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05958 369 AVVGHPDesrGVVVKAFVVLRPGVIPGPV-LARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
6-463 |
4.53e-64 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 216.56 E-value: 4.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVI--EDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGL 83
Cdd:PRK12583 36 ALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 84 TD-------PAHAVGD-HPVLADLMPMLDLDDP----------------IAPAAP-----------------------IT 116
Cdd:PRK12583 116 SGvrwvicaDAFKTSDyHAMLQELLPGLAEGQPgalacerlpelrgvvsLAPAPPpgflawhelqargetvsrealaeRQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 117 GSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVrLHP 195
Cdd:PRK12583 196 ASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMvLANLGCMTVGACL-VYP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 196 R--FDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRF-IMWGAT-PVtvsiaETVTRRTGVRWVP----A 267
Cdd:PRK12583 275 NeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTgIMAGAPcPI-----EVMRRVMDEMHMAevqiA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 268 YGTTEL-PVI---ACNPPEQSRLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDG 341
Cdd:PRK12583 350 YGMTETsPVSlqtTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWnnPEATAESIDEDG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVA 421
Cdd:PRK12583 429 WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLH-PGHAASE 507
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 576413765 422 AELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK12583 508 EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
12-462 |
7.41e-64 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 215.69 E-value: 7.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD------ 85
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAEskvlvv 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 ---------PAHAVGDHPVLADLMPML--DLDDP-------IAP-------AAPITGSPRPGDDAV--LVFSSGTTGLPK 138
Cdd:PRK13295 134 pktfrgfdhAAMARRLRPELPALRHVVvvGGDGAdsfeallITPaweqepdAPAILARLRPGPDDVtqLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 139 AVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLL-NILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAV 217
Cdd:PRK13295 214 GVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMyGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMAS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 218 APIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE---LPVIACNPPEQSRLDSVGRPVA 294
Cdd:PRK13295 294 TPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEngaVTLTKLDDPDERASTTDGCPLP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 295 GVDVRIVSLDtGEPVGPGDVGEIQARSASLMAGYLPAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIkVRGFQV 374
Cdd:PRK13295 374 GVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGEN 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 375 AP-AEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTA-----RVAAQLAPykrlSRVVFVPEIP 448
Cdd:PRK13295 452 IPvVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR-PGQSLDFEEMVEflkaqKVAKQYIP----ERLVVRDALP 526
|
490
....*....|....*...
gi 576413765 449 RLPSGKV----LRRVLKE 462
Cdd:PRK13295 527 RTPSGKIqkfrLREMLRG 544
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
123-457 |
7.82e-64 |
|
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: 209.66 E-value: 7.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDR 201
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYkAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 202 ILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWV-PAYGTTELPVIACNP 280
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVlTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 281 PEQSRLD---SVGRPVAGVDVRIvsldtgepvgpGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNG 355
Cdd:cd17638 161 PGDDAETvatTCGRACPGFEVRI-----------ADDGEVLVRGYNVMQGYLddPEATAEAIDADGWLHTGDVGELDERG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 356 WLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPY 435
Cdd:cd17638 230 YLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA-RPGVTLTEEDVIAWCRERLANY 308
|
330 340
....*....|....*....|..
gi 576413765 436 KRLSRVVFVPEIPRLPSGKVLR 457
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
6-460 |
3.18e-63 |
|
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: 211.23 E-value: 3.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd05930 5 AVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDhpvladlmpmldlddpiapaapitgsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd05930 85 AKLVLTD----------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQALASHPRLEsyDLSSLRFIM 242
Cdd:cd05930 137 VLQFTSFSFDVSVWEIFGALLAGATLVVLPeevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 243 WGATPVTVSIAETVTRR-TGVRWVPAYGTTELPVIACN---PPEQSRLDSV--GRPVAGVDVRIVSlDTGEPVGPGDVGE 316
Cdd:cd05930 215 VGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYyrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 317 IQARSASLMAGYL-PAAANAEVWRD----GW---YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPA 388
Cdd:cd05930 294 LYIGGAGLARGYLnRPELTAERFVPnpfgPGermYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPG 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576413765 389 VKDCAVFGVPDGvNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd05930 374 VREAAVVAREDG-DGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
5-462 |
1.99e-61 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 208.40 E-value: 1.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 5 AALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHAL--- 81
Cdd:PRK12406 3 ATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILeds 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 82 ------GLTDPAHAVGDH-----PVLADLMP-------------------MLDLDDPIAPAAPITGSPRPGDdAVLVFSS 131
Cdd:PRK12406 83 garvliAHADLLHGLASAlpagvTVLSVPTPpeiaaayrispalltppagAIDWEGWLAQQEPYDGPPVPQP-QSMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 132 GTTGLPKAVRHTHASLDAAVRQWRDALR---LTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIEN 208
Cdd:PRK12406 162 GTTGHPKGVRRAAPTPEQAAAAEQMRALiygLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 209 DRITIEMAVAPIAQALASHP--RLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQ--S 284
Cdd:PRK12406 242 HRITHMHMVPTMFIRLLKLPeeVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDalS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 285 RLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASlMAGYL---PAAANAEVWRDGWYRTGDVGWLDGNGWLRITD 361
Cdd:PRK12406 322 HPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAG-NPDFTyhnKPEKRAEIDRGGFITSGDVGYLDADGYLFLCD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 362 RLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRV 441
Cdd:PRK12406 400 RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQ-PGATLDEADIRAQLKARLAGYKVPKHI 478
|
490 500
....*....|....*....|.
gi 576413765 442 VFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK12406 479 EIMAELPREDSGKIFKRRLRD 499
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
6-463 |
1.26e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 206.82 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVlisPAWKR---DEVDH--- 79
Cdd:PRK07470 25 ALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV---PTNFRqtpDEVAYlae 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 80 ------ALGLTD-PAHAVGDHPVLADLMPMLDLDDPIA----PAAPITGSPRPGDDAVL--------VFSSGTTGLPKAV 140
Cdd:PRK07470 102 asgaraMICHADfPEHAAAVRAASPDLTHVVAIGGARAgldyEALVARHLGARVANAAVdhddpcwfFFTSGTTGRPKAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 141 RHTHASLDAAVRQWRDALR--LTERDRIQVATPPSHILGLLNILTALRVGTSVRL-HPRFDVDRILRHIENDRITIEMAV 217
Cdd:PRK07470 182 VLTHGQMAFVITNHLADLMpgTTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLpSERFDPAEVWALVERHRVTNLFTV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 218 APIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE-------LPVIACNPPE--QSRLDS 288
Cdd:PRK07470 262 PTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEvtgnitvLPPALHDAEDgpDARIGT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 289 VGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMI 367
Cdd:PRK07470 342 CGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNnPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 368 KVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGvAAELTARVAAQLAPYKRLSRVVFVPEI 447
Cdd:PRK07470 421 ISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD-EAELLAWLDGKVARYKLPKRFFFWDAL 499
|
490
....*....|....*.
gi 576413765 448 PRLPSGKVLRRVLKEL 463
Cdd:PRK07470 500 PKSGYGKITKKMVREE 515
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
6-460 |
1.35e-60 |
|
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: 205.66 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--- 82
Cdd:cd17651 13 ALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLAdag 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ----LTDPAHAVGDHPVLADLMPMLDLDDPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDAL 158
Cdd:cd17651 93 pvlvLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 159 RLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDL 235
Cdd:cd17651 173 SLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWG--ATPVTVSIAETVTRRTGVRWVPAYGTTELPVIAC-----NPPEQSRLDSVGRPVAGVDVRIvsLDT-GE 307
Cdd:cd17651 253 AALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTAlslpgDPAAWPAPPPIGRPIDNTRVYV--LDAaLR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 308 PVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGW------YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEV 379
Cdd:cd17651 331 PVPPGVPGELYIGGAGLARGYLnrPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 380 ETVLHSHPAVKDCAVFGVPDGvNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRV 459
Cdd:cd17651 411 EAALARHPGVREAVVLAREDR-PGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRA 489
|
.
gi 576413765 460 L 460
Cdd:cd17651 490 L 490
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-455 |
1.38e-60 |
|
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: 205.64 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 121 PGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPR-FD 198
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLtGCLWLPLLSGIKVVFHPNpLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 199 VDRILRHIENDRITIEMAVAPIAQALAShpRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIA 277
Cdd:cd05909 226 YKKIPELIYDKKATILLGTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECsPVIS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 278 CNPPEQ-SRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYLPA-AANAEVWRDGWYRTGDVGWLDGNG 355
Cdd:cd05909 304 VNTPQSpNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEpELTSFAFGDGWYDTGDIGKIDGEG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 356 WLRITDRLKEMIKVRGFQVAPAEVETVLHSH-PAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAp 434
Cdd:cd05909 384 FLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLA- 462
|
330 340
....*....|....*....|.
gi 576413765 435 ykRLSRVVFVPEIPRLPSGKV 455
Cdd:cd05909 463 --KPSYIHQVEEIPLLGTGKP 481
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
26-462 |
8.03e-60 |
|
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: 204.40 E-value: 8.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIwrLGAAAVL------------------------------------IS 69
Cdd:cd12119 38 LANALRRLGVKPGDRVATLAWNTHRHLELYYAV--PGMGAVLhtinprlfpeqiayiinhaedrvvfvdrdflplleaIA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 70 PAWKRdeVDHALGLTDPAHAVGDHPVLAdlmpmLDLDDPIAPAAPITGSPR--PGDDAVLVFSSGTTGLPKAVRHTHAS- 146
Cdd:cd12119 116 PRLPT--VEHVVVMTDDAAMPEPAGVGV-----LAYEELLAAESPEYDWPDfdENTAAAICYTSGTTGNPKGVVYSHRSl 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 147 -LDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRL-HPRFDVDRILRHIENDRITIEMAVAPIAQAL 224
Cdd:cd12119 189 vLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLpGPYLDPASLAELIEREGVTFAAGVPTVWQGL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 225 ASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRtGVRWVPAYGTTEL-PVIACN--PPEQSRLD---------SVGRP 292
Cdd:cd12119 269 LDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETsPLGTVArpPSEHSNLSedeqlalraKQGRP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 293 VAGVDVRIVSLDTGE-PVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVR 370
Cdd:cd12119 348 VPGVELRIVDDDGRElPWDGKAVGELQVRGPWVTKSYYkNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 371 GFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRL 450
Cdd:cd12119 428 GEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVL-KEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKT 506
|
490
....*....|..
gi 576413765 451 PSGKVLRRVLKE 462
Cdd:cd12119 507 STGKIDKKALRE 518
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
123-461 |
1.65e-59 |
|
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: 199.04 E-value: 1.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAV-LVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRL-HPRFDV 199
Cdd:cd05917 2 DDVInIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSvLGVLACLTHGATMVFpSPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 200 DRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRF-IMWGAtPVTVSIAETVTRRTGVRWVP-AYGTTEL-PVI 276
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTgIMAGA-PCPPELMKRVIEVMNMKDVTiAYGMTETsPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 277 ACNPPEQS---RLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWL 351
Cdd:cd05917 161 TQTRTDDSiekRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWndPEKTAEAIDGDGWLHTGDLAVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 352 DGNGWLRITDRLKEMIkVRGFQ-VAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAA 430
Cdd:cd05917 241 DEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLK-EGAELTEEDIKAYCKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 576413765 431 QLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05917 319 KIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
19-468 |
2.48e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 203.86 E-value: 2.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 19 LDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDpAHAVGDHPVLAD 98
Cdd:PRK07786 48 LDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 99 LM----------------------PMLDLDDPIAPAAPitgSPRPGD-----DAVLVFSSGTTGLPKAVRHTHASLDAAV 151
Cdd:PRK07786 127 VAtavrdivpllstvvvaggssddSVLGYEDLLAEAGP---AHAPVDipndsPALIMYTSGTTGRPKGAVLTHANLTGQA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 152 RQWRDALRLTERDRIQ-VATPPSHILGLLNILTALRVGTSVRLHP--RFDVDRILRHIENDRITIEMAVAPIAQALASHP 228
Cdd:PRK07786 204 MTCLRTNGADINSDVGfVGVPLFHIAGIGSMLPGLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 229 RLESYDLSsLRFIMWGATPVTvsiaETVTRRT-----GVRWVPAYGTTELPVIAC---NPPEQSRLDSVGRPVAGVDVRI 300
Cdd:PRK07786 284 QARPRDLA-LRVLSWGAAPAS----DTLLRQMaatfpEAQILAAFGQTEMSPVTCmllGEDAIRKLGSVGKVIPTVAARV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 301 VSlDTGEPVGPGDVGEIQARSASLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEV 379
Cdd:PRK07786 359 VD-ENMNDVPVGEVGEIVYRAPTLMSGYWNnPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEV 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 380 ETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRV 459
Cdd:PRK07786 438 ENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTE 517
|
....*....
gi 576413765 460 LKELHGCPS 468
Cdd:PRK07786 518 LRERYGACV 526
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
6-463 |
7.33e-59 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 202.73 E-value: 7.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDR--RVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG- 82
Cdd:PRK08315 34 ALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 -------LTDPAHAVGDHPVLADLMP-------------------------------MLDLDDPIAPA--------APIT 116
Cdd:PRK08315 114 sgckaliAADGFKDSDYVAMLYELAPelatcepgqlqsarlpelrrviflgdekhpgMLNFDELLALGravddaelAARQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 117 GSPRPgDDAVLV-FSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVG-TSVRL 193
Cdd:PRK08315 194 ATLDP-DDPINIqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMvLGNLACVTHGaTMVYP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 194 HPRFDVDRILRHIENDRITIEMAVaP---IAQAlaSHPRLESYDLSSLRF-IMWGAT-PVTVsiAETVTRRTGVRWVP-A 267
Cdd:PRK08315 273 GEGFDPLATLAAVEEERCTALYGV-PtmfIAEL--DHPDFARFDLSSLRTgIMAGSPcPIEV--MKRVIDKMHMSEVTiA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 268 YGTTEL-PVI---ACNPPEQSRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGY--LPAAANAEVWRDG 341
Cdd:PRK08315 348 YGMTETsPVStqtRTDDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYwnDPEKTAEAIDADG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 WYRTGDVGWLDGNGWLRITDRLKEMIkVRGFQ-VAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGV 420
Cdd:PRK08315 428 WMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGEnIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILR-PGATLT 505
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 576413765 421 AAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK08315 506 EEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
5-461 |
8.61e-59 |
|
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: 201.44 E-value: 8.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 5 AALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLIS--------------- 69
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNtlltpddyayyleds 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 70 -----------------PAWKRDEVDHALGLTDPAHAVGDHPVLADLMPmlDLDDPIAPAAPitgspRPGDDAVLVFSSG 132
Cdd:cd05959 101 rarvvvvsgelapvlaaALTKSEHTLVVLIVSGGAGPEAGALLLAELVA--AEAEQLKPAAT-----HADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 133 TTGLPKAVRHTHASLDAAVRQW-RDALRLTERDRIQVATPPSHILGLLNILT-ALRVGTSVRLHP-RFDVDRILRHIEND 209
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTfPLSVGATTVLMPeRPTPAAVFKRIRRY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 210 RITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIAC-NPPEQSRLDS 288
Cdd:cd05959 254 RPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLsNRPGRVRYGT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 289 VGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMI 367
Cdd:cd05959 334 TGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWnNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDML 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 368 KVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVnGEAVVAAVATHAPGNTGVAA---ELTARVAAQLAPYKRLSRVVFV 444
Cdd:cd05959 413 KVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED-GLTKPKAFVVLRPGYEDSEAleeELKEFVKDRLAPYKYPRWIVFV 491
|
490
....*....|....*..
gi 576413765 445 PEIPRLPSGKVLRRVLK 461
Cdd:cd05959 492 DELPKTATGKIQRFKLR 508
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
6-461 |
2.60e-58 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 201.40 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--- 82
Cdd:PRK07059 41 AFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKdsg 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ------LTDPAHAVGD--------HPVLADLMPMLDLDDPI-----------APAAPITGSPR----------------- 120
Cdd:PRK07059 121 aeaivvLENFATTVQQvlaktavkHVVVASMGDLLGFKGHIvnfvvrrvkkmVPAWSLPGHVRfndalaegarqtfkpvk 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 121 --PGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQ---WRDALrLTERDRIQ-----VATPPSHILGL-LNILTALRVGT 189
Cdd:PRK07059 201 lgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQmeaWLQPA-FEKKPRPDqlnfvCALPLYHIFALtVCGLLGMRTGG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 190 SVRL--HPRfDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPA 267
Cdd:PRK07059 280 RNILipNPR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 268 YGTTEL-PVIACNPPEQSRLD-SVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWY 343
Cdd:PRK07059 359 YGLSETsPVATCNPVDATEFSgTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWnrPDETAKVMTADGFF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 344 RTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTgvAAE 423
Cdd:PRK07059 438 RTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALT--EED 515
|
490 500 510
....*....|....*....|....*....|....*...
gi 576413765 424 LTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:PRK07059 516 VKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-464 |
3.49e-58 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 199.72 E-value: 3.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 1 MTEPAALVIED---RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEV 77
Cdd:PRK07514 13 FADRDAPFIETpdgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 78 DHALGLTDPAHAVGDHPVLADLMPM-----------LDLD------DPIAPAAP-ITGSPRPGDD-AVLVFSSGTTGLPK 138
Cdd:PRK07514 93 DYFIGDAEPALVVCDPANFAWLSKIaaaagaphvetLDADgtgsllEAAAAAPDdFETVPRGADDlAAILYTSGTTGRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 139 AVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIEndRITIEMAV 217
Cdd:PRK07514 173 GAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLfVATNVALLAGASMIFLPKFDPDAVLALMP--RATVMMGV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 218 APIAQALASHPRLESYDLSSLRFIMWGATPVtvsIAETVTR---RTGVRWVPAYGTTELPVIACNPPEQSRL-DSVGRPV 293
Cdd:PRK07514 251 PTFYTRLLQEPRLTREAAAHMRLFISGSAPL---LAETHREfqeRTGHAILERYGMTETNMNTSNPYDGERRaGTVGFPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 294 AGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGY--LPAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRG 371
Cdd:PRK07514 328 PGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYwrMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 372 FQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLP 451
Cdd:PRK07514 408 YNVYPKEVEGEIDELPGVVESAVIGVPHPDFGE-GVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNT 486
|
490
....*....|...
gi 576413765 452 SGKVLRRVLKELH 464
Cdd:PRK07514 487 MGKVQKNLLREQY 499
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
6-461 |
6.48e-58 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 197.30 E-value: 6.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDevDHALGLTD 85
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPD--DYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVgdhpVLADlmpmldlddpiapaapitgsprpGDD-AVLVFSSGTTGLPKAVRHTHASLDAAVRQW-RDALRLTER 163
Cdd:cd05919 81 CEARL----VVTS-----------------------ADDiAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 164 DRIQVATPPSHILGLLNILT-ALRVGTSVRLHP-RFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFI 241
Cdd:cd05919 134 DRVFSSAKMFFGYGLGNSLWfPLAVGASAVLNPgWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 242 MWGATPVTVSIAETVTRRTGVRWVPAYGTTE-LPVIACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQAR 320
Cdd:cd05919 214 VSAGEALPRGLGERWMEHFGGPILDGIGATEvGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 321 SASLMAGYLPAAANAE-VWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPD 399
Cdd:cd05919 293 GPSAAVGYWNNPEKSRaTFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPE 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576413765 400 GvNGEAVVAAVATHAPGNT---GVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05919 373 S-TGLSRLTAFVVLKSPAApqeSLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
26-460 |
2.25e-57 |
|
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: 196.28 E-value: 2.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPvladlmpmldl 105
Cdd:cd05907 18 LAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVEDP----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 106 DDPiapaapitgsprpgddAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTA- 184
Cdd:cd05907 87 DDL----------------ATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 185 LRVGTSVRLHPRFDVDRI-LRHIendRITIEMAV--------APIAQALASHPRLESYDL---SSLRFIMWGATPVTVSI 252
Cdd:cd05907 151 LLAGARIYFASSAETLLDdLSEV---RPTVFLAVprvwekvyAAIKVKAVPGLKRKLFDLavgGRLRFAASGGAPLPAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 253 AETVtRRTGVRWVPAYGTTEL-PVIACNPPEQSRLDSVGRPVAGVDVRIvsldtgepvgpGDVGEIQARSASLMAGYL-- 329
Cdd:cd05907 228 LHFF-RALGIPVYEGYGLTETsAVVTLNPPGDNRIGTVGKPLPGVEVRI-----------ADDGEILVRGPNVMLGYYkn 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 330 PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQ-VAPAEVETVLHSHPAVKDCAVFG------------ 396
Cdd:cd05907 296 PEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKnISPEPIENALKASPLISQAVVIGdgrpflvalivp 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 397 ----VPDGVNGEAVVAAVATHAPGNTGVAAELTARVA---AQLAPYKRLSRVVFVPEIPRL------PSGKVLRRVL 460
Cdd:cd05907 376 dpeaLEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEaanARLSRYEQIKKFLLLPEPFTIengeltPTLKLKRPVI 452
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
39-461 |
2.66e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 194.23 E-value: 2.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 39 ERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPVLADL----MPMLDLDD---PIAP 111
Cdd:PRK07638 51 KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLpdeeGRVIEIDEwkrMIEK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 112 AAPitgSPRPGDDAVLV-----FSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALR 186
Cdd:PRK07638 131 YLP---TYAPIENVQNApfymgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLY 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 187 VGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALAshpRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVP 266
Cdd:PRK07638 208 VGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLY---KENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 267 AYGTTELPVIACNPPEQSRL--DSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARSASLMAGYLPAAANA-EVWRDGWY 343
Cdd:PRK07638 285 FYGASELSFVTALVDEESERrpNSVGRPFHNVQVRICNEA-GEEVQKGEIGTVYVKSPQFFMGYIIGGVLArELNADGWM 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 344 RTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPgntgvAAE 423
Cdd:PRK07638 364 TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSAT-----KQQ 438
|
410 420 430
....*....|....*....|....*....|....*...
gi 576413765 424 LTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:PRK07638 439 LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
5-463 |
3.21e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 195.53 E-value: 3.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 5 AALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKR---------- 74
Cdd:PRK07788 66 AALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGpqlaevaare 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 75 --------DEVDHALG---------LTDPAHAVGDHPVLADLmpmLDLDDPIAP--AAPITGSPRPGddAVLVFSSGTTG 135
Cdd:PRK07788 146 gvkalvydDEFTDLLSalppdlgrlRAWGGNPDDDEPSGSTD---ETLDDLIAGssTAPLPKPPKPG--GIVILTSGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 136 LPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEM 215
Cdd:PRK07788 221 TPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEATLEDIAKHKATALV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 216 AVAPIAQALASHP--RLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQSRLD--SVGR 291
Cdd:PRK07788 301 VVPVMLSRILDLGpeVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEApgTVGR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 292 PVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYLPAAANAEVwrDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRG 371
Cdd:PRK07788 381 PPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGG 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 372 FQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLP 451
Cdd:PRK07788 458 ENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVK-APGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNP 536
|
490
....*....|..
gi 576413765 452 SGKVLRRVLKEL 463
Cdd:PRK07788 537 TGKVLKRELREM 548
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-463 |
3.51e-56 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 195.36 E-value: 3.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 7 LVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDP 86
Cdd:PRK06155 40 LVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 87 AHAVGDHPVLADLMPMLDLDDPI------------------------APAAPIT-GSPRPGDDAVLVFSSGTTGLPKAVR 141
Cdd:PRK06155 120 RLLVVEAALLAALEAADPGDLPLpavwlldapasvsvpagwstaplpPLDAPAPaAAVQPGDTAAILYTSGTTGPSKGVC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 142 HTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIA 221
Cdd:PRK06155 200 CPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 222 QALASHPRLESYDLSSLRFIMWGATPvtVSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQSRLDSVGRPVAGVDVRIV 301
Cdd:PRK06155 280 SILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQRPGSMGRLAPGFEARVV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 302 SlDTGEPVGPGDVGEIQARSA---SLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPA 377
Cdd:PRK06155 358 D-EHDQELPDGEPGELLLRADepfAFATGYFGmPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSF 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 378 EVETVLHSHPAVKDCAVFGVPDGVnGEAVVAAVATHAPGNTGVAAELTARVAAQLaPYKRLSRVV-FVPEIPRLPSGKVL 456
Cdd:PRK06155 437 EVEQVLLSHPAVAAAAVFPVPSEL-GEDEVMAAVVLRDGTALEPVALVRHCEPRL-AYFAVPRYVeFVAALPKTENGKVQ 514
|
....*..
gi 576413765 457 RRVLKEL 463
Cdd:PRK06155 515 KFVLREQ 521
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
126-457 |
6.50e-56 |
|
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: 189.02 E-value: 6.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 126 VLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRH 205
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 206 IENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTrrtGVRWVPAYGTTELPVIACNPPEQSR 285
Cdd:cd17637 84 IEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPETIQRFEETT---GATFWSLYGQTETSGLVTLSPYRER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 286 LDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRL- 363
Cdd:cd17637 161 PGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWnLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 364 -KEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVV 442
Cdd:cd17637 240 eKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLK-PGATLTADELIEFVGSRIARYKKPRYVV 318
|
330
....*....|....*
gi 576413765 443 FVPEIPRLPSGKVLR 457
Cdd:cd17637 319 FVEALPKTADGSIDR 333
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
14-463 |
8.60e-56 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 194.68 E-value: 8.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 14 VSRHALDALSDGLGATLHHR-GVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGD 92
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 93 HPVLADLMPM----------LDLDDPIAPAAP----ITGSPRPG--------DDAVLVFSSGTTGLPKAVRHTH----AS 146
Cdd:PLN02574 147 PENVEKLSPLgvpvigvpenYDFDSKRIEFPKfyelIKEDFDFVpkpvikqdDVAAIMYSSGTTGASKGVVLTHrnliAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 147 LDAAVRQWRDALRLTERDRIQVAT-PPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQAL 224
Cdd:PLN02574 227 VELFVRFEASQYEYPGSDNVYLAAlPMFHIYGLsLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMAL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 225 ASHPR-LESYDLSSLRFIMWGATPVT-VSIAETVTRRTGVRWVPAYGTTELPVIAC---NPPEQSRLDSVGRPVAGVDVR 299
Cdd:PLN02574 307 TKKAKgVCGEVLKSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgfNTEKLSKYSSVGLLAPNMQAK 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 300 IVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPA 377
Cdd:PLN02574 387 VVDWSTGCLLPPGNCGELWIQGPGVMKGYLnnPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPA 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 378 EVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLR 457
Cdd:PLN02574 467 DLEAVLISHPEIIDAAVTAVPDKECGE-IPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILR 545
|
....*.
gi 576413765 458 RVLKEL 463
Cdd:PLN02574 546 RELKRS 551
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
3-460 |
1.13e-55 |
|
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: 192.72 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDR--RVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHA 80
Cdd:cd05923 16 DACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 81 LG---LTDPAHAVGDHPVLAD---LMPMLDLDDPIAPAAPITGSP-------RPGDDAVLVFSSGTTGLPKA--VRHTHA 145
Cdd:cd05923 96 IErgeMTAAVIAVDAQVMDAIfqsGVRVLALSDLVGLGEPESAGPliedpprEPEQPAFVFYTSGTTGLPKGavIPQRAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 146 SLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILT-ALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQAL 224
Cdd:cd05923 176 ESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVaALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDAL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 225 ASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPpeQSRLDSVGRPVAGVDVRIVSLD 304
Cdd:cd05923 256 AAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMR--DARTGTEMRPGFFSEVRIVRIG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 305 TG--EPVGPGDVGEI--QARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEV 379
Cdd:cd05923 334 GSpdEALANGEEGELivAAAADAAFTGYLnQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 380 ETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARvAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRV 459
Cdd:cd05923 414 ERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCR-ASELADFKRPRRYFFLDELPKNAMNKVLRRQ 492
|
.
gi 576413765 460 L 460
Cdd:cd05923 493 L 493
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
6-463 |
2.23e-55 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 192.00 E-value: 2.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHR-GVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHAL--- 81
Cdd:PRK06839 20 AIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLkds 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 82 GLT------DPAHAVGDHPVLADLMPMLDLDDP--IAPAAPITGSPRPGDDAVLV-FSSGTTGLPKAVRHTHASLDAAVR 152
Cdd:PRK06839 100 GTTvlfvekTFQNMALSMQKVSYVQRVISITSLkeIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGAVLTQENMFWNAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 153 QWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLE 231
Cdd:PRK06839 180 NNTFAIDLTMHDRSIVLLPLFHIGGIgLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 232 SYDLSSLRFIMWGATPVTVSIAETVTRRtGVRWVPAYGTTEL-PVIACNPPEQSR--LDSVGRPVAGVDVRIVSLDTGEp 308
Cdd:PRK06839 260 TTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsPTVFMLSEEDARrkVGSIGKPVLFCDYELIDENKNK- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 309 VGPGDVGEIQARSASLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHP 387
Cdd:PRK06839 338 VEVGEVGELLIRGPNVMKEYWNrPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLS 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 388 AVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK06839 418 DVYEVAVVGRQHVKWGEIPIAFIVKK-SSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
3-461 |
3.16e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 190.97 E-value: 3.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGviageRVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDPAHAVGDHPVLADLMPMLDLDdPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAV----RHTHASLDAAVRQWRdal 158
Cdd:PRK07787 90 DSGAQAWLGPAPDDPAGLPHVPVR-LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVvlsrRAIAADLDALAEAWQ--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 159 rLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIeNDRITIEMAVAPIAQALASHPRLeSYDLSS 237
Cdd:PRK07787 166 -WTADDVLVHGLPLFHVHGLvLGVLGPLRIGNRFVHTGRPTPEAYAQAL-SEGGTLYFGVPTVWSRIAADPEA-ARALRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 238 LRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE-LPVIACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGD--V 314
Cdd:PRK07787 243 ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTEtLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPHDGetV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 315 GEIQARSASLMAGYL-PAAANAEVWR-DGWYRTGDVGWLDGNGWLRITDRLK-EMIKVRGFQVAPAEVETVLHSHPAVKD 391
Cdd:PRK07787 322 GELQVRGPTLFDGYLnRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVRE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 392 CAVFGVPDGVNGEAVVAAVATHAPGNtgvAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:PRK07787 402 AAVVGVPDDDLGQRIVAYVVGADDVA---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
12-463 |
6.02e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 190.79 E-value: 6.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVG 91
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 92 DHPVLADLMPMLDLDDPIAPAAPITGSPRPGDDA----VLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQ 167
Cdd:PRK09088 101 DDAVAAGRTDVEDLAAFIASADALEPADTPSIPPervsLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 168 VATPPSHILGLL-NILTALRVGTSVRLHPRFDVDRILRHIENDR--ITIEMAVAPIAQALASHPRLESYDLSSLRFIMWG 244
Cdd:PRK09088 181 CDAPMFHIIGLItSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAlgITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 245 ATPvtvSIAETVTR--RTGVRWVPAYGTTELPVIACNPPE----QSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQ 318
Cdd:PRK09088 261 GAP---HAAEDILGwlDDGIPMVDGFGMSEAGTVFGMSVDcdviRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 319 ARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFG 396
Cdd:PRK09088 337 LRGPNLSPGYWrrPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 397 VPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK09088 417 MADAQWGE-VGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
123-462 |
7.05e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 192.17 E-value: 7.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAVRHTHASLDAAVR---QWRDALRLTERDRIQVaTPPSHILGLLNILT-ALRVGTSVRLHPRFD 198
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSNTLmgvQWLYNCKEGEEVVLGV-LPFFHVYGMTAVMNlSIMQGYKMVLIPKFD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 199 VDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIA 277
Cdd:PRK06710 286 MKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESsPVTH 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 278 CNPPEQSRL-DSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNG 355
Cdd:PRK06710 366 SNFLWEKRVpGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWnKPEETAAVLQDGWLHTGDVGYMDEDG 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 356 WLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHApGNTGVAAELTARVAAQLAPY 435
Cdd:PRK06710 446 FFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE-GTECSEEELNQFARKYLAAY 524
|
330 340
....*....|....*....|....*..
gi 576413765 436 KRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK06710 525 KVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
6-460 |
9.25e-55 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 189.85 E-value: 9.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd05920 33 AVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDHpvladlmpMLDLDDPIAPAAPITGSPRpgDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd05920 113 AVAYIVPD--------RHAGFDHRALARELAESIP--EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSH--ILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMW 243
Cdd:cd05920 183 YLAVLPAAHnfPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 244 GATPVTVSIAETVTRRTGVRWVPAYGTTE--LPVIACNPPEQSRLDSVGRPVAGVD-VRIVSLDtGEPVGPGDVGEIQAR 320
Cdd:cd05920 263 GGARLSPALARRVPPVLGCTLQQVFGMAEglLNYTRLDDPDEVIIHTQGRPMSPDDeIRVVDEE-GNPVPPGEEGELLTR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 321 SASLMAGYLPA-AANAEVWR-DGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVP 398
Cdd:cd05920 342 GPYTIRGYYRApEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMP 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 399 DGVNGEA--VVAAVATHAPGNTGVAAELTARvaaQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd05920 422 DELLGERscAFVVLRDPPPSAAQLRRFLRER---GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
3-465 |
2.17e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 189.33 E-value: 2.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 -------LTDP----------AHAVGDHPVLADLMPMLDLDDPIAPAAPItgspRPGDDAVLVFSSGTTGLPKAVRHTHA 145
Cdd:PRK06145 97 dagakllLVDEefdaivaletPKIVIDAAAQADSRRLAQGGLEIPPQAAV----APTDLVRLMYTSGTTDRPKGVMHSYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 146 SLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQAL 224
Cdd:PRK06145 173 NLHWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 225 ASHPRLESYDLSSLRFIMWGA--TPvTVSIAETVTRRTGVRWVPAYGTTElpviACNPP-------EQSRLDSVGRPVAG 295
Cdd:PRK06145 253 LTVPDRDRFDLDSLAWCIGGGekTP-ESRIRDFTRVFTRARYIDAYGLTE----TCSGDtlmeagrEIEKIGSTGRALAH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 296 VDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYLPAA-ANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQV 374
Cdd:PRK06145 328 VEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPeKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 375 APAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGK 454
Cdd:PRK06145 407 ASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVL-NPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGK 485
|
490
....*....|..
gi 576413765 455 VLRRVLK-ELHG 465
Cdd:PRK06145 486 VLKRVLRdELNG 497
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
19-394 |
2.62e-54 |
|
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: 187.09 E-value: 2.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 19 LDALSDGLGATLH-HRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPVLA 97
Cdd:TIGR01733 5 LDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 98 DLMPM-----------LDLDDPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRI 166
Cdd:TIGR01733 85 RLAGLvlpvilldpleLAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 167 QVATPPSHILGLLNILTALRVGTSVRLHP----RFDVDRILRHIENDRITIEMAVAPIAQALASHPRlesYDLSSLRFIM 242
Cdd:TIGR01733 165 LQFASLSFDASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSLLALLAAALP---PALASLRLVI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 243 WGATPVTVSIAETV-TRRTGVRWVPAYGTTELPVIACN------PPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVG 315
Cdd:TIGR01733 242 LGGEALTPALVDRWrARGPGARLINLYGPTETTVWSTAtlvdpdDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 316 EIQARSASLMAGYL-PAAANAEVW---------RDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHS 385
Cdd:TIGR01733 321 ELYIGGPGVARGYLnRPELTAERFvpdpfaggdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400
|
....*....
gi 576413765 386 HPAVKDCAV 394
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
21-461 |
2.68e-54 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 188.03 E-value: 2.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 21 ALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIW----RLGAAAVLISPAWKRDEVDHALGLTDPAHAVGD---- 92
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAyaggRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADagaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 93 ------HPVLADLMPMLDLDDPIAPAAPITGSPRPGDD-AVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd05922 81 drlrdaLPASPDPGTVLDADGIRAARASAPAHEVSHEDlALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDR-ILRHIENDRITIEMAVAPIAQALASHPRlESYDLSSLRFIMW- 243
Cdd:cd05922 161 ALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATGLAGVPSTYAMLTRLGF-DPAKLPSLRYLTQa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 244 -GATPvTVSIAETVTRRTGVRWVPAYGTTE-LPVIACNPPEQ--SRLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQA 319
Cdd:cd05922 240 gGRLP-QETIARLRELLPGAQVYVMYGQTEaTRRMTYLPPERilEKPGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 320 RSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGV 397
Cdd:cd05922 318 RGPNVMKGYWndPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 398 PDGVNgeAVVAAVATHAPGNTgvAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05922 398 PDPLG--EKLALFVTAPDKID--PKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
6-460 |
2.68e-54 |
|
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: 189.02 E-value: 2.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--- 82
Cdd:cd17646 16 AVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLAdag 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ----LTDPAhAVGDHPVLADLMPMLDLDDPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDAL 158
Cdd:cd17646 96 pavvLTTAD-LAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 159 RLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESydL 235
Cdd:cd17646 175 PLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARpggHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGS--C 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPV----IACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGP 311
Cdd:cd17646 253 ASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvthWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 312 GDVGEIQARSASLMAGYLPAAA-NAEVWRDGW-------YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVL 383
Cdd:cd17646 332 GVPGELYLGGVQLARGYLGRPAlTAERFVPDPfgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAAL 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576413765 384 HSHPAVKDCAVFGVPDGvNGEAVVAAVATHAPGNTGV-AAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd17646 412 AAHPAVTHAVVVARAAP-AGAARLVGYVVPAAGAAGPdTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
4-465 |
3.88e-54 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 189.71 E-value: 3.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 4 PAALVIEDRRVSRHA-LDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEvdhalg 82
Cdd:PRK05852 33 PALVVTADRIAISYRdLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDPAHAVGDHPVLADLMPMLDLDDPIAPAAPI---------------------TGSPRP---------GDDAVLVFSSG 132
Cdd:PRK05852 107 QRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLtvnvggdsgpsggtlsvhldaATEPTPatstpeglrPDDAMIMFTGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 133 TTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIEND 209
Cdd:PRK05852 187 TTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPargRFSAHTFWDDIKAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 210 RITIEMAVAPIAQALASHPRLESYDLS--SLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTElpviACNPPEQSRLD 287
Cdd:PRK05852 267 GATWYTAVPTIHQILLERAATEPSGRKpaALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTE----ATHQVTTTQIE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 288 SVGR---PVA---------GVDVRIVSLDtGEPVGPGDVGEIQARSASLMAGYLPAAAN-AEVWRDGWYRTGDVGWLDGN 354
Cdd:PRK05852 343 GIGQtenPVVstglvgrstGAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTItAANFTDGWLRTGDLGSLSAA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 355 GWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTgVAAELTARVAAQLAP 434
Cdd:PRK05852 422 GDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPP-TAEELVQFCRERLAA 500
|
490 500 510
....*....|....*....|....*....|.
gi 576413765 435 YKRLSRVVFVPEIPRLPSGKVLRRVLKELHG 465
Cdd:PRK05852 501 FEIPASFQEASGLPHTAKGSLDRRAVAEQFG 531
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
38-462 |
5.59e-54 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 189.49 E-value: 5.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 38 GERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG---------LTDPAHA----VGDHPV-------LA 97
Cdd:PRK08974 74 GDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNdsgakaiviVSNFAHTlekvVFKTPVkhviltrMG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 98 D-------------------LMPMLDLDDPIAPAAPITGSPR-----P---GDD-AVLVFSSGTTGLPKAVRHTHASLDA 149
Cdd:PRK08974 154 DqlstakgtlvnfvvkyikrLVPKYHLPDAISFRSALHKGRRmqyvkPelvPEDlAFLQYTGGTTGVAKGAMLTHRNMLA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 150 AVRQ--WRDALRLTERDRIQV-ATPPSHILGL-LNILTALRVGTSVRL--HPRfDVDRILRHIENDRITIEMAVAPIAQA 223
Cdd:PRK08974 234 NLEQakAAYGPLLHPGKELVVtALPLYHIFALtVNCLLFIELGGQNLLitNPR-DIPGFVKELKKYPFTAITGVNTLFNA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 224 LASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIACNPPEQSRLD-SVGRPVAGVDVRIV 301
Cdd:PRK08974 313 LLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECsPLVSVNPYDLDYYSgSIGLPVPSTEIKLV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 302 SlDTGEPVGPGDVGEIQARSASLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVE 380
Cdd:PRK08974 393 D-DDGNEVPPGEPGELWVKGPQVMLGYWQrPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 381 TVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTgvAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:PRK08974 472 DVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLT--EEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
..
gi 576413765 461 KE 462
Cdd:PRK08974 550 RD 551
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
6-460 |
1.24e-53 |
|
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: 187.02 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd12117 15 AVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDHP---VLADLMPMLDLDDPI--APAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQwRDALRL 160
Cdd:cd12117 95 AKVLLTDRSlagRAGGLEVAVVIDEALdaGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 161 TERDRIQVATPPSHILGLLNILTALRVGTSVRLHPR---FDVDRILRHIENDRITIEMAVAPIAQALASHpRLESydLSS 237
Cdd:cd12117 174 GPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLADE-DPEC--FAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 238 LRFIMWGATPVTVSIAETVTRRT-GVRWVPAYGTTELPVIACN---PPEQSRLDSV--GRPVAGVDVRIVSlDTGEPVGP 311
Cdd:cd12117 251 LRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTFTTShvvTELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 312 GDVGEIQARSASLMAGYLP-AAANAEV-----WRDG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVL 383
Cdd:cd12117 330 GVPGELYVGGDGLALGYLNrPALTAERfvadpFGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAAL 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576413765 384 HSHPAVKDCAVFGVPD-GVNGEAVVAAVATHAPGntgvAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd12117 410 RAHPGVREAVVVVREDaGGDKRLVAYVVAEGALD----AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
18-462 |
1.29e-53 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 188.42 E-value: 1.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 18 ALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGL-------------- 83
Cdd:PRK06087 54 ALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKcqakmffaptlfkq 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 84 TDPAHAVgdHPVLADLmPMLD---LDDPIAPAA-------------PITGSPR-PGDD-AVLVFSSGTTGLPKAVRHTHA 145
Cdd:PRK06087 134 TRPVDLI--LPLQNQL-PQLQqivGVDKLAPATsslslsqiiadyePLTTAITtHGDElAAVLFTSGTEGLPKGVMLTHN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 146 SLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTA-LRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQAL 224
Cdd:PRK06087 211 NILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTApFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 225 ASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRtGVRWVPAYGTTE-LPVIACNP--PEQSRLDSVGRPVAGVDVRIV 301
Cdd:PRK06087 291 LNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTEsSPHAVVNLddPLSRFMHTDGYAAAGVEIKVV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 302 SlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIkVRGFQ-VAPAE 378
Cdd:PRK06087 370 D-EARKTLPPGCEGEEASRGPNVFMGYLdePELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGEnISSRE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 379 VETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQ-LAPYKRLSRVVFVPEIPRLPSGKVLR 457
Cdd:PRK06087 448 VEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQK 527
|
....*
gi 576413765 458 RVLKE 462
Cdd:PRK06087 528 FLLRK 532
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
6-460 |
2.13e-53 |
|
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: 185.96 E-value: 2.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--- 82
Cdd:cd12116 5 AVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEdae 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ----LTDPAhavGDHPVLADLM-PMLDLDDPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDA 157
Cdd:cd12116 85 palvLTDDA---LPDRLPAGLPvLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 158 LRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPR---FDVDRILRHIENDRITIEMAVAPIAQALASHprlESYD 234
Cdd:cd12116 162 LGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDA---GWQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 235 LSSLRfIMWGATPVTVSIAETVTRRTGVRWvPAYGTTELPVIACNPPEQSRLDSV--GRPVAGVDVRIVSlDTGEPVGPG 312
Cdd:cd12116 239 RAGLT-ALCGGEALPPDLAARLLSRVGSLW-NLYGPTETTIWSTAARVTAAAGPIpiGRPLANTQVYVLD-AALRPVPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 313 DVGEIQARSASLMAGYL--PAAAnAEVWRDG--------WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETV 382
Cdd:cd12116 316 VPGELYIGGDGVAQGYLgrPALT-AERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576413765 383 LHSHPAVKDCAVFGVPDGvnGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd12116 395 LAAHPGVAQAAVVVREDG--GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
34-462 |
3.56e-53 |
|
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: 185.66 E-value: 3.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 34 GVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEvdhALGLTDPAHAVGdhPVLADLMPMLdLDDPIAPAA 113
Cdd:cd05929 38 GVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE---ACAIIEIKAAAL--VCGLFTGGGA-LDGLEDYEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 114 PITGSPRPGDDAV-----LVFSSGTTGLPKAVR--HTHASLDAA-VRQWRDALRLTERDRIQVATPPSHILGLLNILTAL 185
Cdd:cd05929 112 AEGGSPETPIEDEaagwkMLYSGGTTGRPKGIKrgLPGGPPDNDtLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 186 RVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLE--SYDLSSLRFIMWGATPVTVSIAETVTRRTGVR 263
Cdd:cd05929 192 FMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVrnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 264 WVPAYGTTELPVIACNPPEQ--SRLDSVGRPVAGvDVRIVSLDtGEPVGPGDVGEIQ-ARSASLMAGYLPAAANAEVWRD 340
Cdd:cd05929 272 IWEYYGGTEGQGLTIINGEEwlTHPGSVGRAVLG-KVHILDED-GNEVPPGEIGEVYfANGPGFEYTNDPEKTAAARNEG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 341 GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATH--APGNT 418
Cdd:cd05929 350 GWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPApgADAGT 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 576413765 419 GVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
123-462 |
6.06e-53 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 186.72 E-value: 6.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAVRHTHASLdaaVRQWRDALRLTERDRI-QVAT----PPSHILGLLNILTA-LRVGTSVRLHPR 196
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNL---VANLCSSLFSVGPEMIgQVVTlgliPFFHIYGITGICCAtLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 197 FDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRF--IMWGATPVTVSIAETVTRR-TGVRWVPAYGTTEL 273
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEH 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 274 PVIACN--PPEQ----SRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRT 345
Cdd:PLN02330 342 SCITLThgDPEKghgiAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYnnKEETDRTIDEDGWLHT 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 346 GDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELT 425
Cdd:PLN02330 422 GDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVIN-PKAKESEEDIL 500
|
330 340 350
....*....|....*....|....*....|....*..
gi 576413765 426 ARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PLN02330 501 NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
12-396 |
1.20e-52 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 186.84 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISP-------AW------------ 72
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPtssaeevAYilndsgakvlfv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 73 -KRDEVDHALGLT------------DPAHAVGDHPV--LADLMPM-LDLDDPIAPAAPITgSPRPGDDAVLVFSSGTTGL 136
Cdd:COG1022 119 eDQEQLDKLLEVRdelpslrhivvlDPRGLRDDPRLlsLDELLALgREVADPAELEARRA-AVKPDDLATIIYTSGTTGR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 137 PKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVrLHPRfDVDRILRHI---------- 206
Cdd:COG1022 198 PKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALAAGATV-AFAE-SPDTLAEDLrevkptfmla 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 207 -----EN--DRITIEMAVAP----------IAQALASHPRLES--------------YDL-----------SSLRFIMWG 244
Cdd:COG1022 276 vprvwEKvyAGIQAKAEEAGglkrklfrwaLAVGRRYARARLAgkspslllrlkhalADKlvfsklrealgGRLRFAVSG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 245 ATPVTVSIAETVtRRTGVRWVPAYGTTEL-PVIACNPPEQSRLDSVGRPVAGVDVRIvsldtgepvgpGDVGEIQARSAS 323
Cdd:COG1022 356 GAALGPELARFF-RALGIPVLEGYGLTETsPVITVNRPGDNRIGTVGPPLPGVEVKI-----------AEDGEILVRGPN 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 324 LMAGYL--PAAaNAEV-WRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVR-GFQVAPAEVETVLHSHPAVKDCAVFG 396
Cdd:COG1022 424 VMKGYYknPEA-TAEAfDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
4-462 |
4.74e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 183.18 E-value: 4.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 4 PAALVIED-RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFV----AALQA-------IWRLGA-------- 63
Cdd:PRK08276 1 PAVIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFevywAARRSglyytpiNWHLTAaeiayivd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 64 ---AAVLISPAWKRDEVDHALGLTdPAHAVGDHPVLADLMPMLDLDDPIA--PAAPITgSPRPGDDavLVFSSGTTGLPK 138
Cdd:PRK08276 81 dsgAKVLIVSAALADTAAELAAEL-PAGVPLLLVVAGPVPGFRSYEEALAaqPDTPIA-DETAGAD--MLYSSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 139 AVRH--THASLDAAVRQwrdALRLTERDRIQVA-------TPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIEND 209
Cdd:PRK08276 157 GIKRplPGLDPDEAPGM---MLALLGFGMYGGPdsvylspAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEALALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 210 RITIEMAVaPIA----QALASHPRlESYDLSSLRFIMWGATPVTVSiaetVTRRTGVRWVPA----YGTTELPVIACNPP 281
Cdd:PRK08276 234 RVTHSQLV-PTMfvrmLKLPEEVR-ARYDVSSLRVAIHAAAPCPVE----VKRAMIDWWGPIiheyYASSEGGGVTVITS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 282 EQ--SRLDSVGRPVAGVdVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWL 357
Cdd:PRK08276 308 EDwlAHPGSVGKAVLGE-VRILD-EDGNELPPGEIGTVYFEMDGYPFEYHndPEKTAAARNPHGWVTVGDVGYLDEDGYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 358 RITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTG--VAAELTARVAAQLAPY 435
Cdd:PRK08276 386 YLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGdaLAAELIAWLRGRLAHY 465
|
490 500
....*....|....*....|....*..
gi 576413765 436 KRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK08276 466 KCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
10-463 |
1.60e-51 |
|
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: 182.82 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLHHRGViAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG------- 82
Cdd:cd05931 21 REETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAiladagp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ---LTDPAHAVGDHPVLA-----DLMPMLDLD-DPIAPAAPITG-SPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVR 152
Cdd:cd05931 100 rvvLTTAAALAAVRAFAAsrpaaGTPRLLVVDlLPDTSAADWPPpSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 153 QWRDALRLTERDRIQVATPPSHILGL-LNILTALRVG-TSVRLHPRFDVDRILRHIEN-DRITIEMAVAP-----IAQAL 224
Cdd:cd05931 180 QIRRAYGLDPGDVVVSWLPLYHDMGLiGGLLTPLYSGgPSVLMSPAAFLRRPLRWLRLiSRYRATISAAPnfaydLCVRR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 225 ASHPRLESYDLSSLRFIMWGATPVTvsiAETVTR------RTGVRW---VPAYG-------------TTELPVI------ 276
Cdd:cd05931 260 VRDEDLEGLDLSSWRVALNGAEPVR---PATLRRfaeafaPFGFRPeafRPSYGlaeatlfvsggppGTGPVVLrvdrda 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 277 --------ACNPPEQSRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWR-------D 340
Cdd:cd05931 337 lagravavAADDPAARELVSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWgRPEATAETFGalaatdeG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 341 GWYRTGDVGWLDGnGWLRITDRLKEMIKVRGFQVAPAEVE-TVLHSHPAVK--DCAVFGVPDGVNGEAVVAAVATHAPGN 417
Cdd:cd05931 417 GWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRpgCVAAFSVPDDGEERLVVVAEVERGADP 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 576413765 418 T---GVAAELTARVAAQ--LAPykrlSRVVFVP--EIPRLPSGKVLRRVLKEL 463
Cdd:cd05931 496 AdlaAIAAAIRAAVAREhgVAP----ADVVLVRpgSIPRTSSGKIQRRACRAA 544
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
109-463 |
1.82e-51 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 187.82 E-value: 1.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 109 IAPA----APITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLL-NILT 183
Cdd:PRK08633 765 LLPArllkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTvTLWL 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 184 ALRVGTSVRLHPR-FDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGV 262
Cdd:PRK08633 845 PLLEGIKVVYHPDpTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGI 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 263 RWVPAYGTTEL-PVIACNPP--------EQ--SRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYLPA 331
Cdd:PRK08633 925 RILEGYGATETsPVASVNLPdvlaadfkRQtgSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 332 AA-NAEVWRD----GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLH--SHPAVKDCAVFGVPDGVNGE 404
Cdd:PRK08633 1005 PEkTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkaLGGEEVVFAVTAVPDEKKGE 1084
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 405 AVVAAvatHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK08633 1085 KLVVL---HTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
10-462 |
1.83e-51 |
|
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: 182.31 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVlisPA----WKRDEV-------- 77
Cdd:cd05970 44 EERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI---PAthqlTAKDIVyriesadi 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 78 --------DHALGLTDPAHA-VGDHPVLADLMPML-----DLDDPIAPAAPITgsPRP-------GDDAVLV-FSSGTTG 135
Cdd:cd05970 121 kmivaiaeDNIPEEIEKAAPeCPSKPKLVWVGDPVpegwiDFRKLIKNASPDF--ERPtansypcGEDILLVyFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 136 LPKAVRHTH---------ASLDAAVRQwrDALRLTERDRIQVATPPSHILGllniltALRVGTSVRL--HPRFDVDRILR 204
Cdd:cd05970 199 MPKMVEHDFtyplghivtAKYWQNVRE--GGLHLTVADTGWGKAVWGKIYG------QWIAGAAVFVydYDKFDPKALLE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 205 HIENDRITIEMAVAPIAQALAsHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPV-IACNPPEQ 283
Cdd:cd05970 271 KLSKYGVTTFCAPPTIYRFLI-REDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLtIATFPWME 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 284 SRLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARSAS-----LMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWL 357
Cdd:cd05970 350 PKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKdAEKTAEVWHDGYYHTGDAAWMDEDGYL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 358 RITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAA---VATHAPGNTgVAAELTARVAAQLAP 434
Cdd:cd05970 429 WFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATivlAKGYEPSEE-LKKELQDHVKKVTAP 507
|
490 500
....*....|....*....|....*...
gi 576413765 435 YKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05970 508 YKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
17-461 |
6.45e-51 |
|
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: 178.85 E-value: 6.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 17 HALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDpAHAVGDHPVL 96
Cdd:cd05969 4 AQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSE-AKVLITTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 97 ADLMpmlDLDDPiapaapitgsprpgddAVLVFSSGTTGLPKAVRHTHaslDAAVRQW---RDALRLTERDRIQVATPPS 173
Cdd:cd05969 83 YERT---DPEDP----------------TLLHYTSGTTGTPKGVLHVH---DAMIFYYftgKYVLDLHPDDIYWCTADPG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 174 HILGLL-NILTALRVG-TSVRLHPRFDVDRILRHIENDRITIeMAVAPIAQAL---ASHPRLESYDLSSLRFIMWGATPV 248
Cdd:cd05969 141 WVTGTVyGIWAPWLNGvTNVVYEGRFDAESWYGIIERVKVTV-WYTAPTAIRMlmkEGDELARKYDLSSLRFIHSVGEPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 249 TVSIAETVTRRTGVRWVPAYGTTELPVIA-CNPPEQS-RLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARSA--SL 324
Cdd:cd05969 220 NPEAIRWGMEVFGVPIHDTWWQTETGSIMiANYPCMPiKPGSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPGwpSM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 325 MAGYLPAAAN-AEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNG 403
Cdd:cd05969 299 FRGIWNDEERyKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRG 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 404 EAVV---AAVATHAPGNT-GVAAELTARV--AAQLAPykrlSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05969 379 EIIKafiSLKEGFEPSDElKEEIINFVRQklGAHVAP----REIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
3-463 |
1.75e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 179.94 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGA------------------- 63
Cdd:PRK06164 25 DAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAtviavntryrshevahilg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 64 ---AAVLI-SPAWKR-------DEVDHALGLTDPAHAVGDH-------PVLADLMPMLDLDDPIAPAAPITGSPRPGDDA 125
Cdd:PRK06164 105 rgrARWLVvWPGFKGidfaailAAVPPDALPPLRAIAVVDDaadatpaPAPGARVQLFALPDPAPPAAAGERAADPDAGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 126 VLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRH 205
Cdd:PRK06164 185 LLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 206 IENDRITIEMAVAPI-AQALASHPrlESYDLSSLRFIMWGA-TPVTVSIAETVTRRtGVRWVPAYGTTEL-PVIACNP-- 280
Cdd:PRK06164 265 LRRHRVTHTFGNDEMlRRILDTAG--ERADFPSARLFGFASfAPALGELAALARAR-GVPLTGLYGSSEVqALVALQPat 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 281 -PEQSRLDSVGRPV-AGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGW 356
Cdd:PRK06164 342 dPVSVRIEGGGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLdnPDATARALTDDGYFRTGDLGYTRGDGQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 357 LRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThaPGNTGVAAELTARVAAQLAPYK 436
Cdd:PRK06164 422 FVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPT--DGASPDEAGLMAACREALAGFK 499
|
490 500 510
....*....|....*....|....*....|
gi 576413765 437 RLSRVVFVPEIPRLPSG---KVLRRVLKEL 463
Cdd:PRK06164 500 VPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
6-460 |
2.49e-50 |
|
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: 177.44 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPawkrdevdhalgltd 85
Cdd:cd05945 9 AVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 pahavgDHPV--LADLMpmldldDPIAPAAPITGsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTER 163
Cdd:cd05945 74 ------SSPAerIREIL------DAAKPALLIAD---GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 164 DRIQVATPPSHILGLLNILTALRVGTSVRLHPR---FDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRF 240
Cdd:cd05945 139 DVFLNQAPFSFDLSVMDLYPALASGATLVPVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 241 IMWGATPVTVSIAETVTRRT-GVRWVPAYGTTELpVIAC-----NPPEQSRLDSV--GRPVAGVDVRIVSlDTGEPVGPG 312
Cdd:cd05945 219 FLFCGEVLPHKTARALQQRFpDARIYNTYGPTEA-TVAVtyievTPEVLDGYDRLpiGYAKPGAKLVILD-EDGRPVPPG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 313 DVGEIQARSASLMAGYL-PAAANAEVWRD----GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHP 387
Cdd:cd05945 297 EKGELVISGPSVSKGYLnNPEKTAAAFFPdegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVP 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576413765 388 AVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd05945 377 GVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
129-457 |
4.62e-50 |
|
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: 172.98 E-value: 4.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 129 FSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIEN 208
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 209 DRITIEMAVAPIAQALASHPRLESydlsSLRFIMWGATPVTVSIAETVTRRT-GVRWVPAYGTTELPVIACNPPEQSR-L 286
Cdd:cd17633 87 YNATVIYLVPTMLQALARTLEPES----KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFNQESRpP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 287 DSVGRPVAGVDVRIVSLDTGEpvgpgdVGEIQARSASLMAGYLPAAANAEvwrDGWYRTGDVGWLDGNGWLRITDRLKEM 366
Cdd:cd17633 163 NSVGRPFPNVEIEIRNADGGE------IGKIFVKSEMVFSGYVRGGFSNP---DGWMSVGDIGYVDEEGYLYLVGRESDM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 367 IKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAthapGNTGVAAELTARVAAQLAPYKRLSRVVFVPE 446
Cdd:cd17633 234 IIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS----GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDS 309
|
330
....*....|.
gi 576413765 447 IPRLPSGKVLR 457
Cdd:cd17633 310 LPYTSSGKIAR 320
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
6-461 |
1.05e-48 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 174.49 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRR--VSRHALDALSDGLGAT---LHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHA 80
Cdd:PRK08008 25 ALIFESSGgvVRRYSYLELNEEINRTanlFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 81 LGLTDPAHAV---------------GDHPV---------LADLMPMLDLDDPIA--PAAPITGSPRPGDD-AVLVFSSGT 133
Cdd:PRK08008 105 LQNSQASLLVtsaqfypmyrqiqqeDATPLrhicltrvaLPADDGVSSFTQLKAqqPATLCYAPPLSTDDtAEILFTSGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 134 TGLPKAVRHTHASLDAA--VRQWRDALRltERDRIQVATPPSHILGLLN-ILTALRVGTSVRLHPRFDVDRILRHIENDR 210
Cdd:PRK08008 185 TSRPKGVVITHYNLRFAgyYSAWQCALR--DDDVYLTVMPAFHIDCQCTaAMAAFSAGATFVLLEKYSARAFWGQVCKYR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 211 ITIEMAVAPIAQALASHPRLESYDLSSLRFIMWgATPVTVSIAETVTRRTGVRWVPAYGTTELPV--IACNPPEQSRLDS 288
Cdd:PRK08008 263 ATITECIPMMIRTLMVQPPSANDRQHCLREVMF-YLNLSDQEKDAFEERFGVRLLTSYGMTETIVgiIGDRPGDKRRWPS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 289 VGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSA---SLMAGY-LPAAANAEVWR-DGWYRTGDVGWLDGNGWLRITDRL 363
Cdd:PRK08008 342 IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGVpgkTIFKEYyLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 364 KEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVF 443
Cdd:PRK08008 421 CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL-NEGETLSEEEFFAFCEQNMAKFKVPSYLEI 499
|
490
....*....|....*...
gi 576413765 444 VPEIPRLPSGKVLRRVLK 461
Cdd:PRK08008 500 RKDLPRNCSGKIIKKNLK 517
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
123-463 |
1.21e-48 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 175.40 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALR---------LTERDRIQVATPP-SHILGL-LNILTALRVGTSV 191
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIAPLPlYHIYAFtANCMCMMVSGNHN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 192 RL--HPRfDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYG 269
Cdd:PRK12492 288 VLitNPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 270 TTEL-PVIACNP-PEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRT 345
Cdd:PRK12492 367 LTETsPVASTNPyGELARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWqqPEATAEALDAEGWFKT 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 346 GDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTgvAAELT 425
Cdd:PRK12492 446 GDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLS--VEELK 523
|
330 340 350
....*....|....*....|....*....|....*...
gi 576413765 426 ARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK12492 524 AYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
23-461 |
1.14e-47 |
|
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: 169.92 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 23 SDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPvladlmpm 102
Cdd:cd05971 16 SNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDGS-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 103 ldlDDPiapaapitgsprpgddAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPP--SHILGLLN 180
Cdd:cd05971 88 ---DDP----------------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPAdwAWIGGLLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 181 IL-TALRVGTSVRLH--PRFDVDRILRHIENDRITieMAVAPiAQAL----ASHPRLESYDLSsLRFIMWGATPVTVSIA 253
Cdd:cd05971 149 VLlPSLYFGVPVLAHrmTKFDPKAALDLMSRYGVT--TAFLP-PTALkmmrQQGEQLKHAQVK-LRAIATGGESLGEELL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 254 ETVTRRTGVRWVPAYGTTELPVIACNPPEQSRLD--SVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQAR--SASLMAGYL 329
Cdd:cd05971 225 GWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKpgSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYW 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 330 --PAAANAEVWRDgWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVV 407
Cdd:cd05971 304 nnPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 408 AAVAThAPGNTG---VAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05971 383 AFVVL-NPGETPsdaLAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
118-462 |
2.39e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 168.79 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 118 SPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDAL--RLTERDRIQVAT-PPSHILGL-LNILTALRVGTSVRL 193
Cdd:PRK05677 203 NPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMgsNLNEGCEILIAPlPLYHIYAFtFHCMAMMLIGNHNIL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 194 --HPRfDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTT 271
Cdd:PRK05677 283 isNPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 272 EL-PVIACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDV 348
Cdd:PRK05677 362 ETsPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWqrPEATDEILDSDGWLKTGDI 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 349 GWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARV 428
Cdd:PRK05677 441 ALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVK-PGETLTKEQVMEHM 519
|
330 340 350
....*....|....*....|....*....|....
gi 576413765 429 AAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK05677 520 RANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
6-462 |
3.02e-46 |
|
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: 172.35 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:COG1020 494 AVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDHPVLADL----MPMLDLDDPI---APAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDAL 158
Cdd:COG1020 574 ARLVLTQSALAARLpelgVPVLALDALAlaaEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 159 RLTERDRIQVATPPSHILGLLNILTALRVGTSVRL---HPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLesyDL 235
Cdd:COG1020 654 GLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLappEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE---AL 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVTRRT-GVRWVPAYGTTELPVIAC-----NPPEQSRLDSVGRPVAGVDVRIVSlDTGEPV 309
Cdd:COG1020 731 PSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTyyevtPPDADGGSVPIGRPIANTRVYVLD-AHLQPV 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 310 GPGDVGEIQARSASLMAGYL-PAAANAE------VWRDG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVE 380
Cdd:COG1020 810 PVGVPGELYIGGAGLARGYLnRPELTAErfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIE 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 381 TVLHSHPAVKDCAVFGVPDGvNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:COG1020 890 AALLQHPGVREAVVVAREDA-PGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
..
gi 576413765 461 KE 462
Cdd:COG1020 969 PA 970
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
19-461 |
6.96e-46 |
|
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: 165.00 E-value: 6.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 19 LDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGltdpahAVGDHPVLAD 98
Cdd:cd05973 6 LRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLR------TSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 99 LMPMLDLDDpiapaapitgsprpgDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL 178
Cdd:cd05973 80 AANRHKLDS---------------DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 179 LNILTA-LRVGT-SVRLHPRFDVDRILRHIENDRITiEMAVAPIA--QALASHPRLESYDLSSLRFIMWGATPVTVSIAE 254
Cdd:cd05973 145 YYAITGpLALGHpTILLEGGFSVESTWRVIERLGVT-NLAGSPTAyrLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 255 TVTRRTGVRWVPAYGTTELPVIACN---PPEQSRLDSVGRPVAGVDVRIVSLDTGEPvGPGDVG--EIQARSASLM--AG 327
Cdd:cd05973 224 WFDAALGVPIHDHYGQTELGMVLANhhaLEHPVHAGSAGRAMPGWRVAVLDDDGDEL-GPGEPGrlAIDIANSPLMwfRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 328 YLPAAANAEVwrDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVV 407
Cdd:cd05973 303 YQLPDTPAID--GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVK 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 408 AAVATHA--PGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05973 381 AFVVLRGghEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
30-457 |
1.28e-45 |
|
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: 164.92 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 30 LHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHA-VGDhpvladlmpmldlddp 108
Cdd:cd05914 24 LKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIfVSD---------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 109 iapaapitgsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLL-NILTALRV 187
Cdd:cd05914 88 ------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTfTLLLPLLN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 188 GTSV-----------------RLHPRFDVDRILRhIENDRITIEM---AVAPIAQALASHPR------------LESYDl 235
Cdd:cd05914 156 GAHVvfldkipsakiialafaQVTPTLGVPVPLV-IEKIFKMDIIpklTLKKFKFKLAKKINnrkirklafkkvHEAFG- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVtRRTGVRWVPAYGTTEL-PVIACNPPEQSRLDSVGRPVAGVDVRIVSLD--TGEpvgpg 312
Cdd:cd05914 234 GNIKEFVIGGAKINPDVEEFL-RTIGFPYTIGYGMTETaPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpaTGE----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 313 dvGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKV-RGFQVAPAEVETVLHSHPAV 389
Cdd:cd05914 308 --GEIIVRGPNVMKGYYknPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 390 ---------KDCAVFGVPD----GVNGEAVVAAVAThapgntgVAAELTARVAAQLAPYKRLSRVVFVPE-IPRLPSGKV 455
Cdd:cd05914 386 leslvvvqeKKLVALAYIDpdflDVKALKQRNIIDA-------IKWEVRDKVNQKVPNYKKISKVKIVKEeFEKTPKGKI 458
|
..
gi 576413765 456 LR 457
Cdd:cd05914 459 KR 460
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
38-462 |
7.74e-45 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 164.66 E-value: 7.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 38 GERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHAL---GL----------TDPAHAVGDHPV-------LA 97
Cdd:PRK08751 76 GDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLidsGAsvlvvidnfgTTVQQVIADTPVkqvittgLG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 98 DLMP---------MLDLDDPIAPAAPITGSPR-------------------PGDDAVLVFSSGTTGLPKAVRHTHASLDA 149
Cdd:PRK08751 156 DMLGfpkaalvnfVVKYVKKLVPEYRINGAIRfrealalgrkhsmptlqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 150 AVRQWRDALRLTER-----DRIQVATPPSHILGLL-NILTALRVGTSVRL--HPRfDVDRILRHIENDRITIEMAVAPIA 221
Cdd:PRK08751 236 NMQQAHQWLAGTGKleegcEVVITALPLYHIFALTaNGLVFMKIGGCNHLisNPR-DMPGFVKELKKTRFTAFTGVNTLF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 222 QALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIAC-NPPEQSRLD-SVGRPVAGVDVR 299
Cdd:PRK08751 315 NGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACiNPLTLKEYNgSIGLPIPSTDAC 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 300 IVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPA 377
Cdd:PRK08751 395 IKD-DAGTVLAIGEIGELCIKGPQVMKGYWkrPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPN 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 378 EVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTgvAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLR 457
Cdd:PRK08751 474 EIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALT--AEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILR 551
|
....*
gi 576413765 458 RVLKE 462
Cdd:PRK08751 552 RELRD 556
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
125-463 |
1.44e-44 |
|
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: 158.65 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 125 AVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDvDRILR 204
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQ-ALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 205 HIENDRITIEMAVAPIAQALASHPRLESydLSSLRFIMWGATPVTVSIAETVTRRtGVRWVPAYGTTEL-PVIACNPPEQ 283
Cdd:cd17630 82 LAPPGVTHVSLVPTQLQRLLDSGQGPAA--LKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETaSQVATKRPDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 284 SRLDSVGRPVAGVDVRIVsldtgepvgpgDVGEIQARSASLMAGYLPAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRL 363
Cdd:cd17630 159 FGRGGVGVLLPGRELRIV-----------EDGEIWVGGASLAMGYLRGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 364 KEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTgvaAELTARVAAQLAPYKRLSRVVF 443
Cdd:cd17630 228 DNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP---AELRAWLKDKLARFKLPKRIYP 304
|
330 340
....*....|....*....|
gi 576413765 444 VPEIPRLPSGKVLRRVLKEL 463
Cdd:cd17630 305 VPELPRTGGGKVDRRALRAW 324
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
52-463 |
6.81e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 163.20 E-value: 6.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 52 VAALQAIWRLGAAAVLisPAWKRdevdHALGLTDPAHAVGDHPVLADLMPMLDlDDPIAPAAPitgspRPGDDAVLVFSS 131
Cdd:PRK07529 155 LPELRTVVEVDLARYL--PGPKR----LAVPLIRRKAHARILDFDAELARQPG-DRLFSGRPI-----GPDDVAAYFHTG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 132 GTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLL-NILTALRVGTSVRL-------HPRFdVDRIL 203
Cdd:PRK07529 223 GTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLvTGLAPLARGAHVVLatpqgyrGPGV-IANFW 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 204 RHIENDRITIEMAVAPIAQALASHPRlESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELP-VIACNPPE 282
Cdd:PRK07529 302 KIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATcVSSVNPPD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 283 -QSRLDSVGRPVAGVDVRIVSLDTG----EPVGPGDVGEIQARSASLMAGYLPAAANAEVW-RDGWYRTGDVGWLDGNGW 356
Cdd:PRK07529 381 gERRIGSVGLRLPYQRVRVVILDDAgrylRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWlEDGWLNTGDLGRIDADGY 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 357 LRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYK 436
Cdd:PRK07529 461 FWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGE-LPVAYVQLKPGASATEAELLAFARDHIAERA 539
|
410 420
....*....|....*....|....*...
gi 576413765 437 RLSR-VVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK07529 540 AVPKhVRILDALPKTAVGKIFKPALRRD 567
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
13-462 |
7.57e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 161.01 E-value: 7.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 13 RVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLG----------------------AAAVLISP 70
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGlyytcvnshltpaeaayivddsGARALITS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 71 AWKRDEVDHALGLTdPAhavGDHPVLAD----LMPMLDLDDPIA--PAAPITGSPRPGDdavLVFSSGTTGLPKAVRHTH 144
Cdd:PRK13391 104 AAKLDVARALLKQC-PG---VRHRLVLDgdgeLEGFVGYAEAVAglPATPIADESLGTD---MLYSSGTTGRPKGIKRPL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 145 ASLDAAvrqwrDALRLTE---------RDRIQVATPP-SHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIE 214
Cdd:PRK13391 177 PEQPPD-----TPLPLTAflqrlwgfrSDMVYLSPAPlYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 215 MAVAPIAQALASHPR--LESYDLSSLRFIMWGATPVTVSIAETVTRRtgvrWVPA----YGTTE-LPVIACNPPEQ-SRL 286
Cdd:PRK13391 252 QLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDW----WGPIiheyYAATEgLGFTACDSEEWlAHP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 287 DSVGRPVAGvDVRIVSlDTGEPVGPGDVGEIQARSASlMAGYLPAAANAEVWRD---GWYRTGDVGWLDGNGWLRITDRL 363
Cdd:PRK13391 328 GTVGRAMFG-DLHILD-DDGAELPPGEPGTIWFEGGR-PFEYLNDPAKTAEARHpdgTWSTVGDIGYVDEDGYLYLTDRA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 364 KEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTG--VAAELTARVAAQLAPYKRLSRV 441
Cdd:PRK13391 405 AFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpaLAAELIAFCRQRLSRQKCPRSI 484
|
490 500
....*....|....*....|.
gi 576413765 442 VFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK13391 485 DFEDELPRLPTGKLYKRLLRD 505
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
6-460 |
1.89e-43 |
|
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: 159.36 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--- 82
Cdd:cd12114 5 AVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILAdag 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ----LTDPAHAVGDHPVLADLMPMLDLDDPIAPAAPITgsPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDAL 158
Cdd:cd12114 85 arlvLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVD--VAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 159 RLTERDRIQVATPPSHILGLLNILTALRVGTSVRL---HPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDL 235
Cdd:cd12114 163 AVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpdeARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVTRRT-GVRWVPAYGTTELPV------IACNPPEQSrldSV--GRPVAGVDVRIVSlDTG 306
Cdd:cd12114 243 PSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIwsiyhpIDEVPPDWR---SIpyGRPLANQRYRVLD-PRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 307 EPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDG----WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVE 380
Cdd:cd12114 319 RDCPDWVPGELWIGGRGVALGYLgdPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 381 TVLHSHPAVKDCAVFGVPDGvNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd12114 399 AALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
6-461 |
1.32e-42 |
|
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: 156.37 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALglTD 85
Cdd:cd17649 5 ALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML--ED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVgdhpVLADlmpmldlddpiapaapitgspRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd17649 83 SGAGL----LLTH---------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGLLNILTALRVGTSVRLHPR---FDVDRILRHIENDRITI-EMAVAPIAQALASHPRLESYDLSSLRFI 241
Cdd:cd17649 138 ELQFASFNFDGAHEQLLPPLICGACVVLRPDelwASADELAEMVRELGVTVlDLPPAYLQQLAEEADRTGDGRPPSLRLY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 242 MWGATPVTVSIAeTVTRRTGVRWVPAYGTTELPV--IACNPPEQSRLDS----VGRPVAGVDVRIvsLDT-GEPVGPGDV 314
Cdd:cd17649 218 IFGGEALSPELL-RRWLKAPVRLFNAYGPTEATVtpLVWKCEAGAARAGasmpIGRPLGGRSAYI--LDAdLNPVPVGVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 315 GEIQARSASLMAGYL-----------PAAANAEVWRdgWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVL 383
Cdd:cd17649 295 GELYIGGEGLARGYLgrpeltaerfvPDPFGAPGSR--LYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAAL 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576413765 384 HSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd17649 373 LEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
3-460 |
2.23e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 157.47 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK13383 50 GRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDPAHAVGDHP----VLADLMPMLDLDDPIAPAAPITGSPR---PGddAVLVFSSGTTGLPKAVRHThASLDAAVRQW- 154
Cdd:PRK13383 130 AHHISTVVADNEfaerIAGADDAVAVIDPATAGAEESGGRPAvaaPG--RIVLLTSGTTGKPKGVPRA-PQLRSAVGVWv 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 155 --RDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITiEMAVAPI--AQALASHPRL 230
Cdd:PRK13383 207 tiLDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRAD-AFTAVPVvlARILELPPRV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 231 ESYD-LSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQSR--LDSVGRPVAGVDVRIVSLDtGE 307
Cdd:PRK13383 286 RARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRdaPETVGKPVAGCPVRILDRN-NR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 308 PVGPGDVGEIQARSASLMAGYLPAAANAEVwrDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHP 387
Cdd:PRK13383 365 PVGPRVTGRIFVGGELAGTRYTDGGGKAVV--DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHP 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576413765 388 AVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:PRK13383 443 AVADNAVIGVPDERFGHRLAAFVVLH-PGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
4-461 |
2.31e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 157.09 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 4 PAALVIED-RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK13390 14 PAVIVAETgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDP-------------AHAVGDHPVLADLMPMLD----LDDPIAPAAPITGSPRPGddAVLVFSSGTTGLPKAV----- 140
Cdd:PRK13390 94 DSGArvlvasaaldglaAKVGADLPLRLSFGGEIDgfgsFEAALAGAGPRLTEQPCG--AVMLYSSGTTGFPKGIqpdlp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 141 -RHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITI-EMAVA 218
Cdd:PRK13390 172 gRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATLGHVERYRITVtQMVPT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 219 PIAQALASHPRLES-YDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE---LPVIAcNPPEQSRLDSVGRPVA 294
Cdd:PRK13390 252 MFVRLLKLDADVRTrYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgMTFID-SPDWLAHPGSVGRSVL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 295 GvDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYLPA----AANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVR 370
Cdd:PRK13390 331 G-DLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDpektAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 371 GFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHA--PGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIP 448
Cdd:PRK13390 409 GVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEgiRGSDELARELIDYTRSRIAHYKAPRSVEFVDELP 488
|
490
....*....|...
gi 576413765 449 RLPSGKVLRRVLK 461
Cdd:PRK13390 489 RTPTGKLVKGLLR 501
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
22-383 |
8.40e-42 |
|
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: 155.90 E-value: 8.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 22 LSDGLGAtlhhRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG--------------LTDPA 87
Cdd:cd05906 52 LAAGLRQ----LGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRklrhiwqllgspvvLTDAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 88 --------HAVGDHPVLADLMPMLDLDDPIAPAAPItgsPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALR 159
Cdd:cd05906 128 lvaefaglETLSGLPGIRVLSIEELLDTAADHDLPQ---SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 160 LTERDRIQVATPPSHILGLLNI-LTALRVGTS--------VRLHPRFDVDRILRHiendRITI----EMAVAPIAQALAS 226
Cdd:cd05906 205 LTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQqvhvpteeILADPLRWLDLIDRY----RVTItwapNFAFALLNDLLEE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 227 HPRlESYDLSSLRFIMWGATPVTVSIAETVTR---RTGVR---WVPAYGTTEL--PVIACNPPEQSRLD------SVGRP 292
Cdd:cd05906 281 IED-GTWDLSSLRYLVNAGEAVVAKTIRRLLRllePYGLPpdaIRPAFGMTETcsGVIYSRSFPTYDHSqalefvSLGRP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 293 VAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYLP-AAANAEVWR-DGWYRTGDVGWLDgNGWLRITDRLKEMIKVR 370
Cdd:cd05906 360 IPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNnPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVN 437
|
410
....*....|...
gi 576413765 371 GFQVAPAEVETVL 383
Cdd:cd05906 438 GVNYYSHEIEAAV 450
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
26-462 |
2.19e-41 |
|
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: 153.99 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPvladlmpmLDL 105
Cdd:cd12118 42 LASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE--------FEY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 106 DDPIAPAAPITGSPRPGDD---AVLVFSSGTTGLPKAVRHTH-----ASLDAAVRqWRdalrLTERDRIQVATPPSHILG 177
Cdd:cd12118 114 EDLLAEGDPDFEWIPPADEwdpIALNYTSGTTGRPKGVVYHHrgaylNALANILE-WE----MKQHPVYLWTLPMFHCNG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 178 LLNILT-ALRVGTSVRLhPRFDVDRILRHIENDRITiEMAVAPIA-QALASHPRLESYDLSSLRFIMWGATPVTVSIAET 255
Cdd:cd12118 189 WCFPWTvAAVGGTNVCL-RKVDAKAIYDLIEKHKVT-HFCGAPTVlNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 256 VTRrTGVRWVPAYGTTEL--PVIAC---------NPPEQSRLDS-VGRPVAGVD-VRIVSLDTGEPVgPGD---VGEIQA 319
Cdd:cd12118 267 MEE-LGFDVTHVYGLTETygPATVCawkpewdelPTEERARLKArQGVRYVGLEeVDVLDPETMKPV-PRDgktIGEIVF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 320 RSASLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVP 398
Cdd:cd12118 345 RGNIVMKGYLKnPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARP 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 399 DGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPeIPRLPSGKVLRRVLKE 462
Cdd:cd12118 425 DEKWGEVPCAFVELK-EGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
6-460 |
1.42e-40 |
|
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: 150.93 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd12115 17 ALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDhpvladlmpmldlddpiapaapitgsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd12115 97 ARLVLTD----------------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGLLNILTALRVGTSVRLhprfdVDRILRHIENDR---ITIEMAVAPIAQALASHPRLESydlsSLRFIM 242
Cdd:cd12115 149 VLASTSICFDLSVFELFGPLATGGKVVL-----ADNVLALPDLPAaaeVTLINTVPSAAAELLRHDALPA----SVRVVN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 243 WGATPVTVSIAETVTRR-TGVRWVPAYGTTE-------LPViacnPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDV 314
Cdd:cd12115 220 LAGEPLPRDLVQRLYARlQVERVVNLYGPSEdttystvAPV----PPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 315 GEIQARSASLMAGYL-------------PAAANAEVwrdgwYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVET 381
Cdd:cd12115 295 GELYIGGAGVARGYLgrpgltaerflpdPFGPGARL-----YRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEA 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 382 VLHSHPAVKDCAVFGVPDGVNgEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd12115 370 ALRSIPGVREAVVVAIGDAAG-ERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
26-446 |
1.71e-40 |
|
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: 151.85 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHAL----------GLTDP----AHAVG 91
Cdd:cd05932 19 LAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLehseskalfvGKLDDwkamAPGVP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 92 DHPVLADLMPMLDL------DDPIAPAAPITGSPRPGDD--AVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTER 163
Cdd:cd05932 99 EGLISISLPPPSAAncqyqwDDLIAQHPPLEERPTRFPEqlATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEEN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 164 DRIQVATPPSHILGLLNI-LTALRVGTSV--------------RLHPR--FDVDR--------ILRHIENDRITIEMAVa 218
Cdd:cd05932 179 DRMLSYLPLAHVTERVFVeGGSLYGGVLVafaesldtfvedvqRARPTlfFSVPRlwtkfqqgVQDKIPQQKLNLLLKI- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 219 PIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVtRRTGVRWVPAYGTTE-LPVIACNPPEQSRLDSVGRPVAGVD 297
Cdd:cd05932 258 PVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWY-RSLGLNILEAYGMTEnFAYSHLNYPGRDKIGTVGNAGPGVE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 298 VRIvsldtgepvgpGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKV-RGFQV 374
Cdd:cd05932 337 VRI-----------SEDGEILVRSPALMMGYYkdPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYV 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 375 APAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTA-------RVAAQLAPYKRLSRVVFVPE 446
Cdd:cd05932 406 APAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLRADAFARAELEAslrahlaRVNSTLDSHEQLAGIVVVKD 484
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
6-444 |
1.72e-40 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 153.11 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:PRK08279 55 ALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDH---PVLADLMPMLDLDDPIAPAAPITGSPRPG-------------------------DDAVLVFSSGTTGLP 137
Cdd:PRK08279 135 AKHLIVGEelvEAFEEARADLARPPRLWVAGGDTLDDPEGyedlaaaaagapttnpasrsgvtakDTAFYIYTSGTTGLP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 138 KAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNIL-TALRVGTSVRLHPRFDVDRILRHIENDRITIEMA 216
Cdd:PRK08279 215 KAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWsSVLAAGATLALRRKFSASRFWDDVRRYRATAFQY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 217 VAPIAQALASHPRLESYDLSSLRfIMWGA--TPvtvSIAETVTRRTGV-RWVPAYGTTELPVIACNPPEQSRldSVGR-- 291
Cdd:PRK08279 295 IGELCRYLLNQPPKPTDRDHRLR-LMIGNglRP---DIWDEFQQRFGIpRILEFYAASEGNVGFINVFNFDG--TVGRvp 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 292 PVAGVDVRIVSLD--TGEP----------VGPGDVGEIQAR--SASLMAGYL-PAAANAEVWRDG------WYRTGDVGW 350
Cdd:PRK08279 369 LWLAHPYAIVKYDvdTGEPvrdadgrcikVKPGEVGLLIGRitDRGPFDGYTdPEASEKKILRDVfkkgdaWFNTGDLMR 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 351 LDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPdgVNGeavvaavathAPGNTGVAA-------- 422
Cdd:PRK08279 449 DDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVE--VPG----------TDGRAGMAAivladgae 516
|
490 500
....*....|....*....|....*.
gi 576413765 423 ----ELTARVAAQLAPYkrlSRVVFV 444
Cdd:PRK08279 517 fdlaALAAHLYERLPAY---AVPLFV 539
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
19-462 |
2.22e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 152.22 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 19 LDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAW---------KRDEVD------HALGL 83
Cdd:PRK13382 74 LDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFagpalaevvTREGVDtviydeEFSAT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 84 TDpaHAVGDHPVLADLMPMLDLDDPIAPAAPITG------SPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDA 157
Cdd:PRK13382 154 VD--RALADCPQATRIVAWTDEDHDLTVEVLIAAhagqrpEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 158 LRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPR--LESYDL 235
Cdd:PRK13382 232 TPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQSR--LDSVGRPVAGVDVRIVSLDTGEpVGPGD 313
Cdd:PRK13382 312 RSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRaaPDTAGRPAEGTEIRILDQDFRE-VPTGE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 314 VGEIQARSASLMAGYLPAAANAevWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCA 393
Cdd:PRK13382 391 VGTIFVRNDTQFDGYTSGSTKD--FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAA 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 394 VFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK13382 469 VIGVDDEQYGQRLAAFVVL-KPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
123-455 |
1.01e-39 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 145.91 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRI 202
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 203 LRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFI--MWGATPVTvsiaeTVTRRTGVRWVPAYGTTELPVIAC-N 279
Cdd:cd17636 81 LELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSpaAPEWNDMA-----TVDTSPWGRKPGGYGQTEVMGLATfA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 280 PPEQSRLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARSASLMAGYLPA-AANAEVWRDGWYRTGDVGWLDGNGWLR 358
Cdd:cd17636 156 ALGGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRpEVNARRTRGGWHHTNDLGRREPDGSLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 359 ITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYKRL 438
Cdd:cd17636 235 FVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ-SVKAIVVLKPGASVTEAELIEHCRARIASYKKP 313
|
330
....*....|....*..
gi 576413765 439 SRVVFVPEIPRLPSGKV 455
Cdd:cd17636 314 KSVEFADALPRTAGGAD 330
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
123-457 |
3.97e-39 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 144.71 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDA-LRLTERDRIQVATPPSHILGLLNILTALRV-GTSVRLHPRFDVD 200
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 201 RILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNP 280
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 281 PEQSRLD--SVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARSASLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWL 357
Cdd:cd17635 162 TDDDSIEinAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNnPERTAEVLIDGWVNTGDLGERREDGFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 358 RITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKR 437
Cdd:cd17635 241 FITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKHTIRRELEPYAR 320
|
330 340
....*....|....*....|
gi 576413765 438 LSRVVFVPEIPRLPSGKVLR 457
Cdd:cd17635 321 PSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
6-462 |
7.95e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 147.52 E-value: 7.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGER-VAVMASNRPEFVAALQAIWRLGAAAVLISP-----AWKRDeVDH 79
Cdd:PRK07867 21 GLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPtrrgaALARD-IAH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 80 A---LGLTDPAHAvgdhPVLADLMP---MLDLD--------DPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHA 145
Cdd:PRK07867 100 AdcqLVLTESAHA----ELLDGLDPgvrVINVDspawadelAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 146 SLDAAVRQWRDALRLTERDRIQVATPPSHILGLL-NILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVA-PIAQA 223
Cdd:PRK07867 176 KVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMaGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGkPLSYV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 224 LASHPRLESYDlSSLRfIMWG--ATPVTVsiaETVTRRTGVRWVPAYGTTELPVIACNPPEqSRLDSVGRPVAGVdvRIV 301
Cdd:PRK07867 256 LATPERPDDAD-NPLR-IVYGneGAPGDI---ARFARRFGCVVVDGFGSTEGGVAITRTPD-TPPGALGPLPPGV--AIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 302 SLDTGEPVGPGD------------VGE-IQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMI 367
Cdd:PRK07867 328 DPDTGTECPPAEdadgrllnadeaIGElVNTAGPGGFEGYYnDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWM 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 368 KVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTARVAAQ--LAPYKRLSRVVFVP 445
Cdd:PRK07867 408 RVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVL-APGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCA 486
|
490
....*....|....*..
gi 576413765 446 EIPRLPSGKVLRRVLKE 462
Cdd:PRK07867 487 ELPRTATFKVLKRQLSA 503
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
121-463 |
1.13e-38 |
|
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: 143.78 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 121 PGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNI-LTALRVGTSVRL------ 193
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTlLTPLASGAHVVLagpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 194 -HPRFdVDRILRHIENDRITIEMAVAPIAQALASHPrlESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE 272
Cdd:cd05944 81 rNPGL-FDNFWKLVERYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 273 LP-VIACNPPE-QSRLDSVGRPVAGVDVRIVSLD----TGEPVGPGDVGEIQARSASLMAGYLPAAANAEVW-RDGWYRT 345
Cdd:cd05944 158 ATcLVAVNPPDgPKRPGSVGLRLPYARVRIKVLDgvgrLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFvADGWLNT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 346 GDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELT 425
Cdd:cd05944 238 GDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGE-LPVAYVQLKPGAVVEEEELL 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 576413765 426 ARVAAQLAPYKRLSRVVFV-PEIPRLPSGKVLRRVLKEL 463
Cdd:cd05944 317 AWARDHVPERAAVPKHIEVlEELPVTAVGKVFKPALRAD 355
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
11-447 |
1.23e-38 |
|
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: 145.57 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 11 DRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHav 90
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 91 gdhpVLADLmpmldlddpiapaapitgsprpgddAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVAT 170
Cdd:cd05940 79 ----LVVDA-------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 171 PPSHILGLL-NILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMW-GATPv 248
Cdd:cd05940 130 PLYHSTALIvGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGnGLRP- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 249 tvSIAETVTRRTGV-RWVPAYGTTE----LPVIACNPPEQSRLDSVGRPVAGVDVRIVSLDTGEP----------VGPGD 313
Cdd:cd05940 209 --DIWEEFKERFGVpRIAEFYAATEgnsgFINFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPirdaegrcikVPRGE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 314 VGEIQARSASL--MAGYL-PAAANAEVWR------DGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLH 384
Cdd:cd05940 287 PGLLISRINPLepFDGYTdPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLG 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 385 SHPAVKDCAVFGVP-DGVNGEAVVAAVATHAPGNTGVAAeLTARVAAQLAPYKRLSRVVFVPEI 447
Cdd:cd05940 367 AFPGVEEANVYGVQvPGTDGRAGMAAIVLQPNEEFDLSA-LAAHLEKNLPGYARPLFLRLQPEM 429
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
3-460 |
1.34e-38 |
|
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: 145.53 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHalg 82
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ltdpahavgdhpVLADLMPMLDLDDPIAPAAPItgsprpgddavlvFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTE 162
Cdd:cd17643 79 ------------ILADSGPSLLLTDPDDLAYVI-------------YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 163 RDRIQVATPPSHILGLLNILTALRVGTSVRLHPRfDVDR----ILRHIENDRITI----EMAVAPIAQALASHPRlesyD 234
Cdd:cd17643 134 DDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPY-EVARspedFARLLRDEGVTVlnqtPSAFYQLVEAADRDGR----D 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 235 LSSLRFIMWGATPVTVSIAETVTRRTGV---RWVPAYGTTEL-------PVIACNPPEQSRlDSVGRPVAGVDVRIVSlD 304
Cdd:cd17643 209 PLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtvhvtfrPLDAADLPAAAA-SPIGRPLPGLRVYVLD-A 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 305 TGEPVGPGDVGEIQARSASLMAGYL-----------PAAANAEVWRdgWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQ 373
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLgrpeltaerfvANPFGGPGSR--MYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 374 VAPAEVETVLHSHPAVKDCAVfGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSG 453
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAV-IVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443
|
....*..
gi 576413765 454 KVLRRVL 460
Cdd:cd17643 444 KLDRAAL 450
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
6-454 |
1.49e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 146.95 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:PRK07798 21 ALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDH---PVLADLMP-------MLDLDDPIAPAAPI----------TGSP------RPGDDAVLVFSSGTTGLPKA 139
Cdd:PRK07798 101 AVALVYERefaPRVAEVLPrlpklrtLVVVEDGSGNDLLPgavdyedalaAGSPerdfgeRSPDDLYLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 140 V--RH-----------THASLDAAVRQWRDALRLTERD--RIQVATPPSHILGLLNILTALRVGTSVRLHP--RFDVDRI 202
Cdd:PRK07798 181 VmwRQedifrvllggrDFATGEPIEDEEELAKRAAAGPgmRRFPAPPLMHGAGQWAAFAALFSGQTVVLLPdvRFDADEV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 203 LRHIENDRITIEMAV-----APIAQALAshpRLESYDLSSLRFIMWGATPVTVSIaetvtRRTGVRWVP------AYGTT 271
Cdd:PRK07798 261 WRTIEREKVNVITIVgdamaRPLLDALE---ARGPYDLSSLFAIASGGALFSPSV-----KEALLELLPnvvltdSIGSS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 272 E----LPVIACNPPEQSrldsvGRPVAGVDVRIVSLD-TGEPVGPGD--VGEIqARSASLMAGYL-PAAANAEVWR--DG 341
Cdd:PRK07798 333 EtgfgGSGTVAKGAVHT-----GGPRFTIGPRTVVLDeDGNPVEPGSgeIGWI-ARRGHIPLGYYkDPEKTAETFPtiDG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 --WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTG 419
Cdd:PRK07798 407 vrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQL-REGARP 485
|
490 500 510
....*....|....*....|....*....|....*
gi 576413765 420 VAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGK 454
Cdd:PRK07798 486 DLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
116-462 |
3.47e-38 |
|
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: 145.69 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 116 TGSPRPgddAVLVFSSGTTGLPKAVRHTHAS----LDAAVRQWRDalrLTERDRIQVATPPSHILGLL-NILTALRVGTS 190
Cdd:cd05928 171 TGSQEP---MAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLD---LTASDIMWNTSDTGWIKSAWsSLFEPWIQGAC 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 191 VRLH--PRFDVDRILRHIENDRITIeMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAY 268
Cdd:cd05928 245 VFVHhlPRFDPLVILKTLSSYPITT-FCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGY 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 269 GTTELPVIACNPP-EQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEI-----QARSASLMAGYLP-AAANAEVWRDG 341
Cdd:cd05928 324 GQTETGLICANFKgMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIgirvkPIRPFGLFSGYVDnPEKTAATIRGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAV------VAAVATHAP 415
Cdd:cd05928 403 FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVkafvvlAPQFLSHDP 482
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 576413765 416 GNtgVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05928 483 EQ--LTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
6-460 |
1.79e-37 |
|
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: 142.01 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHalgltd 85
Cdd:cd17652 5 AVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 pahavgdhpVLADLMPMLDLDDPIAPAAPItgsprpgddavlvFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd17652 79 ---------MLADARPALLLTTPDNLAYVI-------------YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGLLNILTALRVGTSVRLHPRFDV---DRILRHIENDRITieMAVAPIAqALAShprLESYDLSSLRFIM 242
Cdd:cd17652 137 VLQFASPSFDASVWELLMALLAGATLVLAPAEELlpgEPLADLLREHRIT--HVTLPPA-ALAA---LPPDDLPDLRTLV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 243 WGATPVTVSIAETVTRrtGVRWVPAYGTTELPVIAC--NPPEQSRLDSVGRPVAGVDVRIvsLDTG-EPVGPGDVGEIQA 319
Cdd:cd17652 211 VAGEACPAELVDRWAP--GRRMINAYGPTETTVCATmaGPLPGGGVPPIGRPVPGTRVYV--LDARlRPVPPGVPGELYI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 320 RSASLMAGYL-------------PAAANAEVWrdgwYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSH 386
Cdd:cd17652 287 AGAGLARGYLnrpgltaerfvadPFGAPGSRM----YRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 387 PAVKDcAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd17652 363 PGVAE-AVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
41-462 |
9.16e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 139.01 E-value: 9.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 41 VAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDE-------VDHALGLTDPAHAvgdhPVLADL----MPMLDLDDP- 108
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAAlaadirrADCQLLVTDAEHR----PLLDGLdlpgVRVLDVDTPa 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 109 ----IAPAAPITGSPRPGDDA--VLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLL-NI 181
Cdd:PRK13388 131 yaelVAAAGALTPHREVDAMDpfMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMaGW 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 182 LTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVA-PIAQALASHPRLESYDlSSLRfIMWGATPVTVSIAETVtRRT 260
Cdd:PRK13388 211 APAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGkPLAYILATPERPDDAD-NPLR-VAFGNEASPRDIAEFS-RRF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 261 GVRWVPAYGTTELPVIACNPPEQSRlDSVGRPVAGVdvRIVSLDTGEPVGPGD-------------VGEI-QARSASLMA 326
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVREPGTPP-GSIGRGAPGV--AIYNPETLTECAVARfdahgallnadeaIGELvNTAGAGFFE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 327 GYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEA 405
Cdd:PRK13388 365 GYYnNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQ 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 406 VVAAVAThAPGNTGVAAELTARVAAQ--LAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK13388 445 VMAALVL-RDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
6-470 |
9.79e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 141.45 E-value: 9.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDH------ 79
Cdd:PRK12467 530 ALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYmlddsg 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 80 -ALGLTDPaHAVGDHPVLADLmPMLDLDDPiapAAPITGSPR--------PGDDAVLVFSSGTTGLPKAVRHTHASLDAA 150
Cdd:PRK12467 610 vRLLLTQS-HLLAQLPVPAGL-RSLCLDEP---ADLLCGYSGhnpevaldPDNLAYVIYTSGSTGQPKGVAISHGALANY 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 151 VRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPR---FDVDRILRHIENDRITIEMAVAPIAQALASH 227
Cdd:PRK12467 685 VCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQA 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 228 PRLESydLSSLRFIMWGATPVTVSIAETVTR-RTGVRWVPAYGTTELPVIA----CNPPEQSRLDS-VGRPVAGVDVRIV 301
Cdd:PRK12467 765 SRVAL--PRPQRALVCGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVstyeLSDEERDFGNVpIGQPLANLGLYIL 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 302 SLDTgEPVGPGDVGEIQARSASLMAGYLPAAA-NAEVW------RDG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRGF 372
Cdd:PRK12467 843 DHYL-NPVPVGVVGELYIGGAGLARGYHRRPAlTAERFvpdpfgADGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGF 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 373 QVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAA---ELTARVAAQLAPYKRLSRVVFVPEIPR 449
Cdd:PRK12467 922 RIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQAtrdELKAQLRQVLPDYMVPAHLLLLDSLPL 1001
|
490 500
....*....|....*....|.
gi 576413765 450 LPSGKVLRRVLKELHGCPSDN 470
Cdd:PRK12467 1002 TPNGKLDRKALPKPDASAVQA 1022
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
14-463 |
1.55e-35 |
|
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: 136.93 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 14 VSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGA----AAVLISPAWKRDEVDHALGltdpAHA 89
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAvvipATTLLTPDDLRDRVDRGGA----VYA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 90 VGDHPVLADlmpmldldDPIapaapitgsprpgddaVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERD-RIQV 168
Cdd:cd05974 77 AVDENTHAD--------DPM----------------LLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDvHWNI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 169 ATPPSHILGLLNILTALRVGTSVRL--HPRFDVDRILRHIENDRITIEMAVAPIAQALASHPrLESYDLSsLRFIMWGAT 246
Cdd:cd05974 133 SSPGWAKHAWSCFFAPWNAGATVFLfnYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD-LASFDVK-LREVVGAGE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 247 PVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPPEQS-RLDSVGRPVAGVDVRIVSLDTGepvgPGDVGEI-----QAR 320
Cdd:cd05974 211 PLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPvKAGSMGRPLPGYRVALLDPDGA----PATEGEValdlgDTR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 321 SASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPD 399
Cdd:cd05974 287 PVGLMKGYAgDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPD 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 400 GVNGEAVVAAVATHAPGNTG--VAAELTARVAAQLAPYKRLSRVVFVpEIPRLPSGKVLRRVLKEL 463
Cdd:cd05974 367 PVRLSVPKAFIVLRAGYEPSpeTALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
6-462 |
1.91e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 138.16 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFV----------AALQAI-WRLGAAAVLIspawkr 74
Cdd:PRK08162 36 AVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVeahfgvpmagAVLNTLnTRLDAASIAF------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 75 dEVDHA---LGLTDPAHAVGDHPVLADL----MPMLDLDDPIAPAAPITGS----------------PRPGD--DAV-LV 128
Cdd:PRK08162 110 -MLRHGeakVLIVDTEFAEVAREALALLpgpkPLVIDVDDPEYPGGRFIGAldyeaflasgdpdfawTLPADewDAIaLN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 129 FSSGTTGLPKAVRHTH--ASLDA------------AVRQWrdalrlterdriqvATPPSHILGLLNILT-ALRVGTSVRL 193
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHrgAYLNAlsnilawgmpkhPVYLW--------------TLPMFHCNGWCFPWTvAARAGTNVCL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 194 HpRFDVDRILRHIENDRITiEMAVAPIAQ-ALASHPRLESYDLS-SLRFIMWGATPVTVSIAETvtRRTGVRWVPAYGTT 271
Cdd:PRK08162 255 R-KVDPKLIFDLIREHGVT-HYCGAPIVLsALINAPAEWRAGIDhPVHAMVAGAAPPAAVIAKM--EEIGFDLTHVYGLT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 272 EL--PVIAC---------NPPEQSRLDS---VGRPVAGvDVRIVSLDTGEPVgPGD---VGEIQARSASLMAGYLP-AAA 333
Cdd:PRK08162 331 ETygPATVCawqpewdalPLDERAQLKArqgVRYPLQE-GVTVLDPDTMQPV-PADgetIGEIMFRGNIVMKGYLKnPKA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 334 NAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVvaavatH 413
Cdd:PRK08162 409 TEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVP------C 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 576413765 414 A-----PGNTGVAAELTARVAAQLAPYKRLSRVVFvPEIPRLPSGKVLRRVLKE 462
Cdd:PRK08162 483 AfvelkDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLRE 535
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
2-462 |
2.32e-35 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 136.29 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 2 TEPAALVIED--RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDH 79
Cdd:cd17653 9 AHPDAVAVESlgGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 80 ALGLTDPAHAVGDhpvladlmpmldlddpiapaapitgsPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALR 159
Cdd:cd17653 89 ILRTSGATLLLTT--------------------------DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 160 LTERDRI-QVATpPSHILGLLNILTAL-RVGTSVRLHPRFDVDRILRHIEndritiemaVAPIAQALASHPRLESYDlsS 237
Cdd:cd17653 143 VGPGSRVaQVLS-IAFDACIGEIFSTLcNGGTLVLADPSDPFAHVARTVD---------ALMSTPSILSTLSPQDFP--N 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 238 LRFIMWGATPVTVSIAEtvTRRTGVRWVPAYGTTELPVIACNP---PEQSrlDSVGRPVAGVDVRIVSLDTgEPVGPGDV 314
Cdd:cd17653 211 LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTellPGQP--VTIGKPIPNSTCYILDADL-QPVPEGVV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 315 GEIQARSASLMAGYL--PAAANAEV----WRDGW--YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVA-PAEVETVLHS 385
Cdd:cd17653 286 GEICISGVQVARGYLgnPALTASKFvpdpFWPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINlEEIEEVVLQS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 386 HPAVKDCAV---------FGVPDGVNGEAvvaavathapgntgvaaeLTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVL 456
Cdd:cd17653 366 QPEVTQAAAivvngrlvaFVTPETVDVDG------------------LRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427
|
....*.
gi 576413765 457 RRVLKE 462
Cdd:cd17653 428 RKALRE 433
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
24-460 |
2.52e-34 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 135.14 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 24 DGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAV---------GDHP 94
Cdd:PRK05857 52 GGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALvapgskmasSAVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 95 VLADLMPMLDLDDPIAPA--------APITGSPRPG-DDAV-LVFSSGTTGLPKAVRHTHASLDAAvrqwRDALR---LT 161
Cdd:PRK05857 132 EALHSIPVIAVDIAAVTResehsldaASLAGNADQGsEDPLaMIFTSGTTGEPKAVLLANRTFFAV----PDILQkegLN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 162 ERDRIQVAT-----PPSHILGLLNILTALRVGTSVRLHPRFDVDriLRHIENDRITIEMAVAP-IAQALASHPRLESYDL 235
Cdd:PRK05857 208 WVTWVVGETtysplPATHIGGLWWILTCLMHGGLCVTGGENTTS--LLEILTTNAVATTCLVPtLLSKLVSELKSANATV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVtvsIAETV--TRRTGVRWVPAYGTTELPVIA-CNPPEQ---SRLD--SVGRPVAGVDVRIVSLDTGE 307
Cdd:PRK05857 286 PSLRLVGYGGSRA---IAADVrfIEATGVRTAQVYGLSETGCTAlCLPTDDgsiVKIEagAVGRPYPGVDVYLAATDGIG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 308 PVGPG-----DVGEIQARSASLMAGYLPAAANA-EVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVET 381
Cdd:PRK05857 363 PTAPGagpsaSFGTLWIKSPANMLGYWNNPERTaEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDR 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 382 VLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQL----APYKRLSRVVFVPEIPRLPSGKVLR 457
Cdd:PRK05857 443 IAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFrresEPMARPSTIVIVTDIPRTQSGKVMR 522
|
...
gi 576413765 458 RVL 460
Cdd:PRK05857 523 ASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-460 |
3.25e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 137.01 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEV----- 77
Cdd:PRK12316 526 EAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLaymle 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 78 DHALGLTDPAHAVGDHPVLADLMPMLDLDDPIA-----PAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVR 152
Cdd:PRK12316 606 DSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAwlegySEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 153 QWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQALASHPR 229
Cdd:PRK12316 686 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAApgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDED 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 230 LESydLSSLRFIMWGATPVTVSIAETV-TRRTGVRWVPAYGTTELPVIACNPP---EQSRLDSVGRPVAGVDVRIVSLDt 305
Cdd:PRK12316 766 VAS--CTSLRRIVCSGEALPADAQEQVfAKLPQAGLYNLYGPTEAAIDVTHWTcveEGGDSVPIGRPIANLACYILDAN- 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 306 GEPVGPGDVGEIQARSASLMAGYLP-AAANAE-----VWRDG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPA 377
Cdd:PRK12316 843 LEPVPVGVLGELYLAGRGLARGYHGrPGLTAErfvpsPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELG 922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 378 EVETVLHSHPAVKDCAVFgvpdGVNGEAVVAAVATHAPGNTGVAAeLTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLR 457
Cdd:PRK12316 923 EIEARLLEHPWVREAAVL----AVDGKQLVGYVVLESEGGDWREA-LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
...
gi 576413765 458 RVL 460
Cdd:PRK12316 998 KAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-460 |
1.16e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.47 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDPAHAVGDHPVLADL-----MPMLDLDDPIAPAAPITGSPRP---GDD-AVLVFSSGTTGLPKAVRHTHASLDAAVRQ 153
Cdd:PRK12316 2098 DSGAALLLTQRHLLERLplpagVARLPLDRDAEWADYPDTAPAVqlaGENlAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 154 WRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP--RFDVDRILRHIENDRITIEMAVAPIAQALASHPRLE 231
Cdd:PRK12316 2178 AGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDdeLWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERD 2257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 232 SYDLsSLRFIMWGATPVTVSIAETVTRRT-GVRWVPAYGTTELPVIA----CNP--PEQSRLDSVGRPVAGVDVRIvsLD 304
Cdd:PRK12316 2258 GRPP-AVRVYCFGGEAVPAASLRLAWEALrPVYLFNGYGPTEAVVTPllwkCRPqdPCGAAYVPIGRALGNRRAYI--LD 2334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 305 TG-EPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGW-------YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQV 374
Cdd:PRK12316 2335 ADlNLLAPGMAGELYLGGEGLARGYLnrPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRI 2414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 375 APAEVETVLHSHPAVKDCAVFGVpDGVNGEAVVAAVATHAPGnTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGK 454
Cdd:PRK12316 2415 ELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAA-EDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGK 2492
|
....*.
gi 576413765 455 VLRRVL 460
Cdd:PRK12316 2493 LDRKAL 2498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
12-448 |
1.61e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 131.43 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALgltdpahavg 91
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 92 dhpvladlmpmldldDPIAPAAPItGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATP 171
Cdd:cd05910 71 ---------------QEAEPDAFI-GIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 172 P----SHILGLLNILTALRVGTSVRLHPRFDVDRILRHiendRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATP 247
Cdd:cd05910 135 LfalfGPALGLTSVIPDMDPTRPARADPQKLVGAIRQY----GVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 248 VTVSIAETVTR--RTGVRWVPAYGTTE-LPVIAC----------NPPEQSRLDSVGRPVAGVDVRIVSLDTGE------- 307
Cdd:cd05910 211 VPIALAARLRKmlSDEAEILTPYGATEaLPVSSIgsrellatttAATSGGAGTCVGRPIPGVRVRIIEIDDEPiaewddt 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 308 -PVGPGDVGEIQARSASLMAGYL---PAAANAEVWRDG---WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVE 380
Cdd:cd05910 291 lELPRGEIGEITVTGPTVTPTYVnrpVATALAKIDDNSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVE 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576413765 381 TVLHSHPAVKDCAVFGVpdGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPY---KRLSRVVFVPEIP 448
Cdd:cd05910 371 RVFNTHPGVRRSALVGV--GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYphtQRIGRFLIHPSFP 439
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
30-459 |
2.13e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 132.43 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 30 LHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLIS--------PAWKRDEVDHALGLTDPAHAVGD-----HPVL 96
Cdd:PRK07768 46 LAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHqptprtdlAVWAEDTLRVIGMIGAKAVVVGEpflaaAPVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 97 ADL-MPMLDLDDpIAPAAPITGSPRPGDD-AVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLT-ERDRIQVATPPS 173
Cdd:PRK07768 126 EEKgIRVLTVAD-LLAADPIDPVETGEDDlALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 174 HILGLLNILTA--LRVGTSVRLHP-RFDVDRIL--RHIENDRITI----EMAVAPIAQALASHPRLESYDLSSLRFIMWG 244
Cdd:PRK07768 205 HDMGMVGFLTVpmYFGAELVKVTPmDFLRDPLLwaELISKYRGTMtaapNFAYALLARRLRRQAKPGAFDLSSLRFALNG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 245 ATPVTVSIAETVTR---RTGVR---WVPAYGTTELPV---------------------------IACNPPEQSRLDSVGR 291
Cdd:PRK07768 285 AEPIDPADVEDLLDagaRFGLRpeaILPAYGMAEATLavsfspcgaglvvdevdadllaalrraVPATKGNTRRLATLGP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 292 PVAGVDVRIVSLDtGEPVGPGDVGEIQARSASLMAGYL-PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVR 370
Cdd:PRK07768 365 PLPGLEVRVVDED-GQVLPPRGVGVIELRGESVTPGYLtMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 371 GFQVAPAEVETVLHSHPAVK-DCAV-FGVPDGVNGEAVVAAVATHAPGN----TGVAAELTARVAAQLAPYKRLSRVVFV 444
Cdd:PRK07768 444 GRNIYPTDIERAAARVEGVRpGNAVaVRLDAGHSREGFAVAVESNAFEDpaevRRIRHQVAHEVVAEVGVRPRNVVVLGP 523
|
490
....*....|....*
gi 576413765 445 PEIPRLPSGKvLRRV 459
Cdd:PRK07768 524 GSIPKTPSGK-LRRA 537
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
6-463 |
2.15e-33 |
|
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: 131.51 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd05918 17 AVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PahavgdHPVLADlmpmldlddpiapaapitgspRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd05918 97 A------KVVLTS---------------------SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 I-QVAtppSHILG--LLNILTALRVGTSVRLHPRFD-VDRILRHIENDRITIEMAVAPIAQALasHPRlesyDLSSLRFI 241
Cdd:cd05918 150 VlQFA---SYTFDvsILEIFTTLAAGGCLCIPSEEDrLNDLAGFINRLRVTWAFLTPSVARLL--DPE----DVPSLRTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 242 MWGATPVTVSIAETVTRRtgVRWVPAYGTTELPV--IACNPPEQSRLDSVGRPVAGVdVRIVSLDT-GEPVGPGDVGEIQ 318
Cdd:cd05918 221 VLGGEALTQSDVDTWADR--VRLINAYGPAECTIaaTVSPVVPSTDPRNIGRPLGAT-CWVVDPDNhDRLVPIGAVGELL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 319 ARSASLMAGYL--PAA-ANAEVWRDGW------------YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVL 383
Cdd:cd05918 298 IEGPILARGYLndPEKtAAAFIEDPAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 384 HSH-PAVKDCAV----------------FGVPDGVNGEAVVAAVATHAPG--NTGVAAELTARVAAQLAPYKRLSRVVFV 444
Cdd:cd05918 378 RQSlPGAKEVVVevvkpkdgssspqlvaFVVLDGSSSGSGDGDSLFLEPSdeFRALVAELRSKLRQRLPSYMVPSVFLPL 457
|
490
....*....|....*....
gi 576413765 445 PEIPRLPSGKVLRRVLKEL 463
Cdd:cd05918 458 SHLPLTASGKIDRRALREL 476
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
120-404 |
1.07e-32 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 131.76 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 120 RPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGL-LNILTALRVGTSVRLHPRFD 198
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLtVGLFTPLLTGAEVFLYPSPL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 199 VDRILRHIENDR-ITIEMAVAPIAQALA--SHPrlesYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-P 274
Cdd:PRK08043 443 HYRIVPELVYDRnCTVLFGTSTFLGNYArfANP----YDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECaP 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 275 VIACNPPEQSRLDSVGRPVAGVDVRIVSLdtgepvgPG--DVGEIQARSASLMAGYL----------PAAANAEVWRD-G 341
Cdd:PRK08043 519 VVSINVPMAAKPGTVGRILPGMDARLLSV-------PGieQGGRLQLKGPNIMNGYLrvekpgvlevPTAENARGEMErG 591
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576413765 342 WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGE 404
Cdd:PRK08043 592 WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE 654
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
10-463 |
1.10e-32 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 130.79 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGA----------------------AAVL 67
Cdd:PRK04319 70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAivgplfeafmeeavrdrledseAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 68 IS--------PAWKRDEVDHALGLTDPAHAVGDHPVLADLMPMLDLDDPIAPAapitgspRPGDDAVLVFSSGTTGLPKA 139
Cdd:PRK04319 150 ITtpallerkPADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQASDEFDIEWT-------DREDGAILHYTSGSTGKPKG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 140 VRHTHaslDAAVRQW---RDALRLTERDRIQVATPPSHILGL-LNILTALRVG-TSVRLHPRFDVDRILRHIENDRITIE 214
Cdd:PRK04319 223 VLHVH---NAMLQHYqtgKYVLDLHEDDVYWCTADPGWVTGTsYGIFAPWLNGaTNVIDGGRFSPERWYRILEDYKVTVW 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 215 MAvAPIAQAL---ASHPRLESYDLSSLRFIMwgatpvtvSIAETVTRRTgVRW-VPAYGtteLPV------------IAC 278
Cdd:PRK04319 300 YT-APTAIRMlmgAGDDLVKKYDLSSLRHIL--------SVGEPLNPEV-VRWgMKVFG---LPIhdnwwmtetggiMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 279 NPPEQS-RLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSA--SLMAGYLPAAAN-AEVWRDGWYRTGDVGWLDGN 354
Cdd:PRK04319 367 NYPAMDiKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKyESYFAGDWYVSGDSAYMDED 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 355 GWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAV---VAAVATHAPGNTgVAAELTA----R 427
Cdd:PRK04319 446 GYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIkafVALRPGYEPSEE-LKEEIRGfvkkG 524
|
490 500 510
....*....|....*....|....*....|....*...
gi 576413765 428 VAAQLAPykrlSRVVFVPEIPRLPSGKVLRRVLK--EL 463
Cdd:PRK04319 525 LGAHAAP----REIEFKDKLPKTRSGKIMRRVLKawEL 558
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
6-460 |
7.37e-32 |
|
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: 126.81 E-value: 7.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGltd 85
Cdd:cd17650 5 AVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 pahavgdhpvladlmpmldldDPIAPAAPItgspRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLterDR 165
Cdd:cd17650 82 ---------------------DSGAKLLLT----QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYEL---DS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVA----TPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSL 238
Cdd:cd17650 134 FPVRllqmASFSFDVFAGDFARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 239 RFIMWGATPVTVSIAETVTRRTG--VRWVPAYGTTELPV------IACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVG 310
Cdd:cd17650 214 RLLIVGSDGCKAQDFKTLAARFGqgMRIINSYGVTEATIdstyyeEGRDPLGDSANVPIGRPLPNTAMYVLD-ERLQPQP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 311 PGDVGEIQARSASLMAGYL-------------PAAANAEVwrdgwYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPA 377
Cdd:cd17650 293 VGVAGELYIGGAGVARGYLnrpeltaerfvenPFAPGERM-----YRTGDLARWRADGNVELLGRVDHQVKIRGFRIELG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 378 EVETVLHSHPAVKDcAVFGVPDGVNGEAVVAAVAThaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLR 457
Cdd:cd17650 368 EIESQLARHPAIDE-AVVAVREDKGGEARLCAYVV--AAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
...
gi 576413765 458 RVL 460
Cdd:cd17650 445 RAL 447
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
7-461 |
6.33e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 123.61 E-value: 6.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 7 LVIEDRRVSRHALDALSDGLgATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEvdhALGLtdp 86
Cdd:PRK08308 2 LIVNDEEYSKSDFDLRLQRY-EEMEQFQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEA---AIRM--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 87 AHAVGDHPVLADlmpmlDLDDPIAPAAPitGSPRPGddAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRI 166
Cdd:PRK08308 75 AKRAGCHGLLYG-----ESDFTKLEAVN--YLAEEP--SLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 167 QVATPPSHILGLL-NILTALRVGTSVRL----HPRFdvdrILRHIENDRITIEMAVAPIAQALASHPRLESydlsslRF- 240
Cdd:PRK08308 146 IVACPVTHSYGLIcGVLAALTRGSKPVIitnkNPKF----ALNILRNTPQHILYAVPLMLHILGRLLPGTF------QFh 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 241 -IMWGATPVTVSIAETVTRRTgVRWVPAYGTTELPVIACNPPEQSRLDsvgrpvAGVDVRIVSLDTGEpvGPGDVGEIQA 319
Cdd:PRK08308 216 aVMTSGTPLPEAWFYKLRERT-TYMMQQYGCSEAGCVSICPDMKSHLD------LGNPLPHVSVSAGS--DENAPEEIVV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 320 RsaslmagylpaAANAEVwrdgwyRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPD 399
Cdd:PRK08308 287 K-----------MGDKEI------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKD 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576413765 400 GVNGEAVVAAVATHAPGNTgvaAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:PRK08308 350 PVAGERVKAKVISHEEIDP---VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
121-399 |
1.52e-30 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 124.16 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 121 PGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILG-----LLNILTALRVGTSVR-LH 194
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfnsctLFPLLSGVPVVFAYNpLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 195 PRfdvdRILRHIENDRITIeMAVAPI--AQALASHPRLESyDLSSLRFIMWGATPVTVSI-AETVTRRTGVRWVPAYGTT 271
Cdd:PRK06334 262 PK----KIVEMIDEAKVTF-LGSTPVffDYILKTAKKQES-CLPSLRFVVIGGDAFKDSLyQEALKTFPHIQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 272 EL-PVIACNPPEQSRLDS-VGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL---PAAANAEVWRDGWYRTG 346
Cdd:PRK06334 336 ECsPVITINTVNSPKHEScVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgedFGQGFVELGGETWYVTG 415
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 576413765 347 DVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHpavkdcavFGVPD 399
Cdd:PRK06334 416 DLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNA 460
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
95-455 |
3.20e-30 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 124.69 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 95 VLADLMPMLDLDDPIAPAAPIT--GSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPP 172
Cdd:PRK06814 764 VRAQIGLADKIKGLLAGRFPLVyfCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPV 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 173 SHILGLLN--ILTALRvGTSVRLHPrfdvdrilrHIENDRITIEMAVAPIAQAL------------ASHPrlesYDLSSL 238
Cdd:PRK06814 844 FHSFGLTGglVLPLLS-GVKVFLYP---------SPLHYRIIPELIYDTNATILfgtdtflngyarYAHP----YDFRSL 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 239 RFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL-PVIACNPPEQSRLDSVGRPVAGVDVRIvsldtgEPVgPG--DVG 315
Cdd:PRK06814 910 RYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETaPVIALNTPMHNKAGTVGRLLPGIEYRL------EPV-PGidEGG 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 316 EIQARSASLMAGYLPAAANA--EVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCA 393
Cdd:PRK06814 983 RLFVRGPNVMLGYLRAENPGvlEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHA 1062
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576413765 394 VFGVPDGVNGEAVVAAVAthapGNTGVAAELTARVAAQLAPYKRLSRVVF-VPEIPRLPSGKV 455
Cdd:PRK06814 1063 AVSIPDARKGERIILLTT----ASDATRAAFLAHAKAAGASELMVPAEIItIDEIPLLGTGKI 1121
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
12-456 |
4.46e-30 |
|
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: 123.07 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLI----SPAWKRDEVDH-------- 79
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfggfAPEAVAGRIIDsssrllit 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 80 ALGLTDPAHAVGDHPVLADLMPM-------------------------LDLDDPIAPAAPITGSPR--PGDDAVLVFSSG 132
Cdd:cd17634 163 ADGGVRAGRSVPLKKNVDDALNPnvtsvehvivlkrtgsdidwqegrdLWWRDLIAKASPEHQPEAmnAEDPLFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 133 TTGLPKAVRHTHAS-LDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTA-LRVGTSVRL------HPrfDVDRILR 204
Cdd:cd17634 243 TTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGpLACGATTLLyegvpnWP--TPARMWQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 205 HIENDRITIeMAVAPIA-QAL--ASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPA---YGTTELPVIAC 278
Cdd:cd17634 321 VVDKHGVNI-LYTAPTAiRALmaAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVvdtWWQTETGGFMI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 279 NP---PEQSRLDSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIqarsasLMAGYLPAAANAEVWR------------DGWY 343
Cdd:cd17634 400 TPlpgAIELKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNL------VITDPWPGQTRTLFGDherfeqtyfstfKGMY 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 344 RTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNT---GV 420
Cdd:cd17634 473 FSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQ-APYAYVVLNHGVEpspEL 551
|
490 500 510
....*....|....*....|....*....|....*.
gi 576413765 421 AAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVL 456
Cdd:cd17634 552 YAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
26-383 |
5.45e-30 |
|
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: 121.70 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHpvladlmpmldl 105
Cdd:cd17640 18 FAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEN------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 106 ddpiapaapitgspRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTAL 185
Cdd:cd17640 86 --------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 186 RVG-----TSVRlHPRFDVDRILRHI--------ENDRITIEMAVA---PIAQALAshprlesydlssLRFIMWGATPVT 249
Cdd:cd17640 152 ACGcsqayTSIR-TLKDDLKRVKPHYivsvprlwESLYSGIQKQVSkssPIKQFLF------------LFFLSGGIFKFG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 250 VSIA-------ETVTRRTGVRWVPAYGTTEL-PVIACNPPEQSRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARS 321
Cdd:cd17640 219 ISGGgalpphvDTFFEAIGIEVLNGYGLTETsPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576413765 322 ASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVR-GFQVAPAEVETVL 383
Cdd:cd17640 299 PQVMKGYYknPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEAL 363
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
17-463 |
7.44e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 122.12 E-value: 7.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 17 HALDALsdglgatlhhrGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDE----VDHA-----------L 81
Cdd:PRK07008 54 QALAAL-----------GVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQiayiVNHAedryvlfdltfL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 82 GLTDPAH----------AVGDHPVL-ADLMPMLDLDDPIAPAAPITGSPRPGDDAV--LVFSSGTTGLPKAVRHTHAS-- 146
Cdd:PRK07008 123 PLVDALApqcpnvkgwvAMTDAAHLpAGSTPLLCYETLVGAQDGDYDWPRFDENQAssLCYTSGTTGNPKGALYSHRStv 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 147 LDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRL-HPRFDVDRILRHIENDRITIEMAVAPIAQALA 225
Cdd:PRK07008 203 LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLpGPDLDGKSLYELIEAERVTFSAGVPTVWLGLL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 226 SHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIA--CN--------PPEQSR--LDSVGRPV 293
Cdd:PRK07008 283 NHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGtlCKlkwkhsqlPLDEQRklLEKQGRVI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 294 AGVDVRIVSLDTGE-PVGPGDVGEIQARSASLMAGYLPAAANAEVwrDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGF 372
Cdd:PRK07008 363 YGVDMKIVGDDGRElPWDGKAFGDLQVRGPWVIDRYFRGDASPLV--DGWFPTGDVATIDADGFMQITDRSKDVIKSGGE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 373 QVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEaVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPS 452
Cdd:PRK07008 441 WISSIDIENVAVAHPAVAEAACIACAHPKWDE-RPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTAT 519
|
490
....*....|.
gi 576413765 453 GKVLRRVLKEL 463
Cdd:PRK07008 520 GKLQKLKLREQ 530
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
26-463 |
1.22e-29 |
|
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: 122.04 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEV----DHA--------------------L 81
Cdd:cd05967 95 LAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELasriDDAkpklivtascgiepgkvvpyK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 82 GLTDPAHAVGDHPVLA------DLMPM--------LDLDDPIAPAAPITGSPRPGDDAVLV-FSSGTTGLPKAV-RHTHA 145
Cdd:cd05967 175 PLLDKALELSGHKPHHvlvlnrPQVPAdltkpgrdLDWSELLAKAEPVDCVPVAATDPLYIlYTSGTTGKPKGVvRDNGG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 146 SLDAAVRQWRDALRLTERDRIQVATPPSHILG---------LLNILTALRVGTSVRlHPrfDVDRILRHIENDRITiEMA 216
Cdd:cd05967 255 HAVALNWSMRNIYGIKPGDVWWAASDVGWVVGhsyivygplLHGATTVLYEGKPVG-TP--DPGAFWRVIEKYQVN-ALF 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 217 VAPIA-QALASHP----RLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELP-VIACNP----PEQSRL 286
Cdd:cd05967 331 TAPTAiRAIRKEDpdgkYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGwPITANPvglePLPIKA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 287 DSVGRPVAGVDVRIVSlDTGEPVGPGDVGEIqarsasLMAGYLPAAANAEVWRD-------------GWYRTGDVGWLDG 353
Cdd:cd05967 411 GSPGKPVPGYQVQVLD-EDGEPVGPNELGNI------VIKLPLPPGCLLTLWKNderfkklylskfpGYYDTGDAGYKDE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 354 NGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGN---TGVAAELTARVAA 430
Cdd:cd05967 484 DGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKitaEELEKELVALVRE 563
|
490 500 510
....*....|....*....|....*....|...
gi 576413765 431 QLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:cd05967 564 QIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
11-404 |
1.31e-29 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 121.83 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 11 DRRVSRHAL--DALSdgLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAH 88
Cdd:PLN02860 30 NRRRTGHEFvdGVLS--LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 89 AVGDH-------PVLADLMPMLD----LDDPIAPAAPI-------------TGSPR-------PGDDAVLVFSSGTTGLP 137
Cdd:PLN02860 108 LVTDEtcsswyeELQNDRLPSLMwqvfLESPSSSVFIFlnsflttemlkqrALGTTeldyawaPDDAVLICFTSGTTGRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 138 KAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAV 217
Cdd:PLN02860 188 KGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 218 APIAQALASHPRLESYDLS--SLRFIMWGATPVTVS-IAETVTRRTGVRWVPAYGTTE----LPVIACNPPEQSRLDS-- 288
Cdd:PLN02860 268 PAMMADLISLTRKSMTWKVfpSVRKILNGGGSLSSRlLPDAKKLFPNAKLFSAYGMTEacssLTFMTLHDPTLESPKQtl 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 289 ------------------VGRPVAGVDVRIvSLDtgepvGPGDVGEIQARSASLMAGY--LPAAANAEVWRDGWYRTGDV 348
Cdd:PLN02860 348 qtvnqtksssvhqpqgvcVGKPAPHVELKI-GLD-----ESSRVGRILTRGPHVMLGYwgQNSETASVLSNDGWLDTGDI 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 349 GWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGE 404
Cdd:PLN02860 422 GWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTE 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-464 |
1.32e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 123.35 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK12467 3110 EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIE 3189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ------LTDPAHAVGDHPVLA-DLMPMLDLDD--PIAPAAPITgSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQ 153
Cdd:PRK12467 3190 dsgvklLLTQAHLLEQLPAPAgDTALTLDRLDlnGYSENNPST-RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCW 3268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 154 WRDALRLTERDRIQVATPPSHILGLLNILTALRVGTS--VRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPrlE 231
Cdd:PRK12467 3269 IAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGClvVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDA--G 3346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 232 SYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVP-AYGTTELPVI----ACNPPEQSRLDSV--GRPVAGVDvrIVSLD 304
Cdd:PRK12467 3347 GADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTnGYGPTEAVVTvtlwKCGGDAVCEAPYApiGRPVAGRS--IYVLD 3424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 305 -TGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGW-------YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQV 374
Cdd:PRK12467 3425 gQLNPVPVGVAGELYIGGVGLARGYHqrPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 3504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 375 APAEVETVLHSHPAVKDCAVFGVpDGVNGEAVVAAVATHAPgNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGK 454
Cdd:PRK12467 3505 ELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADP-QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGK 3582
|
490
....*....|
gi 576413765 455 VLRRVLKELH 464
Cdd:PRK12467 3583 VDRKALPDPD 3592
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
6-460 |
3.87e-29 |
|
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: 118.81 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHalgltd 85
Cdd:cd17645 16 AVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAY------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 pahavgdhpVLADLMPMLDLDDpiapaapitgsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd17645 90 ---------MLADSSAKILLTN-------------PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQalashpRLESYDLSSLRFIM 242
Cdd:cd17645 148 SLVYASFSFDASAWEIFPHLTAGAALHVVPserRLDLDALNDYFNQEGITISFLPTGAAE------QFMQLDNQSLRVLL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 243 WGATPVTVSiaetvtRRTGVRWVPAYGTTELPVIAC----NPPEQSRldSVGRPVAgvDVRIVSLDTGEPVGP-GDVGEI 317
Cdd:cd17645 222 TGGDKLKKI------ERKGYKLVNNYGPTENTVVATsfeiDKPYANI--PIGKPID--NTRVYILDEALQLQPiGVAGEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 318 QARSASLMAGYLPAA--------ANAEVWRDGWYRTGD-VGWL-DGNgwLRITDRLKEMIKVRGFQVAPAEVETVLHSHP 387
Cdd:cd17645 292 CIAGEGLARGYLNRPeltaekfiVHPFVPGERMYRTGDlAKFLpDGN--IEFLGRLDQQVKIRGYRIEPGEIEPFLMNHP 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576413765 388 AVKDCAVFGVPDGvNGEAVVAAVAThaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd17645 370 LIELAAVLAKEDA-DGRKYLVAYVT--APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
6-463 |
4.35e-29 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 119.71 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:PRK10946 41 AVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGD--HPVLAD-----------------LM----PMLDLDDPIA-PAAPITGSPRPGDD-AVLVFSSGTTGLPKAV 140
Cdd:PRK10946 121 PALLIADrqHALFSDddflntlvaehsslrvvLLlnddGEHSLDDAINhPAEDFTATPSPADEvAFFQLSGGSTGTPKLI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 141 RHTHASLDAAVRQWRDALRLTERDRIQVATPPSHIL-----GLLNILTAlrvGTSVRLHPRFDVDRILRHIENDRITIeM 215
Cdd:PRK10946 201 PRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYpmsspGALGVFLA---GGTVVLAPDPSATLCFPLIEKHQVNV-T 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 216 AVAPIAQAL---ASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPV--IACNPPEQSRLDSVG 290
Cdd:PRK10946 277 ALVPPAVSLwlqAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVnyTRLDDSDERIFTTQG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 291 RPVAGVD-VRIVSLDtGEPVGPGDVGEIQARSASLMAGYLPAAA-NAEVW-RDGWYRTGDVGWLDGNGWLRITDRLKEMI 367
Cdd:PRK10946 357 RPMSPDDeVWVADAD-GNPLPQGEVGRLMTRGPYTFRGYYKSPQhNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 368 KVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNtgvAAELTARVAAQ-LAPYKRLSRVVFVPE 446
Cdd:PRK10946 436 NRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLK---AVQLRRFLREQgIAEFKLPDRVECVDS 512
|
490
....*....|....*..
gi 576413765 447 IPRLPSGKVLRRVLKEL 463
Cdd:PRK10946 513 LPLTAVGKVDKKQLRQW 529
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
10-461 |
4.91e-29 |
|
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: 120.29 E-value: 4.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLI------SPAWKR--------- 74
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIfsgfgkEAAATRlqdaeakal 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 75 ----------------DEVDHA---------------LGLTDPAHAVGDhpvladlmpmLDLDDPIAPAAPITGSPRPGD 123
Cdd:cd05968 168 itadgftrrgrevnlkEEADKAcaqcptvekvvvvrhLGNDFTPAKGRD----------LSYDEEKETAGDGAERTESED 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 124 DAVLVFSSGTTGLPKAVRHTH------ASLDAAVrqwrdALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLH--- 194
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHagfplkAAQDMYF-----QFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYdga 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 195 PRFD-VDRILRHIENDRITIEMAVAPIAQALASHPR--LESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAY--- 268
Cdd:cd05968 313 PDHPkADRLWRMVEDHEITHLGLSPTLIRALKPRGDapVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIInys 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 269 GTTELP--VIACNPPEQSRLDSVGRPVAGVDVRIVSlDTGEPVgPGDVGEIQARSA--SLMAGYlpaaanaevWRDG--- 341
Cdd:cd05968 393 GGTEISggILGNVLIKPIKPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPwpGMTRGF---------WRDEdry 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 ----WYRT------GDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVA 411
Cdd:cd05968 462 letyWSRFdnvwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVV 541
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 576413765 412 THaPGNT---GVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:cd05968 542 LK-PGVTpteALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
3-462 |
7.21e-29 |
|
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: 118.58 E-value: 7.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:cd17655 12 DHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDPAHAVGDHPV---LADLMPMLDLDDPIAPAAPITGSP---RPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRD 156
Cdd:cd17655 92 DSGADILLTQSHLqppIAFIGLIDLLDEDTIYHEESENLEpvsKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 157 ALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPR---FDVDRILRHIENDRITIemavAPIAQALASHprLESY 233
Cdd:cd17655 172 VIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKetvLDGQALTQYIRQNRITI----IDLTPAHLKL--LDAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 234 DLS---SLRFIMWGATPVTVSIAETVTR--RTGVRWVPAYGTTELPVIACN---PPEQSRLDSV--GRPVAGVDVRIvsL 303
Cdd:cd17655 246 DDSeglSLKHLIVGGEALSTELAKKIIElfGTNPTITNAYGPTETTVDASIyqyEPETDQQVSVpiGKPLGNTRIYI--L 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 304 DT-GEPVGPGDVGEIQARSASLMAGYL-------------PAAANAEVwrdgwYRTGDVG-WL-DGNgwLRITDRLKEMI 367
Cdd:cd17655 324 DQyGRPQPVGVAGELYIGGEGVARGYLnrpeltaekfvddPFVPGERM-----YRTGDLArWLpDGN--IEFLGRIDHQV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 368 KVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGvNGEAVVAAVATHAPGNTgvAAELTARVAAQLAPYKRLSRVVFVPEI 447
Cdd:cd17655 397 KIRGYRIELGEIEARLLQHPDIKEAVVIARKDE-QGQNYLCAYIVSEKELP--VAQLREFLARELPDYMIPSYFIKLDEI 473
|
490
....*....|....*
gi 576413765 448 PRLPSGKVLRRVLKE 462
Cdd:cd17655 474 PLTPNGKVDRKALPE 488
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
12-448 |
4.52e-28 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 116.92 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKR-------DEVDHALGLT 84
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIknlkqclAEAQPDAFIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 85 DP-AH-----------------AVGDhpvlADLMPMLDLDDPIAPAAPITGSPR---PGDDAVLVFSSGTTGLPKAVRHT 143
Cdd:PRK09274 120 IPkAHlarrlfgwgkpsvrrlvTVGG----RLLWGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 144 HASLDAAVRQWRDALRLtERDRIQVATPPshILGLLNIltALRVGTSVrlhPRFD------VD--RILRHIENDRITiEM 215
Cdd:PRK09274 196 HGMFEAQIEALREDYGI-EPGEIDLPTFP--LFALFGP--ALGMTSVI---PDMDptrpatVDpaKLFAAIERYGVT-NL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 216 AVAP-----IAQALASHPRlesyDLSSL-RFIMWGAtPVTVSIAETVTR--RTGVRWVPAYGTTE-LPVIACNPPEQsrL 286
Cdd:PRK09274 267 FGSPallerLGRYGEANGI----KLPSLrRVISAGA-PVPIAVIERFRAmlPPDAEILTPYGATEaLPISSIESREI--L 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 287 DS------------VGRPVAGVDVRIVSLDTG--------EPVGPGDVGEIQARSASLMAGYL--PAA-ANAEVWRDG-- 341
Cdd:PRK09274 340 FAtraatdngagicVGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYnrPEAtRLAKIPDGQgd 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 -WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVpdGVNGEAVVAAVATHAPG---- 416
Cdd:PRK09274 420 vWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGV--GVPGAQRPVLCVELEPGvacs 497
|
490 500 510
....*....|....*....|....*....|..
gi 576413765 417 NTGVAAELTARvAAQLAPYKRLSRVVFVPEIP 448
Cdd:PRK09274 498 KSALYQELRAL-AAAHPHTAGIERFLIHPSFP 528
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
22-396 |
1.88e-27 |
|
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: 115.01 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 22 LSDGLGATLHHRGV--IAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPV---- 95
Cdd:cd05927 14 RADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGVkvys 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 96 LADLMPMLDLDdpIAPAAPitgsPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAV----RQWRDALRLTERDRIQVATP 171
Cdd:cd05927 94 LEEFEKLGKKN--KVPPPP----PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 172 PSHILGLLNILTALRVGTSV---------------RLHPRF--DVDRILRHIEnDRITIEMAVAP--------------I 220
Cdd:cd05927 168 LAHIFERVVEALFLYHGAKIgfysgdirlllddikALKPTVfpGVPRVLNRIY-DKIFNKVQAKGplkrklfnfalnykL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 221 AQALASHPRLESY-D-----------LSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE-LPVIACNPPEQSRLD 287
Cdd:cd05927 247 AELRSGVVRASPFwDklvfnkikqalGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTEcTAGATLTLPGDTSVG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 288 SVGRPVAGVDVRIVSLDTGE--PVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRL 363
Cdd:cd05927 327 HVGGPLPCAEVKLVDVPEMNydAKDPNPRGEVCIRGPNVFSGYYkdPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRK 406
|
410 420 430
....*....|....*....|....*....|....
gi 576413765 364 KEMIK-VRGFQVAPAEVETVLHSHPAVKDCAVFG 396
Cdd:cd05927 407 KNIFKlSQGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
5-460 |
2.84e-27 |
|
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: 113.65 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 5 AALVIEDRRVSRHALDALSDGLGATLHHRGVI-AGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGL 83
Cdd:cd17648 4 VAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 84 TDpAHAVgdhpvladlmpmldlddpiapaapITGsprPGDDAVLVFSSGTTGLPKAVRHTHASldaaVRQWRDALRlter 163
Cdd:cd17648 84 TG-ARVV------------------------ITN---STDLAYAIYTSGTTGKPKGVLVEHGS----VVNLRTSLS---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 164 DRIQVATPPSH-ILGLLN---------ILTALRVGTSVRLHP---RFDVDRILRHIENDRITIemavapiaqaLASHPR- 229
Cdd:cd17648 128 ERYFGRDNGDEaVLFFSNyvfdffveqMTLALLNGQKLVVPPdemRFDPDRFYAYINREKVTY----------LSGTPSv 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 230 LESYDLS---SLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIACNPPE--QSRLD-SVGRPVAGVDVRIVSL 303
Cdd:cd17648 198 LQQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFpgDQRFDkSLGRPVRNTKCYVLND 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 304 DTgEPVGPGDVGEIQARSASLMAGYL-------------PAAANAEVwRDG----WYRTGD-VGWLdGNGWLRITDRLKE 365
Cdd:cd17648 278 AM-KRVPVGAVGELYLGGDGVARGYLnrpeltaerflpnPFQTEQER-ARGrnarLYKTGDlVRWL-PSGELEYLGRNDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 366 MIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPD-GVNGEAVVAAVATHAPGNTGV--AAELTARVAAQLAPYKRLSRVV 442
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDaSQAQSRIQKYLVGYYLPEPGHvpESDLLSFLRAKLPRYMVPARLV 434
|
490
....*....|....*...
gi 576413765 443 FVPEIPRLPSGKVLRRVL 460
Cdd:cd17648 435 RLEGIPVTINGKLDVRAL 452
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
120-454 |
3.41e-27 |
|
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: 112.09 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 120 RPGDDAVLVFSSGTTGLPKAV--RH-----------THASLDAAVRQWRDALRLTERDRIQVATPP-SHILGLLNILTAL 185
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVmwRQedifrmlmggaDFGTGEFTPSEDAHKAAAAAAGTVMFPAPPlMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 186 RVGTSVRLH-PRFDVDRILRHIENDRITIEMAV-----APIAQAL-ASHPrlesYDLSSLRFIMWGATPVTVSIAETVTR 258
Cdd:cd05924 81 LGGQTVVLPdDRFDPEEVWRTIEKHKVTSMTIVgdamaRPLIDALrDAGP----YDLSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 259 RTGVRWVP-AYGTTELPVIACNPPEQSRLDSVGRPVAGVDVRIVSLDTGE-PVGPGDVGEIqARSASLMAGYL-PAAANA 335
Cdd:cd05924 157 LVPNITLVdAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVvPPGSGGVGWI-ARRGHIPLGYYgDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 336 EVWR--DG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVA 411
Cdd:cd05924 236 ETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQ 315
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 576413765 412 ThAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGK 454
Cdd:cd05924 316 L-REGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
26-461 |
7.31e-27 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 113.97 E-value: 7.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRD-----EVDHALGLTDPAHAVGDHPVLADLM 100
Cdd:PRK06060 43 LGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDdhalaARNTEPALVVTSDALRDRFQPSRVA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 101 PMLDLDDPIAPAAPITGSPRPGDDAVL-VFSSGTTGLPKAVRHTHASLDAAVRQW-RDALRLTERDRIQVATPPSHILGL 178
Cdd:PRK06060 123 EAAELMSEAARVAPGGYEPMGGDALAYaTYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 179 LN------------ILTALRVGTSV--RLHPRFDvDRILRHIENDRITIEMAVAPiaqalashprlESYdlSSLRFIMWG 244
Cdd:PRK06060 203 GNsvwfplatggsaVINSAPVTPEAaaILSARFG-PSVLYGVPNFFARVIDSCSP-----------DSF--RSLRCVVSA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 245 ATPVTVSIAETVTRR-TGVRWVPAYGTTEL-PVIACNPPEQSRLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIQARSA 322
Cdd:PRK06060 269 GEALELGLAERLMEFfGGIPILDGIGSTEVgQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 323 SLMAGYLpAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDgVN 402
Cdd:PRK06060 348 AIAKGYW-NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRE-ST 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576413765 403 GEAVVAAVATHAPG---NTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:PRK06060 426 GASTLQAFLVATSGatiDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
2-458 |
7.81e-27 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 113.32 E-value: 7.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 2 TEPAALVIEDRRV---SRH---ALDALSDGLGATLHHRGVIAGerVAVMASNRPEFVAALQAIWrLGAAAVLISPA---- 71
Cdd:PRK05851 14 ASGRDLVVLDRESglwRRHpwpEVHGRAENVAARLLDRDRPGA--VGLVGEPTVELVAAIQGAW-LAGAAVSILPGpvrg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 72 -----WKRDEVDHALGL-TDPAHAVGDHpvLADL------MPMLDLDDPIAPAAPITGSPRP-GDDAVLVFSSGTTGLPK 138
Cdd:PRK05851 91 addgrWADATLTRFAGIgVRTVLSHGSH--LERLravdssVTVHDLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 139 AVRHTHASLDAAVRQWRDALRLTE-RDRIQVATPPSHILGLLNILTALRVGTSVRLHPR--FDVD--RILRHIENDRITI 213
Cdd:PRK05851 169 TAILSPGAVLSNLRGLNARVGLDAaTDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTtaFSASpfRWLSWLSDSRATL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 214 ----EMAVAPIAQALAshpRLESYDLSSLRFIMWGATPVTVSIAE---TVTRRTGVR---WVPAYGTTE--LPVIACNPP 281
Cdd:PRK05851 249 taapNFAYNLIGKYAR---RVSDVDLGALRVALNGGEPVDCDGFErfaTAMAPFGFDagaAAPSYGLAEstCAVTVPVPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 282 EQSRLDSV--------------GRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYLPAAAnaeVWRDGWYRTGD 347
Cdd:PRK05851 326 IGLRVDEVttddgsgarrhavlGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP---IDPDDWFPTGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 348 VGWLdGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATH--APGNTGVAAELT 425
Cdd:PRK05851 403 LGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEfrGPDEAGARSEVV 481
|
490 500 510
....*....|....*....|....*....|....*..
gi 576413765 426 ARVAAQ--LAPykrlSRVVFVP--EIPRLPSGKvLRR 458
Cdd:PRK05851 482 QRVASEcgVVP----SDVVFVApgSLPRTSSGK-LRR 513
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-462 |
5.91e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 112.18 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK05691 1146 ERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ------LTDPAHAVGDHP----VLADLMPMLDLDD-PI-APAAPITGsprpGDDAVLVFSSGTTGLPKAVRHTHASLdAA 150
Cdd:PRK05691 1226 dsgvelLLTQSHLLERLPqaegVSAIALDSLHLDSwPSqAPGLHLHG----DNLAYVIYTSGSTGQPKGVGNTHAAL-AE 1300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 151 VRQW-RDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLH---PRFDVDRILRHIENDRITIEMAVAPIAQALAS 226
Cdd:PRK05691 1301 RLQWmQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID 1380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 227 HPRLEsyDLSSLRFIMWGATPVTVSIAETVTRR-TGVRWVPAYGTTELPVIA----CNPPEQSRlDSVGRPVAGVDVRIV 301
Cdd:PRK05691 1381 EPLAA--ACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAINVthwqCQAEDGER-SPIGRPLGNVLCRVL 1457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 302 SLDTgEPVGPGDVGEIQARSASLMAGYLPAAA-NAEVW------RDG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRGF 372
Cdd:PRK05691 1458 DAEL-NLLPPGVAGELCIGGAGLARGYLGRPAlTAERFvpdplgEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGF 1536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 373 QVAPAEVETVLHSHPAVKDCAVFgVPDGVNGeAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPS 452
Cdd:PRK05691 1537 RVEPEEIQARLLAQPGVAQAAVL-VREGAAG-AQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPS 1614
|
490
....*....|
gi 576413765 453 GKVLRRVLKE 462
Cdd:PRK05691 1615 GKLDRRALPE 1624
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
50-463 |
8.06e-26 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 109.31 E-value: 8.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 50 EFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPahavgdhpvlaDLMPMLDL--DDPIAPAAPITGSPRPGDDAVL 127
Cdd:PRK07445 57 QFLAAFLAAVAAGCPVFLANPHWGQQEWQQVLNLVQP-----------DQIWGLDQlkLSHPPPLPSQGILPNLETGWIM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 128 VFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTerdriQVAT----PPSHILGLLNILTALRVGTSVRLHPRFDVDR-I 202
Cdd:PRK07445 126 IPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQ-----QVNSfcvlPLYHVSGLMQFMRSFLTGGKLVILPYKRLKSgQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 203 LRHIENDRITIEMAVAPIAQALASHPRLesydLSSLRFIMWGATPVTVSIAETvTRRTGVRWVPAYGTTELPV-IACNPP 281
Cdd:PRK07445 201 ELPPNPSDFFLSLVPTQLQRLLQLRPQW----LAQFRTILLGGAPAWPSLLEQ-ARQLQLRLAPTYGMTETASqIATLKP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 282 EQSRL--DSVGRPVAGVDVRIVsldtgepvgPGDVGEIQARSASLMAGYLPAAANAevwrDGWYRTGDVGWLDGNGWLRI 359
Cdd:PRK07445 276 DDFLAgnNSSGQVLPHAQITIP---------ANQTGNITIQAQSLALGYYPQILDS----QGIFETDDLGYLDAQGYLHI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 360 TDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAvatHAPGNTGVAAE-LTARVAAQLAPYKRL 438
Cdd:PRK07445 343 LGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAI---YVPKDPSISLEeLKTAIKDQLSPFKQP 419
|
410 420
....*....|....*....|....*
gi 576413765 439 SRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK07445 420 KHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
16-462 |
9.57e-26 |
|
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: 109.89 E-value: 9.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 16 RHALDALSDGLGAtLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAwkrDEVDHALGLTDPAHAVGDHPV 95
Cdd:cd05908 19 RHLREEALGYLGA-LQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIG---SNEEHKLKLNKVWNTLKNPYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 96 LADLMPMLDLDDPIApaapitgsprpgddaVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHI 175
Cdd:cd05908 95 ITEEEVLCELADELA---------------FIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 176 LGLLNI-LTALRVGTSVRLHPR--FDVDRI--LRHIENDRITI----EMAVAPIAQALASHpRLESYDLSSLRFIMWGAT 246
Cdd:cd05908 160 MGLIAFhLAPLIAGMNQYLMPTrlFIRRPIlwLKKASEHKATIvsspNFGYKYFLKTLKPE-KANDWDLSSIRMILNGAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 247 PVTVSIAETVT--------RRTGVrwVPAYGTTELPVIACNPPEQSRLD-----------------------------SV 289
Cdd:cd05908 239 PIDYELCHEFLdhmskyglKRNAI--LPVYGLAEASVGASLPKAQSPFKtitlgrrhvthgepepevdkkdsecltfvEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 290 GRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDgNGWLRITDRLKEMI 367
Cdd:cd05908 317 GKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYnnPEATAKVFTDDGWLKTGDLGFIR-NGRLVITGREKDII 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 368 KVRGFQVAPAEVETVLHSHPAVK--DCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAeLTARVAAQLAPYK--RLSRVVF 443
Cdd:cd05908 395 FVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYP-LGKKIKKHLNKRGgwQINEVLP 473
|
490
....*....|....*....
gi 576413765 444 VPEIPRLPSGKVLRRVLKE 462
Cdd:cd05908 474 IRRIPKTTSGKVKRYELAQ 492
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
6-460 |
3.16e-25 |
|
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: 107.95 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd17656 6 AVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAV--GDHPV-LADLMPMLDLDDPI---APAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRD-AL 158
Cdd:cd17656 86 VRVVLtqRHLKSkLSFNKSTILLEDPSisqEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREkTN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 159 RLTERDRIQVATPpSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRItiEMAVAPIA--QALASHPRL-ES 232
Cdd:cd17656 166 INFSDKVLQFATC-SFDVCYQEIFSTLLSGGTLYIIReetKRDVEQLFDLVKRHNI--EVVFLPVAflKFIFSEREFiNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 233 YDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIAC---NP-PEQSRLDSVGRPVAGVDVRIVSlDTGEP 308
Cdd:cd17656 243 FPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTytiNPeAEIPELPPIGKPISNTWIYILD-QEQQL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 309 VGPGDVGEIQARSASLMAGYL-------------PAAANAEVwrdgwYRTGDVG-WL-DGNgwLRITDRLKEMIKVRGFQ 373
Cdd:cd17656 322 QPQGIVGELYISGASVARGYLnrqeltaekffpdPFDPNERM-----YRTGDLArYLpDGN--IEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 374 VAPAEVETVLHSHPAVKDCAVFgvpDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSG 453
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVL---DKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNG 471
|
....*..
gi 576413765 454 KVLRRVL 460
Cdd:cd17656 472 KVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-463 |
4.48e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 109.66 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK12316 4566 DAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMME 4645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ------LTDPAHAVGDHPVlADLMPMLDLD-----------DPIAPAAPitgsprpGDDAVLVFSSGTTGLPKAVRHTHA 145
Cdd:PRK12316 4646 dsgaalLLTQSHLLQRLPI-PDGLASLALDrdedwegfpahDPAVRLHP-------DNLAYVIYTSGSTGRPKGVAVSHG 4717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 146 SLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP--RFDVDRILRHIENDRITIEMAVAPIAQA 223
Cdd:PRK12316 4718 SLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDdsLWDPERLYAEIHEHRVTVLVFPPVYLQQ 4797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 224 LASHPRlESYDLSSLRFIMWGATPVTVSIAETVTRRTG-VRWVPAYGTTELPVI----ACNPPEQSRLDSV--GRPVAGV 296
Cdd:PRK12316 4798 LAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKpVYLFNGYGPTETTVTvllwKARDGDACGAAYMpiGTPLGNR 4876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 297 DVRIVSlDTGEPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGW-------YRTGDVGWLDGNGWLRITDRLKEMI 367
Cdd:PRK12316 4877 SGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLerPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQV 4955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 368 KVRGFQVAPAEVETVLHSHPAVKDCAVFGVpDGVNGEAVVAAVATHAP-------GNTGVAAELTARVAAQLAPYKRLSR 440
Cdd:PRK12316 4956 KIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGYVVPQDPaladadeAQAELRDELKAALRERLPEYMVPAH 5034
|
490 500
....*....|....*....|...
gi 576413765 441 VVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK12316 5035 LVFLARMPLTPNGKLDRKALPQP 5057
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
6-460 |
9.42e-25 |
|
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: 106.37 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:cd17644 18 AVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAhavgdhpVLadlmpmldlddpiapaapITgspRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDR 165
Cdd:cd17644 98 IS-------VL------------------LT---QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 166 IQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDL-SSLRFI 241
Cdd:cd17644 150 VLQFASIAFDVAAEEIYVTLLSGATLVLRPeemRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 242 MWGATPVTVSIAETVTRRTG--VRWVPAYGTTELPVIA--CNP----PEQSRLDSVGRPVAGVDVRIvsLD-TGEPVGPG 312
Cdd:cd17644 230 IVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAAtvCRLtqltERNITSVPIGRPIANTQVYI--LDeNLQPVPVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 313 DVGEIQARSASLMAGYL--PAAANAEVWRDGW--------YRTGDVG-WL-DGNgwLRITDRLKEMIKVRGFQVAPAEVE 380
Cdd:cd17644 308 VPGELHIGGVGLARGYLnrPELTAEKFISHPFnsseserlYKTGDLArYLpDGN--IEYLGRIDNQVKIRGFRIELGEIE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 381 TVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPgNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:cd17644 386 AVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYE-ESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
11-461 |
1.19e-24 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 106.36 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 11 DRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLtdpAHAv 90
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITV---SKA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 91 gdHPVLADLMPMLDLDDPIAPAAPITGSPRpgDDAVLVFSSGTTGLPKA--VRHTHASLDAAVRQWrdALRLTERDRIQV 168
Cdd:cd05939 77 --KALIFNLLDPLLTQSSTEPPSQDDVNFR--DKLFYIYTSGTTGLPKAavIVHSRYYRIAAGAYY--AFGMRPEDVVYD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 169 ATPPSHILG-LLNILTALRVGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRfIMWGaTP 247
Cdd:cd05939 151 CLPLYHSAGgIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVR-LAVG-NG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 248 VTVSIAETVTRRTGVRWVPA-YGTTElpviaCNPPEQSRLDSVG----RPVAGVDVRIVSL-----DTGE---------- 307
Cdd:cd05939 229 LRPQIWEQFVRRFGIPQIGEfYGATE-----GNSSLVNIDNHVGacgfNSRILPSVYPIRLikvdeDTGElirdsdglci 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 308 PVGPGD----VGEIQARSASL-MAGYLPAAANA-----EVWRDG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVA 375
Cdd:cd05939 304 PCQPGEpgllVGKIIQNDPLRrFDGYVNEGATNkkiarDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 376 PAEVETVLHSHPAVKDCAVFGVpdgvngeavvaaVATHAPGNTGVAA-----------ELTARVAAQLAPYKRLSRVVFV 444
Cdd:cd05939 384 TTEVEGILSNVLGLEDVVVYGV------------EVPGVEGRAGMAAivdperkvdldRFSAVLAKSLPPYARPQFIRLL 451
|
490
....*....|....*..
gi 576413765 445 PEIPRLPSGKVLRRVLK 461
Cdd:cd05939 452 PEVDKTGTFKLQKTDLQ 468
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
125-462 |
1.37e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 106.76 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 125 AVLVFSSGTTGLPKAVRHTHAS--LDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTS-VRLHPRFDVDR 201
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKlVMPGAKLDGAS 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 202 ILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAEtVTRRTGVRWVPAYGTTE--------- 272
Cdd:PRK06018 260 VYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIK-AFEDMGVEVRHAWGMTEmsplgtlaa 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 273 LPVIACNPPEQSRLDSV---GRPVAGVDVRIVSlDTGEPVgPGD---VGEIQARSASLMAGYLPAAANAeVWRDGWYRTG 346
Cdd:PRK06018 339 LKPPFSKLPGDARLDVLqkqGYPPFGVEMKITD-DAGKEL-PWDgktFGRLKVRGPAVAAAYYRVDGEI-LDDDGFFDTG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 347 DVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNTGVAAELTA 426
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQL-KPGETATREEILK 494
|
330 340 350
....*....|....*....|....*....|....*.
gi 576413765 427 RVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PRK06018 495 YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
206-463 |
3.64e-24 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 105.80 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 206 IENDRITIeMAVAPIA-QALASHPR--LESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL--PVIACNP 280
Cdd:PRK10524 323 VEKYKVNR-MFSAPTAiRVLKKQDPalLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETgwPILAIAR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 281 ---PEQSRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIqarsasLMAGYLPAAANAEVWRDG-------W-------Y 343
Cdd:PRK10524 402 gveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVL------VIEGPLPPGCMQTVWGDDdrfvktyWslfgrqvY 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 344 RTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVV-------AAVATHAPG 416
Cdd:PRK10524 476 STFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVafvvpkdSDSLADREA 555
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 576413765 417 NTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK10524 556 RLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAI 602
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
26-399 |
4.34e-24 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 104.99 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHavgdhpvladlmpmldl 105
Cdd:cd17639 18 FGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 106 ddpiapaapITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDAL--RLTERDRIQVATPPSHILGLLNILT 183
Cdd:cd17639 81 ---------IFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeLLGPDDRYLAYLPLAHIFELAAENV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 184 AL----RVGTSvrlHPRFDVDRILRHIEND----RITIEMAVA------------------PIAQALASHP---RLESYD 234
Cdd:cd17639 152 CLyrggTIGYG---SPRTLTDKSKRGCKGDltefKPTLMVGVPaiwdtirkgvlaklnpmgGLKRTLFWTAyqsKLKALK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 235 L--------------------SSLRFIMWGATPVTVSIAETVTRrTGVRWVPAYGTTELPVIAC-NPPEQSRLDSVGRPV 293
Cdd:cd17639 229 EgpgtplldelvfkkvraalgGRLRYMLSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTvQDPGDLETGRVGPPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 294 AGVDVRIVSLDTG--EPVGPGDVGEIQARSASLMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKV 369
Cdd:cd17639 308 PCCEIKLVDWEEGgySTDKPPPRGEILIRGPNVFKGYYknPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKL 387
|
410 420 430
....*....|....*....|....*....|.
gi 576413765 370 R-GFQVAPAEVETVLHSHPAVKDCAVFGVPD 399
Cdd:cd17639 388 QnGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-460 |
4.83e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.19 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALG 82
Cdd:PRK12316 3072 DAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLE 3151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 ------LTDPAHAVGDHPVLADLMpMLDLDDPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRD 156
Cdd:PRK12316 3152 dsgaqlLLSQSHLRLPLAQGVQVL-DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ 3230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 157 ALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDRILRHIE-NDRITIEMAVAPIAQALASHPRLESYDL 235
Cdd:PRK12316 3231 AYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVElINSEGVDVLHAYPSMLQAFLEEEDAHRC 3310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVTrrTGVRWVPAYGTTELPVIA----CNPPEQSRLdSVGRPVAGVDVRIVSlDTGEPVGP 311
Cdd:PRK12316 3311 TSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVthwqCVEEGKDAV-PIGRPIANRACYILD-GSLEPVPV 3386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 312 GDVGEIQARSASLMAGYLPAAA--------NAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVL 383
Cdd:PRK12316 3387 GALGELYLGGEGLARGYHNRPGltaerfvpDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL 3466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 384 HSHPAVKDCAVFgvpdGVNGEAVVAAVATHAPgNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:PRK12316 3467 LEHPWVREAVVL----AVDGRQLVAYVVPEDE-AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-460 |
2.06e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 104.47 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEV----- 77
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLaymie 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 78 DHALGLTDPAHAVGDHPVLADLMPMLDLDDPIA------PAAPITgSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAV 151
Cdd:PRK12467 1669 DSGIELLLTQSHLQARLPLPDGLRSLVLDQEDDwlegysDSNPAV-NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL 1747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 152 RQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQALASHP 228
Cdd:PRK12467 1748 CATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpgaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD 1827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 229 RLESYDLSsLRFIMWGATPVTVSIAETVTRRTGVRW-VPAYGTTELPV------IACNPPEQSRLDSVGRPVAGVDVRIv 301
Cdd:PRK12467 1828 EQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGlFNLYGPTETAVdvthwtCRRKDLEGRDSVPIGQPIANLSTYI- 1905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 302 sLDTG-EPVGPGDVGEIQARSASLMAGYLP-AAANAEVW------RDG--WYRTGDVGWLDGNGWLRITDRLKEMIKVRG 371
Cdd:PRK12467 1906 -LDASlNPVPIGVAGELYLGGVGLARGYLNrPALTAERFvadpfgTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRG 1984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 372 FQVAPAEVETVLHSHPAVKDCAVFGVpDGVNGEAVVAAVATHAPG-------NTGVAAELTARVAAQLAPYKRLSRVVFV 444
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGlvdddeaQVALRAILKNHLKASLPEYMVPAHLVFL 2063
|
490
....*....|....*.
gi 576413765 445 PEIPRLPSGKVLRRVL 460
Cdd:PRK12467 2064 ARMPLTPNGKLDRKAL 2079
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
6-398 |
3.05e-23 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 101.87 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:PRK09029 21 ALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHAVGDHPvlADLMPMLDLDDPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTH-ASLDAA--VRQWrdaLRLTE 162
Cdd:PRK09029 101 LDFALVLEG--ENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAqAHLASAegVLSL---MPFTA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 163 RDRIQVATPPSHILGLLNILTALRVGTsvRLHPRfdvdrilrhiendritiemAVAPIAQALA--SH----P----RLES 232
Cdd:PRK09029 176 QDSWLLSLPLFHVSGQGIVWRWLYAGA--TLVVR-------------------DKQPLEQALAgcTHaslvPtqlwRLLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 233 YDLS--SLRFIMWGATPVTVSIAETVTRRtGVR-WVpAYGTTELPVIACnPPEQSRLDSVGRPVAGVDVRIVSldtgepv 309
Cdd:PRK09029 235 NRSEplSLKAVLLGGAAIPVELTEQAEQQ-GIRcWC-GYGLTEMASTVC-AKRADGLAGVGSPLPGREVKLVD------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 310 gpgdvGEIQARSASLMAGYlpaaanaevWRD----------GWYRTGDVG-WLDGNgwLRITDRLKEMIKVRGFQVAPAE 378
Cdd:PRK09029 305 -----GEIWLRGASLALGY---------WRQgqlvplvndeGWFATRDRGeWQNGE--LTILGRLDNLFFSGGEGIQPEE 368
|
410 420
....*....|....*....|
gi 576413765 379 VETVLHSHPAVKDcaVFGVP 398
Cdd:PRK09029 369 IERVINQHPLVQQ--VFVVP 386
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
112-465 |
5.01e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 100.12 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 112 AAPITGSPRPGDD-----AVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDalRLTERDRIQVATPPSHILGLLNILTALR 186
Cdd:PRK07824 20 AALLRDALRVGEPidddvALVVATSGTTGTPKGAMLTAAALTASADATHD--RLGGPGQWLLALPAHHIAGLQVLVRSVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 187 VGTS---VRLHPRFDVD---RILRHIENDRITIEMAVAPIAQALASHPRLESydLSSLRFIMWGATPVTVSIAETVTrRT 260
Cdd:PRK07824 98 AGSEpveLDVSAGFDPTalpRAVAELGGGRRYTSLVPMQLAKALDDPAATAA--LAELDAVLVGGGPAPAPVLDAAA-AA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 261 GVRWVPAYGTTELPViACnppeqsrldsV--GRPVAGVDVRIVSldtgepvgpgdvGEIQARSASLMAGYLPAAANAEVW 338
Cdd:PRK07824 175 GINVVRTYGMSETSG-GC----------VydGVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVDPDPFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 339 RDGWYRTGDVGWLDgNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVAThAPGNT 418
Cdd:PRK07824 232 EPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG-DGGPA 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 576413765 419 GVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKELHG 465
Cdd:PRK07824 310 PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFA 356
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
12-463 |
2.45e-22 |
|
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: 99.94 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHAldalsdglgATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGA----------------------AAVLIS 69
Cdd:cd05966 92 REVCRFA---------NVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhsvvfagfsaesladrindaqCKLVIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 70 P--AWKRDE-------VDHALGLTDPAHAV-----GDHPVlaDLMPMLDLD-DPIAPAAPITGSPRP---GDDAVLVFSS 131
Cdd:cd05966 163 AdgGYRGGKviplkeiVDEALEKCPSVEKVlvvkrTGGEV--PMTEGRDLWwHDLMAKQSPECEPEWmdsEDPLFILYTS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 132 GTTGLPKAVRHTHAS-LDAAVRQWRDALRLTERDR------IQVATPPSHIL-G-LLNILTALrVGTSVRLHPrfDVDRI 202
Cdd:cd05966 241 GSTGKPKGVVHTTGGyLLYAATTFKYVFDYHPDDIywctadIGWITGHSYIVyGpLANGATTV-MFEGTPTYP--DPGRY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 203 LRHIENDRITIeMAVAPIA-QALASHPR--LESYDLSSLRFI------------MWGATPV---TVSIAETvtrrtgvrw 264
Cdd:cd05966 318 WDIVEKHKVTI-FYTAPTAiRALMKFGDewVKKHDLSSLRVLgsvgepinpeawMWYYEVIgkeRCPIVDT--------- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 265 vpaYGTTELP--VIACNPPEQS-RLDSVGRPVAGVDVRIVSLDtGEPVGPGDvgeiqarsaslmAGYL------PAAANA 335
Cdd:cd05966 388 ---WWQTETGgiMITPLPGATPlKPGSATRPFFGIEPAILDEE-GNEVEGEV------------EGYLvikrpwPGMART 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 336 eVWRD-------------GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVN 402
Cdd:cd05966 452 -IYGDheryedtyfskfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 403 GEAVV---AAVATHAPgNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:cd05966 531 GEAIYafvTLKDGEEP-SDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
34-404 |
3.08e-22 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 99.69 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 34 GVIAGERVAVMASNRPEFVAA-----------------------------LQAIWRLGAAAVLISPAWKRDEVDHALGLT 84
Cdd:PRK09192 70 GLKPGDRVALIAETDGDFVEAffacqyaglvpvplplpmgfggresyiaqLRGMLASAQPAAIITPDELLPWVNEATHGN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 85 DPAHAVGdhPVLADLMPmldldDPIAPAAPITgsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQW-RDALRLTER 163
Cdd:PRK09192 150 PLLHVLS--HAWFKALP-----EADVALPRPT----PDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIsHDGLKVRPG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 164 DRIQVATPPSHILGLLN-ILTALRVGTSVRLHPRFDVDR----ILRHIENDRITIemAVAP-----IAQALASHPRLESY 233
Cdd:PRK09192 219 DRCVSWLPFYHDMGLVGfLLTPVATQLSVDYLPTRDFARrplqWLDLISRNRGTI--SYSPpfgyeLCARRVNSKDLAEL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 234 DLSSLRFIMWGATPVTVSIAETVTRRTGVR------WVPAYGTTE--LPV-----------------------IACNPPE 282
Cdd:PRK09192 297 DLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEatLAVsfsplgsgivveevdrdrleyqgKAVAPGA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 283 QSRLDS----VGRPVAGVDVRIVSlDTGEPVGPGDVGEIQARSASLMAGYLPAAANAEVWR-DGWYRTGDVGWLDgNGWL 357
Cdd:PRK09192 377 ETRRVRtfvnCGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAaDGWLDTGDLGYLL-DGYL 454
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 576413765 358 RITDRLKEMIKVRGFQVAPAEVETVLHSHPAVK--DCAVFGVPDGvNGE 404
Cdd:PRK09192 455 YITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGE 502
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
123-463 |
3.33e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 99.71 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 123 DDAVLVFSSGTTGLPKAV--RHTHASLDA--AVRQWrdalrlterdriQVATPPSHILGL---------LNILTALRVGT 189
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVviSHRGAYLSTlsAIIGW------------EMGTCPVYLWTLpmfhcngwtFTWGTAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 190 SVRLHpRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVtRRTGVRWVPAYG 269
Cdd:PLN03102 255 SVCMR-HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 270 TTEL--PVIACN-------PPEQSRLDSVGRP------VAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYLP-AAA 333
Cdd:PLN03102 333 LTEAtgPVLFCEwqdewnrLPENQQMELKARQgvsilgLADVDVKNKETQESVPRDGKTMGEIVIKGSSIMKGYLKnPKA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 334 NAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATH 413
Cdd:PLN03102 413 TSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 414 ApGNTGVAAELTARVAAQ--LAPYKRLS--------RVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PLN03102 493 K-GETTKEDRVDKLVTRErdLIEYCRENlphfmcprKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
10-462 |
4.34e-22 |
|
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: 98.66 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLH-HRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTdpah 88
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 89 avGDHPVLADlmpmldlddpiapaapitgsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQV 168
Cdd:cd05937 78 --GSRFVIVD----------------------PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 169 ATP----PSHILGLLNILTAlrvGTSVRLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRlESYDLSSLRFIMWG 244
Cdd:cd05937 134 CMPlyhgTAAFLGACNCLMS---GGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPP-SPYDRDHKVRVAWG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 245 ---------------ATPV-------TVSIAETVTRRTG-------------VRWVpaYGTTELPViACNPPEQsrlDSV 289
Cdd:cd05937 210 nglrpdiwerfrerfNVPEigefyaaTEGVFALTNHNVGdfgagaighhgliRRWK--FENQVVLV-KMDPETD---DPI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 290 GRPVAGVDVRIvsldtgePVG-PGD-VGEIQARSASLMAGYLPAAANAE------VWRDG--WYRTGDVGWLDGNGWLRI 359
Cdd:cd05937 284 RDPKTGFCVRA-------PVGePGEmLGRVPFKNREAFQGYLHNEDATEsklvrdVFRKGdiYFRTGDLLRQDADGRWYF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 360 TDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVP----DGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPY 435
Cdd:cd05937 357 LDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDGRAGCAAITLEESSAVPTEFTKSLLASLARKNLPSY 436
|
490 500
....*....|....*....|....*..
gi 576413765 436 KRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05937 437 AVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
30-396 |
3.52e-21 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 96.34 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 30 LHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAV-------------LISPAWKR-------DEVDHALGLTDPAHA 89
Cdd:cd17641 28 LLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLgiyqdsmaeevayLLNYTGARvviaedeEQVDKLLEIADRIPS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 90 VG-------------DHPVLADLMPMLDLDDPIAPAAPITG-----SPRPGDDAVLVFSSGTTGLPKAVRHTHASLdaaV 151
Cdd:cd17641 108 VRyviycdprgmrkyDDPRLISFEDVVALGRALDRRDPGLYerevaAGKGEDVAVLCTTSGTTGKPKLAMLSHGNF---L 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 152 RQWRDALRLTERDRIQ--VATPPSHILG--LLNILTALRVGTSV--------------RLHPRFDV--DRILRHIENDrI 211
Cdd:cd17641 185 GHCAAYLAADPLGPGDeyVSVLPLPWIGeqMYSVGQALVCGFIVnfpeepetmmedlrEIGPTFVLlpPRVWEGIAAD-V 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 212 TIEMAVA-PIAQ------------ALASHPRLESYDLSsLRFIMWGATPVT------------VSIAET----------- 255
Cdd:cd17641 264 RARMMDAtPFKRfmfelgmklglrALDRGKRGRPVSLW-LRLASWLADALLfrplrdrlgfsrLRSAATggaalgpdtfr 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 256 VTRRTGVRWVPAYGTTELPVIACNPPE-QSRLDSVGRPVAGVDVRIVsldtgepvgpgDVGEIQARSASLMAGYL--PAA 332
Cdd:cd17641 343 FFHAIGVPLKQLYGQTELAGAYTVHRDgDVDPDTVGVPFPGTEVRID-----------EVGEILVRSPGVFVGYYknPEA 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576413765 333 ANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKV-RGFQVAPAEVETVLHSHPAVKDCAVFG 396
Cdd:cd17641 412 TAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
6-460 |
5.07e-21 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 96.65 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTD 85
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDAR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PA---HAVGDHPVLADL--MPMLDLDDPIAPA-APITGSPRPGDDAVLVFSSGTTGLPKAVRHTHaslDAAVRQ--W-RD 156
Cdd:PRK10252 556 PSlliTTADQLPRFADVpdLTSLCYNAPLAPQgAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ---TAIVNRllWmQN 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 157 ALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHP---RFDVDRILRHIENDRITIEMAVAPIAQAL--ASHPRLE 231
Cdd:PRK10252 633 HYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEpeaHRDPLAMQQFFAEYGVTTTHFVPSMLAAFvaSLTPEGA 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 232 SYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPV-IACNPPEQSRLDSV-------GRPVAGVDVRIVSl 303
Cdd:PRK10252 713 RQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdVSWYPAFGEELAAVrgssvpiGYPVWNTGLRILD- 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 304 DTGEPVGPGDVGEIQARSASLMAGYL-------------PAAANAEVwrdgwYRTGDVG-WLDgNGWLRITDRLKEMIKV 369
Cdd:PRK10252 792 ARMRPVPPGVAGDLYLTGIQLAQGYLgrpdltasrfiadPFAPGERM-----YRTGDVArWLD-DGAVEYLGRSDDQLKI 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 370 RGFQVAPAEVETVLHSHPAVKD-----CAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFV 444
Cdd:PRK10252 866 RGQRIELGEIDRAMQALPDVEQavthaCVINQAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQL 945
|
490
....*....|....*.
gi 576413765 445 PEIPRLPSGKVLRRVL 460
Cdd:PRK10252 946 DQLPLSANGKLDRKAL 961
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
116-396 |
3.31e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 93.73 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 116 TGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVR-------QWRDalRLTERDRIQVATPPSHILGLLNILTALRVG 188
Cdd:PLN02430 214 TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlfmeQFED--KMTHDDVYLSFLPLAHILDRMIEEYFFRKG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 189 TSV---------------RLHPRF--DVDRILRHIENDritIEMAV-------------------------------API 220
Cdd:PLN02430 292 ASVgyyhgdlnalrddlmELKPTLlaGVPRVFERIHEG---IQKALqelnprrrlifnalykyklawmnrgyshkkaSPM 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 221 AQALASHpRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL--PVIACNPPEQSRLDSVGRPVAGVDV 298
Cdd:PLN02430 369 ADFLAFR-KVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlgPTTLGFPDEMCMLGTVGAPAVYNEL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 299 RI--VSLDTGEPVGPGDVGEIQARSASLMAGYL--PAAANaEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKV-RGFQ 373
Cdd:PLN02430 448 RLeeVPEMGYDPLGEPPRGEICVRGKCLFSGYYknPELTE-EVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEY 526
|
330 340
....*....|....*....|...
gi 576413765 374 VAPAEVETVLHSHPAVKDCAVFG 396
Cdd:PLN02430 527 VALEYLENVYGQNPIVEDIWVYG 549
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
116-462 |
8.03e-20 |
|
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: 92.11 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 116 TGSP-----RPGDDA---VLVFSSGTTGLPKAVRHTH--ASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTAL 185
Cdd:cd05915 139 EALGeeadpVRVPERaacGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAAT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 186 RVGtsvrlhprfDVDRILRHIENDRITIEMAVAPIAQALASHPRL--------ESYDLS---SLRFIMWGATPVTVSIae 254
Cdd:cd05915 219 LVG---------AKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVwlaladylESTGHRlktLRRLVVGGSAAPRSLI-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 255 TVTRRTGVRWVPAYGTTE----------LPVIACNPPEQS-RL---DSVGRPVAGVDVrivsLDTGEPVGPGD---VGEI 317
Cdd:cd05915 288 ARFERMGVEVRQGYGLTEtspvvvqnfvKSHLESLSEEEKlTLkakTGLPIPLVRLRV----ADEEGRPVPKDgkaLGEV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 318 QARSASLMAGYLP--AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVF 395
Cdd:cd05915 364 QLKGPWITGGYYGneEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVV 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 396 GVPDGVNGEAV-VAAVATHAPGNTGVAAELTARvaaQLAPYKRLSR-VVFVPEIPRLPSGKVLRRVLKE 462
Cdd:cd05915 444 AIPHPKWQERPlAVVVPRGEKPTPEELNEHLLK---AGFAKWQLPDaYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
21-404 |
4.92e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 89.84 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 21 ALSDGLGATlhhrgviAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDhPVLAD-L 99
Cdd:PRK05620 54 ALHDELGIT-------GDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEqL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 100 MPML---------------DLDDPIAPAAP----------ITGSPRPGD--------DAVLVFSSGTTGLPKAVRHTHAS 146
Cdd:PRK05620 126 GEILkecpcvravvfigpsDADSAAAHMPEgikvysyealLDGRSTVYDwpeldettAAAICYSTGTTGAPKGVVYSHRS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 147 LDAAVRQWR--DALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLhPRFDVD--RILRHIENDRITIEMAVAPIAQ 222
Cdd:PRK05620 206 LYLQSLSLRttDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVF-PGPDLSapTLAKIIATAMPRVAHGVPTLWI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 223 ALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIA--CNPPE----QSRLD---SVGRPV 293
Cdd:PRK05620 285 QLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGtvARPPSgvsgEARWAyrvSQGRFP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 294 AGVDVRIVslDTGEPVGPGD--VGEIQARSASLMAGYL---------PAA---------ANAEVWRDGWYRTGDVGWLDG 353
Cdd:PRK05620 365 ASLEYRIV--NDGQVMESTDrnEGEIQVRGNWVTASYYhspteegggAAStfrgedvedANDRFTADGWLRTGDVGSVTR 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 576413765 354 NGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGE 404
Cdd:PRK05620 443 DGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGE 493
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
249-461 |
1.85e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 84.90 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 249 TVSIAETVTRRTGVRWVPAYgtTELPviacnPPEQSRLDS------VGrpVAGVDVriVSLDTGEPVgPGD---VGEIQA 319
Cdd:PLN02479 340 TYGLSETYGPSTVCAWKPEW--DSLP-----PEEQARLNArqgvryIG--LEGLDV--VDTKTMKPV-PADgktMGEIVM 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 320 RSASLMAGYLP-AAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVP 398
Cdd:PLN02479 408 RGNMVMKGYLKnPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 399 DGVNGEA----VVAAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPeIPRLPSGKVLRRVLK 461
Cdd:PLN02479 488 DERWGESpcafVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLR 553
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
121-459 |
2.15e-17 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 84.05 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 121 PGDDAVLVF-SSGTTGLPKAVRHTHASLDAAVRQWRDALR---LTERDRIQVATPpshiLGL----LNILTAL-RVGTSV 191
Cdd:COG1541 81 PLEEIVRIHaSSGTTGKPTVVGYTRKDLDRWAELFARSLRaagVRPGDRVQNAFG----YGLftggLGLHYGAeRLGATV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 192 RLHPRFDVDRILRHIENDRITIEMAVAPIAQALASHPRLESYDL--SSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYG 269
Cdd:COG1541 157 IPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 270 TTEL-PVIACNPPEQSRL----DSVgrpvagvDVRIVSLDTGEPVGPGDVGEIqarsaslmagylpaaanaeVW----RD 340
Cdd:COG1541 237 LTEVgPGVAYECEAQDGLhiweDHF-------LVEIIDPETGEPVPEGEEGEL-------------------VVttltKE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 341 GW----YRTGDVG-WLDGN---GW-----LRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVpDGVNGEAVV 407
Cdd:COG1541 291 AMplirYRTGDLTrLLPEPcpcGRthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVV-DREGGLDEL 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 576413765 408 AAVATHAPGNTgvAAELTARVAAQLAPYKRLS-RVVFVP--EIPRLPsGKVlRRV 459
Cdd:COG1541 370 TVRVELAPGAS--LEALAEAIAAALKAVLGLRaEVELVEpgSLPRSE-GKA-KRV 420
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
119-396 |
3.16e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 84.38 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 119 PRPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHpRFD 198
Cdd:PLN02736 218 PKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFY-QGD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 199 VDRILRHIENDRITI------------------------------EMAVAPIAQALAS----HPRLESYDLSSL------ 238
Cdd:PLN02736 297 NLKLMDDLAALRPTIfcsvprlynriydgitnavkesgglkerlfNAAYNAKKQALENgknpSPMWDRLVFNKIkaklgg 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 239 --RFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELP-VIACNPPEQSRLDSVGRPVAGVDVRIVSLD----TGEPvGP 311
Cdd:PLN02736 377 rvRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETScVISGMDEGDNLSGHVGSPNPACEVKLVDVPemnyTSED-QP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 312 GDVGEIQARSASLMAGYLPAAANA-EVW-RDGWYRTGDVG-WLDGnGWLRITDRLKEMIKV-RGFQVAPAEVETVLHSHP 387
Cdd:PLN02736 456 YPRGEICVRGPIIFKGYYKDEVQTrEVIdEDGWLHTGDIGlWLPG-GRLKIIDRKKNIFKLaQGEYIAPEKIENVYAKCK 534
|
....*....
gi 576413765 388 AVKDCAVFG 396
Cdd:PLN02736 535 FVAQCFVYG 543
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
12-391 |
4.44e-17 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 83.72 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVG 91
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 92 dhpvladlmpmldlddpIAPAAPITGsprPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQVATP 171
Cdd:cd17647 99 -----------------IRAAGVVVG---PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 172 PSHILGLLNILTALRVGTSVRLHPRFDV---DRILRHIENDRITIE-----MAVAPIAQALASHPRLesydlssLRFIMW 243
Cdd:cd17647 159 IAHDPIQRDMFTPLFLGAQLLVPTQDDIgtpGRLAEWMAKYGATVThltpaMGQLLTAQATTPFPKL-------HHAFFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 244 GATPVTVSIAETVTRRTGVRWVPAYGTTE---------LPVIACNPPEQSRLDSV---GRPVAGVDVRIVS-LDTGEPVG 310
Cdd:cd17647 232 GDILTKRDCLRLQTLAENVRIVNMYGTTEtqravsyfeVPSRSSDPTFLKNLKDVmpaGRGMLNVQLLVVNrNDRTQICG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 311 PGDVGEIQARSASLMAGY--LPA---------------------AANAEVWRDGW-------YRTGDVGWLDGNGWLRIT 360
Cdd:cd17647 312 IGEVGEIYVRAGGLAEGYrgLPElnkekfvnnwfvepdhwnyldKDNNEPWRQFWlgprdrlYRTGDLGRYLPNGDCECC 391
|
410 420 430
....*....|....*....|....*....|.
gi 576413765 361 DRLKEMIKVRGFQVAPAEVETVLHSHPAVKD 391
Cdd:cd17647 392 GRADDQVKIRGFRIELGEIDTHISQHPLVRE 422
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
10-442 |
7.20e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.06 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLHHRGVIaGERVAVMASNRPEFVAALQAIWRLGAAAVlisPAW-----KR---------- 74
Cdd:PRK05691 37 EGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PAYppesaRRhhqerllsii 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 75 DEVDHALGLTD----PAHAVGDHPVLADLMPMLDLD--DPIAPAAPITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLD 148
Cdd:PRK05691 113 ADAEPRLLLTVadlrDSLLQMEELAAANAPELLCVDtlDPALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 149 AAVRQWRD--ALRLTERDRIQVATPPSHILGLL-NILTALRVGTS-VRLHPRFDVDRILRHIE---NDRITI-------- 213
Cdd:PRK05691 193 ANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIgGLLQPIFSGVPcVLMSPAYFLERPLRWLEaisEYGGTIsggpdfay 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 214 EMAVAPIAQAlashpRLESYDLSSLRFIMWGATPVTVSIAETVTRR------TGVRWVPAYGTTE-------------LP 274
Cdd:PRK05691 273 RLCSERVSES-----ALERLDLSRWRVAYSGSEPIRQDSLERFAEKfaacgfDPDSFFASYGLAEatlfvsggrrgqgIP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 275 VIACN----------PPEQSRLDSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYL---PAAANAEVWRDG 341
Cdd:PRK05691 348 ALELDaealarnraePGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWrnpEASAKTFVEHDG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 --WYRTGDVGWLDgNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAV---KDCAVFGVPDgvNGEAvvaavathapg 416
Cdd:PRK05691 428 rtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkGRVAAFAVNH--QGEE----------- 493
|
490 500
....*....|....*....|....*....
gi 576413765 417 NTGVAAELTARVAAQLAP---YKRLSRVV 442
Cdd:PRK05691 494 GIGIAAEISRSVQKILPPqalIKSIRQAV 522
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
127-460 |
9.96e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 82.87 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 127 LVFSSGTTGLPKA-VRHTHASLDAAVRQWR------DALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDV 199
Cdd:PTZ00237 259 ILYTSGTTGNSKAvVRSNGPHLVGLKYYWRsiiekdIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKHIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 200 DRILRHIENDRITIEMAVA----------PIAQALAShprleSYDLSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYG 269
Cdd:PTZ00237 339 DDLWNTIEKHKVTHTLTLPktiryliktdPEATIIRS-----KYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 270 TTE------LPVIACNPPeqsrLDSVGRPVAGVDVRIVSLDtGEPVGPGDVGEIqarsaSLMAGYLPAAA-----NAEVW 338
Cdd:PTZ00237 414 QTEigitylYCYGHINIP----YNATGVPSIFIKPSILSED-GKELNVNEIGEV-----AFKLPMPPSFAttfykNDEKF 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 339 RD------GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGV--PDGVNGEAVV--- 407
Cdd:PTZ00237 484 KQlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIydPDCYNVPIGLlvl 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 576413765 408 -AAVATHAPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:PTZ00237 564 kQDQSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
378-454 |
1.93e-16 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 73.73 E-value: 1.93e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576413765 378 EVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHaPGNTGVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGK 454
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLK-PGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-460 |
3.97e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 81.75 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 3 EPAALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDH--- 79
Cdd:PRK05691 2203 QAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYmie 2282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 80 ----ALGLTDPA--HAVGDHPV------LADLMPMLDlDDPIAPAAPITGsprPGDDAVLVFSSGTTGLPKAVRHTHASL 147
Cdd:PRK05691 2283 dsgiGLLLSDRAlfEALGELPAgvarwcLEDDAAALA-AYSDAPLPFLSL---PQHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 148 DAAVRQWRDALRLTERD--------RIQVATPpshilgllNILTALRVGTSV--RLHPRFDVDRILRHIENDRITIeMAV 217
Cdd:PRK05691 2359 AMHCQAVIERFGMRADDcelhfysiNFDAASE--------RLLVPLLCGARVvlRAQGQWGAEEICQLIREQQVSI-LGF 2429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 218 AP-----IAQALASHprlesYDLSSLRFIMWGATPVTvsiAETVTRRTGVrWVP-----AYGTTELPV--IACNPPEQSR 285
Cdd:PRK05691 2430 TPsygsqLAQWLAGQ-----GEQLPVRMCITGGEALT---GEHLQRIRQA-FAPqlffnAYGPTETVVmpLACLAPEQLE 2500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 286 LDSVGRP---VAGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGYLP-AAANAEVW------RDG--WYRTGDVGWLDG 353
Cdd:PRK05691 2501 EGAASVPigrVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDrPGLTAERFvadpfaADGgrLYRTGDLVRLRA 2580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 354 NGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVAAVATHAPGNTGVAAELTARVAA--- 430
Cdd:PRK05691 2581 DGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALREALKAhlk 2660
|
490 500 510
....*....|....*....|....*....|.
gi 576413765 431 -QLAPYKRLSRVVFVPEIPRLPSGKVLRRVL 460
Cdd:PRK05691 2661 qQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
10-398 |
9.69e-16 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 79.64 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLH-HRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAH 88
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 89 AVGD---HPVLADLMPML--------------------DLDDPI--APAAPITGSPRPG----DDAVLVFSSGTTGLPKA 139
Cdd:cd05938 82 LVVApelQEAVEEVLPALradgvsvwylshtsntegviSLLDKVdaASDEPVPASLRAHvtikSPALYIYTSGTTGLPKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 140 VRHTHasldaaVRQWRDA--LRL---TERDRIQVATPPSHILG-LLNILTALRVGTSVRLHPRFDVDRILRHIENDRITI 213
Cdd:cd05938 162 ARISH------LRVLQCSgfLSLcgvTADDVIYITLPLYHSSGfLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 214 EMAVAPIAQALASHPRLESYDLSSLRFIMwgATPVTVSIAETVTRRTG-VRWVPAYGTTELPVIACNPPeqSRLDSVGRp 292
Cdd:cd05938 236 IQYIGELLRYLCNQPQSPNDRDHKVRLAI--GNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNYT--GKIGAVGR- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 293 vAGVDVRIVS--------LDTGEP----------VGPGDVGEIQAR--SASLMAGYLPAAANAE------VWRDG--WYR 344
Cdd:cd05938 311 -VSYLYKLLFpfelikfdVEKEEPvrdaqgfcipVAKGEPGLLVAKitQQSPFLGYAGDKEQTEkkllrdVFKKGdvYFN 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 576413765 345 TGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVP 398
Cdd:cd05938 390 TGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
288-463 |
6.54e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 74.02 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 288 SVGRPVAGVDVRIVSlDTGEPVGPGDvgeiqarsaslmAGYL------PAAANAeVWRD-------------GWYRTGDV 348
Cdd:PRK00174 425 SATRPLPGIQPAVVD-EEGNPLEGGE------------GGNLvikdpwPGMMRT-IYGDherfvktyfstfkGMYFTGDG 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 349 GWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEAVVA--AVATHAPGNTGVAAELTA 426
Cdd:PRK00174 491 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAfvTLKGGEEPSDELRKELRN 570
|
170 180 190
....*....|....*....|....*....|....*..
gi 576413765 427 RVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PRK00174 571 WVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKI 607
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
25-401 |
4.27e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 71.55 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 25 GLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPVLADLMPMLD 104
Cdd:PTZ00216 133 NFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 105 LDdpIAPAAPI-----------------------------TGSPRPG------DDAVLV-FSSGTTGLPKAVRHTHASLD 148
Cdd:PTZ00216 213 SG--GMPNTTIiyldslpasvdtegcrlvawtdvvakghsAGSHHPLnipennDDLALImYTSGTTGDPKGVMHTHGSLT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 149 A---AVRQW-RDALRLTERDRIQVA-TPPSHI--LGLLNILTALRV----GTSVRL-----HPRFD-----------VDR 201
Cdd:PTZ00216 291 AgilALEDRlNDLIGPPEEDETYCSyLPLAHImeFGVTNIFLARGAligfGSPRTLtdtfaRPHGDltefrpvfligVPR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 202 ILRHIendRITIEMAVAPIA--------QALAShpRL----ESYDL----------------SSLRFIMWGATPVTVSIA 253
Cdd:PTZ00216 371 IFDTI---KKAVEAKLPPVGslkrrvfdHAYQS--RLralkEGKDTpywnekvfsapravlgGRVRAMLSGGGPLSAATQ 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 254 ETVTRRTGvRWVPAYGTTElpvIACNPPEQSRLD----SVGRPVAGVDVRIVSL------DTGEPVGpgdvgEIQARSAS 323
Cdd:PTZ00216 446 EFVNVVFG-MVIQGWGLTE---TVCCGGIQRTGDlepnAVGQLLKGVEMKLLDTeeykhtDTPEPRG-----EILLRGPF 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 324 LMAGYL--PAAANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIK-VRGFQVAPAEVETVLHSHPAVkdcavfgVPDG 400
Cdd:PTZ00216 517 LFKGYYkqEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNELV-------VPNG 589
|
.
gi 576413765 401 V 401
Cdd:PTZ00216 590 V 590
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
237-396 |
4.80e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 71.21 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 237 SLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE--LPVIACNPPEQSRLDSVGRPVAGVDVRIVSLDTGE--PVGPG 312
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEydALAST 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 313 DVGEIQARSASLMAGYLPAA-ANAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKV-RGFQVAPAEVETVLHSHPAVK 390
Cdd:PLN02614 467 PRGEICIRGKTLFSGYYKREdLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVD 546
|
....*.
gi 576413765 391 DCAVFG 396
Cdd:PLN02614 547 SVWVYG 552
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
41-392 |
6.36e-13 |
|
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: 70.85 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 41 VAVMASNRPE-FVAALQAIwRLGAAAVLISPAWKRDEVDHALgltDPAHA----VGDHPVLADLMPMLD----------L 105
Cdd:cd05933 36 VGILGFNSPEwFIAAVGAI-FAGGIAVGIYTTNSPEACQYVA---ETSEAnilvVENQKQLQKILQIQDklphlkaiiqY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 106 DDPIAPAAP----------------------ITGSPRPGDDAVLVFSSGTTGLPKAVRHTHASLD---AAVRQWRDALRL 160
Cdd:cd05933 112 KEPLKEKEPnlyswdefmelgrsipdeqldaIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITwtaKAASQHMDLRPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 161 TERDRIQVA-TPPSHILG-LLNILTALRVG-------------------TSVRLHPRFDVDRILRHIENDRITIEMAVAP 219
Cdd:cd05933 192 TVGQESVVSyLPLSHIAAqILDIWLPIKVGgqvyfaqpdalkgtlvktlREVRPTAFMGVPRVWEKIQEKMKAVGAKSGT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 220 IAQALA------------------SHPRL--------------ESYDLSSLRFIMWGATPVTvsiAETVTRRTGV--RWV 265
Cdd:cd05933 272 LKRKIAswakgvgletnlklmggeSPSPLfyrlakklvfkkvrKALGLDRCQKFFTGAAPIS---RETLEFFLSLniPIM 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 266 PAYGTTEL--PVIACNPpEQSRLDSVGRPVAGVDVRIVsldtgEPVGPGDvGEIQARSASLMAGYL--PAAANAEVWRDG 341
Cdd:cd05933 349 ELYGMSETsgPHTISNP-QAYRLLSCGKALPGCKTKIH-----NPDADGI-GEICFWGRHVFMGYLnmEDKTEEAIDEDG 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 576413765 342 WYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQ-VAPAEVETvlhshpAVKDC 392
Cdd:cd05933 422 WLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIED------AVKKE 467
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
23-398 |
1.14e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 70.15 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 23 SDGLGATLHHRGviagERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPVLADLMPM 102
Cdd:PLN02387 120 ASGLVALGHNKE----ERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 103 ------------LDLDDPIAPAAPITGS-----------------------PRPGDDAVLVFSSGTTGLPKAVRHTHASL 147
Cdd:PLN02387 196 ssqletvkrviyMDDEGVDSDSSLSGSSnwtvssfseveklgkenpvdpdlPSPNDIAVIMYTSGSTGLPKGVMMTHGNI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 148 DAAVRQWRDAL-RLTERDRIQVATPPSHILGLLNILTALRVGTSV---RLHPRFDV-DRILRHIEND----RITIEMAVA 218
Cdd:PLN02387 276 VATVAGVMTVVpKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIgygSPLTLTDTsNKIKKGTKGDasalKPTLMTAVP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 219 PI------------------AQAL---ASHPRLESYDLS--------------------------SLRFIMWGATPVTVS 251
Cdd:PLN02387 356 AIldrvrdgvrkkvdakgglAKKLfdiAYKRRLAAIEGSwfgawglekllwdalvfkkiravlggRIRFMLSGGAPLSGD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 252 IAETVTRRTGVRWVPAYGTTElpviACNPPEQSRLD--SVGR---PVAGVDVRIVSLDTGepvG------PGDVGEIQAR 320
Cdd:PLN02387 436 TQRFINICLGAPIGQGYGLTE----TCAGATFSEWDdtSVGRvgpPLPCCYVKLVSWEEG---GylisdkPMPRGEIVIG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 321 SASLMAGYLPAAANA-EVWRDG-----WYRTGDVGWLDGNGWLRITDRLKEMIKVR-GFQVAPAEVETVLHSHPAVKDCA 393
Cdd:PLN02387 509 GPSVTLGYFKNQEKTdEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIM 588
|
....*
gi 576413765 394 VFGVP 398
Cdd:PLN02387 589 VHADP 593
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2-470 |
1.23e-12 |
|
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: 69.99 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 2 TEPAALVI----EDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFV------AALQAIWR-----LGAAAV 66
Cdd:cd05943 83 DDPAAIYAaedgERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVvamlatASIGAIWSscspdFGVPGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 67 L-----ISPA---------WKRDEVDHA-------LGLTDPAHAV------GDHPV-LADLMPMLDLDDPIA--PAAPIT 116
Cdd:cd05943 163 LdrfgqIEPKvlfavdaytYNGKRHDVRekvaelvKGLPSLLAVVvvpytvAAGQPdLSKIAKALTLEDFLAtgAAGELE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 117 GSPRPGDDAVLV-FSSGTTGLPKAVRHTHASLdaaVRQWRDALRL----TERDRIQVATPPSHIlgLLNIL-TALRVGTS 190
Cdd:cd05943 243 FEPLPFDHPLYIlYSSGTTGLPKCIVHGAGGT---LLQHLKEHILhcdlRPGDRLFYYTTCGWM--MWNWLvSGLAVGAT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 191 VRL------HPrfDVDRILRHIENDRITIEMAVAPIAQALAS---HPRlESYDLSSLRFIMWGATPVTVSiaetvtrrtG 261
Cdd:cd05943 318 IVLydgspfYP--DTNALWDLADEEGITVFGTSAKYLDALEKaglKPA-ETHDLSSLRTILSTGSPLKPE---------S 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 262 VRWVPAYGTTELP---------VIAC----NPpeqsrLDSVGR-----PVAGVDVRIVSlDTGEPVgPGDVGEIQARSAS 323
Cdd:cd05943 386 FDYVYDHIKPDVLlasisggtdIISCfvggNP-----LLPVYRgeiqcRGLGMAVEAFD-EEGKPV-WGEKGELVCTKPF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 324 L-MAGYLPAAANAEVWRD-------GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVF 395
Cdd:cd05943 459 PsMPVGFWNDPDGSRYRAayfakypGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVV 538
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 396 GVpDGVNGEAVVAAVATHAPGNT---GVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE-LHGCPSDN 470
Cdd:cd05943 539 GQ-EWKDGDERVILFVKLREGVElddELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKiIAGRPVKN 616
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-463 |
4.81e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 68.66 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 11 DRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLT------ 84
Cdd:PRK05691 3743 DQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSrtpvlv 3822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 85 -DPAHAVGDHPVLADL----MPMLDLDDPIAPAAPITGSPR----PGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWR 155
Cdd:PRK05691 3823 cSAACREQARALLDELgcanRPRLLVWEEVQAGEVASHNPGiysgPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKV 3902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 156 DALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPR---FDVDRILRHIENDRITIEMAVAPIAQALASHPRLEs 232
Cdd:PRK05691 3903 PYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNaiaHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA- 3981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 233 ydLSSLRFIM--WGATPVTVSiAETVTRRTGVRWVPAYGTTE-------LPVIACNppEQSRLDSVGRPVAgvDVRIVSL 303
Cdd:PRK05691 3982 --LDGLRWMLptGEAMPPELA-RQWLQRYPQIGLVNAYGPAEcsddvafFRVDLAS--TRGSYLPIGSPTD--NNRLYLL 4054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 304 DTGEPVGP-GDVGEIQARSASLMAGYL-------------PAAANAEvwrdGWYRTGDVGWLDGNGWLRITDRLKEMIKV 369
Cdd:PRK05691 4055 DEALELVPlGAVGELCVAGTGVGRGYVgdplrtalafvphPFGAPGE----RLYRTGDLARRRSDGVLEYVGRIDHQVKI 4130
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 370 RGFQVAPAEVETVLHSHPAVKDCAVfGVPDGVNGEAVV----AAVATHAPGntGVAAELTARVAAQLAPYKRLSRVVFVP 445
Cdd:PRK05691 4131 RGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVgylvPHQTVLAQG--ALLERIKQRLRAELPDYMVPLHWLWLD 4207
|
490
....*....|....*...
gi 576413765 446 EIPRLPSGKVLRRVLKEL 463
Cdd:PRK05691 4208 RLPLNANGKLDRKALPAL 4225
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
6-458 |
6.19e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 68.21 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISP------AWKRDEVDH 79
Cdd:PRK07868 465 FLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPdtdlaaAVRLGGVTE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 80 AlgLTDPAH--AVGDHPV--------------LADLMPMLDLD--DPIAPAAPITGSPRPG---DDAVLVFS-SGTTGLP 137
Cdd:PRK07868 545 I--ITDPTNleAARQLPGrvlvlgggesrdldLPDDADVIDMEkiDPDAVELPGWYRPNPGlarDLAFIAFStAGGELVA 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 138 KAVRHTHASLDAAVRQwrDALRLTERDRIQVATPPSHILGLLNILTALRVGTS-VRLHPRFDVDRILRHIENDRITI--- 213
Cdd:PRK07868 623 KQITNYRWALSAFGTA--SAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSrIALSRGLDPDRFVQEVRQYGVTVvsy 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 214 ------EMAVAPIAQALASHPrlesydlssLRFIMWGATPVTVSiaetvtRRTGVRWVPA-----YGTTELPVIACNpPE 282
Cdd:PRK07868 701 twamlrEVVDDPAFVLHGNHP---------VRLFIGSGMPTGLW------ERVVEAFAPAhvvefFATTDGQAVLAN-VS 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 283 QSRLDSVGRPVAG-----------VDVRIVSLDTG--EPVGPGDVGEIQAR-------SASLMAGYLPAAanaevwrDGW 342
Cdd:PRK07868 765 GAKIGSKGRPLPGagrvelaaydpEHDLILEDDRGfvRRAEVNEVGVLLARargpidpTASVKRGVFAPA-------DTW 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 343 YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGvnGEAVVAAVATHAPGNTGVAA 422
Cdd:PRK07868 838 ISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVG--GRQLAVAAVTLRPGAAITAA 915
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 576413765 423 ELTARVAAqLAPYKRLSRVVFVPEIPRL----PSGKVLRR 458
Cdd:PRK07868 916 DLTEALAS-LPVGLGPDIVHVVPEIPLSatyrPTVSALRA 954
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
6-465 |
6.99e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 67.23 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 6 ALVIEDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLI---SPAwkrDEVDHALG 82
Cdd:PRK04813 20 AYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVdvsSPA---ERIEMIIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 83 LTDPAH--AVGDHPVLADLMPMLDLDD----PIAPAAPITGSPRPGDDAV-LVFSSGTTGLPKAVRHTHASLDAAVrQWR 155
Cdd:PRK04813 97 VAKPSLiiATEELPLEILGIPVITLDElkdiFATGNPYDFDHAVKGDDNYyIIFTSGTTGKPKGVQISHDNLVSFT-NWM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 156 -DALRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDR---ILRHIENDRITI--------EMAvapiaqa 223
Cdd:PRK04813 176 lEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANfkqLFETLPQLPINVwvstpsfaDMC------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 224 LAShPRLESYDLSSL-RFIMWGATpVTVSIAET-VTRRTGVRWVPAYGTTELPV----IACNPPEQSRLDS--VGRPVAg 295
Cdd:PRK04813 249 LLD-PSFNEEHLPNLtHFLFCGEE-LPHKTAKKlLERFPSATIYNTYGPTEATVavtsIEITDEMLDQYKRlpIGYAKP- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 296 vDVRIVSLD-TGEPVGPGDVGEIQARSASLMAGYL--PA-AANAEVWRDGW--YRTGDVGWLDgNGWLRITDRLKEMIKV 369
Cdd:PRK04813 326 -DSPLLIIDeEGTKLPDGEQGEIVISGPSVSKGYLnnPEkTAEAFFTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 370 RGFQVAPAEVETVLHSHPAVKDCAVfgVP---DG-----------VNGEAVVAAVATHApgntgVAAELTARVAAQLAPy 435
Cdd:PRK04813 404 NGYRIELEEIEQNLRQSSYVESAVV--VPynkDHkvqyliayvvpKEEDFEREFELTKA-----IKKELKERLMEYMIP- 475
|
490 500 510
....*....|....*....|....*....|.
gi 576413765 436 krlSRVVFVPEIPRLPSGKVLR-RVLKELHG 465
Cdd:PRK04813 476 ---RKFIYRDSLPLTPNGKIDRkALIEEVNK 503
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
49-394 |
4.31e-11 |
|
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: 64.80 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 49 PEFVAALQAIWRLGAAAVLISPAWKRDEVDHALGLTDPAHAVGDHPVLadlmpmlDLDDPIAPAAPITGSPRPGDDAVLV 128
Cdd:cd17654 52 TESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKELD-------NAPLSFTPEHRHFNIRTDECLAYVI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 129 FSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTeRDRIQVATPPSH--------ILGLLNILTALRVGTSVRLHPRFDVD 200
Cdd:cd17654 125 HTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT-SEDILFLTSPLTfdpsvveiFLSLSSGATLLIVPTSVKVLPSKLAD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 201 RILRHienDRITIEMAVAPIAQALASHPRLESY--DLSSLRFIMWGATPvTVSIAETVTRR---TGVRWVPAYGTTELPV 275
Cdd:cd17654 204 ILFKR---HRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEP-FPSLVILSSWRgkgNRTRIFNIYGITEVSC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 276 IACN---PPEQSRLdSVGRPVAGVDVRIVSLDTGEPVGPGDVGEIQARsaslmaGYLPAAANaeVWRDGWYRTGDvgWLD 352
Cdd:cd17654 280 WALAykvPEEDSPV-QLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRV------CILDDEVT--VPKGTMRATGD--FVT 348
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 576413765 353 -GNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAV 394
Cdd:cd17654 349 vKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV 391
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
341-463 |
1.46e-10 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 63.38 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 341 GWYRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHSHPAVKDCAVFGVPDGVNGEA--VVAAVATHAPGNT 418
Cdd:PLN02654 513 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGiyAFVTLVEGVPYSE 592
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 576413765 419 GVAAELTARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKEL 463
Cdd:PLN02654 593 ELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
12-396 |
1.96e-10 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 62.83 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 12 RRVS-RHALDAlSDGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHA-----LGLTD 85
Cdd:cd05921 24 RRVTyAEALRQ-VRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAklkhlFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 86 PAHA-VGDHPVLADLMPMLDLDD-------------------------PIAPAAPITGSPRPGDDAVLVFSSGTTGLPKA 139
Cdd:cd05921 103 PGLVfAQDAAPFARALAAIFPLGtplvvsrnavagrgaisfaelaatpPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 140 VRHTHASLdAAVRQWRDALRLTERDRIQVAT---PPSHILGL-LNILTALRVGTSVRL---HP---RFdvDRILRHIEND 209
Cdd:cd05921 183 VINTQRML-CANQAMLEQTYPFFGEEPPVLVdwlPWNHTFGGnHNFNLVLYNGGTLYIddgKPmpgGF--EETLRNLREI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 210 RITIEMAV----APIAQALASHPRLESYDLSSLRFIMWGATPVTVSIAETVTR----RTG--VRWVPAYGTTELPVIACN 279
Cdd:cd05921 260 SPTVYFNVpagwEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGerIPMMAGLGATETAPTATF 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 280 PPE-QSRLDSVGRPVAGVDVRIVsldtgePVgpGDVGEIQARSASLMAGYLPAA-ANAEVW-RDGWYRTGDVGWL----D 352
Cdd:cd05921 340 THWpTERSGLIGLPAPGTELKLV------PS--GGKYEVRVKGPNVTPGYWRQPeLTAQAFdEEGFYCLGDAAKLadpdD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 576413765 353 GNGWLRITDRLKEMIKVRG---FQVAPAEVETVLHSHPAVKDCAVFG 396
Cdd:cd05921 412 PAKGLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVVAG 458
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
38-458 |
2.22e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.84 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 38 GERVAVMASNRPEFVAALQAIWRLGAAAV-LISPAWkrdevdhalgltdPAHAVGDHPVLADLMP--------------- 101
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVpLFAPEL-------------PGHAERLDTALRDAEPtvvltttaaaeaveg 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 102 ------------MLDLDD-PIAPAAPITGSPRPGDD-AVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQ 167
Cdd:PRK12476 159 flrnlprlrrprVIAIDAiPDSAGESFVPVELDTDDvSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 168 VA-TPPSHILGLLNI-LTALRVGTSVRLHPRFDVDRILRHI----ENDRITIEMAVAP-IAQALASH----PRLESYDLS 236
Cdd:PRK12476 239 VSwLPLYHDMGLSMIgFPAVYGGHSTLMSPTAFVRRPQRWIkalsEGSRTGRVVTAAPnFAYEWAAQrglpAEGDDIDLS 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 237 SLRFIMwGATPVTVSIAETVTR--------RTGVRwvPAYGTTE--LPVIACNP---PEQSRLD----SVGR--PVAGVD 297
Cdd:PRK12476 319 NVVLII-GSEPVSIDAVTTFNKafapyglpRTAFK--PSYGIAEatLFVATIAPdaePSVVYLDreqlGAGRavRVAADA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 298 VR-----------------IVSLDTGEPVGPGDVGEIQARSASLMAGY------------------LPAAANAEVWRDG- 341
Cdd:PRK12476 396 PNavahvscgqvarsqwavIVDPDTGAELPDGEVGEIWLHGDNIGRGYwgrpeetertfgaklqsrLAEGSHADGAADDg 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 342 -WYRTGDVG-WLDGNgwLRITDRLKEMIKVRGFQVAPAEVE-TVLHSHPAVKD--CAVFGVPDGVNGEAVVAAVATHAPG 416
Cdd:PRK12476 476 tWLRTGDLGvYLDGE--LYITGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRgyVTAFTVPAEDNERLVIVAERAAGTS 553
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 576413765 417 NTGVAAELTARVAAQLAPYK-RLSRVVFVPE--IPRLPSGKVLRR 458
Cdd:PRK12476 554 RADPAPAIDAIRAAVSRRHGlAVADVRLVPAgaIPRTTSGKLARR 598
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
121-391 |
5.41e-10 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 62.00 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 121 PGDDAVLVFSSGTTGLPKAVRHTHASLdAAVRQWR-DALRLTERDR-----------IQ--VATPpsHILGL-LNILTAL 185
Cdd:TIGR03443 414 PDSNPTLSFTSGSEGIPKGVLGRHFSL-AYYFPWMaKRFGLSENDKftmlsgiahdpIQrdMFTP--LFLGAqLLVPTAD 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 186 RVGTSVRLHPRF-DVDRILRHIendriTIEMAVAPIAQALASHPRLE----------SYDLSSLRfimwgatpvtvSIAE 254
Cdd:TIGR03443 491 DIGTPGRLAEWMaKYGATVTHL-----TPAMGQLLSAQATTPIPSLHhaffvgdiltKRDCLRLQ-----------TLAE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 255 TVtrrtgvRWVPAYGTTE---------LPVIACNPPEQSRLDSV---GRPVAGVDVRIVS-LDTGEPVGPGDVGEIQARS 321
Cdd:TIGR03443 555 NV------CIVNMYGTTEtqravsyfeIPSRSSDSTFLKNLKDVmpaGKGMKNVQLLVVNrNDRTQTCGVGEVGEIYVRA 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 322 ASLMAGYL--PAA---------------------ANAEVWRDGW-------YRTGDVGWLDGNGWLRITDRLKEMIKVRG 371
Cdd:TIGR03443 629 GGLAEGYLglPELnaekfvnnwfvdpshwidldkENNKPEREFWlgprdrlYRTGDLGRYLPDGNVECCGRADDQVKIRG 708
|
330 340
....*....|....*....|
gi 576413765 372 FQVAPAEVETVLHSHPAVKD 391
Cdd:TIGR03443 709 FRIELGEIDTHLSQHPLVRE 728
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
38-398 |
7.83e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 61.28 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 38 GERVAVMASNRPEFVAALQAIWRLGAAAV-LISPAwkrdevdhalgltDPAHAVGDHPVLADLMPMLDLDDPIAPAA--- 113
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVpLFDPA-------------EPGHVGRLHAVLDDCTPSAILTTTDSAEGvrk 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 114 -----PITGSPR-------PG--------------DDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERDRIQ 167
Cdd:PRK07769 146 ffrarPAKERPRviavdavPDevgatwvppeanedTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 168 VATPPSHILGLLNILTALRVGTSVRL-HPRFDVDRILRHI-----ENDRITIEMAVAP-IAQALASHPRL-----ESYDL 235
Cdd:PRK07769 226 SWLPFFHDMGLITVLLPALLGHYITFmSPAAFVRRPGRWIrelarKPGGTGGTFSAAPnFAFEHAAARGLpkdgePPLDL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 236 SSLRFIMWGATPVTVSIAETVT--------RRTGVRwvPAYGTTELPVIACNPP--EQSRLDSV-------GRPV----- 293
Cdd:PRK07769 306 SNVKGLLNGSEPVSPASMRKFNeafapyglPPTAIK--PSYGMAEATLFVSTTPmdEEPTVIYVdrdelnaGRFVevpad 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 294 ---------AGVDVR-----IVSLDTGEPVGPGDVGEIQARSASLMAGYLP-----------------AAANAEVWRDG- 341
Cdd:PRK07769 384 apnavaqvsAGKVGVsewavIVDPETASELPDGQIGEIWLHGNNIGTGYWGkpeetaatfqnilksrlSESHAEGAPDDa 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576413765 342 -WYRTGDVG-WLDGNgwLRITDRLKEMIKVRGFQVAPAEVE-TVLHSHPAVKD--CAVFGVP 398
Cdd:PRK07769 464 lWVRTGDYGvYFDGE--LYITGRVKDLVIIDGRNHYPQDLEyTAQEATKALRTgyVAAFSVP 523
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
10-242 |
2.08e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 59.81 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 10 EDRRVSRHALDALSDGLGATLHHRGVIAGERVAVMASNRPEFVAA------LQAIWR-----LGAAAVL-----ISPA-- 71
Cdd:PRK03584 111 PRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAmlatasLGAIWSscspdFGVQGVLdrfgqIEPKvl 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 72 ------W-------KRDEVDH-ALGLTDPAHAV-----GDHPVLADLMPMLDLDDPIAP--AAPITGSPRPGDDAV-LVF 129
Cdd:PRK03584 191 iavdgyRyggkafdRRAKVAElRAALPSLEHVVvvpylGPAAAAAALPGALLWEDFLAPaeAAELEFEPVPFDHPLwILY 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 130 SSGTTGLPKAVRHTHASLdaaVRQWRDALRL----TERDRIQVATPPS------HILGLLniltalrVGTSVRL------ 193
Cdd:PRK03584 271 SSGTTGLPKCIVHGHGGI---LLEHLKELGLhcdlGPGDRFFWYTTCGwmmwnwLVSGLL-------VGATLVLydgspf 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 576413765 194 HPrfDVDRILRHIENDRITIEMAVAPIAQALAS---HPRlESYDLSSLRFIM 242
Cdd:PRK03584 341 YP--DPNVLWDLAAEEGVTVFGTSAKYLDACEKaglVPG-ETHDLSALRTIG 389
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
24-349 |
2.10e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 59.67 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 24 DGLGATLHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPAWKRDEVDHAlGLTDPAHAVGDHPVLADLMPM- 102
Cdd:PRK12582 91 DALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHA-KLKHLFDLVKPRVVFAQSGAPf 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 103 ------LDLDDP--IAPAAPITGSP---------------------RPGDDAV--LVFSSGTTGLPKAVRHTHASLdAAV 151
Cdd:PRK12582 170 aralaaLDLLDVtvVHVTGPGEGIAsiafadlaatpptaavaaaiaAITPDTVakYLFTSGSTGMPKAVINTQRMM-CAN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 152 RQWRDALRLTERDriqvaTPPSHIL----------GLLNILTALRVGTSVRLHP------RFDVD-RILRHIEndriTIE 214
Cdd:PRK12582 249 IAMQEQLRPREPD-----PPPPVSLdwmpwnhtmgGNANFNGLLWGGGTLYIDDgkplpgMFEETiRNLREIS----PTV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 215 MAVAPIA-QALASH----PRLESYDLSSLRFIMWGATPVTVSIAETV----TRRTGVRWV--PAYGTTELPVIACN---P 280
Cdd:PRK12582 320 YGNVPAGyAMLAEAmekdDALRRSFFKNLRLMAYGGATLSDDLYERMqalaVRTTGHRIPfyTGYGATETAPTTTGthwD 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576413765 281 PEQSRLdsVGRPVAGVDVRIVsldtgePVgpGDVGEIQARSASLMAGY-----LPAAANAEvwrDGWYRTGDVG 349
Cdd:PRK12582 400 TERVGL--IGLPLPGVELKLA------PV--GDKYEVRVKGPNVTPGYhkdpeLTAAAFDE---EGFYRLGDAA 460
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
30-395 |
2.39e-09 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 59.28 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 30 LHHRGVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPA-----------------WKRDEVDH-ALGLTDPAHAVG 91
Cdd:cd05905 32 QKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPdisqqlgfllgtckvrvALTVEACLkGLPKKLLKSKTA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 92 DHPVLADLMPML-DLDD-PI---APAAPITGSPR--PGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTERD 164
Cdd:cd05905 112 AEIAKKKGWPKIlDFVKiPKskrSKLKKWGPHPPtrDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 165 RIQVATPPSHILGL-LNILTALRVGTSVRLHPRFDVDR----ILRHIENDRI--------TIEMAVAPIAQALAsHPRLE 231
Cdd:cd05905 192 PLVTVLDFKSGLGLwHGCLLSVYSGHHTILIPPELMKTnpllWLQTLSQYKVrdayvklrTLHWCLKDLSSTLA-SLKNR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 232 SYDLSSLRFIMWGATP-----VTVSIAEtVTRRTGVRWV---PAYGTTELP-------------------------VIAC 278
Cdd:cd05905 271 DVNLSSLRMCMVPCENrprisSCDSFLK-LFQTLGLSPRavsTEFGTRVNPficwqgtsgpepsrvyldmralrhgVVRL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 279 N----PPEQSRLDSVGRPVaGVDVRIVSLDTGEPVGPGDVGEIQARSASLMAGY--LPAAANAE------------VWRD 340
Cdd:cd05905 350 DerdkPNSLPLQDSGKVLP-GAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYflLDGETNDTfkvfpstrlstgITNN 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 341 GWYRTGDVGWL------DGNGW----LRITDRLKEMIKVRGFQVAPAEVE-TVLHSHPAVKDCAVF 395
Cdd:cd05905 429 SYARTGLLGFLrptkctDLNVEehdlLFVVGSIDETLEVRGLRHHPSDIEaTVMRVHPYRGRCAVF 494
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
120-396 |
9.06e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 57.93 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 120 RPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQWRDALRLTER-----DRIQVATPPSHILGLLNILTALRVGTSVRLH 194
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRvateeDSYFSYLPLAHVYDQVIETYCISKGASIGFW 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 195 pRFDVDRILRHIENDRITIEMAV--------APIAQALASHPRLE--------SYDLSSL-------------------- 238
Cdd:PLN02861 298 -QGDIRYLMEDVQALKPTIFCGVprvydriyTGIMQKISSGGMLRkklfdfayNYKLGNLrkglkqeeasprldrlvfdk 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 239 ---------RFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTE-----LPVIAcnpPEQSRLDSVGRPVAGVDVRIVSLD 304
Cdd:PLN02861 377 ikeglggrvRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEscggcFTSIA---NVFSMVGTVGVPMTTIEARLESVP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 305 TGEPVGPGDV--GEIQARSASLMAGYLPAAA-NAEVWRDGWYRTGDVGWLDGNGWLRITDRLKEMIKV-RGFQVAPAEVE 380
Cdd:PLN02861 454 EMGYDALSDVprGEICLRGNTLFSGYHKRQDlTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLE 533
|
330
....*....|....*.
gi 576413765 381 TVLHSHPAVKDCAVFG 396
Cdd:PLN02861 534 NTYSRCPLIASIWVYG 549
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
127-461 |
3.67e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 55.86 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 127 LVFSSGTTGLPKAVRHTHAS-LDAAVRQWRDaLRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDR-ILR 204
Cdd:PLN03052 361 ILFSSGTTGEPKAIPWTQLTpLRAAADAWAH-LDIRKGDIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPLGRgFAK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 205 HIENDRITIEMAVAPIAQALASHPRLESYDLSSLRFimWGATPVTVSIAETV--TRRTGVRWVPAY-GTTEL--PVIACN 279
Cdd:PLN03052 440 FVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRC--FGSTGEASSVDDYLwlMSRAGYKPIIEYcGGTELggGFVTGS 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 280 PPEQSRLDSVGRPVAGVDVRIVSlDTGEPVgPGDV---GEIQARSASLMAGY-LPAAANAEVWRDG---WY-----RTGD 347
Cdd:PLN03052 518 LLQPQAFAAFSTPAMGCKLFILD-DSGNPY-PDDApctGELALFPLMFGASStLLNADHYKVYFKGmpvFNgkilrRHGD 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 348 VGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVETVLHS-HPAVKDCAVFGVPDGVNG--EAVVAAVATHAPGNTGVAAEL 424
Cdd:PLN03052 596 IFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNEL 675
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 576413765 425 ----TARVAAQLAPYKRLSRVVFVPEIPRLPSGKVLRRVLK 461
Cdd:PLN03052 676 kkifNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLR 716
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
26-347 |
2.30e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 53.34 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 26 LGATLHHRGVIAGERVAVMASNRPE-FVAALQAIWrLGAAAVLISPAWKRDEVD-----HALGLTDPAHA-VGDHPVLAD 98
Cdd:PRK08180 82 IAQALLDRGLSAERPLMILSGNSIEhALLALAAMY-AGVPYAPVSPAYSLVSQDfgklrHVLELLTPGLVfADDGAAFAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 99 LMPMLDLDDP--IAPAAPITGSP-----------------------RPGDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQ 153
Cdd:PRK08180 161 ALAAVVPADVevVAVRGAVPGRAatpfaallatpptaavdaahaavGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 154 WRDALR-LTERDRIQVATPP-------SHILGLlniltALRVGTSVRLHP-RFDVDRILRHIENDRitiemAVAP----- 219
Cdd:PRK08180 241 LAQTFPfLAEEPPVLVDWLPwnhtfggNHNLGI-----VLYNGGTLYIDDgKPTPGGFDETLRNLR-----EISPtvyfn 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 220 -------IAQALASHPRLESYDLSSLRFIMWGATPVTVSI--------AETVTRRtgVRWVPAYGTTEL-PVIACNPPEQ 283
Cdd:PRK08180 311 vpkgwemLVPALERDAALRRRFFSRLKLLFYAGAALSQDVwdrldrvaEATCGER--IRMMTGLGMTETaPSATFTTGPL 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 284 SRLDSVGRPVAGVDVRIVsldtgePVGpgDVGEIQARSASLMAGYLPAA-ANAEVW-RDGWYRTGD 347
Cdd:PRK08180 389 SRAGNIGLPAPGCEVKLV------PVG--GKLEVRVKGPNVTPGYWRAPeLTAEAFdEEGYYRSGD 446
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
34-449 |
2.39e-07 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 53.23 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 34 GVIAGERVAVMASNRPEFVAALQAIWRLGAAAVLISPA--------WKRDEVDHALGLTDPAHAVGDHPVLADLMPMLDL 105
Cdd:cd17632 126 GASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTpprlvvfdHRPEVDAHRAALESARERLAAVGIPVTTLTLIAV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 106 DDPIAPAAPITGsPRPGDD--AVLVFSSGTTGLPKAVRHTHAsldAAVRQWRDALRLTERDRIQVAT----PPSHILGLL 179
Cdd:cd17632 206 RGRDLPPAPLFR-PEPDDDplALLIYTSGSTGTPKGAMYTER---LVATFWLKVSSIQDIRPPASITlnfmPMSHIAGRI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 180 NILTALRVG-----------------------TSVRLHPRFdVDRILRHI--ENDRITIEMAVAPIAQALASHPRLESYD 234
Cdd:cd17632 282 SLYGTLARGgtayfaaasdmstlfddlalvrpTELFLVPRV-CDMLFQRYqaELDRRSVAGADAETLAERVKAELRERVL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 235 LSSLRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTELPVIacnppeqSRLDSVGRPvAGVDVRIVslDTGEpVG---- 310
Cdd:cd17632 361 GGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAV-------ILDGVIVRP-PVLDYKLV--DVPE-LGyfrt 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 311 --PGDVGEIQARSASLMAGYLPAA-ANAEVW-RDGWYRTGDVGWLDGNGWLRITDRLKEMIKV-RGFQVAPAEVETVLHS 385
Cdd:cd17632 430 drPHPRGELLVKTDTLFPGYYKRPeVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAA 509
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 386 HPAVKDCAVFGvpdgvNGEAV---VAAVATHAPGNTGVAAELTARV---------AAQLAPYkrlsrvvfvpEIPR 449
Cdd:cd17632 510 SPLVRQIFVYG-----NSERAyllAVVVPTQDALAGEDTARLRAALaeslqriarEAGLQSY----------EIPR 570
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
96-390 |
1.10e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 50.70 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 96 LADL--MPMLDLDDPI--APAAPITGsprPGDDAVLVF-SSGTTGLPKAVRHTHASLDAAVRQWRDALR---LTERDRIQ 167
Cdd:cd05913 50 LDDLrkLPFTTKEDLRdnYPFGLFAV---PREKVVRIHaSSGTTGKPTVVGYTKNDLDVWAELVARCLDaagVTPGDRVQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 168 VATPPSHILGLLNILTAL-RVGTSVrlhprfdV-------DRILRHIENDRITIEMAVAPIAQALASHPRLESYDL--SS 237
Cdd:cd05913 127 NAYGYGLFTGGLGFHYGAeRLGALV-------IpagggntERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPreLS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 238 LRFIMWGATPVTVSIAETVTRRTGVRWVPAYGTTEL--PVIACNPPEQsrldsVGRPVA--GVDVRIVSLDTGEPVGPGD 313
Cdd:cd05913 200 LKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIigPGVAFECEEK-----DGLHIWedHFIPEIIDPETGEPVPPGE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 314 VGEIQArsASLMAGYLPaaanaeVWRdgwYRTGD-VGWLDGNGW--------LRITDRLKEMIKVRGFQVAPAEVETVLH 384
Cdd:cd05913 275 VGELVF--TTLTKEAMP------LIR---YRTRDiTRLLPGPCPcgrthrriDRITGRSDDMLIIRGVNVFPSQIEDVLL 343
|
....*.
gi 576413765 385 SHPAVK 390
Cdd:cd05913 344 KIPGLG 349
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
30-458 |
1.45e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 50.71 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 30 LHHRGVIaGERVAVMASNRPE----FVAALQAiwrlGAAAVLISP--AWKRDE-VDHALGLTDP---------AHAVGDH 93
Cdd:PRK05850 52 LRRHGST-GDRAVILAPQGLEyivaFLGALQA----GLIAVPLSVpqGGAHDErVSAVLRDTSPsvvlttsavVDDVTEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 94 PVLADLMP--------MLDLDDPIAPAAPITGSPrpgDDAVLVFSSGTTGLPKAVRHTHASLDAAVRQ-WRDALRlterD 164
Cdd:PRK05850 127 VAPQPGQSappvievdLLDLDSPRGSDARPRDLP---STAYLQYTSGSTRTPAGVMVSHRNVIANFEQlMSDYFG----D 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 165 RIQVATPPS---------HILGL-LNILTALRVG-TSVRLHPRFDVDRILRHIendritiemavapiaQALASHPR---- 229
Cdd:PRK05850 200 TGGVPPPDTtvvswlpfyHDMGLvLGVCAPILGGcPAVLTSPVAFLQRPARWM---------------QLLASNPHafsa 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 230 -----------------LESYDLSSLRFIMWGATPVTVSIAETVTRR--------TGVRwvPAYGTTELPV-----IACN 279
Cdd:PRK05850 265 apnfafelavrktsdddMAGLDLGGVLGIISGSERVHPATLKRFADRfapfnlreTAIR--PSYGLAEATVyvatrEPGQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 280 PPEQSRLD----SVGR-----PVAGVD-----------VRIVSLDTGEPVGPGDVGEIQARSASLMAGYL---------- 329
Cdd:PRK05850 343 PPESVRFDyeklSAGHakrceTGGGTPlvsygsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWqkpeetertf 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 330 ------PAAANAEvwrDGWYRTGDVGWLDGnGWLRITDRLKEMIKVRGFQVAPAEVETvlhshpAVKD-----CAVFGVP 398
Cdd:PRK05850 423 gatlvdPSPGTPE---GPWLRTGDLGFISE-GELFIVGRIKDLLIVDGRNHYPDDIEA------TIQEitggrVAAISVP 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576413765 399 DGvNGEAVVAAVATHAPGNTGVAA-----ELTARVAAQLAPYKRLS--RVVFVP--EIPRLPSGKVLRR 458
Cdd:PRK05850 493 DD-GTEKLVAIIELKKRGDSDEEAmdrlrTVKREVTSAISKSHGLSvaDLVLVApgSIPITTSGKIRRA 560
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
127-462 |
1.59e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 44.04 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 127 LVFSSGTTGLPKAVRHTHAS-LDAAVRQWRDaLRLTERDRIQVATPPSHILGLLNILTALRVGTSVRLHPRFDVDR-ILR 204
Cdd:PLN03051 124 ILFSSGTTGEPKAIPWTHLSpLRCASDGWAH-MDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPLGRgFGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 205 HIENDRITIEMAVAPIAQALASH--PRLESYDLSSLRFImwgATPVTVSIAETV----TRRTGVRWVPAY-GTTEL---- 273
Cdd:PLN03051 203 FVQDAGVTVLGLVPSIVKAWRHTgaFAMEGLDWSKLRVF---ASTGEASAVDDVlwlsSVRGYYKPVIEYcGGTELasgy 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 274 ----PVIACNPPEQSrldsvgrpVAGVDVRIVSLDTGEPVGPGD---VGEIQARSASLMAG-YLPAAANAEVWRDGW--- 342
Cdd:PLN03051 280 isstLLQPQAPGAFS--------TASLGTRFVLLNDNGVPYPDDqpcVGEVALAPPMLGASdRLLNADHDKVYYKGMpmy 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576413765 343 -------YRTGDVGWLDGNGWLRITDRLKEMIKVRGFQVAPAEVE-TVLHSHPAVKDCAVFGV-PDGVNGEAVVAAVATH 413
Cdd:PLN03051 352 gskgmplRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIErACDRAVAGIAETAAVGVaPPDGGPELLVIFLVLG 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 576413765 414 APGNTGVAAELTARVAA-------QLAPYKRLSRVVFVPEIPRLPSGKVLRRVLKE 462
Cdd:PLN03051 432 EEKKGFDQARPEALQKKfqeaiqtNLNPLFKVSRVKIVPELPRNASNKLLRRVLRD 487
|
|
| |
