|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1-306 |
7.95e-164 |
|
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: 463.30 E-value: 7.95e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWekfLSSETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqDFLRAVCEEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd05941 161 FLPKFDPKEVA---ISRLMPSITVFMGVPTIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEIGMALSGPLTtAARLPGSVGTPLPGVQVRIVSENPQRegcsytihaegdergtkvtPGLEEKEGEL 160
Cdd:cd05941 235 ITGHTLLERYGMTEIGMALSNPLD-GERRPGTVGMPLPGVQARIVDEETGE-------------------PLPRGEVGEI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 161 LVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAV 239
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 240 IGVPDMTWGQRVTAVVTLREG-HSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd05941 375 IGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-308 |
1.07e-97 |
|
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: 295.18 E-value: 1.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRhftqphAQDFLRAVceekiRLMVSGSAALPLPVLEKWKN 80
Cdd:COG0318 172 LLPRFDPERVLELI---ERERVTVLFGVPTMLARLLRHPEF------ARYDLSSL-----RLVVSGGAPLPPELLERFEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEIGMALSG-PLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGE 159
Cdd:COG0318 238 RFGVRIVEGYGLTETSPVVTVnPEDPGERRPGSVGRPLPGVEVRIV-----------------DEDGRELPPG---EVGE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:COG0318 298 IVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAA 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:COG0318 376 VVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1-304 |
4.00e-81 |
|
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: 253.25 E-value: 4.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravceEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd05936 199 LIPRFRPIGVLKEI---RKHRVTIFPGVPTMYIALLNAPEFKKRDF-----------SSLRLCISGGAPLPVEVAERFEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEigmalSGPLTTA-----ARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGlee 155
Cdd:cd05936 265 LTGVPIVEGYGLTE-----TSPVVAVnpldgPRKPGSIGIPLPGTEVKIV-----------------DDDGEELPPG--- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 156 KEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 234
Cdd:cd05936 320 EVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAV 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 235 TDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05936 398 AEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1-300 |
5.84e-80 |
|
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: 246.04 E-value: 5.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHftqPHAQDFLRAVCeekirlmvSGSAALPLPVLEKWKN 80
Cdd:cd04433 71 LLPKFDPEAALELI---EREKVTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEIG-MALSGPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGE 159
Cdd:cd04433 137 APGIKLVNGYGLTETGgTVATGPPDDDARKPGSVGRPVPGVEVRIV-----------------DPDGGELPPG---EIGE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETkSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd04433 197 LVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLdEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAA 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:cd04433 275 VVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
24-306 |
1.28e-77 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 244.13 E-value: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 24 VFMAVPTIYTKLMEYYDrhftqpHAQDFLRAvceekiRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGpL 103
Cdd:PRK07787 219 LYFGVPTVWSRIAADPE------AARALRGA------RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLST-R 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 104 TTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVtPGLEEKEGELLVRGPSVFREYWNKPEETKSAFT 183
Cdd:PRK07787 286 ADGERRPGWVGLPLAGVETRLV-----------------DEDGGPV-PHDGETVGELQVRGPTLFDGYLNRPDATAAAFT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 184 LDGWFKTGDTVVFK-DGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGhs 262
Cdd:PRK07787 348 ADGWFRTGDVAVVDpDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD-- 425
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034116931 263 LSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK07787 426 VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-304 |
2.43e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 237.01 E-value: 2.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKN 80
Cdd:PRK06187 238 IPRRFDPENLLDLI---ETERVTFFFAVPTIWQMLLKAPR-----AYFVDFSS------LRLVIYGGAALPPALLREFKE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEigmalSGPLTTAARLP----------GSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVT 150
Cdd:PRK06187 304 KFGIDLVQGYGMTE-----TSPVVSVLPPEdqlpgqwtkrRSAGRPLPGVEARIV-----------------DDDGDELP 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 151 PGLEEKeGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLL 229
Cdd:PRK06187 362 PDGGEV-GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIdEDGYLYITDRIK-DVIISGGENIYPRELEDALY 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 230 AHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK06187 439 GHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-301 |
1.44e-70 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 224.80 E-value: 1.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTqphaqDFLRavceekIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd17631 170 ILRKFDPETVLDLI---ERHRVTSFFLVPTMIQALLQHPRFATT-----DLSS------LRAVIYGGAPMPERLLRALQA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ItGHTLLERYGMTEIGMALSG-PLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGE 159
Cdd:cd17631 236 R-GVKFVQGYGMTETSPGVTFlSPEDHRRKLGSAGRPVFFVEVRIV-----------------DPDGREVPPG---EVGE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd17631 295 IVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLdEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
2-304 |
2.06e-70 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 226.30 E-value: 2.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 2 MPEFSPQQVWEKFlssetPRINVFMAVPTIYTKLMEyyDRHFTQPHAQdflravceeKIRLMVSGSAALPLPVLEKWKNI 81
Cdd:PRK07514 229 LPKFDPDAVLALM-----PRATVMMGVPTFYTRLLQ--EPRLTREAAA---------HMRLFISGSAPLLAETHREFQER 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 TGHTLLERYGMTEIGMALSGPLTtAARLPGSVGTPLPGVQVRIVsenpqregcsytihaeGDERGTKVTPGleeKEGELL 161
Cdd:PRK07514 293 TGHAILERYGMTETNMNTSNPYD-GERRAGTVGFPLPGVSLRVT----------------DPETGAELPPG---EIGMIE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 162 VRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVI 240
Cdd:PRK07514 353 VKGPNVFKGYWRMPEKTAEEFRADGFFITGDLgKIDERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVI 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 241 GVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07514 432 GVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
21-304 |
1.96e-65 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 214.98 E-value: 1.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDRHftqPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMA-L 99
Cdd:COG0365 278 GVTVFFTAPTAIRALMKAGDEP---LKKYDL------SSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfI 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 100 SGPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRG--PSVFREYWNKPEE 177
Cdd:COG0365 349 SNLPGLPVK-PGSMGKPVPGYDVAVV-----------------DEDGNPVPPG---EEGELVIKGpwPGMFRGYWNDPER 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 178 TKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:COG0365 408 YRETYfgRFPGWYRTGDGARRdEDGYFWILGRSD-DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAF 486
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 255 VTLREGHSLS---HRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:COG0365 487 VVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1-304 |
1.97e-64 |
|
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: 210.63 E-value: 1.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTQPHAqdflravceeKIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd05926 221 LPPRFSASTFWPDV---RDYNATWYTAVPTIHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEIG--MAlSGPLTTAARLPGSVGTPLpGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEG 158
Cdd:cd05926 288 TFGAPVLEAYGMTEAAhqMT-SNPLPPGPRKPGSVGKPV-GVEVRIL-----------------DEDGEILPPG---VVG 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 159 ELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDV 237
Cdd:cd05926 346 EICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDaDGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEA 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034116931 238 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05926 425 VAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
27-299 |
1.40e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 210.24 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 27 AVPTIYTKLMEYYDRHftqphaqdflrAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MALSGPLTT 105
Cdd:PRK05605 316 GVPPLYEKIAEAAEER-----------GVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 106 AARlPGSVGTPLPGVQVRIVS-ENPQREgcsytihaegdergtkVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFtL 184
Cdd:PRK05605 385 DRR-PGYVGVPFPDTEVRIVDpEDPDET----------------MPDG---EEGELLVRGPQVFKGYWNRPEETAKSF-L 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 185 DGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSL 263
Cdd:PRK05605 444 DGWFRTGDVVVMEeDGFIRIVDRIK-ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAL 522
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034116931 264 SHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK05605 523 DPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-304 |
1.26e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 198.59 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVwekFLSSETPRINVFMAVPTIYTKLMEYYDRHftqphAQDFlravceEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:PRK07656 238 PLPVFDPDEV---FRLIETERITVLPGPPTMYNSLLQHPDRS-----AEDL------SSLRLAVTGAASMPVALLERFES 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITG-HTLLERYGMTEigmalSGPLTTAARL-------PGSVGTPLPGVQVRIVSENpqregcsytihaeGDERGTKVTpg 152
Cdd:PRK07656 304 ELGvDIVLTGYGLSE-----ASGVTTFNRLdddrktvAGTIGTAIAGVENKIVNEL-------------GEEVPVGEV-- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 153 leekeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 231
Cdd:PRK07656 364 -----GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEH 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 232 PSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07656 438 PAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1-304 |
5.46e-54 |
|
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: 183.72 E-value: 5.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEF-SPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFLRavceekIRLMVSGSAALPLPVLEKWK 79
Cdd:cd05959 236 LMPERpTPAAVFKRI---RRYRPTVFFGVPTLYAAMLAAPN-----LPSRDLSS------LRLCVSAGEALPAEVGERWK 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 80 NITGHTLLERYGMTEIGMALSGPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGE 159
Cdd:cd05959 302 ARFGLDILDGIGSTEMLHIFLSNRPGRVR-YGTTGKPVPGYEVELR-----------------DEDGGDVADG---EPGE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAA 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHS---LSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05959 439 VVGVEDEDGLTKPKAFVVLRPGYEdseALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
27-304 |
1.24e-52 |
|
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: 180.13 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 27 AVPTIYTKLMEYYDRHftqPHAQDFLRAVceekirlmVSGSAALPLPVLEKWKNItGHTLLERYGMTEigmalSGPLTTA 106
Cdd:cd12119 260 GVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIEAFEER-GVRVIHAWGMTE-----TSPLGTV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 107 ARLPGSV---------------GTPLPGVQVRIVSENpqregcsytihaegdergTKVTPGLEEKEGELLVRGPSVFREY 171
Cdd:cd12119 323 ARPPSEHsnlsedeqlalrakqGRPVPGVELRIVDDD------------------GRELPWDGKAVGELQVRGPWVTKSY 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 172 WNKPEETKsAFTLDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQR 250
Cdd:cd12119 385 YKNDEESE-ALTEDGWLRTGDvATIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGER 462
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 251 VTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12119 463 PLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2-304 |
1.04e-51 |
|
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: 175.60 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 2 MPEFSPQQVWEKfLSSEtpRINVFMAVPTIYTKLMEyydrhfTQPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNI 81
Cdd:cd05972 156 GPRFDAERILEL-LERY--GVTSFCGPPTAYRMLIK------QDLSSYKFSH------LRLVVSAGEPLNPEVIEWWRAA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 TGHTLLERYGMTEIGMALSGPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELL 161
Cdd:cd05972 221 TGLPIRDGYGQTETGLTVGNFPDMPVK-PGSMGRPTPGYDVAII-----------------DDDGRELPPG---EEGDIA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 162 VR--GPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05972 280 IKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDRAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAA 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05972 358 VVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1-299 |
1.44e-50 |
|
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: 173.94 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLMEYydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWK 79
Cdd:cd05911 219 IMPKFDS----ELFLDLiEKYKITFLYLVPPIAAALAKS-----PLLDKYDL------SSLRVILSGGAPLSKELQELLA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 80 NITGHT-LLERYGMTEIGMALSgPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTpGLEEkEG 158
Cdd:cd05911 284 KRFPNAtIKQGYGMTETGGILT-VNPDGDDKPGSVGRLLPNVEAKIV-----------------DDDGKDSL-GPNE-PG 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 159 ELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDV 237
Cdd:cd05911 344 EICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFdEDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADA 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 238 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYavpSEL----VLVEEIPRNQMGKI 299
Cdd:cd05911 423 AVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKI 485
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
2-301 |
1.47e-49 |
|
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: 167.45 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 2 MPEFSPQQVWEKflsSETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqDFLRAVceekirlmvsgsAALPLP-VLEKWKN 80
Cdd:cd17637 72 MEKFDPAEALEL---IEEEKVTLMGSFPPILSNLLDAAEKSGVDL---SSLRHV------------LGLDAPeTIQRFEE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEIgmalSGPLTTA--ARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEG 158
Cdd:cd17637 134 TTGATFWSLYGQTET----SGLVTLSpyRERPGSAGRPGPLVRVRIV-----------------DDNDRPVPAG---ETG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 159 ELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSV-DIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:cd17637 190 EIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFdEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAE 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17637 269 VCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
46-304 |
3.08e-49 |
|
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: 171.48 E-value: 3.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 46 PHAQDFLRAVCEEK-----IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmalsGPLTTAaRL--P-----GSV 113
Cdd:COG1021 283 PLALLWLDAAERSRydlssLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE------GLVNYT-RLddPeevilTTQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 114 GTPL-PGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 192
Cdd:COG1021 356 GRPIsPDDEVRIV-----------------DEDGNPVPPG---EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 193 TVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLReGHSLSHRELKEW 271
Cdd:COG1021 416 LVRRtPDGYLVVEGR-AKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRF 493
|
250 260 270
....*....|....*....|....*....|....
gi 1034116931 272 ARDV-LAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:COG1021 494 LRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
21-304 |
6.39e-49 |
|
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: 168.79 E-value: 6.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDrhftqpHAQDFLRAvceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:cd05919 182 RPTVLYGVPTFYANLLDSCA------GSPDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 101 GPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKS 180
Cdd:cd05919 251 SNRPGAWR-LGSTGRPVPGYEIRLV-----------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWNNPEKSRA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 181 AFtLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRE 259
Cdd:cd05919 310 TF-NGGWYRTGDKFCRdADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034116931 260 GHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05919 388 PAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-305 |
2.67e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 169.44 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:PRK06710 280 LIPKFDMKMVFEAI---KKHKVTLFPGAPTIYIALLN-----------SPLLKEYDISSIRACISGSAPLPVEVQEKFET 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEigmalSGPLTTA-----ARLPGSVGTPLPGVQVRIVSEnpqregcsytihaegdERGTKVTPGlee 155
Cdd:PRK06710 346 VTGGKLVEGYGLTE-----SSPVTHSnflweKRVPGSIGVPWPDTEAMIMSL----------------ETGEALPPG--- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 156 KEGELLVRGPSVFREYWNKPEETkSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 234
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVgYMDEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKV 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 235 TDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 305
Cdd:PRK06710 480 QEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
66-304 |
7.52e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 167.42 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 66 GSAALPLPVLEKwknitghtLLER---------YGMTEIGmalsgPLTTA------ARLPGSVGTPLPGVQVRIVsenpq 130
Cdd:PRK08316 294 GASIMPVEVLKE--------LRERlpglrfyncYGQTEIA-----PLATVlgpeehLRRPGSAGRPVLNVETRVV----- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 131 regcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSv 209
Cdd:PRK08316 356 ------------DDDGNDVAPGEV---GEIVHRSPQLMLGYWDDPEKTAEAFR-GGWFHSGDLGVMdEEGYITVVDRKK- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 210 DIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVE 289
Cdd:PRK08316 419 DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVD 498
|
250
....*....|....*
gi 1034116931 290 EIPRNQMGKIDKKAL 304
Cdd:PRK08316 499 ELPRNPSGKILKREL 513
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1-304 |
1.79e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 166.70 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFlravceEKIRLMVSGSAALpLPV-LEKW 78
Cdd:PRK06188 238 VLAKFDP----AEVLRAiEEQRITATFLVPTMIYALLDHPD-----LRTRDL------SSLETVYYGASPM-SPVrLAEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 79 KNITGHTLLERYGMTEIGMALS------GPLTTAARLpGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPG 152
Cdd:PRK06188 302 IERFGPIFAQYYGQTEAPMVITylrkrdHDPDDPKRL-TSCGRPTPGLRVALL-----------------DEDGREVAQG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 153 leeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 231
Cdd:PRK06188 364 ---EVGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDvAREDEDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEH 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 232 PSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK06188 439 PAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
18-306 |
1.54e-46 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 163.49 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMEYYDRHFTqphaqDFlravceEKIRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTE--- 94
Cdd:PRK06839 235 EKHKVTVVMGVPTIHQALINCSKFETT-----NL------QSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtsp 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 95 -IGMALSgplTTAARLPGSVGTPLPGVQVRIVSENpqregcsytihaegderGTKVTPGleeKEGELLVRGPSVFREYWN 173
Cdd:PRK06839 303 tVFMLSE---EDARRKVGSIGKPVLFCDYELIDEN-----------------KNKVEVG---EVGELLIRGPNVMKEYWN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 174 KPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVT 252
Cdd:PRK06839 360 RPDATEETIQ-DGWLCTGDLARVdEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPI 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 253 AVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK06839 438 AFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1-305 |
1.70e-46 |
|
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: 162.08 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEyydrhfTQPHAQDflravCEEKIRLmVSGSAALPLpVLEKWKN 80
Cdd:cd05934 153 LLPRFSASRFWSDVRRY---GATVTNYLGAMLSYLLA------QPPSPDD-----RAHRLRA-AYGAPNPPE-LHEEFEE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTEIGMALSGPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGEL 160
Cdd:cd05934 217 RFGVRLLEGYGMTETIVGVIGPRDEPRR-PGSIGRPAPGYEVRIV-----------------DDDGQELPAG---EPGEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 161 LVR---GPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:cd05934 276 VIRglrGWGFFKGYYNMPEATAEAMR-NGWFHTGDLGYRdADGFFYFVDRKK-DMIRRRGENISSAEVERAILRHPAVRE 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 305
Cdd:cd05934 354 AAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
60-304 |
2.11e-46 |
|
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: 162.88 E-value: 2.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPL-PGVQVRIVsenpqregcsyti 138
Cdd:cd05920 257 LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMsPDDEIRVV------------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 139 haegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV-VFKDGQYWIRGRTSvDIIKTGGY 217
Cdd:cd05920 324 ----DEEGNPVPPG---EEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 218 KVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLReGHSLSHRELKEWARDV-LAPYAVPSELVLVEEIPRNQM 296
Cdd:cd05920 396 KIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAV 474
|
....*...
gi 1034116931 297 GKIDKKAL 304
Cdd:cd05920 475 GKIDKKAL 482
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
46-301 |
3.48e-46 |
|
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: 161.39 E-value: 3.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 46 PHAQDFLRAVCEE-----KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMAL-SGPLTTAARLPGSVGTPLPG 119
Cdd:cd05903 191 PFLTDLLNAVEEAgeplsRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVtSITPAPEDRRLYTDGRPLPG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 120 VQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVFKDG 199
Cdd:cd05903 271 VEIKVV-----------------DDTGATLAPG---VEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDED 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 200 QYW-IRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW-ARDVLA 277
Cdd:cd05903 330 GYLrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYlDRQGVA 408
|
250 260
....*....|....*....|....
gi 1034116931 278 PYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd05903 409 KQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
21-304 |
5.71e-46 |
|
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: 161.11 E-value: 5.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDrhFTQPHAQdflravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:cd05958 187 KPTVLFTAPTAYRAMLAHPD--AAGPDLS---------SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 101 GPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVfreYWNKPEETKS 180
Cdd:cd05958 256 SARPGDAR-PGATGKPVPGYEAKVV-----------------DDEGNPVPDG---TIGRLAVRGPTG---CRYLADKRQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 181 AFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRE 259
Cdd:cd05958 312 TYVQGGWNITGDTySRDPDGYFRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRP 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034116931 260 GHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05958 391 GVIPGPvlaRELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
18-307 |
8.81e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 160.89 E-value: 8.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMEyydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEiGM 97
Cdd:PRK07529 305 ERYRINFLSGVPTVYAALLQ------VPVDGHDI------SSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-AT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 ALS--GPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaEGDERGTKVTPGLEEKEGELLVRGPSVFREYWNkP 175
Cdd:PRK07529 372 CVSsvNPPDGERR-IGSVGLRLPYQRVRVV---------------ILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLE-A 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 176 EETKSAFTLDGWFKTGDTV-VFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:PRK07529 435 AHNKGLWLEDGWLNTGDLGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 255 VTLREGHSLSHRELKEWARD-VLAPYAVPSELVLVEEIPRNQMGKIDKKALIRH 307
Cdd:PRK07529 514 VQLKPGASATEAELLAFARDhIAERAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
63-304 |
9.14e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 156.12 E-value: 9.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 63 MVSGSAALPLPVLEKWKNiTGHTLLERYGMTEIGMALSGPL---TTAARLpGSVGTPLPGVQVRIVsenpqregcsytih 139
Cdd:PRK09088 257 LFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVdcdVIRAKA-GAAGIPTPTVQTRVV-------------- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 140 aegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYK 218
Cdd:PRK09088 321 ---DDQGNDCPAGVP---GELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDaDGFFWVVDRKK-DMFISGGEN 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 219 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:PRK09088 394 VYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGK 473
|
....*.
gi 1034116931 299 IDKKAL 304
Cdd:PRK09088 474 LQKARL 479
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
4-304 |
1.50e-43 |
|
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: 154.58 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 4 EFSPQQvWEKFLSSEtpRINVFMAVPTIYTKLMEYYDrhftqphaqDFLRAVCEEKIRLMVSGSAALPlPVLEKW-KNIT 82
Cdd:cd05969 165 RFDAES-WYGIIERV--KVTVWYTAPTAIRMLMKEGD---------ELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 83 GHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRIVSENpqregcsytihaegderGTKVTPGleeKEGELLV 162
Cdd:cd05969 232 GVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDEN-----------------GNELPPG---TKGILAL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 163 RG--PSVFREYWNKPEETKSAFtLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAV 239
Cdd:cd05969 292 KPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRdEDGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGV 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 240 IGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05969 370 IGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
46-304 |
3.07e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 155.60 E-value: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 46 PHAQDFLRAVCEE-----KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMA-LSGPLTTAARLPGSVGTPLPG 119
Cdd:PRK13295 295 PFLTDLTRAVKESgrpvsSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVtLTKLDDPDERASTTDGCPLPG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 120 VQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFtlDGWFKTGDtVVFKDG 199
Cdd:PRK13295 375 VEVRVV-----------------DADGAPLPAG---QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGD-LARIDA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 200 QYWIR--GRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARDV 275
Cdd:PRK13295 432 DGYIRisGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFlkAQKV 510
|
250 260
....*....|....*....|....*....
gi 1034116931 276 LAPYaVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK13295 511 AKQY-IPERLVVRDALPRTPSGKIQKFRL 538
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1-306 |
5.70e-43 |
|
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: 152.50 E-value: 5.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEYYDRHftqphaqdflravCEEKIRLMVSGSAALPLPVLE--KW 78
Cdd:cd05912 148 LVDKFDAEQVLHLINSG---KVTIISVVPTMLQRLLEILGEG-------------YPNNLRCILLGGGPAPKPLLEqcKE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 79 KNITghtLLERYGMTEIG---MALSgPLTTAARLpGSVGTPLPGVQVRIVSENpqregcsytihaegdergtkvtpGLEE 155
Cdd:cd05912 212 KGIP---VYQSYGMTETCsqiVTLS-PEDALNKI-GSAGKPLFPVELKIEDDG-----------------------QPPY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 156 KEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 234
Cdd:cd05912 264 EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIgYLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAI 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034116931 235 TDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd05912 342 KEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
21-304 |
6.87e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 152.28 E-value: 6.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDrhFTQphaQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MAL 99
Cdd:PRK12492 307 RFSALLGLNTLFVALMDHPG--FKD---LDF------SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVAS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 100 SGPLTTAARLpGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETK 179
Cdd:PRK12492 376 TNPYGELARL-GTVGIPVPGTALKVI-----------------DDDGNELPLG---ERGELCIKGPQVMKGYWQQPEATA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 180 SAFTLDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLR 258
Cdd:PRK12492 435 EALDAEGWFKTGDiAVIDPDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVAR 513
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034116931 259 EGhSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12492 514 DP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-215 |
1.01e-41 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 149.00 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFLSSETPRINVFMAVPTIYTKLMEyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:pfam00501 231 LPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGHTLLERYGMTE--IGMALSGPLTTAARLPGSVGTPLPGVQVRIVSENPQREgcsytihaegdergtkVTPGleeKEG 158
Cdd:pfam00501 300 LFGGALVNGYGLTEttGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEP----------------VPPG---EPG 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 159 ELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTG 215
Cdd:pfam00501 361 ELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
59-304 |
1.39e-41 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 151.36 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmalSGPLTTA-----ARLPGSVGTPLPGVQVRIVsenpqreg 133
Cdd:PRK08974 326 SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTE-----CSPLVSVnpydlDYYSGSIGLPVPSTEIKLV-------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 134 csytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDII 212
Cdd:PRK08974 393 ---------DDDGNEVPPG---EPGELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMdEEGFLRIVDRKK-DMI 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 213 KTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREgHSLSHRELKEWARDVLAPYAVPSELVLVEEIP 292
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELP 537
|
250
....*....|..
gi 1034116931 293 RNQMGKIDKKAL 304
Cdd:PRK08974 538 KSNVGKILRREL 549
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
34-306 |
1.50e-41 |
|
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: 149.12 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 34 KLMEYY--DRHFTQPHAQDFLRAVCEEK----IRLMVSGSAALPL-PVLEKW-KNITGHTLLERYGMTEIGMALSGPLTT 105
Cdd:cd05971 175 DLMSRYgvTTAFLPPTALKMMRQQGEQLkhaqVKLRAIATGGESLgEELLGWaREQFGVEVNEFYGQTECNLVIGNCSAL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 106 AARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPS--VFREYWNKPEETKSAFT 183
Cdd:cd05971 255 FPIKPGSMGKPIPGHRVAIV-----------------DDNGTPLPPG---EVGEIAVELPDpvAFLGYWNNPSATEKKMA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 184 LDgWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS 262
Cdd:cd05971 315 GD-WLLTGDLgRKDSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET 392
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034116931 263 LSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd05971 393 PSDalaREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-301 |
1.59e-41 |
|
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: 147.04 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKwknitghtLLERYGMTEI----GMALSGPLTTAARLP-------GSVGTPLPGVQVRIVSEn 128
Cdd:cd05917 120 LRTGIMAGAPCPPELMKR--------VIEVMNMKDVtiayGMTETSPVSTQTRTDdsiekrvNTVGRIMPHTEAKIVDP- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 129 pqregcsytihaegderGTKVTPGLEEKeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRT 207
Cdd:cd05917 191 -----------------EGGIVPPVGVP-GELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 208 SvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVL 287
Cdd:cd05917 253 K-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFF 331
|
250
....*....|....
gi 1034116931 288 VEEIPRNQMGKIDK 301
Cdd:cd05917 332 VDEFPLTVSGKIQK 345
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
21-304 |
1.79e-41 |
|
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: 147.24 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEyydrhftQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:cd05944 97 RITSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 101 GPLTTAARLPGSVGTPLPGVQVRIVSENPQREgcsYTIHAEGDErgtkvtpgleekEGELLVRGPSVFREYWNKpEETKS 180
Cdd:cd05944 164 VNPPDGPKRPGSVGLRLPYARVRIKVLDGVGR---LLRDCAPDE------------VGEICVAGPGVFGGYLYT-EGNKN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 181 AFTLDGWFKTGDTV-VFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRE 259
Cdd:cd05944 228 AFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034116931 260 GHSLSHRELKEWARDVLAPY-AVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05944 307 GAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
59-286 |
5.68e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 150.25 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEigmalSGPLTTA----ARLPGSVGTPLPGVQVRIvsenpqregc 134
Cdd:COG1022 348 RLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTE-----TSPVITVnrpgDNRIGTVGPPLPGVEVKI---------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 135 sytihAEgdergtkvtpgleekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIK 213
Cdd:COG1022 412 -----AE---------------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELdEDGFLRITGRKK-DLIV 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 214 T-GGYKVSALEVEWHLLAHPSITDVAVIGvpDmtwgQR--VTAVVTLREGhslshrELKEWARDVLAPYAVPSELV 286
Cdd:COG1022 471 TsGGKNVAPQPIENALKASPLIEQAVVVG--D----GRpfLAALIVPDFE------ALGEWAEENGLPYTSYAELA 534
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
2-301 |
1.62e-40 |
|
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: 147.06 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 2 MPEFSPQQVWEkflSSETPRINVFMAVPTIYTKLMEyydrhftqphAQDFLRAVCEEKIRLMVSGSAAlPLPVLEKWKNI 81
Cdd:cd12118 205 LRKVDAKAIYD---LIEKHKVTHFCGAPTVLNMLAN----------APPSDARPLPHRVHVMTAGAPP-PAAVLAKMEEL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 tGHTLLERYGMTEIgmalSGPLTTAARLPGSVGTPLPgVQVRIVSenpqREGCSYTIHAE---GDERGTKVTPGLEEKEG 158
Cdd:cd12118 271 -GFDVTHVYGLTET----YGPATVCAWKPEWDELPTE-ERARLKA----RQGVRYVGLEEvdvLDPETMKPVPRDGKTIG 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 159 ELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDV 237
Cdd:cd12118 341 EIVFRGNIVMKGYLKNPEATAEAFR-GGWFHSGDlAVIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEA 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 238 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVlVEEIPRNQMGKIDK 301
Cdd:cd12118 419 AVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQK 481
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-304 |
2.36e-40 |
|
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: 146.13 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDRhftqphaQDFlravceEKIRLMVSGSAALPLPVLEKW-KNITGHTLLERYGMTEI-GMA 98
Cdd:cd05930 184 GITVLHLTPSLLRLLLQELEL-------AAL------PSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEAtVDA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 99 LSGPLTTAARLPGSV--GTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPE 176
Cdd:cd05930 251 TYYRVPPDDEEDGRVpiGRPIPNTRVYVL-----------------DENLRPVPPG---VPGELYIGGAGLARGYLNRPE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 177 ETKSAFTLDGWF------KTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ 249
Cdd:cd05930 311 LTAERFVPNPFGpgermyRTGDLVRWLpDGNLEFLGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEK 389
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 250 RVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05930 390 RLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
18-301 |
6.78e-40 |
|
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: 142.25 E-value: 6.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMEYydrhftqPHAQDFLRAvceeKIRLMVSGSAALPLPVLEKWKNITG-HTLLERYGMTEIG 96
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 97 MA-LSGPLTTAARLPGSVGTPLPGVQVRIVSEnpqregcsytihaegdergtkvtpgleekeGELLVRGPSVFREYWNKP 175
Cdd:cd17638 155 VAtMCRPGDDAETVATTCGRACPGFEVRIADD------------------------------GEVLVRGYNVMQGYLDDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 176 EETKSAFTLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:cd17638 205 EATAEAIDADGWLHTGDVGELDErGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAF 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034116931 255 VTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17638 284 VVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
28-308 |
7.34e-40 |
|
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: 142.08 E-value: 7.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 28 VPTIYTKLMeyyDRHFTQPhAQDFLRAVceekirlmVSGSAALPLPVLEKWKNiTGHTLLERYGMTEIGMALSGpLTTAA 107
Cdd:cd17630 93 VPTQLQRLL---DSGQGPA-ALKSLRAV--------LLGGAPIPPELLERAAD-RGIPLYTTYGMTETASQVAT-KRPDG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 108 RLPGSVGTPLPGVQVRIVSEnpqregcsytihaegdergtkvtpgleekeGELLVRGPSVFREYWNKPEEtkSAFTLDGW 187
Cdd:cd17630 159 FGRGGVGVLLPGRELRIVED------------------------------GEIWVGGASLAMGYLRGQLV--PEFNEDGW 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 188 FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLShr 266
Cdd:cd17630 207 FTTKDLGELhADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA-- 283
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034116931 267 ELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:cd17630 284 ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2-306 |
1.41e-39 |
|
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: 145.72 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 2 MPEFSPQQVWEKFlssETPRINVFMAVPTIYTKL----MEYYDRhftqphaqdflravceEKIRLMVSGSAALPLPVLEK 77
Cdd:cd05970 260 YDKFDPKALLEKL---SKYGVTTFCAPPTIYRFLiredLSRYDL----------------SSLRYCTTAGEALNPEVFNT 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 78 WKNITGHTLLERYGMTEIGMALsGPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKE 157
Cdd:cd05970 321 FKEKTGIKLMEGFGQTETTLTI-ATFPWMEPKPGSMGKPAPGYEIDLI-----------------DREGRSCEAG---EE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVR---GPSV--FREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 231
Cdd:cd05970 380 GEIVIRtskGKPVglFGGYYKDAEKTAEVWH-DGYYHTGDAAWMdEDGYLWFVGRTD-DLIKSSGYRIGPFEVESALIQH 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 232 PSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIdKKALIR 306
Cdd:cd05970 458 PAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEelkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI-RRVEIR 534
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
60-304 |
2.08e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 145.29 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAARLpGSVGTPLPGVQVRIVsenpqregcsytih 139
Cdd:PRK05677 328 LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQV-GTIGIPVPSTLCKVI-------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 140 aegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYK 218
Cdd:PRK05677 393 ---DDDGNELPLG---EVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKK-DMILVSGFN 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 219 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
....*.
gi 1034116931 299 IDKKAL 304
Cdd:PRK05677 546 ILRREL 551
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
18-304 |
2.91e-39 |
|
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: 143.00 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMeyydrhftqphAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIgM 97
Cdd:cd05935 170 EKYKVTFWTNIPTMLVDLL-----------ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET-M 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 ALSGPLTTAARLPGSVGTPLPGVQVRIVSEnpqregcsytihaegdERGTKVTPGleeKEGELLVRGPSVFREYWNKPEE 177
Cdd:cd05935 238 SQTHTNPPLRPKLQCLGIP*FGVDARVIDI----------------ETGRELPPN---EVGEIVVRGPQIFKGYWNRPEE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 178 TKSAFTLDG---WFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTA 253
Cdd:cd05935 299 TEESFIEIKgrrFFRTGDLgYMDEEGYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKA 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 254 VVTLREGH--SLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05935 378 FIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
59-304 |
3.01e-39 |
|
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: 144.30 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTE---IGMALSGPLTTAARlPGSVGTPLPGVQVRIVSEnpqregc 134
Cdd:cd05904 276 SLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTEstgVVAMCFAPEKDRAK-YGSVGRLVPNVEAKIVDP------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 135 sytihaegdERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIK 213
Cdd:cd05904 348 ---------ETGESLPPN---QTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIdEDGYLFIVDRLK-ELIK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 214 TGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW-ARDVlAPYAVPSELVLVEEIP 292
Cdd:cd05904 415 YKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFvAKQV-APYKKVRKVAFVDAIP 493
|
250
....*....|..
gi 1034116931 293 RNQMGKIDKKAL 304
Cdd:cd05904 494 KSPSGKILRKEL 505
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
1-301 |
6.39e-39 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 143.44 E-value: 6.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEF-SPQQVWEKFLSSETpriNVFMAVPTIYTKLMeyydrhftqphAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWK 79
Cdd:TIGR02262 234 LMGERpTPDAVFDRLRRHQP---TIFYGVPTLYAAML-----------ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 80 NITGHTLLERYGMTEIGMALSGPLTTAARLpGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGE 159
Cdd:TIGR02262 300 ARFGVDIVDGIGSTEMLHIFLSNLPGDVRY-GTSGKPVPGYRLRLV-----------------GDGGQDVADG---EPGE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:TIGR02262 359 LLISGPSSATMYWNNRAKSRDTF-QGEWTRSGDKyVRNDDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAA 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:TIGR02262 437 VVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
5-306 |
9.45e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 143.26 E-value: 9.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 5 FSPQQVWEKFlssETPRINVFMAVPTIYTKLMEY--YDRHftqPHAQdfLRAVceekIRL---MVSGSAALPLPVLekwk 79
Cdd:PRK07470 241 FDPAEVWALV---ERHRVTNLFTVPTILKMLVEHpaVDRY---DHSS--LRYV----IYAgapMYRADQKRALAKL---- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 80 nitGHTLLERYGMTEIgmalSGPLTTaarLPGSVGTPLPGVQVRIVSENPQREGCSYTIHaegDERGTKVTPGleeKEGE 159
Cdd:PRK07470 305 ---GKVLVQYFGLGEV----TGNITV---LPPALHDAEDGPDARIGTCGFERTGMEVQIQ---DDEGRELPPG---ETGE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK07470 369 ICVIGPAVFAGYYNNPEANAKAFR-DGWFRTGDLgHLDARGFLYITGRAS-DMYISGGSNVYPREIEEKLLTHPAVSEVA 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKaLIR 306
Cdd:PRK07470 447 VLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK-MVR 513
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
22-304 |
1.73e-38 |
|
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: 141.23 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 22 INVFMAVPTIYTKLMEyyDRHFTQPHAQDfLRAV--CEEkirlmvsgsaALPLPVLEKWKNIT-GHTLLERYGMTEIGMA 98
Cdd:cd05945 189 ITVWVSTPSFAAMCLL--SPTFTPESLPS-LRHFlfCGE----------VLPHKTARALQQRFpDARIYNTYGPTEATVA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 99 LSG------PLTTAARLPgsVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYW 172
Cdd:cd05945 256 VTYievtpeVLDGYDRLP--IGYAKPGAKLVIL-----------------DEDGRPVPPG---EKGELVISGPSVSKGYL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 173 NKPEETKSAFTLD---GWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWG 248
Cdd:cd05945 314 NNPEKTAAAFFPDegqRAYRTGDLVRLEaDGLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKV 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034116931 249 QRVTAVVTLREGHSLSH-RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05945 393 TELIAFVVPKPGAEAGLtKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
4-304 |
2.24e-38 |
|
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: 141.49 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 4 EFSPQQVWEKFlssETPRINVFMAVPTIYTKLMeyydrhftqpHAQDFLRAVCEEKIRLMVSGsAALPLPVLEKWKNITG 83
Cdd:cd05923 227 EFDPADALKLI---EQERVTSLFATPTHLDALA----------AAAEFAGLKLSSLRHVTFAG-ATMPDAVLERVNQHLP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 84 HTLLERYGMTEIGMALSGPlttAARlPGSVGTPLPGVQVRIVSENpqreGCSYTIHAEGDErgtkvtpgleekeGELLVR 163
Cdd:cd05923 293 GEKVNIYGTTEAMNSLYMR---DAR-TGTEMRPGFFSEVRIVRIG----GSPDEALANGEE-------------GELIVA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 164 --GPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVI 240
Cdd:cd05923 352 aaADAAFTGYLNQPEATAKKLQ-DGWYRTGDVgYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 241 GVPDMTWGQRVTAVVTLREGhSLSHRELKEWARDV-LAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05923 430 GVADERWGQSVTACVVPREG-TLSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
70-304 |
2.72e-38 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 141.74 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 70 LPLPVLEKWKNIT--GHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGT 147
Cdd:PRK08008 297 LNLSDQEKDAFEErfGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIR-----------------DDHNR 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 148 KVTPGleeKEGELLVRG---PSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALE 223
Cdd:PRK08008 360 PLPAG---EIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTgYVDEEGFFYFVDR-RCNMIKRGGENVSCVE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 224 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKA 303
Cdd:PRK08008 436 LENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKN 515
|
.
gi 1034116931 304 L 304
Cdd:PRK08008 516 L 516
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
82-304 |
4.41e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 140.79 E-value: 4.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 TGHTLLERYGMTEigmALSG-PLTTAAR---LPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGLEeke 157
Cdd:PRK06145 289 TRARYIDAYGLTE---TCSGdTLMEAGReieKIGSTGRALAHVEIRIA-----------------DGAGRWLPPNMK--- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PRK06145 346 GEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEeGFLYLTDRKK-DMIISGGENIASSEVERVIYELPEVAE 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK06145 424 AAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
21-304 |
4.80e-38 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 141.70 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMeyydrhftqpHAQDFlRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:PRK07059 301 QVHIFPAVNTLYNALL----------NNPDF-DKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVAT 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 101 GPLTTAARLPGSVGTPLPGVQVRIvsenpqRegcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKS 180
Cdd:PRK07059 370 CNPVDATEFSGTIGLPLPSTEVSI------R-----------DDDGNDLPLG---EPGEICIRGPQVMAGYWNRPDETAK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 181 AFTLDGWFKTGDTVVFKDgqywiRGRTSV-----DIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVV 255
Cdd:PRK07059 430 VMTADGFFRTGDVGVMDE-----RGYTKIvdrkkDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034116931 256 tLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07059 505 -VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-304 |
6.75e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 140.10 E-value: 6.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEkflSSETPRINVFMAVPTIYTKLMEYYDRHftqphaqdflraVCEEKIRLMVSGSAALPLPVLE--KW 78
Cdd:PRK03640 212 LVEKFDAEKINK---LLQTGGVTIISVVSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEqcKE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 79 KNITghtLLERYGMTEIG---MALSgPLTTAARLpGSVGTPLPGVQVRIVSENpqregcsytihaegdergtkvTPGLEE 155
Cdd:PRK03640 277 KGIP---VYQSYGMTETAsqiVTLS-PEDALTKL-GSAGKPLFPCELKIEKDG---------------------VVVPPF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 156 KEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 234
Cdd:PRK03640 331 EEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLdEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGV 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 235 TDVAVIGVPDMTWGQRVTAVVTLreGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK03640 409 AEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
43-299 |
8.35e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 140.87 E-value: 8.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 43 FTQPHAQDFlravCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTE-IGMALSGPLTTAARlpGSVGTPLPGVQ 121
Cdd:PRK08314 294 LASPGLAER----DLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPKL--QCLGIPTFGVD 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 122 VRIVseNPqregcsytihaegdERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAF-TLDG--WFKTGDT-VVFK 197
Cdd:PRK08314 368 ARVI--DP--------------ETLEELPPG---EVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRTGDLgRMDE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 198 DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGH--SLSHRELKEWARDV 275
Cdd:PRK08314 429 EGYFFITDRLK-RMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREH 507
|
250 260
....*....|....*....|....
gi 1034116931 276 LAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK08314 508 MAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
77-304 |
1.66e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 140.18 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 77 KWKNITGHTLLE-RYGMTEI-------------GMALSGPlttaarlPGSVGTPLPGVQVRIVSEnpqregcsytihaeg 142
Cdd:PRK06178 346 RWRALTGSVLAEaAWGMTEThtcdtftagfqddDFDLLSQ-------PVFVGLPVPGTEFKICDF--------------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 143 dERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVFkDGQYWIR--GRTSvDIIKTGGYKVS 220
Cdd:PRK06178 404 -ETGELLPLG---AEGEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDIGKI-DEQGFLHylGRRK-EMLKVNGMSVF 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 221 ALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPsELVLVEEIPRNQMGKID 300
Cdd:PRK06178 477 PSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVR 555
|
....
gi 1034116931 301 KKAL 304
Cdd:PRK06178 556 KQDL 559
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
24-286 |
1.91e-37 |
|
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: 138.50 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 24 VFMAVPTIYTKLMEYYDRHFTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPL 103
Cdd:cd05907 177 VFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 104 TTAARlPGSVGTPLPGVQVRIVSEnpqregcsytihaegdergtkvtpgleekeGELLVRGPSVFREYWNKPEETKSAFT 183
Cdd:cd05907 256 PGDNR-IGTVGKPLPGVEVRIADD------------------------------GEILVRGPNVMLGYYKNPEATAEALD 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 184 LDGWFKTGDTVVFK-DGQYWIRGRtSVDIIKT-GGYKVSALEVEWHLLAHPSITDVAVIGvpDmtwgQR--VTAVVTLRE 259
Cdd:cd05907 305 ADGWLHTGDLGEIDeDGFLHITGR-KKDLIITsGGKNISPEPIENALKASPLISQAVVIG--D----GRpfLVALIVPDP 377
|
250 260
....*....|....*....|....*..
gi 1034116931 260 GhslshrELKEWARDVLAPYAVPSELV 286
Cdd:cd05907 378 E------ALEAWAEEHGIAYTDVAELA 398
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
4-299 |
7.72e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 138.49 E-value: 7.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 4 EFSPQQvWEKFLSSEtpRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRAVCeekirlmvsgSAALPL-PVLEKW-KNI 81
Cdd:PRK04319 281 RFSPER-WYRILEDY--KVTVWYTAPTAIRMLMGAGDDLVKK-YDLSSLRHIL----------SVGEPLnPEVVRWgMKV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 TGHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELL 161
Cdd:PRK04319 347 FGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIV-----------------DDQGNELPPN---RMGNLA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 162 VRG--PSVFREYWNKPEETKSAFtLDGWFKTGDtVVFKD--GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDV 237
Cdd:PRK04319 407 IKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGD-SAYMDedGYFWFQGRVD-DVIKTSGERVGPFEVESKLMEHPAVAEA 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 238 AVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK04319 484 GVIGKPDPVRGEIIKAFVALRPGYEPSEelkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
21-304 |
3.16e-36 |
|
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: 135.13 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDRHFTQPHAqdflravceekIRLMVSGSAALPLPVLEKWKNITGH---TLLERYGMTEIGM 97
Cdd:cd17643 184 GVTVLNQTPSAFYQLVEAADRDGRDPLA-----------LRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 ALSGPLTTAARLPGS----VGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWN 173
Cdd:cd17643 253 HVTFRPLDAADLPAAaaspIGRPLPGLRVYVL-----------------DADGRPVPPG---VVGELYVSGAGVARGYLG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 174 KPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 245
Cdd:cd17643 313 RPELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 246 TWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17643 392 PGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
2-304 |
5.22e-36 |
|
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: 135.67 E-value: 5.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 2 MPEFSPQQVWEKFlsSETPrINVFMAVPTIYTKLMeyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNI 81
Cdd:cd05928 250 LPRFDPLVILKTL--SSYP-ITTFCGAPTVYRMLV------------QQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 TGHTLLERYGMTEIGMALSGPLTTAARlPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELL 161
Cdd:cd05928 315 TGLDIYEGYGQTETGLICANFKGMKIK-PGSMGKASPPYDVQII-----------------DDNGNVLPPG---TEGDIG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 162 VR-GP----SVFREYWNKPEETKSAFTLDGWFkTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSIT 235
Cdd:cd05928 374 IRvKPirpfGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVV 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 236 DVAVIGVPDMTWGQRVTAVVTLREGHsLSH------RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05928 452 ESAVVSSPDPIRGEVVKAFVVLAPQF-LSHdpeqltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
90-300 |
6.94e-36 |
|
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: 131.66 E-value: 6.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEIGmalsGPLTTAA---RLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPS 166
Cdd:cd17636 143 YGQTEVM----GLATFAAlggGAIGGAGRPSPLVQVRIL-----------------DEDGREVPDG---EVGEIVARGPT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 167 VFREYWNKPEETkSAFTLDGWFKTGD--------TVVFkdgqywIRGRTSvdIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd17636 199 VMAGYWNRPEVN-ARRTRGGWHHTNDlgrrepdgSLSF------VGPKTR--MIKSGAENIYPAEVERCLRQHPAVADAA 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:cd17636 270 VIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
46-306 |
8.31e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 135.26 E-value: 8.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 46 PHAQDFLRAVCEEK-----IRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTE-IGMALSGPLTTAARLPGSVGTPLPG 119
Cdd:PRK06087 285 PFIYDLLNLLEKQPadlsaLRFFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 120 VQVRIVSENPQregcsytihaegdergtKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KD 198
Cdd:PRK06087 364 VEIKVVDEARK-----------------TLPPG---CEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMdEA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 199 GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREG-HSLSHRELKEW-ARDVL 276
Cdd:PRK06087 424 GYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPhHSLTLEEVVAFfSRKRV 502
|
250 260 270
....*....|....*....|....*....|
gi 1034116931 277 APYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK06087 503 AKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
53-304 |
9.30e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 134.90 E-value: 9.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 53 RAVCEE--------KIRLMVSGSAALPLPVL-EKWKNITGHTLLERYGMTEIGmalsgPLTT------AARLPGSVGTPL 117
Cdd:PRK07786 277 QAVCAEqqarprdlALRVLSWGAAPASDTLLrQMAATFPEAQILAAFGQTEMS-----PVTCmllgedAIRKLGSVGKVI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 118 PGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTV-VF 196
Cdd:PRK07786 352 PTVAARVV-----------------DENMNDVPVG---EVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVrQD 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 197 KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLR-EGHSLSHRELKEWARDV 275
Cdd:PRK07786 411 EEGYVWVVDRKK-DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnDDAALTLEDLAEFLTDR 489
|
250 260
....*....|....*....|....*....
gi 1034116931 276 LAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07786 490 LARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-308 |
9.46e-36 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 135.01 E-value: 9.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 25 FMAVPTIYTKLMEyydrhftQPHAQDFLRAvcEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEI-------GM 97
Cdd:PRK05852 271 YTAVPTIHQILLE-------RAATEPSGRK--PAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttQI 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 ALSGPLTTAARLPGSVGTPlPGVQVRIVSENpqregcsytihaegderGTKVTPGleeKEGELLVRGPSVFREYWNKPEE 177
Cdd:PRK05852 342 EGIGQTENPVVSTGLVGRS-TGAQIRIVGSD-----------------GLPLPAG---AVGEVWLRGTTVVRGYLGDPTI 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 178 TKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVT 256
Cdd:PRK05852 401 TAANFT-DGWLRTGDLgSLSAAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV 478
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034116931 257 LREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:PRK05852 479 PRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
66-308 |
1.12e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 131.71 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 66 GSAALPLPVLEKWKNItGHTLLERYGMTEigmalsgpltTAArlpGSV--GTPLPGVQVRIVsenpqregcsytihaegd 143
Cdd:PRK07824 159 GGGPAPAPVLDAAAAA-GINVVRTYGMSE----------TSG---GCVydGVPLDGVRVRVE------------------ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 144 ergtkvtpgleekEGELLVRGPSVFREYWNKPEEtkSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:PRK07824 207 -------------DGRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 224 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKA 303
Cdd:PRK07824 271 VEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRA 350
|
....*
gi 1034116931 304 LIRHF 308
Cdd:PRK07824 351 LVRRF 355
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
90-301 |
1.95e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 134.52 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEIG--MALSGPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSV 167
Cdd:PRK12583 350 YGMTETSpvSLQTTAADDLERRVETVGRTQPHLEVKVV-----------------DPDGATVPRG---EIGELCTRGYSV 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 168 FREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMT 246
Cdd:PRK12583 410 MKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGR-SKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 247 WGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:PRK12583 489 YGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1-305 |
1.68e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 131.18 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLM-------EYYDRhftqphaqdflravceEKIRLMVSGSAALPL 72
Cdd:PRK08276 217 VMEKFDA----EEALALiERYRVTHSQLVPTMFVRMLklpeevrARYDV----------------SSLRVAIHAAAPCPV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 73 PVleKWKNIT--GHTLLERYGMTE-IGMALSGPLTTAARlPGSVGTPLPGVqVRIVsenpqregcsytihaegDERGTKV 149
Cdd:PRK08276 277 EV--KRAMIDwwGPIIHEYYASSEgGGVTVITSEDWLAH-PGSVGKAVLGE-VRIL-----------------DEDGNEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 150 TPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHL 228
Cdd:PRK08276 336 PPG---EIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVgYLDEDGYLYLTDRKS-DMIISGGVNIYPQEIENLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 229 LAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 305
Cdd:PRK08276 412 VTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
5-301 |
2.23e-34 |
|
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: 127.52 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 5 FSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYdrhftqphaqdflraVCEEKIRLMVSGSAALPLPVLEKWKNITGH 84
Cdd:cd17633 75 FNPKSWIRKI---NQYNATVIYLVPTMLQALARTL---------------EPESKIKSIFSSGQKLFESTKKKLKNIFPK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 85 T-LLERYGMTEIGMaLSGPLTTAARLPGSVGTPLPGVQVRIvsenpqREgcsytihAEGDERGTkvtpgleekegeLLVR 163
Cdd:cd17633 137 AnLIEFYGTSELSF-ITYNFNQESRPPNSVGRPFPNVEIEI------RN-------ADGGEIGK------------IFVK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 164 GPSVFREYWNKPEETKsaftlDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 242
Cdd:cd17633 191 SEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDeEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 243 PDMTWGQRVTAVVTlreGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17633 265 PDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
21-304 |
3.29e-34 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 129.49 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDRhftqphaqdflravcEEKIRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTEIG--MA 98
Cdd:TIGR01923 197 RVTHISLVPTQLNRLLDEGGH---------------NENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTETCsqVT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 99 LSGPLTTAARlpGSVGTPLPGVQVRIVSENpqregcsytihaegdergtkvtpglEEKEGELLVRGPSVFREYWNkPEET 178
Cdd:TIGR01923 261 TATPEMLHAR--PDVGRPLAGREIKIKVDN-------------------------KEGHGEIMVKGANLMKGYLY-QGEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 179 KSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTL 257
Cdd:TIGR01923 313 TPAFEQQGWFNTGDIGELDgEGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVS 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034116931 258 REghSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:TIGR01923 392 ES--DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
47-304 |
1.21e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 129.30 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 47 HAQDFLRAVCEEKIRLMVSGsAALPLPVLEKWKNItGHTLLERYGMTEIgmalSGPLTTAARLPGSVGTPLPGvQVRIVS 126
Cdd:PRK08162 286 NAPAEWRAGIDHPVHAMVAG-AAPPAAVIAKMEEI-GFDLTHVYGLTET----YGPATVCAWQPEWDALPLDE-RAQLKA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 127 enpqREGCSYtiHAEGD------ERGTKVtPGLEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDG 199
Cdd:PRK08162 359 ----RQGVRY--PLQEGvtvldpDTMQPV-PADGETIGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDlAVLHPDG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 200 QYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPY 279
Cdd:PRK08162 431 YIKIKDR-SKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGF 509
|
250 260
....*....|....*....|....*
gi 1034116931 280 AVPSELVLvEEIPRNQMGKIDKKAL 304
Cdd:PRK08162 510 KVPKAVVF-GELPKTSTGKIQKFVL 533
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
90-301 |
4.45e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 127.62 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEigmalSGPLTTAARLP-------GSVGTPLPGVQVRIVSEnpqregcsytihaegdERGTKVTPGleeKEGELLV 162
Cdd:PRK08315 348 YGMTE-----TSPVSTQTRTDdplekrvTTVGRALPHLEVKIVDP----------------ETGETVPRG---EQGELCT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 163 RGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:PRK08315 404 RGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMdEEGYVNIVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVG 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 242 VPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:PRK08315 483 VPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQK 542
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
60-300 |
1.20e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 126.15 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKW----KNITghtLLERYGMTEIGMALSGplTTAarlPGSVGTPLPGVQVRivsenpqregcS 135
Cdd:PRK07798 298 LFAIASGGALFSPSVKEALlellPNVV---LTDSIGSSETGFGGSG--TVA---KGAVHTGGPRFTIG-----------P 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 136 YTIHAegDERGTKVTPGlEEKEGeLLVRGPSVFREYWNKPEETKSAF-TLDG--WFKTGD-TVVFKDGQYWIRGRTSVdI 211
Cdd:PRK07798 359 RTVVL--DEDGNPVEPG-SGEIG-WIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDrARVEADGTITLLGRGSV-C 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 212 IKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEI 291
Cdd:PRK07798 434 INTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEV 513
|
....*....
gi 1034116931 292 PRNQMGKID 300
Cdd:PRK07798 514 QRSPAGKAD 522
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3-300 |
2.04e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 123.26 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 3 PEFSPQQVWEkflSSETPRINVFMAVPTIYTK-LMEYYDRhftqPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNI 81
Cdd:cd05924 91 DRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLIDALRD----AGPYDL------SSLFAISSGGALLSPEVKQGLLEL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 TGH-TLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRivsenpqregcsytihaegDERGTKVTPGlEEKEGEL 160
Cdd:cd05924 158 VPNiTLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVL-------------------DDDGRVVPPG-SGGVGWI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 161 LVRGpSVFREYWNKPEETKSAF-TLDG--WFKTGD-TVVFKDGQYWIRGRTSVdIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:cd05924 218 ARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDrATVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAVYD 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:cd05924 296 VLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
21-304 |
5.73e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 124.60 E-value: 5.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEyydrhfTQPHAQ-DFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MA 98
Cdd:PRK08751 303 RFTAFTGVNTLFNGLLN------TPGFDQiDF------SSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 99 LSGPLTTAaRLPGSVGTPLPGVQVRIvsenpqregcsytihaeGDERGTKVTPGleeKEGELLVRGPSVFREYWNKPEET 178
Cdd:PRK08751 371 CINPLTLK-EYNGSIGLPIPSTDACI-----------------KDDAGTVLAIG---EIGELCIKGPQVMKGYWKRPEET 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 179 KSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQrVTAVVTL 257
Cdd:PRK08751 430 AKVMDADGWLHTGDIARMdEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE-IVKVVIV 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034116931 258 REGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK08751 508 KKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
13-308 |
9.72e-32 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 124.12 E-value: 9.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 13 KFLSSETPRinVFMAVPTIYTKLMEYYDRHftqPHAQDFLRAVceekirlmVSGSAALPLPVLEKWKnitghtllERYGM 92
Cdd:PRK05620 266 KIIATAMPR--VAHGVPTLWIQLMVHYLKN---PPERMSLQEI--------YVGGSAVPPILIKAWE--------ERYGV 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 93 TEI---GMALSGPLTTAARLPGSVGTplpgvQVRI---VSENPQREGCSYTIHAEGdergtKVTPGLEEKEGELLVRGPS 166
Cdd:PRK05620 325 DVVhvwGMTETSPVGTVARPPSGVSG-----EARWayrVSQGRFPASLEYRIVNDG-----QVMESTDRNEGEIQVRGNW 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 167 VFREYWNKP----------------EETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLL 229
Cdd:PRK05620 395 VTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVgSVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIM 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 230 AHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK05620 474 AAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
..
gi 1034116931 307 HF 308
Cdd:PRK05620 554 HL 555
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
5-306 |
7.78e-31 |
|
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: 120.32 E-value: 7.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 5 FSPQQVWEKFlssETPRINVFMAVPTIYTKLMeyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPL-PVLEKWKNIT- 82
Cdd:cd05973 165 FSVESTWRVI---ERLGVTNLAGSPTAYRLLM------------AAGAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAl 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 83 GHTLLERYGMTEIGMALSGPLTTAARL-PGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELL 161
Cdd:cd05973 230 GVPIHDHYGQTELGMVLANHHALEHPVhAGSAGRAMPGWRVAVL-----------------DDDGDELGPG---EPGRLA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 162 V---RGPSV-FREYWNKPEETKSAftldGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:cd05973 290 IdiaNSPLMwFRGYQLPDTPAIDG----GYYLTGDTVEFDpDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAE 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd05973 365 AAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
2-304 |
1.10e-30 |
|
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: 120.17 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 2 MPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLMEYYDrhfTQPHAQDF--LRAVCEekirlmvsgsAALPLPVL--E 76
Cdd:cd05929 200 MEKFDP----EEFLRLiERYRVTFAQFVPTMFVRLLKLPE---AVRNAYDLssLKRVIH----------AAAPCPPWvkE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 77 KWKNITGHTLLERYGMTE-IGM-ALSGP--LTTaarlPGSVGTPLPGVqVRIVsenpqregcsytihaegDERGTKVTPG 152
Cdd:cd05929 263 QWIDWGGPIIWEYYGGTEgQGLtIINGEewLTH----PGSVGRAVLGK-VHIL-----------------DEDGNEVPPG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 153 leeKEGELLVRGPSVFrEYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 231
Cdd:cd05929 321 ---EIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRS-DMIISGGVNIYPQEIENALIAH 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034116931 232 PSITDVAVIGVPDMTWGQRVTAVVT----LREGHSLSHrELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05929 396 PKVLDAAVVGVPDEELGQRVHAVVQpapgADAGTALAE-ELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-306 |
1.74e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 120.42 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEIGMAlsgplTTA-----ARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRG 164
Cdd:PRK07788 355 YGSTEVAFA-----TIAtpedlAEAPGTVGRPPKGVTVKIL-----------------DENGNEVPRG---VVGRIFVGN 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 165 PSVFREYWNkpeeTKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 243
Cdd:PRK07788 410 GFPFEGYTD----GRDKQIIDGLLSSGDVGYFdEDGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 244 DMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK07788 485 DEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
46-304 |
2.18e-30 |
|
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: 118.89 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 46 PHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTE--IGMALSGPLTTAARLPgsVGTPLPGVQVR 123
Cdd:cd17652 192 PAALAALPPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTEttVCATMAGPLPGGGVPP--IGRPVPGTRVY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 124 IVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVF 196
Cdd:cd17652 268 VL-----------------DARLRPVPPGVP---GELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARW 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 197 K-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDV 275
Cdd:cd17652 328 RaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAER 406
|
250 260
....*....|....*....|....*....
gi 1034116931 276 LAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17652 407 LPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
90-299 |
2.75e-30 |
|
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: 120.36 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEIGMALSGPLTTAARL-PGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPgleEKEGELLVRG--PS 166
Cdd:cd05966 388 WWQTETGGIMITPLPGATPLkPGSATRPFFGIEPAIL-----------------DEEGNEVEG---EVEGYLVIKRpwPG 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 167 VFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 243
Cdd:cd05966 448 MARTIYGDHERYEDTYfsKFPGYYFTGDGARRdEDGYYWITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRP 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 244 DMTWGQRVTAVVTLREGHSLSHR---ELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd05966 527 HDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1-304 |
2.99e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 119.11 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhftqphaqdfLRAVCEEKIRLMVSGsAALPLPVLEKWKN 80
Cdd:PRK07638 214 LMRKFIPNQVLDKL---ETENISVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKN 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 81 ITGH-TLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRIVSENpqregcsytihaegderGTKVTPGleeKEGE 159
Cdd:PRK07638 276 IFPYaKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEA-----------------GEEVQKG---EIGT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETKSaFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK07638 336 VYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVgYEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 239 VIGVPDMTWGQRVTAVVtlrEGHSLShRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07638 414 VIGVPDSYWGEKPVAII---KGSATK-QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1-304 |
3.63e-30 |
|
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: 119.55 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIY-----TKLMEYYDRHftqphaqdflravceekiRLMVSGSAALPLpv 74
Cdd:cd17642 258 LMYKFEE----ELFLRSlQDYKVQSALLVPTLFaffakSTLVDKYDLS------------------NLHEIASGGAPL-- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 75 lekwKNITGHTLLERYGMTEI--GMALSGplTTAARL--------PGSVGTPLPGVQVRIVSENpqregcsytihaegde 144
Cdd:cd17642 314 ----SKEVGEAVAKRFKLPGIrqGYGLTE--TTSAILitpegddkPGAVGKVVPFFYAKVVDLD---------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 145 rgTKVTPGLEEKeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:cd17642 372 --TGKTLGPNER-GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 224 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYA-VPSELVLVEEIPRNQMGKIDKK 302
Cdd:cd17642 448 LESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRR 527
|
..
gi 1034116931 303 AL 304
Cdd:cd17642 528 KI 529
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
18-304 |
4.08e-30 |
|
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: 118.55 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMEyydrhfTQPHAQDFLRAVCeekirlmvsGSAALPlPVLEKWKNITGHTLLERYGMTEIGM 97
Cdd:cd12116 214 EAHSITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLYGPTETTI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 ALSGPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEE 177
Cdd:cd12116 278 WSTAARVTAAAGPIPIGRPLANTQVYVL-----------------DAALRPVPPGVP---GELYIGGDGVAQGYLGRPAL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 178 TKSAFTLDG-------WFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTwGQ 249
Cdd:cd12116 338 TAERFVPDPfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-DR 415
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 250 RVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12116 416 RLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
61-304 |
5.60e-30 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 119.09 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 61 RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLttAARLPGSVGTPLPGVQVRIVsenpqregcsytiha 140
Cdd:PRK06155 295 RVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTH--GSQRPGSMGRLAPGFEARVV--------------- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 141 egDERGTKVTPGleeKEGELLVRG--PSVFRE-YWNKPEETKSAFTlDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGG 216
Cdd:PRK06155 358 --DEHDQELPDG---EPGELLLRAdePFAFATgYFGMPEKTVEAWR-NLWFHTGDRVVRDaDGWFRFVDRIK-DAIRRRG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 217 YKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQM 296
Cdd:PRK06155 431 ENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTEN 510
|
....*...
gi 1034116931 297 GKIDKKAL 304
Cdd:PRK06155 511 GKVQKFVL 518
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
53-304 |
1.40e-29 |
|
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: 117.44 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 53 RAVCEEKIRLMVsgsAALPlpvlekwknitGHTLLERYGMTEIGMALSGPL---TTAARLPGSVGTPLPGVQVRIVsenp 129
Cdd:cd17651 264 QLVLTEDLREFC---AGLP-----------GLRLHNHYGPTETHVVTALSLpgdPAAWPAPPPIGRPIDNTRVYVL---- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 130 qregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVF-KDGQYW 202
Cdd:cd17651 326 -------------DAALRPVPPGVP---GELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWlPDGELE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 203 IRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVP 282
Cdd:cd17651 390 FLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVP 468
|
250 260
....*....|....*....|..
gi 1034116931 283 SELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17651 469 SAFVLLDALPLTPNGKLDRRAL 490
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
60-234 |
4.72e-29 |
|
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: 115.62 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPLTTAARLpGSVGTPLPGVQVRIVSENPQREgcsytih 139
Cdd:cd05914 236 IKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRL-GSAGKVIDGVEVRIDSPDPATG------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 140 aegdergtkvtpgleekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQY-WIRGRTSVDIIKTGGYK 218
Cdd:cd05914 307 -----------------EGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKN 369
|
170
....*....|....*.
gi 1034116931 219 VSALEVEWHLLAHPSI 234
Cdd:cd05914 370 IYPEEIEAKINNMPFV 385
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
28-307 |
4.96e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 116.40 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 28 VPTIYTKLMEYYDrhftqphaqDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAA 107
Cdd:PRK13382 291 VPVMFDRIMDLPA---------EVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 108 RLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRGPSVFREYwnKPEETKSafTLDGW 187
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRIL-----------------DQDFREVPTG---EVGTIFVRNDTQFDGY--TSGSTKD--FHDGF 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 188 FKTGDTVVFKD-GQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHR 266
Cdd:PRK13382 418 MASGDVGYLDEnGRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPE 496
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034116931 267 ELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRH 307
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
24-304 |
6.30e-29 |
|
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: 115.51 E-value: 6.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 24 VFMAVPTiytkLMEYYDRhftQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPL 103
Cdd:cd05909 240 ILLGTPT----FLRGYAR---AAHPEDF------SSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 104 TTAARLPGSVGTPLPGVQVRIVSEnpqregcsytihaEGDErgtkvtPGLEEKEGELLVRGPSVFREYWNKPEETKSAFT 183
Cdd:cd05909 307 PQSPNKEGTVGRPLPGMEVKIVSV-------------ETHE------EVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFG 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 184 lDGWFKTGDTVVFKDGQY-WIRGRTSvDIIKTGGYKVSALEVEWHLLAH-PSITDVAVIGVPDMTWGQRVTAVVTlreGH 261
Cdd:cd05909 368 -DGWYDTGDIGKIDGEGFlTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT---TT 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034116931 262 SLSHRELKEWARDVLAP-YAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05909 443 DTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
28-301 |
7.19e-29 |
|
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: 113.12 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 28 VPTIYTKLMEYYdrhftqphaQDFLRAVceEKIRLMVSGSAalpLPVLEKWKNI--TGHT-LLERYGMTEIGMALSGPLT 104
Cdd:cd17635 98 VPTLLSKLVSEL---------KSANATV--PSLRLIGYGGS---RAIAADVRFIeaTGLTnTAQVYGLSETGTALCLPTD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 105 TAARLPGSVGTPLPGVQVRIVSenpqregcsytihaegdergTKVTPGLEEKEGELLVRGPSVFREYWNKPEETKSAFTl 184
Cdd:cd17635 164 DDSIEINAVGRPYPGVDVYLAA--------------------TDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 185 DGWFKTGDTV-VFKDGQYWIRGRTSVDIIKtGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSL 263
Cdd:cd17635 223 DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDE 301
|
250 260 270
....*....|....*....|....*....|....*....
gi 1034116931 264 SH-RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17635 302 NAiRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
7-304 |
9.13e-29 |
|
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: 114.84 E-value: 9.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 7 PQQVWEKFlssETPRINVFMAVPTIYTKL--MEYYD------RHFTQPHA---QDFLRAVCEekirlmvsgsaALPlpvl 75
Cdd:cd05922 195 DDAFWEDL---REHGATGLAGVPSTYAMLtrLGFDPaklpslRYLTQAGGrlpQETIARLRE-----------LLP---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 76 ekwknitGHTLLERYGMTEIGMALSG-PLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGle 154
Cdd:cd05922 257 -------GAQVYVMYGQTEATRRMTYlPPERILEKPGSIGLAIPGGEFEIL-----------------DDDGTPTPPG-- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 155 eKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS 233
Cdd:cd05922 311 -EPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGRRD-RMIKLFGNRISPTEIEAAARSIGL 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 234 ITDVAVIGVPDmTWGQRVTAVVTLREGHSLShrELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05922 389 IIEAAAVGLPD-PLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
21-308 |
1.67e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 114.94 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMeyydrHFTQPHAqdflrAVCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTE-IGMA 98
Cdd:PLN02574 292 KVTHFPVVPPILMALT-----KKAKGVC-----GEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEsTAVG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 99 LSGPLTTAARLPGSVGTPLPGVQVRIVSEnpqregcsytihaegdERGTKVTPGleeKEGELLVRGPSVFREYWNKPEET 178
Cdd:PLN02574 362 TRGFNTEKLSKYSSVGLLAPNMQAKVVDW----------------STGCLLPPG---NCGELWIQGPGVMKGYLNNPKAT 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 179 KSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTL 257
Cdd:PLN02574 423 QSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVR 501
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 258 REGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:PLN02574 502 RQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
21-306 |
6.15e-28 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 113.36 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIG--- 96
Cdd:PLN02860 260 NVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEACssl 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 97 --MALSGPL---------------TTAARLPGS--VGTPLPGVQVRIVSENPQREGcsytihaegdergtkvtpgleeke 157
Cdd:PLN02860 331 tfMTLHDPTlespkqtlqtvnqtkSSSVHQPQGvcVGKPAPHVELKIGLDESSRVG------------------------ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 gELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PLN02860 387 -RILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVYPEEVEAVLSQHPGVAS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREG--------------HSLSHRELKEWARDV-LAPYAVPSELVLVEE-IPRNQMGKId 300
Cdd:PLN02860 465 VVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKI- 543
|
....*.
gi 1034116931 301 KKALIR 306
Cdd:PLN02860 544 RRDEVR 549
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
60-304 |
9.46e-28 |
|
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: 111.69 E-value: 9.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKnITGHTLLERYGMTE--IGMALSGPLTTAARLPGSV--GTPLPGVQVRIVsenpqregcs 135
Cdd:cd17649 214 LRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEatVTPLVWKCEAGAARAGASMpiGRPLGGRSAYIL---------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 136 ytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDG-------WFKTGDTVVFK-DGQYWIRGRt 207
Cdd:cd17649 283 -------DADLNPVPVGVT---GELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGR- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 208 sVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSH--RELKEWARDVLAPYAVPSE 284
Cdd:cd17649 352 -VDhQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAH 429
|
250 260
....*....|....*....|
gi 1034116931 285 LVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17649 430 LVFLARLPLTPNGKLDRKAL 449
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1-304 |
1.00e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 112.10 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 1 MMPEFSPqqvwEKFLSS-ETPRI-NVFMaVPTIYTKLM-------EYYDrhftqphaQDFLRAVceekirlmVSGSAALP 71
Cdd:PRK12406 226 LQPRFDP----EELLQLiERHRItHMHM-VPTMFIRLLklpeevrAKYD--------VSSLRHV--------IHAAAPCP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 72 LPV----LEKWknitGHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGT 147
Cdd:PRK12406 285 ADVkramIEWW----GPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFV-----------------DEDGR 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 148 KVTPGleeKEGELLVRGPSV--FrEYWNKPEEtKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEV 224
Cdd:PRK12406 344 PLPQG---EIGEIYSRIAGNpdF-TYHNKPEK-RAEIDRGGFITSGDVgYLDADGYLFLCDRKR-DMVISGGVNIYPAEI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 225 EWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12406 418 EAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
13-241 |
1.18e-27 |
|
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: 111.68 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 13 KFLSSETPRIN--VFMAVPTIYTKLME-YYDRHFTQPHAQDFL--RAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLL 87
Cdd:cd17640 163 RTLKDDLKRVKphYIVSVPRLWESLYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 88 ERYGMTEigmalSGPLTTAARLP----GSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPglEEKEGELLVR 163
Cdd:cd17640 242 NGYGLTE-----TSPVVSARRLKcnvrGSVGRPLPGTEIKIV-----------------DPEGNVVLP--PGEKGIVWVR 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 164 GPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:cd17640 298 GPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
21-304 |
2.44e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 111.24 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDRhftqPHAQDFLravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMals 100
Cdd:PRK13383 264 RADAFTAVPVVLARILELPPR----VRARNPL-----PQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGI--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 101 GPLTTAARL---PGSVGTPLPGVQVRIVSENPQREGCSYT--IHAEGDERGTKVTPGleekegellvRGPSVfreywnkp 175
Cdd:PRK13383 332 GALATPADLrdaPETVGKPVAGCPVRILDRNNRPVGPRVTgrIFVGGELAGTRYTDG----------GGKAV-------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 176 eetksaftLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:PRK13383 394 --------VDGMTSTGDMGYLDNaGRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAF 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034116931 255 VTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK13383 465 VVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
73-304 |
2.49e-27 |
|
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: 111.64 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 73 PVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAARLP---GSVGTPLPGVQVRIVSENpqregcsytihaegderGTKV 149
Cdd:cd05967 370 PTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPikaGSPGKPVPGYQVQVLDED-----------------GEPV 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 150 TPGleeKEGELLVRGP---SVFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:cd05967 433 GPN---ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKdEDGYLFIMGRTD-DVINVAGHRLSTGE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 224 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS----HRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
....*
gi 1034116931 300 DKKAL 304
Cdd:cd05967 589 LRRTL 593
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
60-304 |
1.16e-26 |
|
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: 109.21 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNITGH-TLLERYGMTE-IGMALSGPLTTAARLPGSV--GTPLPGVQVRIVsenpqregcs 135
Cdd:cd12117 251 LRELLTGGEVVSPPHVRRVLAACPGlRLVNGYGPTEnTTFTTSHVVTELDEVAGSIpiGRPIANTRVYVL---------- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 136 ytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTS 208
Cdd:cd12117 321 -------DEDGRPVPPGVP---GELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 209 vDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGhsLSHRELKEWARDVLAPYAVPSELVLV 288
Cdd:cd12117 391 -DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA--LDAAELRAFLRERLPAYMVPAAFVVL 467
|
250
....*....|....*.
gi 1034116931 289 EEIPRNQMGKIDKKAL 304
Cdd:cd12117 468 DELPLTANGKVDRRAL 483
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
92-299 |
1.52e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 109.46 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 92 MTEIGMALSGPLTTAARL-PGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRG--PSVF 168
Cdd:PRK00174 404 QTETGGIMITPLPGATPLkPGSATRPLPGIQPAVV-----------------DEEGNPLEGG---EGGNLVIKDpwPGMM 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 169 REYWNKPEE-TKSAF-TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 245
Cdd:PRK00174 464 RTIYGDHERfVKTYFsTFKGMYFTGDGARRdEDGYYWITGRVD-DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDD 542
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034116931 246 TWGQRVTAVVTLREGHSLS---HRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK00174 543 IKGQGIYAFVTLKGGEEPSdelRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKI 599
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
33-304 |
1.70e-26 |
|
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: 108.57 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 33 TKLMEYYDRH------FTQPHAQ--DFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGMTEIGM-ALSG 101
Cdd:cd17655 218 QALTQYIRQNritiidLTPAHLKllDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVdASIY 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 102 PLTTAARLPGSV--GTPLPGVQVRIVSEN--PQREGCSytihaegdergtkvtpgleekeGELLVRGPSVFREYWNKPEE 177
Cdd:cd17655 298 QYEPETDQQVSVpiGKPLGNTRIYILDQYgrPQPVGVA----------------------GELYIGGEGVARGYLNRPEL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 178 TKSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQR 250
Cdd:cd17655 356 TAEKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNY 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 251 VTAVVTLREghSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17655 435 LCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
61-304 |
2.09e-26 |
|
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: 108.52 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 61 RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAARLPGSV--GTPLPGVQVRIVsenpqregcsyti 138
Cdd:cd17646 256 RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVpiGRPVPNTRLYVL------------- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 139 haegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDgWF-------KTGDTVVFK-DGQYWIRGRTSvD 210
Cdd:cd17646 323 ----DDALRPVPVGVP---GELYLGGVQLARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-D 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 211 IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS-LSHRELKEWARDVLAPYAVPSELVLVE 289
Cdd:cd17646 394 QVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLD 473
|
250
....*....|....*
gi 1034116931 290 EIPRNQMGKIDKKAL 304
Cdd:cd17646 474 ALPLTANGKLDRAAL 488
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
18-304 |
4.30e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 107.87 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMEYydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGm 97
Cdd:PRK07008 264 EAERVTFSAGVPTVWLGLLNH-----MREAGLRF------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMS- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 alsgPLTTAARL-------PGSV--------GTPLPGVQVRIVSENPQR---EGCSYtihaegdergtkvtpgleekeGE 159
Cdd:PRK07008 332 ----PLGTLCKLkwkhsqlPLDEqrkllekqGRVIYGVDMKIVGDDGRElpwDGKAF---------------------GD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETksafTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK07008 387 LQVRGPWVIDRYFRGDASP----LVDGWFPTGDVATIdADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAEAA 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07008 462 CIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
8-308 |
4.70e-26 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.92 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 8 QQVWEkFLSSEtpRINVFMAVPTIYTKLMEYYDRH-FTQPHaqdflravceekIRLMVSGSAALPLPVLEKWKNItGHTL 86
Cdd:PRK06018 258 ASVYE-LLDTE--KVTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAFEDM-GVEV 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 87 LERYGMTEIGmalsgPLTTAARLPGSV---------------GTPLPGVQVRIVsenpqregcsytihaegDERGTKVtP 151
Cdd:PRK06018 322 RHAWGMTEMS-----PLGTLAALKPPFsklpgdarldvlqkqGYPPFGVEMKIT-----------------DDAGKEL-P 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 152 GLEEKEGELLVRGPSVFREYWnkpEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLA 230
Cdd:PRK06018 379 WDGKTFGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVaTIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVG 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 231 HPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:PRK06018 455 HPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
60-304 |
8.14e-26 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 107.41 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAalPLPVLEKWKNITGHTLLERYGMTEIgmalSGPLTTAA------RLPGSVGTPLPgvqvrivsenpQREG 133
Cdd:PLN03102 303 VHVLTGGSP--PPAALVKKVQRLGFQVMHAYGLTEA----TGPVLFCEwqdewnRLPENQQMELK-----------ARQG 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 134 CSYTIHAEGDERGTKV---TPGLEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRtSV 209
Cdd:PLN03102 366 VSILGLADVDVKNKETqesVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVgVIHPDGHVEIKDR-SK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 210 DIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS----------LSHRELKEWARDVLAPY 279
Cdd:PLN03102 444 DIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPHF 523
|
250 260
....*....|....*....|....*
gi 1034116931 280 AVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PLN03102 524 MCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
37-304 |
1.47e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 106.37 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 37 EYYDR-HFTQPHAQDFLRAvceekiRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTE-IGMALSGPLTTAAR---LPG 111
Cdd:PRK06164 278 EMLRRiLDTAGERADFPSA------RLFGFASFAPALGELAALARARGVPLTGLYGSSEvQALVALQPATDPVSvriEGG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 112 svGTPL-PGVQVRIVseNPQRegcsytihaegderGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKT 190
Cdd:PRK06164 352 --GRPAsPEARVRAR--DPQD--------------GALLPDG---ESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRT 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 191 GD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELK 269
Cdd:PRK06164 411 GDlGYTRGDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLM 488
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034116931 270 EWARDVLAPYAVPSELVLVEEIPRNQMG---KIDKKAL 304
Cdd:PRK06164 489 AACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
90-304 |
1.84e-25 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 105.46 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEigmalsgpltTAAR----LPG-------SVGTPLPGVQVRIvsenpqregCSYTIhaegdergtkvtpgleekeG 158
Cdd:PRK07445 261 YGMTE----------TASQiatlKPDdflagnnSSGQVLPHAQITI---------PANQT-------------------G 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 159 ELLVRGPSVFREYWNKPEETKSAFTLD--GWFKtgdtvvfKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PRK07445 303 NITIQAQSLALGYYPQILDSQGIFETDdlGYLD-------AQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGLVQD 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGhSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07445 375 VCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
40-299 |
2.87e-25 |
|
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: 105.74 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 40 DRH-----FTQPHAQDFLRAVCEEKIR------LMVSGSAALPL---PVLEKWKNITGH--TLLERYGMTEIGMALSGPL 103
Cdd:cd17634 323 DKHgvnilYTAPTAIRALMAAGDDAIEgtdrssLRILGSVGEPInpeAYEWYWKKIGKEkcPVVDTWWQTETGGFMITPL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 104 TTAARL-PGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGleeKEGELLVRG--PSVFREYWNKPEETKS 180
Cdd:cd17634 403 PGAIELkAGSATRPVFGVQPAVV-----------------DNEGHPQPGG---TEGNLVITDpwPGQTRTLFGDHERFEQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 181 AF--TLDGWFKTGDTV-VFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTL 257
Cdd:cd17634 463 TYfsTFKGMYFSGDGArRDEDGYYWITGR-SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVL 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034116931 258 REGHSLS---HRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd17634 542 NHGVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
47-304 |
9.16e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 104.62 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 47 HAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG--MALSGP--------LTTAARlPGSVGTP 116
Cdd:PRK08633 893 HPLMF------ASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSpvASVNLPdvlaadfkRQTGSK-EGSVGMP 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 117 LPGVQVRIVseNPqregcsytihaegdERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFT---LDGWFKTGDT 193
Cdd:PRK08633 966 LPGVAVRIV--DP--------------ETFEELPPG---EDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDK 1026
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 194 -VVFKDGQYWIRGRTSvDIIKTGGYKVS--ALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS-HRELK 269
Cdd:PRK08633 1027 gHLDEDGFLTITDRYS-RFAKIGGEMVPlgAVEEELAKALGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEElKRAIK 1105
|
250 260 270
....*....|....*....|....*....|....*
gi 1034116931 270 EWArdvLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK08633 1106 ESG---LPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
83-306 |
2.41e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 102.80 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 83 GHTLLERYGMTEIGMALSGPLTTAarlPGSVGTPLPGVqvRIVseNPQ-REGCSYtihAEGDERGTKVTPglEEKEGELL 161
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVREPGTP---PGSIGRGAPGV--AIY--NPEtLTECAV---ARFDAHGALLNA--DEAIGELV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 162 VR-GPSVFREYWNKPEETKSAFTlDGWFKTGDtVVFKDGQYWI--RGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK13388 356 NTaGAGFFEGYYNNPEATAERMR-HGMYWSGD-LAYRDADGWIyfAGRTA-DWMRVDGENLSAAPIERILLRHPAINRVA 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK13388 433 VYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
28-304 |
4.82e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.01 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 28 VPTIYTKLMeyYDRHFTqphaqdflrAVCEEKIRLMV-SGSAALPLPVleKWKNITGHTLLERYGMTEIG-MALSGPLTT 105
Cdd:PRK05857 267 VPTLLSKLV--SELKSA---------NATVPSLRLVGyGGSRAIAADV--RFIEATGVRTAQVYGLSETGcTALCLPTDD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 106 A--ARL-PGSVGTPLPGVQVRIVSENPqregcsytihaegderGTKVTPGLEEKE--GELLVRGPSVFREYWNKPEETKS 180
Cdd:PRK05857 334 GsiVKIeAGAVGRPYPGVDVYLAATDG----------------IGPTAPGAGPSAsfGTLWIKSPANMLGYWNNPERTAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 181 AFtLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV-TAVVTLR 258
Cdd:PRK05857 398 VL-IDGWVNTGDLLERReDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVgLAVVASA 475
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 259 EGHSLSHRELKewaRDVLAPY-------AVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK05857 476 ELDESAARALK---HTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
60-304 |
6.80e-24 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 101.46 E-value: 6.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAalPLPVLEKWKNITGHTLLERYGMTEIgmalSGPLTTAARLPGSVGTPlPGVQVRIVSenpqREGCSYtIH 139
Cdd:PLN02479 313 VHVMTAGAA--PPPSVLFAMSEKGFRVTHTYGLSET----YGPSTVCAWKPEWDSLP-PEEQARLNA----RQGVRY-IG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 140 AEG----DERGTKVTPGLEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVV-FKDGQYWIRGRtSVDIIKT 214
Cdd:PLN02479 381 LEGldvvDTKTMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFA-NGWFHSGDLGVkHPDGYIEIKDR-SKDIIIS 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 215 GGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH-----RELKEWARDVLAPYAVPSELVLvE 289
Cdd:PLN02479 459 GGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDeaalaEDIMKFCRERLPAYWVPKSVVF-G 537
|
250
....*....|....*
gi 1034116931 290 EIPRNQMGKIDKKAL 304
Cdd:PLN02479 538 PLPKTATGKIQKHVL 552
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
52-280 |
8.88e-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: 101.14 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 52 LRAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEI--GMALSGP--LTTaarlpGSVGTPLPGVQVRIVSE 127
Cdd:cd17639 244 VRAALGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETcaGGTVQDPgdLET-----GRVGPPLPCCEIKLVDW 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 128 npqregcsytihAEGdergtKVTPGLEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGR 206
Cdd:cd17639 318 ------------EEG-----GYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFhPDGTLKIIDR 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034116931 207 TSvDIIKT--GGYkvSALE-VEWHLLAHPSITDVAVIGVPDMTwgqRVTAVVTLREGHslshreLKEWARDVLAPYA 280
Cdd:cd17639 381 KK-DLVKLqnGEY--IALEkLESIYRSNPLVNNICVYADPDKS---YPVAIVVPNEKH------LTKLAEKHGVINS 445
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
102-304 |
2.07e-23 |
|
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: 99.31 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 102 PLTTAARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSA 181
Cdd:cd12115 259 PVPPGASGEVSIGRPLANTQAYVL-----------------DRALQPVPLGVP---GELYIGGAGVARGYLGRPGLTAER 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 182 FTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:cd12115 319 FLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAY 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034116931 255 VTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12115 398 IVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
82-305 |
2.28e-23 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 99.58 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 82 TGHTLLER---------YGMTEIGMALSG------PLTTAARLPgsVGTPLPGVQVRIVsenpqregcsytihaegDERG 146
Cdd:PRK04813 276 TAKKLLERfpsatiyntYGPTEATVAVTSieitdeMLDQYKRLP--IGYAKPDSPLLII-----------------DEEG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 147 TKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAF-TLDGW--FKTGDTVVFKDGQYWIRGRtsVDI-IKTGGYKVSAL 222
Cdd:PRK04813 337 TKLPDG---EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLEDGLLFYQGR--IDFqIKLNGYRIELE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 223 EVEWHLLAHPSItDVAVIgVPDMTwGQRVT---AVVTLREGH-----SLSHrELKEWARDVLAPYAVPSELVLVEEIPRN 294
Cdd:PRK04813 412 EIEQNLRQSSYV-ESAVV-VPYNK-DHKVQyliAYVVPKEEDferefELTK-AIKKELKERLMEYMIPRKFIYRDSLPLT 487
|
250
....*....|.
gi 1034116931 295 QMGKIDKKALI 305
Cdd:PRK04813 488 PNGKIDRKALI 498
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
143-304 |
3.64e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 99.29 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 143 DERGTKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSA 221
Cdd:PRK10946 369 DADGNPLPQG---EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIdPDGYITVVGREK-DQINRGGEKIAA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 222 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARDV-LAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:PRK10946 445 EEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE--PLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVD 522
|
....
gi 1034116931 301 KKAL 304
Cdd:PRK10946 523 KKQL 526
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
83-304 |
9.72e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 98.21 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 83 GHTLLERYGMTEIGMALSGPLTTAarlPGSVGTPLPGVQVRivseNPQ-REGCSytiHAEGDERGTkvtPGLEEKEGELL 161
Cdd:PRK07867 290 GCVVVDGFGSTEGGVAITRTPDTP---PGALGPLPPGVAIV----DPDtGTECP---PAEDADGRL---LNADEAIGELV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 162 -VRGPSVFREYWNKPEETkSAFTLDGWFKTGDtVVFKD--GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK07867 357 nTAGPGGFEGYYNDPEAD-AERMRGGVYWSGD-LAYRDadGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVA 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07867 434 VYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
5-304 |
1.03e-22 |
|
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: 97.54 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 5 FSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravceEKIRLMVSGSAALPLpvleKWKNitgh 84
Cdd:cd17650 172 LDPAALYDLILKS---RITLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKA----QDFK---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 85 TLLER----------YGMTEIGMALSGPLTTAARLPGS----VGTPLPGVQVRIVSE--NPQREGCSytihaegdergtk 148
Cdd:cd17650 230 TLAARfgqgmriinsYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDErlQPQPVGVA------------- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 149 vtpgleekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSA 221
Cdd:cd17650 297 ---------GELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 222 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRegHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17650 367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
...
gi 1034116931 302 KAL 304
Cdd:cd17650 445 RAL 447
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
61-304 |
3.35e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 95.87 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 61 RLMVSGsAALPLPVLEKWKNITGHtLLERYGMTEIG-MALSGPLTTaarlPGSVGTPLPGVQVRIVSEnpqregcsytih 139
Cdd:PRK08308 216 AVMTSG-TPLPEAWFYKLRERTTY-MMQQYGCSEAGcVSICPDMKS----HLDLGNPLPHVSVSAGSD------------ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 140 aegdergtkvtpglEEKEGELLVRgpsvfreywnkpEETKSAFTLD-GWFKTGDTVVFkdgqywiRGRTSvDIIKTGGYK 218
Cdd:PRK08308 278 --------------ENAPEEIVVK------------MGDKEIFTKDlGYKSERGTLHF-------MGRMD-DVINVSGLN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 219 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRegHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:PRK08308 324 VYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGK 401
|
....*.
gi 1034116931 299 IDKKAL 304
Cdd:PRK08308 402 VSRKLL 407
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
18-304 |
5.11e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 95.85 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRAVCEekirlmvsgsAALPLPVLEKWKNIT--GHTLLERYGMTEI 95
Cdd:PRK13390 239 ERYRITVTQMVPTMFVRLLKLDADVRTR-YDVSSLRAVIH----------AAAPCPVDVKHAMIDwlGPIVYEYYSSTEA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 96 -GMALsgpLTTAARL--PGSVGTPLPGvqvrivsenpqregcsyTIHAeGDERGTKVTPGleeKEGELLVRGPSVFREYW 172
Cdd:PRK13390 308 hGMTF---IDSPDWLahPGSVGRSVLG-----------------DLHI-CDDDGNELPAG---RIGTVYFERDRLPFRYL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 173 NKPEETKSA------FtldgWFKTGDT-VVFKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 245
Cdd:PRK13390 364 NDPEKTAAAqhpahpF----WTTVGDLgSVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVIGVPDP 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034116931 246 TWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK13390 439 EMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
59-192 |
5.13e-22 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 96.13 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEI--GMALSGPLTTAArlpGSVGTPLPGVQVRIVSEnPQREgcsY 136
Cdd:cd05927 275 NVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLPGDTSV---GHVGGPLPCAEVKLVDV-PEMN---Y 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 137 tiHAEGdergtkvtpglEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 192
Cdd:cd05927 348 --DAKD-----------PNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
90-225 |
5.22e-22 |
|
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: 95.81 E-value: 5.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEI--GMALSGPLTTAARLPG----SVGTPLPGVQVRIVSENpqregcsytihaegdergtkvTPGLEEKE-GELLV 162
Cdd:cd05906 327 FGMTETcsGVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDE---------------------GQLLPEGEvGRLQV 385
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 163 RGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVE 225
Cdd:cd05906 386 RGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIE 447
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
21-304 |
8.07e-22 |
|
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: 96.08 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYydrhftQPHAQDFLRavceekiRLMVSGSAaLPLPVLEKWKNITGHT-LLERYGMTE--IGm 97
Cdd:COG1020 708 RVTVLNLTPSLLRALLDA------APEALPSLR-------LVLVGGEA-LPPELVRRWRARLPGArLVNLYGPTEttVD- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 ALSGPLTTAARLPGSV--GTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKP 175
Cdd:COG1020 773 STYYEVTPPDADGGSVpiGRPIANTRVYVL-----------------DAHLQPVPVGVP---GELYIGGAGLARGYLNRP 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 176 EETKSAF-----TLDG--WFKTGD--------TVVF---KDGQYWIRG-RtsvdiIKTGgykvsalEVEWHLLAHPSITD 236
Cdd:COG1020 833 ELTAERFvadpfGFPGarLYRTGDlarwlpdgNLEFlgrADDQVKIRGfR-----IELG-------EIEAALLQHPGVRE 900
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:COG1020 901 AVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
59-304 |
1.21e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 95.05 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVSGSAALPLPVLEKWKN-ITGHTLLERYGMTE---IGMALSGPLT---TAARlpGSVGTPLPGVQVRIVseNPQr 131
Cdd:PLN02330 304 KLQAIMTAAAPLAPELLTAFEAkFPGVQVQEAYGLTEhscITLTHGDPEKghgIAKK--NSVGFILPNLEVKFI--DPD- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 132 EGCSYTihaegdergtKVTPGleekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvD 210
Cdd:PLN02330 379 TGRSLP----------KNTPG------ELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIgYIDDDGDIFIVDRIK-E 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 211 IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEE 290
Cdd:PLN02330 442 LIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDS 521
|
250
....*....|....
gi 1034116931 291 IPRNQMGKIDKKAL 304
Cdd:PLN02330 522 IPKSLSGKIMRRLL 535
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
60-304 |
1.63e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 94.71 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALSGPLTTAARlPGSVGTPLPGVQVRIVSENpqregcsyti 138
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVGQTFVSNRVDEWR-LGTLGRVLPPYEIRVVAPD---------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 139 haegderGTKVTPGLEekeGELLVRGPSVFREYWNKPEetkSAFTLDGWFKTGDTVVFkDGQYWIR-GRTSVDIIKTGGY 217
Cdd:PRK06060 331 -------GTTAGPGVE---GDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCI-DSDGWVTyRCRADDTEVIGGV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 218 KVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDV---LAPYAVPSELVLVEEIPRN 294
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLlnrLSAFKVPHRFAVVDRLPRT 476
|
250
....*....|
gi 1034116931 295 QMGKIDKKAL 304
Cdd:PRK06060 477 PNGKLVRGAL 486
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
223-298 |
1.99e-21 |
|
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: 86.06 E-value: 1.99e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 223 EVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
60-304 |
2.17e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 94.28 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAAL----------PLPvlekwknitGHTLLERYGMTEIGMALSGPLTTAAR----LPGSVGTPLPGVQVRIV 125
Cdd:PLN02246 300 IRMVLSGAAPLgkeledafraKLP---------NAVLGQGYGMTEAGPVLAMCLAFAKEpfpvKSGSCGTVVRNAELKIV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 126 seNPQrEGCSYTihaegdergtkvtpglEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIR 204
Cdd:PLN02246 371 --DPE-TGASLP----------------RNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIgYIDDDDELFIV 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 205 GRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSE 284
Cdd:PLN02246 432 DRLK-ELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHK 510
|
250 260
....*....|....*....|
gi 1034116931 285 LVLVEEIPRNQMGKIDKKAL 304
Cdd:PLN02246 511 VFFVDSIPKAPSGKILRKDL 530
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
60-309 |
8.29e-21 |
|
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: 92.22 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWknITGHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVqVRIVS-ENPQR---EGCs 135
Cdd:cd05918 217 LRTLVLGGEALTQSDVDTW--ADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDpDNHDRlvpIGA- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 136 ytihaegdergtkvtpgleekEGELLVRGPSVFREYWNKPEETKSAFTLD-GW------------FKTGD--------TV 194
Cdd:cd05918 293 ---------------------VGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDlvrynpdgSL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 195 VF---KDGQYWIRG-RtsVDIiktggykvsaLEVEWHLLAHPSITDVAVIGV---PDMTWGQRVTAVVTLREGHSLSH-- 265
Cdd:cd05918 352 EYvgrKDTQVKIRGqR--VEL----------GEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGdg 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 266 ---------------RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHFH 309
Cdd:cd05918 420 dslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
22-306 |
1.29e-20 |
|
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: 91.22 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 22 INVFMAVPTIYTKLmeyydrhftqpHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTEIGMALsg 101
Cdd:cd17653 190 VDALMSTPSILSTL-----------SPQDFPN------LKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISS-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 102 plTTAARLPG---SVGTPLPGVQVRIVSENPQregcsytihaegdergtkvtPGLEEKEGELLVRGPSVFREYWNKPEET 178
Cdd:cd17653 249 --TMTELLPGqpvTIGKPIPNSTCYILDADLQ--------------------PVPEGVVGEICISGVQVARGYLGNPALT 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 179 KSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLA-HPSITDVAVIGVpdmtwGQR 250
Cdd:cd17653 307 ASKFVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQsQPEVTQAAAIVV-----NGR 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 251 VTAVVTlreGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd17653 381 LVAFVT---PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
68-304 |
3.03e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 90.91 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 68 AALPLPVLEKWKNIT--GHTLLERYGMTEigmalsGPLTTAARL------PGSVGTPLPGVqVRIVsenpqregcsytih 139
Cdd:PRK13391 283 AAAPCPPQVKEQMIDwwGPIIHEYYAATE------GLGFTACDSeewlahPGTVGRAMFGD-LHIL-------------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 140 aegDERGTKVTPGleeKEGELLVRGPSVFrEYWNKPEETKSAFTLDG-WFKTGDT-VVFKDGQYWIRGRTSVDIIkTGGY 217
Cdd:PRK13391 342 ---DDDGAELPPG---EPGTIWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIgYVDEDGYLYLTDRAAFMII-SGGV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 218 KVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARDVLAPYAVPSELVLVEEIPRN 294
Cdd:PRK13391 414 NIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRL 493
|
250
....*....|
gi 1034116931 295 QMGKIDKKAL 304
Cdd:PRK13391 494 PTGKLYKRLL 503
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
58-241 |
4.90e-20 |
|
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: 90.22 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 58 EKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEiGMALSGPLTTAARLPGSVGTPLPGVQVRIvsenpqregcsyt 137
Cdd:cd05932 275 DQCRLAGCGSAPVPPALLEWYRSL-GLNILEAYGMTE-NFAYSHLNYPGRDKIGTVGNAGPGVEVRI------------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 138 ihaegdergtkvtpgleEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTG- 215
Cdd:cd05932 340 -----------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKgELDADGNLTITGRVK-DIFKTSk 401
|
170 180
....*....|....*....|....*.
gi 1034116931 216 GYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:cd05932 402 GKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
18-304 |
2.48e-19 |
|
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: 87.71 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYTKLMEYYDRHFTQPHAqdfLRAVceekirlMVSG---SAALPLPVLEKWKNITGHTLlerYGMTE 94
Cdd:cd12114 214 ERHGVTLWNSVPALLEMLLDVLEAAQALLPS---LRLV-------LLSGdwiPLDLPARLRALAPDARLISL---GGATE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 95 IGM-ALSGPLTTAARLPGSV--GTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREY 171
Cdd:cd12114 281 ASIwSIYHPIDEVPPDWRSIpyGRPLANQRYRVL-----------------DPRGRDCPDWVP---GELWIGGRGVALGY 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 172 WNKPEETKSAF----TLDGWFKTGDTVVFK-DGQYWIRGRtsVDI-IKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 245
Cdd:cd12114 341 LGDPELTAARFvthpDGERLYRTGDLGRYRpDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 246 TWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12114 419 GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
22-239 |
5.59e-19 |
|
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: 86.55 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 22 INVFMAVPTIYtklmeyydRHFTQPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALS 100
Cdd:TIGR01733 213 VTVLNLTPSLL--------ALLAAALPPALAS------LRLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWST 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 101 GPLTTAARLPG----SVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPE 176
Cdd:TIGR01733 279 ATLVDPDDAPRespvPIGRPLANTRLYVL-----------------DDDLRPVPVGVV---GELYIGGPGVARGYLNRPE 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034116931 177 ETKSAFTLDG--------WFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAV 239
Cdd:TIGR01733 339 LTAERFVPDPfaggdgarLYRTGDLVRYlPDGNLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
21-304 |
1.07e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.49 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 21 RINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRavceekirlmVSGSAALPL-PVLEKW-KNITGHT---LLERYGMTEI 95
Cdd:PLN02654 369 KVTIFYTAPTLVRSLMRDGDEYVTR-HSRKSLR----------VLGSVGEPInPSAWRWfFNVVGDSrcpISDTWWQTET 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 96 GMALSGPLTTA-ARLPGSVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTpglEEKEGELLVRG--PSVFREYW 172
Cdd:PLN02654 438 GGFMITPLPGAwPQKPGSATFPFFGVQPVIV-----------------DEKGKEIE---GECSGYLCVKKswPGAFRTLY 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 173 NKPE--ETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ 249
Cdd:PLN02654 498 GDHEryETTYFKPFAGYYFSGDGCSRdKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQ 576
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034116931 250 RVTAVVTLREGHSLS---HRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PLN02654 577 GIYAFVTLVEGVPYSeelRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
58-304 |
5.31e-18 |
|
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: 84.02 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 58 EKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGMTEIGMALS----GPLTTAARLPGSVGTPLPGVQVRIVSENPQr 131
Cdd:cd17644 224 SSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAATvcrlTQLTERNITSVPIGRPIANTQVYILDENLQ- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 132 egcsytihaegdergtKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW--------FKTGDTVVF-KDGQYW 202
Cdd:cd17644 303 ----------------PVPVGVP---GELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYlPDGNIE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 203 IRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVP 282
Cdd:cd17644 364 YLGRID-NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIP 442
|
250 260
....*....|....*....|..
gi 1034116931 283 SELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17644 443 SAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-304 |
5.71e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 42 HFTQPHAQDFLRAVCEEKIR---LMVSGSAALPLPVLEKWKNIT-GHTLLERYGMTEIGMALS-GPLTTAARLPGSV--G 114
Cdd:PRK12467 752 KIVPSHLQALLQASRVALPRpqrALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVStYELSDEERDFGNVpiG 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 115 TPLPGVQVRIV--SENPQREGCSytihaegdergtkvtpgleekeGELLVRGPSVFREYWNKPEETKSAFTLDGW----- 187
Cdd:PRK12467 832 QPLANLGLYILdhYLNPVPVGVV----------------------GELYIGGAGLARGYHRRPALTAERFVPDPFgadgg 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 188 --FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS 264
Cdd:PRK12467 890 rlYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAE 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034116931 265 HR----ELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12467 969 HQatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
83-304 |
7.72e-18 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 83.37 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 83 GHTLLERYGMTEIG-MALSGPLTTA-ARLPgsVGTPLPGVQVRIVSEnpqregcsytihaegderGTKVTPglEEKEGEL 160
Cdd:cd17645 234 GYKLVNNYGPTENTvVATSFEIDKPyANIP--IGKPIDNTRVYILDE------------------ALQLQP--IGVAGEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 161 LVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS 233
Cdd:cd17645 292 CIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPL 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 234 ITDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17645 371 IELAAVLAKEDADGRKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
46-299 |
3.18e-17 |
|
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: 82.15 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 46 PHAQDFLRAvcEEKIRLMVSGSAALPLPvLEKWKNITGHTLLERY------GMTEIGMALSGPLTTAARLPGSVGTPLPG 119
Cdd:cd05968 345 PRGDAPVNA--HDLSSLRVLGSTGEPWN-PEPWNWLFETVGKGRNpiinysGGTEISGGILGNVLIKPIKPSSFNGPVPG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 120 VQVRIVsenpqregcsytihaegDERGTKVTPgleeKEGELLVRGP--SVFREYWNKPEETKSAF--TLDGWFKTGDTVV 195
Cdd:cd05968 422 MKADVL-----------------DESGKPARP----EVGELVLLAPwpGMTRGFWRDEDRYLETYwsRFDNVWVHGDFAY 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 196 F-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEW 271
Cdd:cd05968 481 YdEEGYFYILGR-SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMER 559
|
250 260
....*....|....*....|....*...
gi 1034116931 272 ARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd05968 560 VADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3-307 |
6.07e-17 |
|
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: 80.69 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 3 PEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhftqphaQDFLRAvcEEKIRLMVSGSAALPLPVLEKWKNIT 82
Cdd:cd05974 161 ARFDAKRVLAAL---VRYGVTTLCAPPTVWRMLIQ-----------QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAW 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 83 GHTLLERYGMTEIgMALSGPLTTAARLPGSVGTPLPGVQVRIVSENpqregcsytihaegdergtkvtpGLEEKEGELLV 162
Cdd:cd05974 225 GLTIRDGYGQTET-TALVGNSPGQPVKAGSMGRPLPGYRVALLDPD-----------------------GAPATEGEVAL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 163 -----RGPSVFREYWNKPEETKSAFTlDGWFKTGDtVVFK--DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 235
Cdd:cd05974 281 dlgdtRPVGLMKGYAGDPDKTAHAMR-GGYYRTGD-IAMRdeDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVA 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 236 DVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVeEIPRNQMGKIDKKALIRH 307
Cdd:cd05974 358 EAAVVPSPDPVRLSVPKAFIVLRAGYEPSPetaLEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
47-300 |
2.57e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 79.62 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 47 HAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG--MALSGPLttaARLPGSVGTPLPGVQVRI 124
Cdd:PRK06814 902 HPYDFRS------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApvIALNTPM---HNKAGTVGRLLPGIEYRL 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 125 VsenpqregcsytihaegdergtKVtPGLEEKeGELLVRGPSVFREYW--NKP---EETKsaftlDGWFKTGDTVVF-KD 198
Cdd:PRK06814 973 E----------------------PV-PGIDEG-GRLFVRGPNVMLGYLraENPgvlEPPA-----DGWYDTGDIVTIdEE 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 199 GQYWIRGRTSvDIIKTGGYKVSALEVE------WHLLAHpsitdvAVIGVPDMTWGQRVtavVTLREGHSLSHRELKEWA 272
Cdd:PRK06814 1024 GFITIKGRAK-RFAKIAGEMISLAAVEelaaelWPDALH------AAVSIPDARKGERI---ILLTTASDATRAAFLAHA 1093
|
250 260
....*....|....*....|....*....
gi 1034116931 273 RDVLAP-YAVPSELVLVEEIPRNQMGKID 300
Cdd:PRK06814 1094 KAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
24-241 |
1.37e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.01 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 24 VFMAVPTIYTKLMEYYDRhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWK----NITGH--TLLERYGMTEigm 97
Cdd:PRK12582 319 VYGNVPAGYAMLAEAMEK-------DDALRRSFFKNLRLMAYGGATLSDDLYERMQalavRTTGHriPFYTGYGATE--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 alSGPLTT----AARLPGSVGTPLPGVQVRIVSEnpqregcsytihaegderGTKVtpgleekegELLVRGPSVFREYWN 173
Cdd:PRK12582 389 --TAPTTTgthwDTERVGLIGLPLPGVELKLAPV------------------GDKY---------EVRVKGPNVTPGYHK 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 174 KPEETKSAFTLDGWFKTGDTVVFKDGQYWIR-----GRTSVDIIKTGGYKVSALEVEWHLLA--HPSITDVAVIG 241
Cdd:PRK12582 440 DPELTAAAFDEEGFYRLGDAARFVDPDDPEKglifdGRVAEDFKLSTGTWVSVGTLRPDAVAacSPVIHDAVVAG 514
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
5-291 |
1.95e-15 |
|
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: 76.69 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 5 FSPQQVWEKFLS------SETPRINVFMAvpTIYTKL-MEYYDRHF--TQPHAQDFLRAVCEEKI--------------R 61
Cdd:cd17641 250 LLPPRVWEGIAAdvrarmMDATPFKRFMF--ELGMKLgLRALDRGKrgRPVSLWLRLASWLADALlfrplrdrlgfsrlR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 62 LMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPLTTAARlPGSVGTPLPGVQVRIvsenpqregcsytihae 141
Cdd:cd17641 328 SAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVD-PDTVGVPFPGTEVRI----------------- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 142 gdergtkvtpgleEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTG-GYKV 219
Cdd:cd17641 389 -------------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAK-DVGTTSdGTRF 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034116931 220 SALEVEWHLLAHPSITDVAVIGVPDmtwgQRVTAVVTLReghslsHRELKEWARDVLAPYAVPSELVLVEEI 291
Cdd:cd17641 455 SPQFIENKLKFSPYIAEAVVLGAGR----PYLTAFICID------YAIVGKWAEQRGIAFTTYTDLASRPEV 516
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
59-192 |
3.43e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 75.91 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGpLTTAARLPGSVGTPLPGVQVRIVSEnPQREgcsYTI 138
Cdd:PLN02736 377 RVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG-MDEGDNLSGHVGSPNPACEVKLVDV-PEMN---YTS 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 139 HAEGDERGtkvtpgleekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 192
Cdd:PLN02736 452 EDQPYPRG------------EICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
112-299 |
4.25e-15 |
|
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: 75.35 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 112 SVGTPLPGVQVRIVseNPQRegcsytiHAEGDERGtkvtpgleekEGELLVRGPSVFREYWNKPEETKSAFTL------D 185
Cdd:cd05931 356 SCGRPLPDQEVRIV--DPET-------GRELPDGE----------VGEIWVRGPSVASGYWGRPEATAETFGAlaatdeG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 186 GWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHL-LAHPSI--TDVAVIGVPDmtwGQRVTAVVTLREGHS 262
Cdd:cd05931 417 GWLRTGDLGFLHDGELYITGRLK-DLIIVRGRNHYPQDIEATAeEAHPALrpGCVAAFSVPD---DGEERLVVVAEVERG 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034116931 263 LSHRELKEWARDVLApyAV-------PSELVLVE--EIPRNQMGKI 299
Cdd:cd05931 493 ADPADLAAIAAAIRA--AVarehgvaPADVVLVRpgSIPRTSSGKI 536
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
53-206 |
4.68e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 75.40 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 53 RAVCEEKIRLMVSGSAALPLPVLEkWKNITGHTLLERYGMTEI----GMALSGPLTtaarlPGSVGTPLPGVQVRIVsen 128
Cdd:PTZ00216 423 RAVLGGRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTETvccgGIQRTGDLE-----PNAVGQLLKGVEMKLL--- 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034116931 129 pqregcsytihaEGDERGTKVTPgleEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGR 206
Cdd:PTZ00216 494 ------------DTEEYKHTDTP---EPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIaANGTLRIIGR 557
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
73-304 |
5.92e-15 |
|
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: 74.74 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 73 PVLEKWKNITGHTLLERYGMTEIGM-ALSGPLTTAARLPGSVGTPLPGVQVRIVSENPQRegcsytihaegdergtkVTP 151
Cdd:cd17648 222 PVFEKLRSRFAGLIINAYGPTETTVtNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKR-----------------VPV 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 152 GleeKEGELLVRGPSVFREYWNKPEETKSAF----------TLDG----WFKTGDTVVFK-DGQYWIRGRTSVDIiKTGG 216
Cdd:cd17648 285 G---AVGELYLGGDGVARGYLNRPELTAERFlpnpfqteqeRARGrnarLYKTGDLVRWLpSGELEYLGRNDFQV-KIRG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 217 YKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ--RVTAVV---TLREGHsLSHRELKEWARDVLAPYAVPSELVLVEEI 291
Cdd:cd17648 361 QRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVgyyLPEPGH-VPESDLLSFLRAKLPRYMVPARLVRLEGI 439
|
250
....*....|...
gi 1034116931 292 PRNQMGKIDKKAL 304
Cdd:cd17648 440 PVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-306 |
7.96e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.38 E-value: 7.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 45 QPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEK-WKNITGHTLLERYGMTEigmALSGPLTTAARLPGSVGTPLPGVQVR 123
Cdd:PRK12316 2248 QQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTE---AVVTPLLWKCRPQDPCGAAYVPIGRA 2324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 124 IvsenpqregcsytihaeGDERGTKVTPGLE----EKEGELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGD 192
Cdd:PRK12316 2325 L-----------------GNRRAYILDADLNllapGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGD 2387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 193 TVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELKE 270
Cdd:PRK12316 2388 LARYRaDGVVEYLGR--IDhQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRA 2464
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034116931 271 WARDVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK12316 2465 WLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
29-277 |
1.00e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 74.53 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 29 PTIYtklmeyydrhFTQPHAQDFLRAVCEE----------KIRLMVSGSAALPLPVLEKWKNITGHTLLER------YGM 92
Cdd:PRK08180 305 PTVY----------FNVPKGWEMLVPALERdaalrrrffsRLKLLFYAGAALSQDVWDRLDRVAEATCGERirmmtgLGM 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 93 TEigmalSGPLTT----AARLPGSVGTPLPGVQVRIVsenPQregcsytihaegderGTKVtpgleekegELLVRGPSVF 168
Cdd:PRK08180 375 TE-----TAPSATfttgPLSRAGNIGLPAPGCEVKLV---PV---------------GGKL---------EVRVKGPNVT 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 169 REYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIR-----GRTSVDIIKTGGYKVSALEVEWHLLAH--PSITDVAVIG 241
Cdd:PRK08180 423 PGYWRAPELTAEAFDEEGYYRSGDAVRFVDPADPERglmfdGRIAEDFKLSSGTWVSVGPLRARAVSAgaPLVQDVVITG 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034116931 242 ----------VPDMTWGQRVTAvvtLREGHS----LSHRELKEWARDVLA 277
Cdd:PRK08180 503 hdrdeigllvFPNLDACRRLAG---LLADASlaevLAHPAVRAAFRERLA 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-306 |
1.25e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.61 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWknITGHTLLERYGMTEIGM-ALSGPLTTAARLPGSVGTPLPGVQVRIVSENpqregcsyti 138
Cdd:PRK12316 3313 LKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATItVTHWQCVEEGKDAVPIGRPIANRACYILDGS---------- 3380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 139 haegdergtkVTPGLEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSVDI 211
Cdd:PRK12316 3381 ----------LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQV 3450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 212 iKTGGYKVSALEVEWHLLAHPSITDVAVIGVPdmtwGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEI 291
Cdd:PRK12316 3451 -KIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERM 3525
|
250
....*....|....*
gi 1034116931 292 PRNQMGKIDKKALIR 306
Cdd:PRK12316 3526 PLTPNGKLDRKALPR 3540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-304 |
2.12e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.84 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 45 QPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEK-WKNITGHTLLERYGMTEIGM------ALSGPLTTAARLPgsVGTPL 117
Cdd:PRK12316 4796 QQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVtvllwkARDGDACGAAYMP--IGTPL 4873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 118 PGVQVRI--VSENPQREGCSytihaegdergtkvtpgleekeGELLVRGPSVFREYWNKPEETKSAFTLDGW-------F 188
Cdd:PRK12316 4874 GNRSGYVldGQLNPLPVGVA----------------------GELYLGGEGVARGYLERPALTAERFVPDPFgapggrlY 4931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 189 KTGDTVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV-------TAVVTLRE 259
Cdd:PRK12316 4932 RTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVgyvvpqdPALADADE 5009
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034116931 260 GHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12316 5010 AQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
160-304 |
2.72e-14 |
|
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: 73.23 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 160 LLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIaVWDEEGYVEIKDR-LKDLIKSGGEWISSVDLENALMGHPKVKEAA 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05915 442 VVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
42-304 |
3.16e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.28 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 42 HFTQPHAQDF----LRAVCEeKIRLMVSGSAALPLP----VLEKWKNITGHTlleRYGMTEIGMALSGPLTTAA---RLP 110
Cdd:PRK05691 1369 HFVPPLLQLFidepLAAACT-SLRRLFSGGEALPAElrnrVLQRLPQVQLHN---RYGPTETAINVTHWQCQAEdgeRSP 1444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 111 gsVGTPLPGVQVRIVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW--- 187
Cdd:PRK05691 1445 --IGRPLGNVLCRVL-----------------DAELNLLPPGVA---GELCIGGAGLARGYLGRPALTAERFVPDPLged 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 188 ----FKTGDTVVFK-DGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLAHPSITDVAVIgVPDMTWGQRVTAVVTLREGHS 262
Cdd:PRK05691 1503 garlYRTGDRARWNaDGALEYLGRLDQQV-KLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQE 1580
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034116931 263 LSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK05691 1581 AEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
155-304 |
5.07e-14 |
|
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: 72.08 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 155 EKEGELLVRGP----SVFREYWNKPEETKSAFTL------DGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:cd05937 297 GEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQdADGRWYFLDRLG-DTFRWKSENVSTTE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 224 VEWHLLAHPSITDVAVIGV--PDMTwGQRVTAVVTLREGHS----LSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMG 297
Cdd:cd05937 376 VADVLGAHPDIAEANVYGVkvPGHD-GRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNH 454
|
....*..
gi 1034116931 298 KIDKKAL 304
Cdd:cd05937 455 KQQKGVL 461
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-304 |
6.04e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.68 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 10 VWEKFLSSETPRiNVFMAVPTIYT---KLMEYYDR------HFTQPHAQDFLR----AVCEEkIRLMVSGSAALPLPVLE 76
Cdd:PRK12316 711 VWEFFWPLMSGA-RLVVAAPGDHRdpaKLVELINRegvdtlHFVPSMLQAFLQdedvASCTS-LRRIVCSGEALPADAQE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 77 K--WKNITGHtLLERYGMTE--IGMALSGPLTTAARLPgSVGTPLPGVQVRIVSE--NPQREGCSytihaegdergtkvt 150
Cdd:PRK12316 789 QvfAKLPQAG-LYNLYGPTEaaIDVTHWTCVEEGGDSV-PIGRPIANLACYILDAnlEPVPVGVL--------------- 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 151 pgleekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:PRK12316 852 -------GELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGE 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 224 VEWHLLAHPSITDVAVIGVPdmtwGQRVTAVVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKA 303
Cdd:PRK12316 924 IEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKA 999
|
.
gi 1034116931 304 L 304
Cdd:PRK12316 1000 L 1000
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
114-298 |
6.32e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 68.88 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 114 GTPLPGVQVRIVSENPQregcsytihaegdergtkVTPglEEKEGELLVRGPSVFREYWNKpEETKSAFTLDGWFKTGDT 193
Cdd:PRK09192 388 GKALPGHEIEIRNEAGM------------------PLP--ERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 194 VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT--DVAVIGVPDMTwGQRVTAVVTLREGHSLSHRELKEW 271
Cdd:PRK09192 447 GYLLDGYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHA 524
|
170 180 190
....*....|....*....|....*....|
gi 1034116931 272 ARDVL-APYAVPSELVLV--EEIPRNQMGK 298
Cdd:PRK09192 525 LAALVrSEFGVEAAVELVppHSLPRTSSGK 554
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
158-304 |
7.64e-13 |
|
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: 68.65 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLA 230
Cdd:cd17656 328 GELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLN 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 231 HPSITDVAVIGVPDMTWGQRVTA-VVTLREghsLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17656 407 HPGVSEAVVLDKADDKGEKYLCAyFVMEQE---LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
24-277 |
1.02e-12 |
|
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: 68.23 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 24 VFMAVPTIYTKLMEYYDRhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNI----TGH--TLLERYGMTEIGM 97
Cdd:cd05921 263 VYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALavatVGEriPMMAGLGATETAP 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 98 ALSGPLTTAARlPGSVGTPLPGVQVRIVSEnpqregcsytihaegderGTKVtpgleekegELLVRGPSVFREYWNKPEE 177
Cdd:cd05921 336 TATFTHWPTER-SGLIGLPAPGTELKLVPS------------------GGKY---------EVRVKGPNVTPGYWRQPEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 178 TKSAFTLDGWFKTGDTVVFKD------GQYWiRGRTSVDIIKTGGYKVS--ALEVEWHLLAHPSITDVAVIG-------- 241
Cdd:cd05921 388 TAQAFDEEGFYCLGDAAKLADpddpakGLVF-DGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGedraevga 466
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034116931 242 --VPDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLA 277
Cdd:cd05921 467 lvFPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLA 504
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
90-285 |
1.57e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 67.59 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEigMAlSgplT-TAAR---LPGsVGTPLPGVQVRIVsenpqregcsytihaegdergtkvtpgleekEGELLVRGP 165
Cdd:PRK09029 271 YGLTE--MA-S---TvCAKRadgLAG-VGSPLPGREVKLV-------------------------------DGEIWLRGA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 166 SVFREYWNKPEETksafTL---DGWFKTGDTVVFKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITDVAVIGV 242
Cdd:PRK09029 313 SLALGYWRQGQLV----PLvndEGWFATRDRGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQHPLVQQVFVVPV 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 243 PDMTWGQRVTAVVtlrEGHSLSHRE-LKEWARDVLA----P---YAVPSEL 285
Cdd:PRK09029 388 ADAEFGQRPVAVV---ESDSEAAVVnLAEWLQDKLArfqqPvayYLLPPEL 435
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
60-273 |
1.78e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 67.62 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNITGHT--LLERYGMTE------IGM--ALSGPLTTAARLPGS-VGTPLPGVQVRIV--S 126
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAMLPPDaeILTPYGATEalpissIESreILFATRAATDNGAGIcVGRPVDGVEVRIIaiS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 127 ENPqregcsytIHAEGDERgtKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFKD-GQY 201
Cdd:PRK09274 370 DAP--------IPEWDDAL--RLATG---EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqGRL 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 202 WIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTwGQRVTAVVTLREGHSLS----HRELKEWAR 273
Cdd:PRK09274 437 WFCGRKA-HRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSksalYQELRALAA 510
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
158-304 |
2.06e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.88 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHL 228
Cdd:PRK12467 3436 GELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARL 3513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 229 LAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLShRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12467 3514 LQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWR-ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
158-304 |
9.92e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.96 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTV-VFKDGQYWIRGRtsVD-IIKTGGYKVSALEVEWHL 228
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLArRRSDGVLEYVGR--IDhQVKIRGYRIELGEIEARL 4144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 229 LAHPSITDVAViGVPDMTWGQRVTAVVTLREGhSLSHREL----KEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK05691 4145 HEQAEVREAAV-AVQEGVNGKHLVGYLVPHQT-VLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
59-192 |
1.08e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 65.25 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmALSGPLTTAAR---LPGSVGTPLPGVQVRIVSenpqregcs 135
Cdd:PLN02861 384 RVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTE---SCGGCFTSIANvfsMVGTVGVPMTTIEARLES--------- 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034116931 136 ytIHAEGDERGTKVtpgleeKEGELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGD 192
Cdd:PLN02861 452 --VPEMGYDALSDV------PRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGD 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
158-304 |
4.55e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRTSVDIiKTGGYKVSALEVEWHLL 229
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQV-KIRGFRIELGEIESRLL 2611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 230 AHPSITDVAVIGVpDMTWGQR-----VTAVVTLREGHSLSHRE-LKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKA 303
Cdd:PRK05691 2612 EHPAVREAVVLAL-DTPSGKQlagylVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRA 2690
|
.
gi 1034116931 304 L 304
Cdd:PRK05691 2691 L 2691
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-279 |
5.19e-11 |
|
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: 62.86 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNITGHT--LLERYGMTE---IGMALSGPLTTAARLPGS------VGTPLPGVQVRIVSEN 128
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLSDEaeILTPYGATEalpVSSIGSRELLATTTAATSggagtcVGRPIPGVRVRIIEID 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 129 PQregcsyTIHAEGDERgtKVTPGleeKEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFKD-GQYWI 203
Cdd:cd05910 281 DE------PIAEWDDTL--ELPRG---EIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWF 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 204 RGRTSVDIIKTGGyKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELKEWARDVLAPY 279
Cdd:cd05910 350 CGRKAHRVITTGG-TLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
43-304 |
1.36e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 62.37 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 43 FTQPHAQDFLRAVCEEKIRLMVSGSAaLPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPLP---- 118
Cdd:PRK10252 703 FVASLTPEGARQSCASLRQVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVPigyp 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 119 --GVQVRIVsenpqregcsytihaegDERGTKVTPGLEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKT 190
Cdd:PRK10252 782 vwNTGLRIL-----------------DARMRPVPPGVA---GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRT 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 191 GDTVVFK-DGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVA----VIGVPDMTWG--QRVTAVVTLREGHSL 263
Cdd:PRK10252 842 GDVARWLdDGAVEYLGR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGdaRQLVGYLVSQSGLPL 920
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034116931 264 SHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK10252 921 DTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
110-304 |
1.83e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 61.50 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 110 PGSVGTPLPGVQVRIVSENPqregcsytihaegderGTKVTPGleEKeGELLVRGP-------SVFRE-------YWnkp 175
Cdd:PRK10524 410 LGSPGVPMYGYNVKLLNEVT----------------GEPCGPN--EK-GVLVIEGPlppgcmqTVWGDddrfvktYW--- 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 176 eetkSAF------TLDgWfktgdTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ 249
Cdd:PRK10524 468 ----SLFgrqvysTFD-W-----GIRDADGYYFILGRTD-DVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQ 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 250 RVTAVVTLREGHSLSHREL-----KEWARDV---LAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK10524 537 VAVAFVVPKDSDSLADREArlaleKEIMALVdsqLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
18-304 |
2.66e-10 |
|
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: 60.95 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 18 ETPRINVFMAVPTIYtklmeyydRHFTQPHAQDFLRAVcEEKIRLMVSGSAALP-LPVLEKWKNITGHT-LLERYGMTEI 95
Cdd:cd17654 207 KRHRITVLQATPTLF--------RRFGSQSIKSTVLSA-TSSLRVLALGGEPFPsLVILSSWRGKGNRTrIFNIYGITEV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 96 GMALSGPLTTAARLPGSVGTPLPGVQVRIVSENPQregcsytihaegdergtkvtpgleEKEGELLVRGPS---VFREYW 172
Cdd:cd17654 278 SCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGS------------------------EGTGQVFLGGLNrvcILDDEV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 173 NKPEETksaftldgWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVigvpdmTW--GQR 250
Cdd:cd17654 334 TVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV------TLsdQQR 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034116931 251 VTAVVTLREGHSLSHRELKewaRDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17654 399 LIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
86-225 |
3.22e-10 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 60.83 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 86 LLERYGMTEIgmalSGPLTT----AARLpGSVGTPLPGVQVRIVSENpqregcsytihAEGDergtkvtpgleekeGELL 161
Cdd:cd05933 347 IMELYGMSET----SGPHTIsnpqAYRL-LSCGKALPGCKTKIHNPD-----------ADGI--------------GEIC 396
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034116931 162 VRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSVDIIKTGGYKVSALEVE 225
Cdd:cd05933 397 FWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLgKLDEDGFLYITGRIKELIITAGGENVPPVPIE 461
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
112-244 |
3.51e-10 |
|
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: 60.58 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 112 SVGTPLPGVQVRIVSENPQREGCSYTIHAEgdERGTKVTPGleekegellvrgpsvfreYWNKPEETKSAFTLDGWFKTG 191
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQ--IRGKNVTPG------------------YYNNPEATAKVFTDDGWLKTG 374
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 192 DTVVFKDGQYWIRGRTSvDIIKTGGYKV-------SALEVEWHLLAHpsitdVAVIGVPD 244
Cdd:cd05908 375 DLGFIRNGRLVITGREK-DIIFVNGQNVyphdierIAEELEGVELGR-----VVACGVNN 428
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
52-290 |
3.59e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.90 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 52 LRAVCEEKIRLMVSGSAALPlPVLEKWKNIT-GHTLLERYGMTEI--GMALSGPLTTAArlpGSVGTPLPgvqvrivsen 128
Cdd:PLN02387 414 IRAVLGGRIRFMLSGGAPLS-GDTQRFINIClGAPIGQGYGLTETcaGATFSEWDDTSV---GRVGPPLP---------- 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 129 pqregCSYTIHAEGDERGTKVT----PgleekEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFK-DG 199
Cdd:PLN02387 480 -----CCYVKLVSWEEGGYLISdkpmP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHpDG 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 200 QYWIRGRTSvDIIKT--GGYkVSALEVEWHLLAHPSITDVAVIGVPDMTWGqrVTAVVTlreghslSHRELKEWARDVLA 277
Cdd:PLN02387 550 CLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSVSPYVDNIMVHADPFHSYC--VALVVP-------SQQALEKWAKKAGI 618
|
250
....*....|...
gi 1034116931 278 PYAVPSELVLVEE 290
Cdd:PLN02387 619 DYSNFAELCEKEE 631
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
39-300 |
5.64e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 60.11 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 39 YDRhFTQPHaqDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAARlPGSVGTPLP 118
Cdd:PRK08043 469 YAR-FANPY--DFAR------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAK-PGTVGRILP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 119 GVQVRIVSenpqregcsytihaegdergtkvTPGLEEKeGELLVRGPSVFREYW--NKPE--ETKSAFTLDG-----WFK 189
Cdd:PRK08043 539 GMDARLLS-----------------------VPGIEQG-GRLQLKGPNIMNGYLrvEKPGvlEVPTAENARGemergWYD 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 190 TGDTVVFKDGQY-WIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQrvtAVVTLREGHSLSHREL 268
Cdd:PRK08043 595 TGDIVRFDEQGFvQIQGRAK-RFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELTREKL 670
|
250 260 270
....*....|....*....|....*....|...
gi 1034116931 269 KEWARDVLAP-YAVPSELVLVEEIPRNQMGKID 300
Cdd:PRK08043 671 QQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
158-199 |
2.61e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 58.19 E-value: 2.61e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV-VFKDG 199
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVqINKNG 584
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
90-299 |
8.46e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 56.29 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEIGMA-------LSGPLTTaarlpgsVGTPLPGVQVRIVSEnpqregcsytihaEGDERGtkvtpglEEKEGEL-- 160
Cdd:PTZ00237 412 YGQTEIGITylycyghINIPYNA-------TGVPSIFIKPSILSE-------------DGKELN-------VNEIGEVaf 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 161 -LVRGPSVFREYWNKPEETKSAFT-LDGWFKTGDtVVFKD--GQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PTZ00237 465 kLPMPPSFATTFYKNDEKFKQLFSkFPGYYNSGD-LGFKDenGYYTIVSR-SDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSH-------RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PTZ00237 543 CCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnklkNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
60-192 |
3.25e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 54.64 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 60 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRIVSenpqregcsyTIH 139
Cdd:PLN02614 388 VRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLES----------VPE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 140 AEGDERGTkvTPgleekEGELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGD 192
Cdd:PLN02614 458 MEYDALAS--TP-----RGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGD 502
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
59-291 |
2.18e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 52.18 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 59 KIRLMVsGSAALPlPVLEKWKNITG-HTLLERYGMTE--IGmalsgpLTTAARLPGSVG-TPLPGV-QVRIV-----SEN 128
Cdd:PRK08279 315 RLRLMI-GNGLRP-DIWDEFQQRFGiPRILEFYAASEgnVG------FINVFNFDGTVGrVPLWLAhPYAIVkydvdTGE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 129 PQRegcsytiHAEGdeRGTKVTPGleekE-GELLVR-GPSVFREYWNKPEETKS-----AFTL-DGWFKTGDtVVFKDGQ 200
Cdd:PRK08279 387 PVR-------DADG--RCIKVKPG----EvGLLIGRiTDRGPFDGYTDPEASEKkilrdVFKKgDAWFNTGD-LMRDDGF 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 201 YWIRgrtSVDII------KtgGYKVSALEVEWHLLAHPSITDVAVIGV--PDMTwGQRVTAVVTLREGHSLSHRELKEWA 272
Cdd:PRK08279 453 GHAQ---FVDRLgdtfrwK--GENVATTEVENALSGFPGVEEAVVYGVevPGTD-GRAGMAAIVLADGAEFDLAALAAHL 526
|
250
....*....|....*....
gi 1034116931 273 RDVLAPYAVPSELVLVEEI 291
Cdd:PRK08279 527 YERLPAYAVPLFVRLVPEL 545
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
12-274 |
4.33e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 51.35 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 12 EKFLSSETP-RINVFMAvptIYTKLMEYYDRHFTQPHAQ---DFL-----RAVCEEKIRLMVSGSAALPLPVLEKWKNIT 82
Cdd:PLN02430 331 QKALQELNPrRRLIFNA---LYKYKLAWMNRGYSHKKASpmaDFLafrkvKAKLGGRLRLLISGGAPLSTEIEEFLRVTS 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 83 GHTLLERYGMTEIgmalSGPLTTA----ARLPGSVGTPLPGVQVRIvSENPQREgcsytihaegdergtkVTPGLEEKEG 158
Cdd:PLN02430 408 CAFVVQGYGLTET----LGPTTLGfpdeMCMLGTVGAPAVYNELRL-EEVPEMG----------------YDPLGEPPRG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 159 ELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALE-VEWHLLAHPSITD 236
Cdd:PLN02430 467 EICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGDIgEILPNGVLKIIDRKK-NLIKLSQGEYVALEyLENVYGQNPIVED 544
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034116931 237 VAVIGvpdMTWGQRVTAVVTLREghslshRELKEWARD 274
Cdd:PLN02430 545 IWVYG---DSFKSMLVAVVVPNE------ENTNKWAKD 573
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
56-223 |
1.30e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.43 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 56 CEEKIRLMVSGSAALPLPVLEKWKNITGH-TLLERYGMTEIGMALSGPLTTAARLPGSVGTPLPGVQVRIVSEnpqregc 134
Cdd:PRK06334 297 CLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSE------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 135 sytihaegdERGTKVTPGleeKEGELLVRGPSVFREYWNKpEETKSAFTLDG--WFKTGDT-VVFKDGQYWIRGRTSvDI 211
Cdd:PRK06334 370 ---------ETKVPVSSG---ETGLVLTRGTSLFSGYLGE-DFGQGFVELGGetWYVTGDLgYVDRHGELFLKGRLS-RF 435
|
170
....*....|....
gi 1034116931 212 IKTGGYKVS--ALE 223
Cdd:PRK06334 436 VKIGAEMVSleALE 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-206 |
1.95e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 112 SVGTPLPGVQVRIVseNPQregcsyTIHAEGDERgtkvtpgleekEGELLVRGPSVFREYWNKPEETKSAFT-LDG--WF 188
Cdd:PRK05691 371 SCGRSQPGHAVLIV--DPQ------SLEVLGDNR-----------VGEIWASGPSIAHGYWRNPEASAKTFVeHDGrtWL 431
|
90
....*....|....*...
gi 1034116931 189 KTGDTVVFKDGQYWIRGR 206
Cdd:PRK05691 432 RTGDLGFLRDGELFVTGR 449
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
158-304 |
3.31e-06 |
|
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: 48.28 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFKD-------GQYWIRGRTSV--------------------- 209
Cdd:cd17647 316 GEIYVRAGGLAEGYRGLPELNKEKF-VNNWFVEPDHWNYLDkdnnepwRQFWLGPRDRLyrtgdlgrylpngdceccgra 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 210 -DIIKTGGYKVSALEVEWHLLAHPSI---------------TDVAVIgVPDM----TWGQRVTA----------VVTLRE 259
Cdd:cd17647 395 dDQVKIRGFRIELGEIDTHISQHPLVrenitlvrrdkdeepTLVSYI-VPRFdkpdDESFAQEDvpkevstdpiVKGLIG 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034116931 260 GHSLSHrELKEWARDVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17647 474 YRKLIK-DIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
143-299 |
3.97e-06 |
|
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: 48.04 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 143 DERGTKVTpglEEKeGELLVRG--PSVFREYWNKPEETK--SAF--TLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTG 215
Cdd:cd05943 439 DEEGKPVW---GEK-GELVCTKpfPSMPVGFWNDPDGSRyrAAYfaKYPGVWAHGDWIEItPRGGVVILGR-SDGTLNPG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 216 GYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIP 292
Cdd:cd05943 514 GVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDIP 593
|
....*..
gi 1034116931 293 RNQMGKI 299
Cdd:cd05943 594 RTLSGKK 600
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
158-206 |
8.48e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 47.03 E-value: 8.48e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAF--TLDG---------------WFKTGDTVVFKDGQYWIRGR 206
Cdd:PRK07769 419 GEIWLHGNNIGTGYWGKPEETAATFqnILKSrlseshaegapddalWVRTGDYGVYFDGELYITGR 484
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
85-291 |
8.50e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 46.96 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 85 TLLERYGMTE--IGmalsgpLTTAARLPGSVG---------TPLPGVQVRIVSENPQREgcsytihAEGdeRGTKVTPGl 153
Cdd:cd05940 222 RIAEFYAATEgnSG------FINFFGKPGAIGrnpsllrkvAPLALVKYDLESGEPIRD-------AEG--RCIKVPRG- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 154 eeKEGELLVR--GPSVFREYWNKPEETKSAFTL-----DGWFKTGDTVVFKDGQYW-IRGRTSvDIIKTGGYKVSALEVE 225
Cdd:cd05940 286 --EPGLLISRinPLEPFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWyFVDRLG-DTFRWKGENVSTTEVA 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 226 WHLLAHPSITDVAVIGV--PDmTWGQRVTAVVTLREGHSLshrELKEWARDV---LAPYAVPSELVLVEEI 291
Cdd:cd05940 363 AVLGAFPGVEEANVYGVqvPG-TDGRAGMAAIVLQPNEEF---DLSALAAHLeknLPGYARPLFLRLQPEM 429
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
158-206 |
1.11e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 46.86 E-value: 1.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAF----------TLDG-WFKTGDTVVFKDGQYWIRGR 206
Cdd:PRK05850 398 GEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGR 457
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
158-292 |
2.95e-05 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 45.52 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV--VFKDGQYWIRGRTSVDIIKTGGY-KVSALEVEWhlLAHPSI 234
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMaeLGPDRLVYVDRRNNVLKLSQGEFvTVARLEAVF--AASPLV 513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 235 TDVAVIG-----------VPdmtwGQRVTAVVTLREGHSLSHRELKEWARDV-LAPYAVPSElVLVEEIP 292
Cdd:cd17632 514 RQIFVYGnserayllavvVP----TQDALAGEDTARLRAALAESLQRIAREAgLQSYEIPRD-FLIETEP 578
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
158-206 |
7.57e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.35 E-value: 7.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034116931 158 GELLVRGPSVFREYWNKPEETKSAF------TLDG------------WFKTGDTVVFKDGQYWIRGR 206
Cdd:PRK12476 430 GEIWLHGDNIGRGYWGRPEETERTFgaklqsRLAEgshadgaaddgtWLRTGDLGVYLDGELYITGR 496
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
169-304 |
1.21e-04 |
|
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: 43.90 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 169 REYWNKPEetksaftlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI------------- 234
Cdd:TIGR03443 669 REFWLGPR--------DRLYRTGDLGRYlPDGNVECCGRAD-DQVKIRGFRIELGEIDTHLSQHPLVrenvtlvrrdkde 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 235 --TDVAVIgVPDMTWGQRVTA------------VVTLREGHSLSHRELKEWARDVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:TIGR03443 740 epTLVSYI-VPQDKSDELEEFksevddeessdpVVKGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVD 818
|
....
gi 1034116931 301 KKAL 304
Cdd:TIGR03443 819 KPAL 822
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
112-225 |
1.26e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 43.45 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 112 SVGTPLPGVQVRIVSENPQREGcsytihaegdERGTkvtpgleekeGELLVRGPSVFREYWNkPEETKSAFTLDGWFKTG 191
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVLP----------PRGV----------GVIELRGESVTPGYLT-MDGFIPAQDADGWLDTG 419
|
90 100 110
....*....|....*....|....*....|....*
gi 1034116931 192 DTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVE 225
Cdd:PRK07768 420 DLGYLTEeGEVVVCGRVK-DVIIMAGRNIYPTDIE 453
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-282 |
3.12e-04 |
|
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: 42.28 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 87 LERYGMTEIGMALsgplTTAARLPGSVG---------TPLPGVQVRIVSENPQREGCSYTIHAEGDERGTKVTPgleeke 157
Cdd:cd05938 286 REFYGSTEGNIGF----FNYTGKIGAVGrvsylykllFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAK------ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 158 gellVRGPSVFREYWNKPEETKSAF------TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLA 230
Cdd:cd05938 356 ----ITQQSPFLGYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQdQQNFLYFHDRVG-DTFRWKGENVATTEVADVLGL 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034116931 231 HPSITDVAVIGVPDMTWGQRV-TAVVTLREGHSLSHRELKEWARDVLAPYAVP 282
Cdd:cd05938 431 LDFLQEVNVYGVTVPGHEGRIgMAAVKLKPGHEFDGKKLYQHVREYLPAYARP 483
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
90-225 |
3.47e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.06 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034116931 90 YGMTEIGMALSGPL--------------TTAARLPGSVGTPLPGVQVRIvsenpqregcsytihAEGDERgtkvtPGLEE 155
Cdd:PRK05851 310 YGLAESTCAVTVPVpgiglrvdevttddGSGARRHAVLGNPIPGMEVRI---------------SPGDGA-----AGVAG 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 156 KE-GELLVRGPSVFREYWNKPeetksAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVE 225
Cdd:PRK05851 370 REiGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIE 434
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
232-299 |
9.57e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 37.47 E-value: 9.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034116931 232 PSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARDVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK03584 544 PEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDalrARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
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