|
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 |
1.13e-163 |
|
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: 462.91 E-value: 1.13e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWekfLSSETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqDFLRAVCEEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd05941 161 FLPKFDPKEVA---ISRLMPSITVFMGVPTIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEIGMALSGPLTtAVRLPGSVGTPLPGVQVRIVSENPQReacsytihaegdergtkvtPGFEEKEGEL 160
Cdd:cd05941 235 ITGHTLLERYGMTEIGMALSNPLD-GERRPGTVGMPLPGVQARIVDEETGE-------------------PLPRGEVGEI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 161 LVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAV 239
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 240 IGVPDMTWGQRVTAVVTLREG-HSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 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 |
4.02e-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: 293.64 E-value: 4.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRhftqphAQDFLRAVceekiRLMVSGSAALPLPVLEKWKN 80
Cdd:COG0318 172 LLPRFDPERVLELI---ERERVTVLFGVPTMLARLLRHPEF------ARYDLSSL-----RLVVSGGAPLPPELLERFEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEIGMALSG-PLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGE 159
Cdd:COG0318 238 RFGVRIVEGYGLTETSPVVTVnPEDPGERRPGSVGRPLPGVEVRIV-----------------DEDGRELPPG---EVGE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:COG0318 298 IVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAA 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 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 |
9.47e-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: 252.10 E-value: 9.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravceEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd05936 199 LIPRFRPIGVLKEI---RKHRVTIFPGVPTMYIALLNAPEFKKRDF-----------SSLRLCISGGAPLPVEVAERFEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEigmalSGPLTTA-----VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfee 155
Cdd:cd05936 265 LTGVPIVEGYGLTE-----TSPVVAVnpldgPRKPGSIGIPLPGTEVKIV-----------------DDDGEELPPG--- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 156 KEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 234
Cdd:cd05936 320 EVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAV 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 235 TDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 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 |
6.44e-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: 6.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHftqPHAQDFLRAVCeekirlmvSGSAALPLPVLEKWKN 80
Cdd:cd04433 71 LLPKFDPEAALELI---EREKVTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEIG-MALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGE 159
Cdd:cd04433 137 APGIKLVNGYGLTETGgTVATGPPDDDARKPGSVGRPVPGVEVRIV-----------------DPDGGELPPGEI---GE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETkSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd04433 197 LVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLdEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAA 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:cd04433 275 VVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
24-306 |
1.36e-77 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 244.13 E-value: 1.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 24 VFMAVPTIYTKLMEYYDrhftqpHAQDFLRAvceekiRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS--- 100
Cdd:PRK07787 219 LYFGVPTVWSRIAADPE------AARALRGA------RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLStra 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 101 -GPlttavRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVtPGFEEKEGELLVRGPSVFREYWNKPEETK 179
Cdd:PRK07787 287 dGE-----RRPGWVGLPLAGVETRLV-----------------DEDGGPV-PHDGETVGELQVRGPTLFDGYLNRPDATA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 180 SAFTLDGWFKTGDTVVFK-DGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLR 258
Cdd:PRK07787 344 AAFTADGWFRTGDVAVVDpDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGA 423
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 546232251 259 EGhsLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK07787 424 DD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-304 |
1.43e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 232.38 E-value: 1.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKN 80
Cdd:PRK06187 238 IPRRFDPENLLDLI---ETERVTFFFAVPTIWQMLLKAPR-----AYFVDFSS------LRLVIYGGAALPPALLREFKE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEigmalSGPLTTAVRLP----------GSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVT 150
Cdd:PRK06187 304 KFGIDLVQGYGMTE-----TSPVVSVLPPEdqlpgqwtkrRSAGRPLPGVEARIV-----------------DDDGDELP 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 151 PGFEEKeGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLL 229
Cdd:PRK06187 362 PDGGEV-GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIdEDGYLYITDRIK-DVIISGGENIYPRELEDALY 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 230 AHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 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 |
2.80e-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: 224.41 E-value: 2.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTqphaqDFLRavceekIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd17631 170 ILRKFDPETVLDLI---ERHRVTSFFLVPTMIQALLQHPRFATT-----DLSS------LRAVIYGGAPMPERLLRALQA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ItGHTLLERYGMTEIGMALSG-PLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGE 159
Cdd:cd17631 236 R-GVKFVQGYGMTETSPGVTFlSPEDHRRKLGSAGRPVFFVEVRIV-----------------DPDGREVPPG---EVGE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd17631 295 IVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLdEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
2-304 |
1.49e-69 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 224.37 E-value: 1.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 2 MPEFSPQQVWEKFlssetPRINVFMAVPTIYTKLMEyyDRHFTQPHAQdflravceeKIRLMVSGSAALPLPVLEKWKNI 81
Cdd:PRK07514 229 LPKFDPDAVLALM-----PRATVMMGVPTFYTRLLQ--EPRLTREAAA---------HMRLFISGSAPLLAETHREFQER 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 TGHTLLERYGMTEIGMALSGPLTTAvRLPGSVGTPLPGVQVRIVsenpqreacsytihaeGDERGTKVTPGfeeKEGELL 161
Cdd:PRK07514 293 TGHAILERYGMTETNMNTSNPYDGE-RRAGTVGFPLPGVSLRVT----------------DPETGAELPPG---EIGMIE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 162 VRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVI 240
Cdd:PRK07514 353 VKGPNVFKGYWRMPEKTAEEFRADGFFITGDLgKIDERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVI 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 546232251 241 GVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07514 432 GVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
21-304 |
2.80e-66 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 217.29 E-value: 2.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDRHftqPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMA-L 99
Cdd:COG0365 278 GVTVFFTAPTAIRALMKAGDEP---LKKYDL------SSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfI 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 100 SGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRG--PSVFREYWNKPEE 177
Cdd:COG0365 349 SNLPGLPVK-PGSMGKPVPGYDVAVV-----------------DEDGNPVPPG---EEGELVIKGpwPGMFRGYWNDPER 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 178 TKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:COG0365 408 YRETYfgRFPGWYRTGDGARRdEDGYFWILGRSD-DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAF 486
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 546232251 255 VTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 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 |
1.39e-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: 211.02 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTQPHAqdflravceeKIRLMVSGSAALPLPVLEKWKN 80
Cdd:cd05926 221 LPPRFSASTFWPDV---RDYNATWYTAVPTIHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEIG--MAlSGPLTTAVRLPGSVGTPLpGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEG 158
Cdd:cd05926 288 TFGAPVLEAYGMTEAAhqMT-SNPLPPGPRKPGSVGKPV-GVEVRIL-----------------DEDGEILPPG---VVG 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 159 ELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDV 237
Cdd:cd05926 346 EICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDaDGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEA 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546232251 238 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05926 425 VAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
27-299 |
5.28e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 208.70 E-value: 5.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 27 AVPTIYTKLMEYYDRHftqphaqdflrAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MALSGPLTT 105
Cdd:PRK05605 316 GVPPLYEKIAEAAEER-----------GVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 106 AvRLPGSVGTPLPGVQVRIVS-ENPQREacsytihaegdergtkVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFtL 184
Cdd:PRK05605 385 D-RRPGYVGVPFPDTEVRIVDpEDPDET----------------MPDG---EEGELLVRGPQVFKGYWNRPEETAKSF-L 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 185 DGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSL 263
Cdd:PRK05605 444 DGWFRTGDVVVMEeDGFIRIVDRIK-ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAL 522
|
250 260 270
....*....|....*....|....*....|....*.
gi 546232251 264 SHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK05605 523 DPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-304 |
6.46e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 196.66 E-value: 6.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVwekFLSSETPRINVFMAVPTIYTKLMEYYDRHftqphAQDFlravceEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:PRK07656 238 PLPVFDPDEV---FRLIETERITVLPGPPTMYNSLLQHPDRS-----AEDL------SSLRLAVTGAASMPVALLERFES 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITG-HTLLERYGMTEigmalSGPLTTAVRL-------PGSVGTPLPGVQVRIVSENpqreacsytihaeGDERGTKVTpg 152
Cdd:PRK07656 304 ELGvDIVLTGYGLSE-----ASGVTTFNRLdddrktvAGTIGTAIAGVENKIVNEL-------------GEEVPVGEV-- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 153 feekeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 231
Cdd:PRK07656 364 -----GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEH 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 232 PSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 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 |
1.14e-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: 185.26 E-value: 1.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEF-SPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFLRavceekIRLMVSGSAALPLPVLEKWK 79
Cdd:cd05959 236 LMPERpTPAAVFKRI---RRYRPTVFFGVPTLYAAMLAAPN-----LPSRDLSS------LRLCVSAGEALPAEVGERWK 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 80 NITGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGE 159
Cdd:cd05959 302 ARFGLDILDGIGSTEMLHIFLSNRPGRVR-YGTTGKPVPGYEVELR-----------------DEDGGDVADG---EPGE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAA 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHS---LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05959 439 VVGVEDEDGLTKPKAFVVLRPGYEdseALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2-304 |
2.68e-53 |
|
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: 179.84 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 2 MPEFSPQQVWEKfLSSEtpRINVFMAVPTIYTKLMEyydrhfTQPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNI 81
Cdd:cd05972 156 GPRFDAERILEL-LERY--GVTSFCGPPTAYRMLIK------QDLSSYKFSH------LRLVVSAGEPLNPEVIEWWRAA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 TGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELL 161
Cdd:cd05972 221 TGLPIRDGYGQTETGLTVGNFPDMPVK-PGSMGRPTPGYDVAII-----------------DDDGRELPPG---EEGDIA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 162 VR--GPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05972 280 IKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDRAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAA 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05972 358 VVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
27-304 |
3.09e-51 |
|
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: 176.67 E-value: 3.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 27 AVPTIYTKLMEYYDRHftqPHAQDFLRAVceekirlmVSGSAALPLPVLEKWKNItGHTLLERYGMTEigmalSGPLTTA 106
Cdd:cd12119 260 GVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIEAFEER-GVRVIHAWGMTE-----TSPLGTV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 107 VRLPGSV---------------GTPLPGVQVRIVSENpqreacsytihaegdergTKVTPGFEEKEGELLVRGPSVFREY 171
Cdd:cd12119 323 ARPPSEHsnlsedeqlalrakqGRPVPGVELRIVDDD------------------GRELPWDGKAVGELQVRGPWVTKSY 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 172 WNKPEETKsAFTLDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQR 250
Cdd:cd12119 385 YKNDEESE-ALTEDGWLRTGDvATIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGER 462
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 546232251 251 VTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12119 463 PLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1-299 |
3.33e-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: 173.17 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLMEYydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWK 79
Cdd:cd05911 219 IMPKFDS----ELFLDLiEKYKITFLYLVPPIAAALAKS-----PLLDKYDL------SSLRVILSGGAPLSKELQELLA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 80 NITGHT-LLERYGMTEIGMALSgPLTTAVRLPGSVGTPLPGVQVRIVSenpqreacsytihaegDERGTKVTPGfeeKEG 158
Cdd:cd05911 284 KRFPNAtIKQGYGMTETGGILT-VNPDGDDKPGSVGRLLPNVEAKIVD----------------DDGKDSLGPN---EPG 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 159 ELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDV 237
Cdd:cd05911 344 EICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFdEDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADA 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 238 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYavpSEL----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 |
2.34e-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: 167.06 E-value: 2.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 2 MPEFSPQQVWEKflsSETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqDFLRAVceekirlmvsgsAALPLP-VLEKWKN 80
Cdd:cd17637 72 MEKFDPAEALEL---IEEEKVTLMGSFPPILSNLLDAAEKSGVDL---SSLRHV------------LGLDAPeTIQRFEE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEIgmalSGPLTTA--VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEG 158
Cdd:cd17637 134 TTGATFWSLYGQTET----SGLVTLSpyRERPGSAGRPGPLVRVRIV-----------------DDNDRPVPAG---ETG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 159 ELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSV-DIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:cd17637 190 EIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFdEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAE 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17637 269 VCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
46-304 |
3.60e-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: 171.10 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 46 PHAQDFLRAVCEEK-----IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmalsGPLTTaVRL--P-----GSV 113
Cdd:COG1021 283 PLALLWLDAAERSRydlssLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE------GLVNY-TRLddPeevilTTQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 114 GTPL-PGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 192
Cdd:COG1021 356 GRPIsPDDEVRIV-----------------DEDGNPVPPG---EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 193 TVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLReGHSLSHRELKEW 271
Cdd:COG1021 416 LVRRtPDGYLVVEGR-AKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRF 493
|
250 260 270
....*....|....*....|....*....|....
gi 546232251 272 ARNV-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 |
3.62e-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: 169.18 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDrhftqpHAQDFLRAvceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:cd05919 182 RPTVLYGVPTFYANLLDSCA------GSPDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 101 GPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKS 180
Cdd:cd05919 251 SNRPGAWR-LGSTGRPVPGYEIRLV-----------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWNNPEKSRA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 181 AFtLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRE 259
Cdd:cd05919 310 TF-NGGWYRTGDKFCRdADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 546232251 260 GHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05919 388 PAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-305 |
3.83e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 169.06 E-value: 3.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:PRK06710 280 LIPKFDMKMVFEAI---KKHKVTLFPGAPTIYIALLN-----------SPLLKEYDISSIRACISGSAPLPVEVQEKFET 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEigmalSGPLTTA-----VRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfee 155
Cdd:PRK06710 346 VTGGKLVEGYGLTE-----SSPVTHSnflweKRVPGSIGVPWPDTEAMIMSL----------------ETGEALPPG--- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 156 KEGELLVRGPSVFREYWNKPEETkSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 234
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVgYMDEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKV 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546232251 235 TDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 305
Cdd:PRK06710 480 QEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
66-304 |
3.82e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 165.88 E-value: 3.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 66 GSAALPLPVLEKwknitghtLLER---------YGMTEIGmalsgPLTTAV------RLPGSVGTPLPGVQVRIVsenpq 130
Cdd:PRK08316 294 GASIMPVEVLKE--------LRERlpglrfyncYGQTEIA-----PLATVLgpeehlRRPGSAGRPVLNVETRVV----- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 131 reacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSv 209
Cdd:PRK08316 356 ------------DDDGNDVAPG---EVGEIVHRSPQLMLGYWDDPEKTAEAFR-GGWFHSGDLGVMdEEGYITVVDRKK- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 210 DIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVE 289
Cdd:PRK08316 419 DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVD 498
|
250
....*....|....*
gi 546232251 290 EIPRNQMGKIDKKAL 304
Cdd:PRK08316 499 ELPRNPSGKILKREL 513
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
60-304 |
5.91e-47 |
|
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: 164.42 E-value: 5.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmalsgPLTTAVRL--PGSV-----GTPL-PGVQVRIVsenpqr 131
Cdd:cd05920 257 LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-------GLLNYTRLddPDEViihtqGRPMsPDDEIRVV------ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 132 eacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV-VFKDGQYWIRGRTSvD 210
Cdd:cd05920 324 -----------DEEGNPVPPG---EEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-D 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 211 IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLReGHSLSHRELKEWARNV-LAPYAVPSELVLVE 289
Cdd:cd05920 389 QINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVD 467
|
250
....*....|....*
gi 546232251 290 EIPRNQMGKIDKKAL 304
Cdd:cd05920 468 SLPLTAVGKIDKKAL 482
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1-304 |
9.90e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 164.77 E-value: 9.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFlravceEKIRLMVSGSAALpLPV-LEKW 78
Cdd:PRK06188 238 VLAKFDP----AEVLRAiEEQRITATFLVPTMIYALLDHPD-----LRTRDL------SSLETVYYGASPM-SPVrLAEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 79 KNITGHTLLERYGMTEIGMALS------GPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPG 152
Cdd:PRK06188 302 IERFGPIFAQYYGQTEAPMVITylrkrdHDPDDPKRL-TSCGRPTPGLRVALL-----------------DEDGREVAQG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 153 feeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 231
Cdd:PRK06188 364 ---EVGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDvAREDEDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEH 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 232 PSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK06188 439 PAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
46-301 |
2.36e-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: 161.78 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 46 PHAQDFLRAVCEE-----KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMAL-SGPLTTAVRLPGSVGTPLPG 119
Cdd:cd05903 191 PFLTDLLNAVEEAgeplsRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVtSITPAPEDRRLYTDGRPLPG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 120 VQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVFKDG 199
Cdd:cd05903 271 VEIKVV-----------------DDTGATLAPG---VEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDED 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 200 QYW-IRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW-ARNVLA 277
Cdd:cd05903 330 GYLrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYlDRQGVA 408
|
250 260
....*....|....*....|....
gi 546232251 278 PYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd05903 409 KQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1-305 |
5.80e-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: 160.53 E-value: 5.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEyydrhfTQPHAQDflravCEEKIRLmVSGSAALPLpVLEKWKN 80
Cdd:cd05934 153 LLPRFSASRFWSDVRRY---GATVTNYLGAMLSYLLA------QPPSPDD-----RAHRLRA-AYGAPNPPE-LHEEFEE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGEL 160
Cdd:cd05934 217 RFGVRLLEGYGMTETIVGVIGPRDEPRR-PGSIGRPAPGYEVRIV-----------------DDDGQELPAG---EPGEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 161 LVR---GPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:cd05934 276 VIRglrGWGFFKGYYNMPEATAEAMR-NGWFHTGDLGYRdADGFFYFVDRKK-DMIRRRGENISSAEVERAILRHPAVRE 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 305
Cdd:cd05934 354 AAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
18-306 |
6.07e-46 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 161.95 E-value: 6.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMEYYDRHFTqphaqDFlravceEKIRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTE--- 94
Cdd:PRK06839 235 EKHKVTVVMGVPTIHQALINCSKFETT-----NL------QSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtsp 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 95 -IGMALSgplTTAVRLPGSVGTPLPGVQVRIVSENpqreacsytihaegderGTKVTPGfeeKEGELLVRGPSVFREYWN 173
Cdd:PRK06839 303 tVFMLSE---EDARRKVGSIGKPVLFCDYELIDEN-----------------KNKVEVG---EVGELLIRGPNVMKEYWN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 174 KPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVT 252
Cdd:PRK06839 360 RPDATEETIQ-DGWLCTGDLARVdEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPI 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 546232251 253 AVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK06839 438 AFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
21-304 |
1.46e-45 |
|
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: 159.95 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDrhFTQPHAQdflravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:cd05958 187 KPTVLFTAPTAYRAMLAHPD--AAGPDLS---------SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 101 GPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVfreYWNKPEETKS 180
Cdd:cd05958 256 SARPGDAR-PGATGKPVPGYEAKVV-----------------DDEGNPVPDG---TIGRLAVRGPTG---CRYLADKRQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 181 AFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRE 259
Cdd:cd05958 312 TYVQGGWNITGDTySRDPDGYFRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRP 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 546232251 260 GHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05958 391 GVIPGPvlaRELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
18-307 |
4.47e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.97 E-value: 4.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMEyydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEiGM 97
Cdd:PRK07529 305 ERYRINFLSGVPTVYAALLQ------VPVDGHDI------SSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-AT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 ALS--GPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaEGDERGTKVTPGFEEKEGELLVRGPSVFREYWNkP 175
Cdd:PRK07529 372 CVSsvNPPDGERR-IGSVGLRLPYQRVRVV---------------ILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLE-A 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 176 EETKSAFTLDGWFKTGDTV-VFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:PRK07529 435 AHNKGLWLEDGWLNTGDLGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 546232251 255 VTLREGHSLSHRELKEWAR-NVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRH 307
Cdd:PRK07529 514 VQLKPGASATEAELLAFARdHIAERAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
4-304 |
1.41e-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: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 4 EFSPQQvWEKFLSSEtpRINVFMAVPTIYTKLMEYYDrhftqphaqDFLRAVCEEKIRLMVSGSAALPlPVLEKW-KNIT 82
Cdd:cd05969 165 RFDAES-WYGIIERV--KVTVWYTAPTAIRMLMKEGD---------ELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 83 GHTLLERYGMTEIG-MALSGPLTTAVRlPGSVGTPLPGVQVRIVSENpqreacsytihaegderGTKVTPGfeeKEGELL 161
Cdd:cd05969 232 GVPIHDTWWQTETGsIMIANYPCMPIK-PGSMGKPLPGVKAAVVDEN-----------------GNELPPG---TKGILA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 162 VRG--PSVFREYWNKPEETKSAFtLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05969 291 LKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRdEDGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAG 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05969 369 VIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
63-304 |
1.98e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 154.96 E-value: 1.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 63 MVSGSAALPLPVLEKWKNiTGHTLLERYGMTEIGMALSGPLTTAV---RLpGSVGTPLPGVQVRIVsenpqreacsytih 139
Cdd:PRK09088 257 LFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDViraKA-GAAGIPTPTVQTRVV-------------- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 140 aegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYK 218
Cdd:PRK09088 321 ---DDQGNDCPAG---VPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDaDGFFWVVDRKK-DMFISGGEN 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 219 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:PRK09088 394 VYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGK 473
|
....*.
gi 546232251 299 IDKKAL 304
Cdd:PRK09088 474 LQKARL 479
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
46-304 |
2.41e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 155.98 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 46 PHAQDFLRAVCEE-----KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAV-RLPGSVGTPLPG 119
Cdd:PRK13295 295 PFLTDLTRAVKESgrpvsSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDeRASTTDGCPLPG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 120 VQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFtlDGWFKTGDtVVFKDG 199
Cdd:PRK13295 375 VEVRVV-----------------DADGAPLPAG---QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGD-LARIDA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 200 QYWIR--GRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARNV 275
Cdd:PRK13295 432 DGYIRisGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFlkAQKV 510
|
250 260
....*....|....*....|....*....
gi 546232251 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 |
1.43e-42 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 151.35 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEYYDRHftqphaqdflravCEEKIRLMVSGSAALPLPVLE--KW 78
Cdd:cd05912 148 LVDKFDAEQVLHLINSG---KVTIISVVPTMLQRLLEILGEG-------------YPNNLRCILLGGGPAPKPLLEqcKE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 79 KNITghtLLERYGMTEIG---MALSgPLTTAVRLpGSVGTPLPGVQVRIVSENpqreacsytihaegdergtkvtpGFEE 155
Cdd:cd05912 212 KGIP---VYQSYGMTETCsqiVTLS-PEDALNKI-GSAGKPLFPVELKIEDDG-----------------------QPPY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 156 KEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 234
Cdd:cd05912 264 EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLdEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAI 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546232251 235 TDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd05912 342 KEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
59-304 |
4.22e-42 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 152.90 E-value: 4.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmalSGPLTTA-----VRLPGSVGTPLPGVQVRIVsenpqrea 133
Cdd:PRK08974 326 SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTE-----CSPLVSVnpydlDYYSGSIGLPVPSTEIKLV-------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 134 csytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDII 212
Cdd:PRK08974 393 ---------DDDGNEVPPG---EPGELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMdEEGFLRIVDRKK-DMI 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 213 KTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREgHSLSHRELKEWARNVLAPYAVPSELVLVEEIP 292
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELP 537
|
250
....*....|..
gi 546232251 293 RNQMGKIDKKAL 304
Cdd:PRK08974 538 KSNVGKILRREL 549
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-215 |
1.12e-41 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 149.00 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFLSSETPRINVFMAVPTIYTKLMEyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKN 80
Cdd:pfam00501 231 LPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGHTLLERYGMTE--IGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREacsytihaegdergtkVTPGfeeKEG 158
Cdd:pfam00501 300 LFGGALVNGYGLTEttGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEP----------------VPPG---EPG 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 159 ELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTG 215
Cdd:pfam00501 361 ELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-301 |
1.22e-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: 147.42 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKwknitghtLLERYGMTEI----GMALSGPLTTAVRLP-------GSVGTPLPGVQVRIVSEn 128
Cdd:cd05917 120 LRTGIMAGAPCPPELMKR--------VIEVMNMKDVtiayGMTETSPVSTQTRTDdsiekrvNTVGRIMPHTEAKIVDP- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 129 pqreacsytihaegderGTKVTPGFEEKeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRT 207
Cdd:cd05917 191 -----------------EGGIVPPVGVP-GELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 208 SvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVL 287
Cdd:cd05917 253 K-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFF 331
|
250
....*....|....
gi 546232251 288 VEEIPRNQMGKIDK 301
Cdd:cd05917 332 VDEFPLTVSGKIQK 345
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
34-306 |
1.40e-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: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 34 KLMEYY--DRHFTQPHAQDFLRAVCEEK----IRLMVSGSAALPL-PVLEKW-KNITGHTLLERYGMTEIGMALSGPLTT 105
Cdd:cd05971 175 DLMSRYgvTTAFLPPTALKMMRQQGEQLkhaqVKLRAIATGGESLgEELLGWaREQFGVEVNEFYGQTECNLVIGNCSAL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 106 AVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPS--VFREYWNKPEETKSAFT 183
Cdd:cd05971 255 FPIKPGSMGKPIPGHRVAIV-----------------DDNGTPLPPG---EVGEIAVELPDpvAFLGYWNNPSATEKKMA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 184 LDgWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS 262
Cdd:cd05971 315 GD-WLLTGDLgRKDSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET 392
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 546232251 263 LSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd05971 393 PSDalaREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
59-286 |
3.47e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 150.64 E-value: 3.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEigmalSGPLTTAVRL----PGSVGTPLPGVQVRIvsenpqreac 134
Cdd:COG1022 348 RLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTE-----TSPVITVNRPgdnrIGTVGPPLPGVEVKI---------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 135 sytihAEgdergtkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIK 213
Cdd:COG1022 412 -----AE---------------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELdEDGFLRITGRKK-DLIV 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 214 T-GGYKVSALEVEWHLLAHPSITDVAVIGvpDmtwgQR--VTAVVTLREGhslshrELKEWARNVLAPYAVPSELV 286
Cdd:COG1022 471 TsGGKNVAPQPIENALKASPLIEQAVVVG--D----GRpfLAALIVPDFE------ALGEWAEENGLPYTSYAELA 534
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
21-304 |
6.21e-41 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 149.59 E-value: 6.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDrhFTQphaQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MAL 99
Cdd:PRK12492 307 RFSALLGLNTLFVALMDHPG--FKD---LDF------SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVAS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 100 SGPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETK 179
Cdd:PRK12492 376 TNPYGELARL-GTVGIPVPGTALKVI-----------------DDDGNELPLG---ERGELCIKGPQVMKGYWQQPEATA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 180 SAFTLDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLR 258
Cdd:PRK12492 435 EALDAEGWFKTGDiAVIDPDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVAR 513
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 546232251 259 EGhSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12492 514 DP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
21-304 |
1.61e-40 |
|
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: 144.55 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEyydrhftQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:cd05944 97 RITSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 101 -GPLTTAVRlPGSVGTPLPGVQVRIVSENPQREacsYTIHAEGDErgtkvtpgfeekEGELLVRGPSVFREYWNKpEETK 179
Cdd:cd05944 164 vNPPDGPKR-PGSVGLRLPYARVRIKVLDGVGR---LLRDCAPDE------------VGEICVAGPGVFGGYLYT-EGNK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 180 SAFTLDGWFKTGDTV-VFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLR 258
Cdd:cd05944 227 NAFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 546232251 259 EGHSLSHRELKEWAR-NVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05944 306 PGAVVEEEELLAWARdHVPERAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
18-301 |
2.13e-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: 143.80 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMEYydrhftqPHAQDFLRAvceeKIRLMVSGSAALPLPVLEKWKNITG-HTLLERYGMTEIG 96
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 97 MA-LSGPLTTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdergtkvtpgfeekeGELLVRGPSVFREYWNKP 175
Cdd:cd17638 155 VAtMCRPGDDAETVATTCGRACPGFEVRIADD------------------------------GEVLVRGYNVMQGYLDDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 176 EETKSAFTLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:cd17638 205 EATAEAIDADGWLHTGDVGELDErGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAF 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 546232251 255 VTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17638 284 VVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-304 |
4.62e-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: 145.36 E-value: 4.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDRhftqphaQDFlravceEKIRLMVSGSAALPLPVLEKW-KNITGHTLLERYGMTEI-GMA 98
Cdd:cd05930 184 GITVLHLTPSLLRLLLQELEL-------AAL------PSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEAtVDA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 99 LSGPLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPE 176
Cdd:cd05930 251 TYYRVPPDDEEDGRVpiGRPIPNTRVYVL-----------------DENLRPVPPG---VPGELYIGGAGLARGYLNRPE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 177 ETKSAFTLDGWF------KTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ 249
Cdd:cd05930 311 LTAERFVPNPFGpgermyRTGDLVRWLpDGNLEFLGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEK 389
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 250 RVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05930 390 RLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2-306 |
5.89e-40 |
|
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: 146.49 E-value: 5.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 2 MPEFSPQQVWEKFlssETPRINVFMAVPTIYTKL----MEYYDRhftqphaqdflravceEKIRLMVSGSAALPLPVLEK 77
Cdd:cd05970 260 YDKFDPKALLEKL---SKYGVTTFCAPPTIYRFLiredLSRYDL----------------SSLRYCTTAGEALNPEVFNT 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 78 WKNITGHTLLERYGMTEIGMALsGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKE 157
Cdd:cd05970 321 FKEKTGIKLMEGFGQTETTLTI-ATFPWMEPKPGSMGKPAPGYEIDLI-----------------DREGRSCEAG---EE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVR---GPSV--FREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 231
Cdd:cd05970 380 GEIVIRtskGKPVglFGGYYKDAEKTAEVWH-DGYYHTGDAAWMdEDGYLWFVGRTD-DLIKSSGYRIGPFEVESALIQH 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 232 PSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIdKKALIR 306
Cdd:cd05970 458 PAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEelkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI-RRVEIR 534
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
1-301 |
6.97e-40 |
|
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: 145.75 E-value: 6.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEF-SPQQVWEKFLSSETpriNVFMAVPTIYTKLMeyydrhftqphAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWK 79
Cdd:TIGR02262 234 LMGERpTPDAVFDRLRRHQP---TIFYGVPTLYAAML-----------ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 80 NITGHTLLERYGMTEIGMALSGPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGE 159
Cdd:TIGR02262 300 ARFGVDIVDGIGSTEMLHIFLSNLPGDVRY-GTSGKPVPGYRLRLV-----------------GDGGQDVADG---EPGE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:TIGR02262 359 LLISGPSSATMYWNNRAKSRDTF-QGEWTRSGDKyVRNDDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAA 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:TIGR02262 437 VVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
59-304 |
1.52e-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: 145.07 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTE---IGMALSGPLTTAVRlPGSVGTPLPGVQVRIVSEnpqreac 134
Cdd:cd05904 276 SLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTEstgVVAMCFAPEKDRAK-YGSVGRLVPNVEAKIVDP------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 135 sytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIK 213
Cdd:cd05904 348 ---------ETGESLPPN---QTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIdEDGYLFIVDRLK-ELIK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 214 TGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPR 293
Cdd:cd05904 415 YKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPK 494
|
250
....*....|.
gi 546232251 294 NQMGKIDKKAL 304
Cdd:cd05904 495 SPSGKILRKEL 505
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
60-304 |
2.02e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 145.29 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytih 139
Cdd:PRK05677 328 LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQV-GTIGIPVPSTLCKVI-------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 140 aegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYK 218
Cdd:PRK05677 393 ---DDDGNELPLG---EVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKK-DMILVSGFN 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 219 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
....*.
gi 546232251 299 IDKKAL 304
Cdd:PRK05677 546 ILRREL 551
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
28-308 |
2.41e-39 |
|
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: 140.54 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 28 VPTIYTKLMeyyDRHFTQPhAQDFLRAVceekirlmVSGSAALPLPVLEKWKNiTGHTLLERYGMTEIGMALSGpLTTAV 107
Cdd:cd17630 93 VPTQLQRLL---DSGQGPA-ALKSLRAV--------LLGGAPIPPELLERAAD-RGIPLYTTYGMTETASQVAT-KRPDG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 108 RLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdergtkvtpgfeekeGELLVRGPSVFREYWNKPEEtkSAFTLDGW 187
Cdd:cd17630 159 FGRGGVGVLLPGRELRIVED------------------------------GEIWVGGASLAMGYLRGQLV--PEFNEDGW 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 188 FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLShr 266
Cdd:cd17630 207 FTTKDLGELhADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA-- 283
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 546232251 267 ELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:cd17630 284 ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-304 |
4.22e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 143.18 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEkflSSETPRINVFMAVPTIYTKLMEYYDRHftqphaqdflraVCEEKIRLMVSGSAALPLPVLE--KW 78
Cdd:PRK03640 212 LVEKFDAEKINK---LLQTGGVTIISVVSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEqcKE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 79 KNITghtLLERYGMTEigmalsgpltTA---VRLP--------GSVGTPLPGVQVRIvsenpqreacsytihaegdERGT 147
Cdd:PRK03640 277 KGIP---VYQSYGMTE----------TAsqiVTLSpedaltklGSAGKPLFPCELKI-------------------EKDG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 148 KVTPGFEEkeGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEW 226
Cdd:PRK03640 325 VVVPPFEE--GEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLdEEGFLYVLDRRS-DLIISGGENIYPAEIEE 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 227 HLLAHPSITDVAVIGVPDMTWGQRVTAVVTLreGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK03640 401 VLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
18-304 |
4.68e-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: 142.23 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMeyydrhftqphAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigm 97
Cdd:cd05935 170 EKYKVTFWTNIPTMLVDLL-----------ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 ALSGPLTTAVRLPGS--VGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKP 175
Cdd:cd05935 236 TMSQTHTNPPLRPKLqcLGIP*FGVDARVIDI----------------ETGRELPPN---EVGEIVVRGPQIFKGYWNRP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 176 EETKSAFTLDG---WFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV 251
Cdd:cd05935 297 EETEESFIEIKgrrFFRTGDLgYMDEEGYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEV 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 252 TAVVTLREGH--SLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05935 376 KAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
2-301 |
5.46e-39 |
|
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: 143.21 E-value: 5.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 2 MPEFSPQQVWEkflSSETPRINVFMAVPTIYTKLMEyydrhftqphAQDFLRAVCEEKIRLMVSGSAAlPLPVLEKWKNI 81
Cdd:cd12118 205 LRKVDAKAIYD---LIEKHKVTHFCGAPTVLNMLAN----------APPSDARPLPHRVHVMTAGAPP-PAAVLAKMEEL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 tGHTLLERYGMTEIgmalSGPLTTAVRLPGSVGTPLPgVQVRIVSenpqREACSYTIHAE---GDERGTKVTPGFEEKEG 158
Cdd:cd12118 271 -GFDVTHVYGLTET----YGPATVCAWKPEWDELPTE-ERARLKA----RQGVRYVGLEEvdvLDPETMKPVPRDGKTIG 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 159 ELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDV 237
Cdd:cd12118 341 EIVFRGNIVMKGYLKNPEATAEAFR-GGWFHSGDlAVIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEA 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 546232251 238 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVlVEEIPRNQMGKIDK 301
Cdd:cd12118 419 AVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQK 481
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
70-304 |
3.11e-38 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 141.74 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 70 LPLPVLEKWKNIT--GHTLLERYGMTE-IGMALSGPLTTAVRLPgSVGTPLPGVQVRIVsenpqreacsytihaegDERG 146
Cdd:PRK08008 297 LNLSDQEKDAFEErfGVRLLTSYGMTEtIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIR-----------------DDHN 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 147 TKVTPGfeeKEGELLVRG---PSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSAL 222
Cdd:PRK08008 359 RPLPAG---EIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTgYVDEEGFFYFVDR-RCNMIKRGGENVSCV 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 223 EVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKK 302
Cdd:PRK08008 435 ELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKK 514
|
..
gi 546232251 303 AL 304
Cdd:PRK08008 515 NL 516
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
5-306 |
4.93e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 141.33 E-value: 4.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 5 FSPQQVWEKFlssETPRINVFMAVPTIYTKLMEY--YDRHftqPHAQdfLRAVceekIRL---MVSGSAALPLPVLekwk 79
Cdd:PRK07470 241 FDPAEVWALV---ERHRVTNLFTVPTILKMLVEHpaVDRY---DHSS--LRYV----IYAgapMYRADQKRALAKL---- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 80 nitGHTLLERYGMTEIgmalSGPLTTavrLPGSVGTPLPGVQVRIVSENPQREACSYTIHaegDERGTKVTPGfeeKEGE 159
Cdd:PRK07470 305 ---GKVLVQYFGLGEV----TGNITV---LPPALHDAEDGPDARIGTCGFERTGMEVQIQ---DDEGRELPPG---ETGE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK07470 369 ICVIGPAVFAGYYNNPEANAKAFR-DGWFRTGDLgHLDARGFLYITGRAS-DMYISGGSNVYPREIEEKLLTHPAVSEVA 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKaLIR 306
Cdd:PRK07470 447 VLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK-MVR 513
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
77-304 |
7.06e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 141.33 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 77 KWKNITGHTLLE-RYGMTEIGMALSgpLTTAVRL--------PGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGT 147
Cdd:PRK06178 346 RWRALTGSVLAEaAWGMTETHTCDT--FTAGFQDddfdllsqPVFVGLPVPGTEFKICDF----------------ETGE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 148 KVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVFkDGQYWIR--GRTSvDIIKTGGYKVSALEVE 225
Cdd:PRK06178 408 LLPLG---AEGEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDIGKI-DEQGFLHylGRRK-EMLKVNGMSVFPSEVE 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 226 WHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPsELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK06178 482 ALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
24-286 |
8.32e-38 |
|
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: 139.27 E-value: 8.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 24 VFMAVPTIYTKLMEYYDRHFTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPL 103
Cdd:cd05907 177 VFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 104 TTAVRlPGSVGTPLPGVQVRIVSEnpqreacsytihaegdergtkvtpgfeekeGELLVRGPSVFREYWNKPEETKSAFT 183
Cdd:cd05907 256 PGDNR-IGTVGKPLPGVEVRIADD------------------------------GEILVRGPNVMLGYYKNPEATAEALD 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 184 LDGWFKTGDTVVFK-DGQYWIRGRtSVDIIKT-GGYKVSALEVEWHLLAHPSITDVAVIGvpDmtwgQR--VTAVVTLRE 259
Cdd:cd05907 305 ADGWLHTGDLGEIDeDGFLHITGR-KKDLIITsGGKNISPEPIENALKASPLISQAVVIG--D----GRpfLVALIVPDP 377
|
250 260
....*....|....*....|....*..
gi 546232251 260 GhslshrELKEWARNVLAPYAVPSELV 286
Cdd:cd05907 378 E------ALEAWAEEHGIAYTDVAELA 398
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
82-304 |
1.17e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 139.64 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 TGHTLLERYGMTEigmALSG-PLTTAVR---LPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKE 157
Cdd:PRK06145 289 TRARYIDAYGLTE---TCSGdTLMEAGReieKIGSTGRALAHVEIRIA-----------------DGAGRWLPPN---MK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PRK06145 346 GEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEeGFLYLTDRKK-DMIISGGENIASSEVERVIYELPEVAE 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK06145 424 AAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
22-304 |
1.23e-37 |
|
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: 138.92 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 22 INVFMAVPTIYTKLMEyyDRHFTQPHAQDfLRAV--CEEkirlmvsgsaALPLPVLEKWKNIT-GHTLLERYGMTEIGMA 98
Cdd:cd05945 189 ITVWVSTPSFAAMCLL--SPTFTPESLPS-LRHFlfCGE----------VLPHKTARALQQRFpDARIYNTYGPTEATVA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 99 LSG------PLTTAVRLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYW 172
Cdd:cd05945 256 VTYievtpeVLDGYDRLP--IGYAKPGAKLVIL-----------------DEDGRPVPPG---EKGELVISGPSVSKGYL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 173 NKPEETKSAFTLD---GWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWG 248
Cdd:cd05945 314 NNPEKTAAAFFPDegqRAYRTGDLVRLEaDGLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKV 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 546232251 249 QRVTAVVTLREGHSLSH-RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05945 393 TELIAFVVPKPGAEAGLtKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
4-304 |
1.40e-37 |
|
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: 139.57 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 4 EFSPQQVWEKFlssETPRINVFMAVPTIYTKLMeyydrhftqpHAQDFLRAVCEEKIRLMVSGsAALPLPVLEKWKNITG 83
Cdd:cd05923 227 EFDPADALKLI---EQERVTSLFATPTHLDALA----------AAAEFAGLKLSSLRHVTFAG-ATMPDAVLERVNQHLP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 84 HTLLERYGMTEIGMALSGPLTTavrlPGSVGTPLPGVQVRIVS--ENPQREAcsytihAEGDErgtkvtpgfeekeGELL 161
Cdd:cd05923 293 GEKVNIYGTTEAMNSLYMRDAR----TGTEMRPGFFSEVRIVRigGSPDEAL------ANGEE-------------GELI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 162 VR--GPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05923 350 VAaaADAAFTGYLNQPEATAKKLQ-DGWYRTGDVgYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVV 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGhSLSHRELKEWAR-NVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05923 428 VIGVADERWGQSVTACVVPREG-TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
21-304 |
2.68e-37 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 139.39 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMeyydrhftqpHAQDFlRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 100
Cdd:PRK07059 301 QVHIFPAVNTLYNALL----------NNPDF-DKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVAT 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 101 GPLTTAVRLPGSVGTPLPGVQVRIvsenpqReacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKS 180
Cdd:PRK07059 370 CNPVDATEFSGTIGLPLPSTEVSI------R-----------DDDGNDLPLG---EPGEICIRGPQVMAGYWNRPDETAK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 181 AFTLDGWFKTGDTVVFKDgqywiRGRTSV-----DIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVV 255
Cdd:PRK07059 430 VMTADGFFRTGDVGVMDE-----RGYTKIvdrkkDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 546232251 256 tLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07059 505 -VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
4-299 |
3.27e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 139.26 E-value: 3.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 4 EFSPQQvWEKFLSSEtpRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRAVCeekirlmvsgSAALPL-PVLEKW-KNI 81
Cdd:PRK04319 281 RFSPER-WYRILEDY--KVTVWYTAPTAIRMLMGAGDDLVKK-YDLSSLRHIL----------SVGEPLnPEVVRWgMKV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 TGHTLLERYGMTEIG--MALSGPlTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGE 159
Cdd:PRK04319 347 FGLPIHDNWWMTETGgiMIANYP-AMDIK-PGSMGKPLPGIEAAIV-----------------DDQGNELPPN---RMGN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRG--PSVFREYWNKPEETKSAFtLDGWFKTGDtVVFKD--GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 235
Cdd:PRK04319 405 LAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGD-SAYMDedGYFWFQGRVD-DVIKTSGERVGPFEVESKLMEHPAVA 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546232251 236 DVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK04319 482 EAGVIGKPDPVRGEIIKAFVALRPGYEPSEelkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
2-304 |
3.34e-37 |
|
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: 138.75 E-value: 3.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 2 MPEFSPQQVWEKFlsSETPrINVFMAVPTIYTKLMeyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNI 81
Cdd:cd05928 250 LPRFDPLVILKTL--SSYP-ITTFCGAPTVYRMLV------------QQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 TGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELL 161
Cdd:cd05928 315 TGLDIYEGYGQTETGLICANFKGMKIK-PGSMGKASPPYDVQII-----------------DDNGNVLPPG---TEGDIG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 162 VR-GP----SVFREYWNKPEETKSAFTLDGWFkTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSIT 235
Cdd:cd05928 374 IRvKPirpfGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVV 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 236 DVAVIGVPDMTWGQRVTAVVTLREGHsLSH------RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05928 452 ESAVVSSPDPIRGEVVKAFVVLAPQF-LSHdpeqltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
43-299 |
5.43e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 138.55 E-value: 5.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 43 FTQPHAQDFlravCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTE-IGMALSGPLTTAVRlpGSVGTPLPGVQ 121
Cdd:PRK08314 294 LASPGLAER----DLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPKL--QCLGIPTFGVD 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 122 VRIVseNPqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAF-TLDG--WFKTGDT-VVFK 197
Cdd:PRK08314 368 ARVI--DP--------------ETLEELPPG---EVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRTGDLgRMDE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 198 DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGH--SLSHRELKEWARNV 275
Cdd:PRK08314 429 EGYFFITDRLK-RMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREH 507
|
250 260
....*....|....*....|....
gi 546232251 276 LAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK08314 508 MAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
21-304 |
7.15e-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: 133.97 E-value: 7.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDRHFTQPHAqdflravceekIRLMVSGSAALPLPVLEKWKNITGH---TLLERYGMTEIGM 97
Cdd:cd17643 184 GVTVLNQTPSAFYQLVEAADRDGRDPLA-----------LRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 ALSGPLTTAVRLPGS----VGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWN 173
Cdd:cd17643 253 HVTFRPLDAADLPAAaaspIGRPLPGLRVYVL-----------------DADGRPVPPG---VVGELYVSGAGVARGYLG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 174 KPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 245
Cdd:cd17643 313 RPELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 246 TWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17643 392 PGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
53-304 |
7.92e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 135.29 E-value: 7.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 53 RAVCEE--------KIRLMVSGSAALPLPVL-EKWKNITGHTLLERYGMTEIGmalsgPLTT------AVRLPGSVGTPL 117
Cdd:PRK07786 277 QAVCAEqqarprdlALRVLSWGAAPASDTLLrQMAATFPEAQILAAFGQTEMS-----PVTCmllgedAIRKLGSVGKVI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 118 PGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTV-VF 196
Cdd:PRK07786 352 PTVAARVV-----------------DENMNDVPVG---EVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVrQD 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 197 KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLR-EGHSLSHRELKEWARNV 275
Cdd:PRK07786 411 EEGYVWVVDRKK-DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnDDAALTLEDLAEFLTDR 489
|
250 260
....*....|....*....|....*....
gi 546232251 276 LAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07786 490 LARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
46-306 |
1.19e-35 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 134.88 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 46 PHAQDFLRAVCEEK-----IRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTE----IGMALSGPLTtavRLPGSVGTP 116
Cdd:PRK06087 285 PFIYDLLNLLEKQPadlsaLRFFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTEssphAVVNLDDPLS---RFMHTDGYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 117 LPGVQVRIVSENPQreacsytihaegdergtKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF 196
Cdd:PRK06087 361 AAGVEIKVVDEARK-----------------TLPPG---CEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRM 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 197 -KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREG-HSLSHRELKEW-AR 273
Cdd:PRK06087 421 dEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPhHSLTLEEVVAFfSR 499
|
250 260 270
....*....|....*....|....*....|...
gi 546232251 274 NVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK06087 500 KRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-308 |
1.41e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 134.63 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 25 FMAVPTIYTKLMEyydrhftQPHAQDFLRAvcEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSgplT 104
Cdd:PRK05852 271 YTAVPTIHQILLE-------RAATEPSGRK--PAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT---T 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 105 TAVRLPGSVGTPL---------PGVQVRIVSENpqreacsytihaegderGTKVTPGfeeKEGELLVRGPSVFREYWNKP 175
Cdd:PRK05852 339 TQIEGIGQTENPVvstglvgrsTGAQIRIVGSD-----------------GLPLPAG---AVGEVWLRGTTVVRGYLGDP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 176 EETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:PRK05852 399 TITAANFT-DGWLRTGDLgSLSAAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAV 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 546232251 255 VTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:PRK05852 477 IVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
90-300 |
1.78e-35 |
|
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: 130.50 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEIGmalsGPLTTA---VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPS 166
Cdd:cd17636 143 YGQTEVM----GLATFAalgGGAIGGAGRPSPLVQVRIL-----------------DEDGREVPDG---EVGEIVARGPT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 167 VFREYWNKPEETkSAFTLDGWFKTGD--------TVVFkdgqywIRGRTSvdIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd17636 199 VMAGYWNRPEVN-ARRTRGGWHHTNDlgrrepdgSLSF------VGPKTR--MIKSGAENIYPAEVERCLRQHPAVADAA 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:cd17636 270 VIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
66-308 |
3.72e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 130.55 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 66 GSAALPLPVLEKWKNItGHTLLERYGMTEIgmalSGplttavrlpGSV--GTPLPGVQVRIVsenpqreacsytihaegd 143
Cdd:PRK07824 159 GGGPAPAPVLDAAAAA-GINVVRTYGMSET----SG---------GCVydGVPLDGVRVRVE------------------ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 144 ergtkvtpgfeekEGELLVRGPSVFREYWNKPEEtkSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:PRK07824 207 -------------DGRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 224 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKA 303
Cdd:PRK07824 271 VEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRA 350
|
....*
gi 546232251 304 LIRHF 308
Cdd:PRK07824 351 LVRRF 355
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
90-301 |
1.25e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 132.20 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEIG--MALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSV 167
Cdd:PRK12583 350 YGMTETSpvSLQTTAADDLERRVETVGRTQPHLEVKVV-----------------DPDGATVPRG---EIGELCTRGYSV 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 168 FREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMT 246
Cdd:PRK12583 410 MKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGR-SKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 247 WGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:PRK12583 489 YGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1-305 |
1.73e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 128.48 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLM-------EYYDRhftqphaqdflravceEKIRLMVSGSAALPL 72
Cdd:PRK08276 217 VMEKFDA----EEALALiERYRVTHSQLVPTMFVRMLklpeevrARYDV----------------SSLRVAIHAAAPCPV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 73 PVleKWKNIT--GHTLLERYGMTE-IGMALSGPlTTAVRLPGSVGTPLPGVqVRIVsenpqreacsytihaegDERGTKV 149
Cdd:PRK08276 277 EV--KRAMIDwwGPIIHEYYASSEgGGVTVITS-EDWLAHPGSVGKAVLGE-VRIL-----------------DEDGNEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 150 TPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHL 228
Cdd:PRK08276 336 PPG---EIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVgYLDEDGYLYLTDRKS-DMIISGGVNIYPQEIENLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 229 LAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 305
Cdd:PRK08276 412 VTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
60-300 |
2.55e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 128.08 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKW----KNITghtLLERYGMTEIGMALSGplTTAvrlPGSVGTPLPGVQVRivsenpqreacS 135
Cdd:PRK07798 298 LFAIASGGALFSPSVKEALlellPNVV---LTDSIGSSETGFGGSG--TVA---KGAVHTGGPRFTIG-----------P 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 136 YTIHAegDERGTKVTPGfEEKEGeLLVRGPSVFREYWNKPEETKSAF-TLDG--WFKTGD-TVVFKDGQYWIRGRTSVdI 211
Cdd:PRK07798 359 RTVVL--DEDGNPVEPG-SGEIG-WIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDrARVEADGTITLLGRGSV-C 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 212 IKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEI 291
Cdd:PRK07798 434 INTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEV 513
|
....*....
gi 546232251 292 PRNQMGKID 300
Cdd:PRK07798 514 QRSPAGKAD 522
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
5-301 |
3.46e-33 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 124.44 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 5 FSPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYdrhftqphaqdflraVCEEKIRLMVSGSAALPLPVLEKWKNITGH 84
Cdd:cd17633 75 FNPKSWIRKI---NQYNATVIYLVPTMLQALARTL---------------EPESKIKSIFSSGQKLFESTKKKLKNIFPK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 85 T-LLERYGMTEIGMaLSGPLTTAVRLPGSVGTPLPGVQVRIvsenpqREAcsytihaEGDERGTkvtpgfeekegeLLVR 163
Cdd:cd17633 137 AnLIEFYGTSELSF-ITYNFNQESRPPNSVGRPFPNVEIEI------RNA-------DGGEIGK------------IFVK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 164 GPSVFREYWNKPEETKsaftlDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 242
Cdd:cd17633 191 SEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDeEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 243 PDMTWGQRVTAVVTlreGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17633 265 PDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
21-304 |
5.31e-33 |
|
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: 126.02 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDRhftqphaqdflravcEEKIRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTEIG---M 97
Cdd:TIGR01923 197 RVTHISLVPTQLNRLLDEGGH---------------NENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTETCsqvT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 ALSGPLTTAvrlPGSVGTPLPGVQVRIVSENpqreacsytihaegdergtkvtpgfEEKEGELLVRGPSVFREYWNkPEE 177
Cdd:TIGR01923 261 TATPEMLHA---RPDVGRPLAGREIKIKVDN-------------------------KEGHGEIMVKGANLMKGYLY-QGE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 178 TKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVT 256
Cdd:TIGR01923 312 LTPAFEQQGWFNTGDIGELDgEGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 546232251 257 LREghSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:TIGR01923 391 SES--DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
90-301 |
7.30e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 127.23 E-value: 7.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEigmalSGPLTTAVRLP-------GSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGELLV 162
Cdd:PRK08315 348 YGMTE-----TSPVSTQTRTDdplekrvTTVGRALPHLEVKIVDP----------------ETGETVPRG---EQGELCT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 163 RGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:PRK08315 404 RGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMdEEGYVNIVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVG 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 242 VPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:PRK08315 483 VPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQK 542
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3-300 |
1.66e-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: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 3 PEFSPQQVWEkflSSETPRINVFMAVPTIYTK-LMEYYDRhftqPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNI 81
Cdd:cd05924 91 DRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLIDALRD----AGPYDL------SSLFAISSGGALLSPEVKQGLLEL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 TGH-TLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRivsenpqreacsytihaegDERGTKVTPGfEEKEGEL 160
Cdd:cd05924 158 VPNiTLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVL-------------------DDDGRVVPPG-SGGVGWI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 161 LVRGpSVFREYWNKPEETKSAF-TLDG--WFKTGD-TVVFKDGQYWIRGRTSVdIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:cd05924 218 ARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDrATVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAVYD 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:cd05924 296 VLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
21-304 |
2.71e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 125.76 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEyydrhfTQPHAQ-DFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MA 98
Cdd:PRK08751 303 RFTAFTGVNTLFNGLLN------TPGFDQiDF------SSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 99 LSGPLTTaVRLPGSVGTPLPGVQVRIvsenpqreacsytihaeGDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEET 178
Cdd:PRK08751 371 CINPLTL-KEYNGSIGLPIPSTDACI-----------------KDDAGTVLAIG---EIGELCIKGPQVMKGYWKRPEET 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 179 KSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQrVTAVVTL 257
Cdd:PRK08751 430 AKVMDADGWLHTGDIARMdEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE-IVKVVIV 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 546232251 258 REGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK08751 508 KKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
5-306 |
2.36e-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: 121.47 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 5 FSPQQVWEKFlssETPRINVFMAVPTIYTKLMeyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPL-PVLEKWKNIT- 82
Cdd:cd05973 165 FSVESTWRVI---ERLGVTNLAGSPTAYRLLM------------AAGAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAl 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 83 GHTLLERYGMTEIGMALSG--PLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGEL 160
Cdd:cd05973 230 GVPIHDHYGQTELGMVLANhhALEHPVHA-GSAGRAMPGWRVAVL-----------------DDDGDELGPG---EPGRL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 161 LV---RGPSV-FREYWNKPEETKSAftldGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 235
Cdd:cd05973 289 AIdiaNSPLMwFRGYQLPDTPAIDG----GYYLTGDTVEFDpDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVA 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 546232251 236 DVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd05973 364 EAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
47-304 |
3.24e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 122.36 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 47 HAQDFLRAVCEEKIRLMVSGsAALPLPVLEKWKNItGHTLLERYGMTEIgmalSGPLTTAVRLPGSVGTPLPGvQVRIVS 126
Cdd:PRK08162 286 NAPAEWRAGIDHPVHAMVAG-AAPPAAVIAKMEEI-GFDLTHVYGLTET----YGPATVCAWQPEWDALPLDE-RAQLKA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 127 enpqREACSYtiHAEGD------ERGTKVtPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDG 199
Cdd:PRK08162 359 ----RQGVRY--PLQEGvtvldpDTMQPV-PADGETIGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDlAVLHPDG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 200 QYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPY 279
Cdd:PRK08162 431 YIKIKDR-SKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGF 509
|
250 260
....*....|....*....|....*
gi 546232251 280 AVPSELVLvEEIPRNQMGKIDKKAL 304
Cdd:PRK08162 510 KVPKAVVF-GELPKTSTGKIQKFVL 533
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
46-304 |
1.48e-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: 119.28 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 46 PHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTE--IGMALSGPLTTAVRLPgsVGTPLPGVQVR 123
Cdd:cd17652 192 PAALAALPPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTEttVCATMAGPLPGGGVPP--IGRPVPGTRVY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 124 IVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVF 196
Cdd:cd17652 268 VL-----------------DARLRPVPPGVP---GELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARW 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 197 K-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNV 275
Cdd:cd17652 328 RaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAER 406
|
250 260
....*....|....*....|....*....
gi 546232251 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 |
1.78e-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: 120.74 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEIGMALSGPLTTAVRL-PGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPgfeEKEGELLVRG--PS 166
Cdd:cd05966 388 WWQTETGGIMITPLPGATPLkPGSATRPFFGIEPAIL-----------------DEEGNEVEG---EVEGYLVIKRpwPG 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 167 VFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 243
Cdd:cd05966 448 MARTIYGDHERYEDTYfsKFPGYYFTGDGARRdEDGYYWITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRP 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 244 DMTWGQRVTAVVTLREGHSLSHR---ELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd05966 527 HDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
13-308 |
1.90e-30 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 120.66 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 13 KFLSSETPRinVFMAVPTIYTKLMEYYDRHftqPHAQDFLRAVceekirlmVSGSAALPLPVLEKWKNITGHTLLERYGM 92
Cdd:PRK05620 266 KIIATAMPR--VAHGVPTLWIQLMVHYLKN---PPERMSLQEI--------YVGGSAVPPILIKAWEERYGVDVVHVWGM 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 93 TEigmalsgplTTAVrlpGSVGTPLPGV--QVRI---VSENPQREACSYTIHAEGdergtKVTPGFEEKEGELLVRGPSV 167
Cdd:PRK05620 333 TE---------TSPV---GTVARPPSGVsgEARWayrVSQGRFPASLEYRIVNDG-----QVMESTDRNEGEIQVRGNWV 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 168 FREYWNKP----------------EETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLA 230
Cdd:PRK05620 396 TASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVgSVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMA 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 231 HPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRH 307
Cdd:PRK05620 475 APEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQH 554
|
.
gi 546232251 308 F 308
Cdd:PRK05620 555 L 555
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1-304 |
2.24e-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: 119.94 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIY-----TKLMEYYDrhftqphaqdfLRAVCEekirlMVSGSAALPLPV 74
Cdd:cd17642 258 LMYKFEE----ELFLRSlQDYKVQSALLVPTLFaffakSTLVDKYD-----------LSNLHE-----IASGGAPLSKEV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 75 LEKWKNITGHTLLER-YGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVSENpqreacsytihaegdergTKVTPGF 153
Cdd:cd17642 318 GEAVAKRFKLPGIRQgYGLTETTSAILITPEGDDK-PGAVGKVVPFFYAKVVDLD------------------TGKTLGP 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 154 EEKeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHP 232
Cdd:cd17642 379 NER-GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELESILLQHP 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 233 SITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW-ARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17642 457 KIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYvASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
2-304 |
2.24e-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: 119.40 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 2 MPEFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLMEYYDrhfTQPHAQDF--LRAVCEekirlmvsgsAALPLPVL--E 76
Cdd:cd05929 200 MEKFDP----EEFLRLiERYRVTFAQFVPTMFVRLLKLPE---AVRNAYDLssLKRVIH----------AAAPCPPWvkE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 77 KWKNITGHTLLERYGMTE-IGM-ALSGplTTAVRLPGSVGTPLPGVqVRIVsenpqreacsytihaegDERGTKVTPGfe 154
Cdd:cd05929 263 QWIDWGGPIIWEYYGGTEgQGLtIING--EEWLTHPGSVGRAVLGK-VHIL-----------------DEDGNEVPPG-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 155 eKEGELLVRGPSVFrEYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS 233
Cdd:cd05929 321 -EIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRS-DMIISGGVNIYPQEIENALIAHPK 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 234 ITDVAVIGVPDMTWGQRVTAVVT----LREGHSLSHrELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05929 398 VLDAAVVGVPDEELGQRVHAVVQpapgADAGTALAE-ELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-306 |
5.26e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 118.88 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEIGMAlsgplTTA-----VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRG 164
Cdd:PRK07788 355 YGSTEVAFA-----TIAtpedlAEAPGTVGRPPKGVTVKIL-----------------DENGNEVPRG---VVGRIFVGN 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 165 PSVFREYWNkpeeTKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 243
Cdd:PRK07788 410 GFPFEGYTD----GRDKQIIDGLLSSGDVGYFdEDGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 244 DMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK07788 485 DEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1-304 |
9.56e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 117.96 E-value: 9.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhftqphaqdfLRAVCEEKIRLMVSGsAALPLPVLEKWKN 80
Cdd:PRK07638 214 LMRKFIPNQVLDKL---ETENISVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKN 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 81 ITGH-TLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENpqreacsytihaegderGTKVTPGfeeKEGE 159
Cdd:PRK07638 276 IFPYaKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEA-----------------GEEVQKG---EIGT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETKSaFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK07638 336 VYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVgYEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 239 VIGVPDMTWGQRVTAVVtlrEGHSLShRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07638 414 VIGVPDSYWGEKPVAII---KGSATK-QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
18-304 |
1.10e-29 |
|
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: 117.39 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMEyydrhfTQPHAQDFLRAVCeekirlmvsGSAALPlPVLEKWKNITGHTLLERYGMTEIGM 97
Cdd:cd12116 214 EAHSITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLYGPTETTI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 -ALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPE 176
Cdd:cd12116 278 wSTAARVTAAAG-PIPIGRPLANTQVYVL-----------------DAALRPVPPGVP---GELYIGGDGVAQGYLGRPA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 177 ETKSAFTLDG-------WFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTwG 248
Cdd:cd12116 337 LTAERFVPDPfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-D 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 249 QRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12116 415 RRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
61-304 |
1.56e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 117.55 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 61 RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLttAVRLPGSVGTPLPGVQVRIVsenpqreacsytiha 140
Cdd:PRK06155 295 RVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTH--GSQRPGSMGRLAPGFEARVV--------------- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 141 egDERGTKVTPGfeeKEGELLVRG--PSVFRE-YWNKPEETKSAFTlDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGG 216
Cdd:PRK06155 358 --DEHDQELPDG---EPGELLLRAdePFAFATgYFGMPEKTVEAWR-NLWFHTGDRVVRDaDGWFRFVDRIK-DAIRRRG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 217 YKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQM 296
Cdd:PRK06155 431 ENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTEN 510
|
....*...
gi 546232251 297 GKIDKKAL 304
Cdd:PRK06155 511 GKVQKFVL 518
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
60-234 |
2.30e-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: 116.39 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPLTTAVRLpGSVGTPLPGVQVRIVSENPQREacsytih 139
Cdd:cd05914 236 IKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRL-GSAGKVIDGVEVRIDSPDPATG------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 140 aegdergtkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQY-WIRGRTSVDIIKTGGYK 218
Cdd:cd05914 307 -----------------EGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKN 369
|
170
....*....|....*.
gi 546232251 219 VSALEVEWHLLAHPSI 234
Cdd:cd05914 370 IYPEEIEAKINNMPFV 385
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
24-304 |
7.31e-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: 115.12 E-value: 7.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 24 VFMAVPTiytkLMEYYDRhftQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPL 103
Cdd:cd05909 240 ILLGTPT----FLRGYAR---AAHPEDF------SSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 104 TTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaEGDErgtkvtPGFEEKEGELLVRGPSVFREYWNKPEETKSAFT 183
Cdd:cd05909 307 PQSPNKEGTVGRPLPGMEVKIVSV-------------ETHE------EVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFG 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 184 lDGWFKTGDTVVFKDGQY-WIRGRTSvDIIKTGGYKVSALEVEWHLLAH-PSITDVAVIGVPDMTWGQRVTAVVTlreGH 261
Cdd:cd05909 368 -DGWYDTGDIGKIDGEGFlTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT---TT 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 546232251 262 SLSHRELKEWARNVLAP-YAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05909 443 DTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
53-304 |
7.45e-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: 115.13 E-value: 7.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 53 RAVCEEKIRLMVsgsAALPlpvlekwknitGHTLLERYGMTE----IGMALSGPLTTAVRLPgSVGTPLPGVQVRIVsen 128
Cdd:cd17651 264 QLVLTEDLREFC---AGLP-----------GLRLHNHYGPTEthvvTALSLPGDPAAWPAPP-PIGRPIDNTRVYVL--- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 129 pqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVF-KDGQY 201
Cdd:cd17651 326 --------------DAALRPVPPG---VPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWlPDGEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 202 WIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAV 281
Cdd:cd17651 389 EFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMV 467
|
250 260
....*....|....*....|...
gi 546232251 282 PSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17651 468 PSAFVLLDALPLTPNGKLDRRAL 490
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
28-301 |
8.91e-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: 112.74 E-value: 8.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 28 VPTIYTKLMEYYdrhftqphaQDFLRAVceEKIRLMVSGSAalpLPVLEKWKNI--TGHT-LLERYGMTEIGMALSGPLT 104
Cdd:cd17635 98 VPTLLSKLVSEL---------KSANATV--PSLRLIGYGGS---RAIAADVRFIeaTGLTnTAQVYGLSETGTALCLPTD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 105 TAVRLPGSVGTPLPGVQVRIVSenpqreacsytihaegdergTKVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTl 184
Cdd:cd17635 164 DDSIEINAVGRPYPGVDVYLAA--------------------TDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 185 DGWFKTGDTV-VFKDGQYWIRGRTSVDIIKtGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSL 263
Cdd:cd17635 223 DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDE 301
|
250 260 270
....*....|....*....|....*....|....*....
gi 546232251 264 SH-RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17635 302 NAiRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1-304 |
1.04e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 115.18 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 1 MMPEFSPqqvwEKFLSS-ETPRI-NVFMaVPTIYTKLM-------EYYDrhftqphaQDFLRAVceekirlmVSGSAALP 71
Cdd:PRK12406 226 LQPRFDP----EELLQLiERHRItHMHM-VPTMFIRLLklpeevrAKYD--------VSSLRHV--------IHAAAPCP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 72 LPV----LEKWknitGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGT 147
Cdd:PRK12406 285 ADVkramIEWW----GPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFV-----------------DEDGR 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 148 KVTPGfeeKEGELLVRGPSV--FrEYWNKPEEtKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEV 224
Cdd:PRK12406 344 PLPQG---EIGEIYSRIAGNpdF-TYHNKPEK-RAEIDRGGFITSGDVgYLDADGYLFLCDRKR-DMVISGGVNIYPAEI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 225 EWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12406 418 EAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
21-308 |
1.14e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.32 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMeyydrHFTQPHAqdflrAVCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTE-IGMA 98
Cdd:PLN02574 292 KVTHFPVVPPILMALT-----KKAKGVC-----GEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEsTAVG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 99 LSGPLTTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEET 178
Cdd:PLN02574 362 TRGFNTEKLSKYSSVGLLAPNMQAKVVDW----------------STGCLLPPG---NCGELWIQGPGVMKGYLNNPKAT 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 179 KSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTL 257
Cdd:PLN02574 423 QSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVR 501
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 546232251 258 REGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:PLN02574 502 RQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
21-306 |
1.87e-28 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 114.90 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIG--- 96
Cdd:PLN02860 260 NVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEACssl 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 97 --MALSGPL---------------TTAVRLPGS--VGTPLPGVQVRIVSENPQREacsytihaegdergtkvtpgfeeke 157
Cdd:PLN02860 331 tfMTLHDPTlespkqtlqtvnqtkSSSVHQPQGvcVGKPAPHVELKIGLDESSRV------------------------- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PLN02860 386 GRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVYPEEVEAVLSQHPGVAS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNV---------------LAPYAVPSELVLVEE-IPRNQMGKId 300
Cdd:PLN02860 465 VVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAKKNLtlssetlrhhcreknLSRFKIPKLFVQWRKpFPLTTTGKI- 543
|
....*.
gi 546232251 301 KKALIR 306
Cdd:PLN02860 544 RRDEVR 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
7-304 |
2.67e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 113.30 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 7 PQQVWEKFlssETPRINVFMAVPTIYTKL--MEYYD------RHFTQPHA---QDFLRAVCEekirlmvsgsaALPlpvl 75
Cdd:cd05922 195 DDAFWEDL---REHGATGLAGVPSTYAMLtrLGFDPaklpslRYLTQAGGrlpQETIARLRE-----------LLP---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 76 ekwknitGHTLLERYGMTEIGMALSG-PLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfe 154
Cdd:cd05922 257 -------GAQVYVMYGQTEATRRMTYlPPERILEKPGSIGLAIPGGEFEIL-----------------DDDGTPTPPG-- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 155 eKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS 233
Cdd:cd05922 311 -EPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGRRD-RMIKLFGNRISPTEIEAAARSIGL 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546232251 234 ITDVAVIGVPDmTWGQRVTAVVTLREGHSLShrELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05922 389 IIEAAAVGLPD-PLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
28-307 |
3.42e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 113.70 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 28 VPTIYTKLMEYYDrhftqphaqDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAV 107
Cdd:PRK13382 291 VPVMFDRIMDLPA---------EVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 108 RLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYwnKPEETKSafTLDGW 187
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRIL-----------------DQDFREVPTG---EVGTIFVRNDTQFDGY--TSGSTKD--FHDGF 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 188 FKTGDTVVFKD-GQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHR 266
Cdd:PRK13382 418 MASGDVGYLDEnGRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPE 496
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 546232251 267 ELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRH 307
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
13-241 |
4.79e-28 |
|
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: 112.84 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 13 KFLSSETPRIN--VFMAVPTIYTKLME-YYDRHFTQPHAQDFL--RAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLL 87
Cdd:cd17640 163 RTLKDDLKRVKphYIVSVPRLWESLYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 88 ERYGMTEigmalSGPLTTAVRLP----GSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPgFEEKeGELLVR 163
Cdd:cd17640 242 NGYGLTE-----TSPVVSARRLKcnvrGSVGRPLPGTEIKIV-----------------DPEGNVVLP-PGEK-GIVWVR 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 164 GPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:cd17640 298 GPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
60-304 |
2.09e-27 |
|
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: 110.92 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTE--IGMALSGPLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacs 135
Cdd:cd17649 214 LRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEatVTPLVWKCEAGAARAGASMpiGRPLGGRSAYIL---------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 136 ytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDG-------WFKTGDTVVFK-DGQYWIRGRt 207
Cdd:cd17649 283 -------DADLNPVPVG---VTGELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGR- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 208 sVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSH--RELKEWARNVLAPYAVPSE 284
Cdd:cd17649 352 -VDhQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAH 429
|
250 260
....*....|....*....|
gi 546232251 285 LVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17649 430 LVFLARLPLTPNGKLDRKAL 449
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
92-299 |
4.77e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 111.00 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 92 MTEIGMALSGPLTTAVRL-PGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRG--PSVF 168
Cdd:PRK00174 404 QTETGGIMITPLPGATPLkPGSATRPLPGIQPAVV-----------------DEEGNPLEGG---EGGNLVIKDpwPGMM 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 169 REYWNKPEE-TKSAF-TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 245
Cdd:PRK00174 464 RTIYGDHERfVKTYFsTFKGMYFTGDGARRdEDGYYWITGRVD-DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDD 542
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 546232251 246 TWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PRK00174 543 IKGQGIYAFVTLKGGEEPSdelRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKI 599
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
73-304 |
5.83e-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: 110.48 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 73 PVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLP---GSVGTPLPGVQVRIVSENpqreacsytihaegderGTKV 149
Cdd:cd05967 370 PTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPikaGSPGKPVPGYQVQVLDED-----------------GEPV 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 150 TPGfeeKEGELLVRGP---SVFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:cd05967 433 GPN---ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKdEDGYLFIMGRTD-DVINVAGHRLSTGE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 224 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS----HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
....*
gi 546232251 300 DKKAL 304
Cdd:cd05967 589 LRRTL 593
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
33-304 |
4.29e-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: 107.41 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 33 TKLMEYYDRH------FTQPHAQ--DFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGMTEIGM-ALSG 101
Cdd:cd17655 218 QALTQYIRQNritiidLTPAHLKllDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVdASIY 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 102 PLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPEETK 179
Cdd:cd17655 298 QYEPETDQQVSVpiGKPLGNTRIYIL-----------------DQYGRPQPVGVA---GELYIGGEGVARGYLNRPELTA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 180 SAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVT 252
Cdd:cd17655 358 EKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLC 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 546232251 253 AVVTLREghSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17655 437 AYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
37-304 |
5.63e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 107.52 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 37 EYYDR-HFTQPHAQDFLRAvceekiRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTE-IGMALSGPLTTAVR---LPG 111
Cdd:PRK06164 278 EMLRRiLDTAGERADFPSA------RLFGFASFAPALGELAALARARGVPLTGLYGSSEvQALVALQPATDPVSvriEGG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 112 svGTPL-PGVQVRIVseNPQReacsytihaegderGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKT 190
Cdd:PRK06164 352 --GRPAsPEARVRAR--DPQD--------------GALLPDG---ESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRT 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 191 GD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELK 269
Cdd:PRK06164 411 GDlGYTRGDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLM 488
|
250 260 270
....*....|....*....|....*....|....*...
gi 546232251 270 EWARNVLAPYAVPSELVLVEEIPRNQMG---KIDKKAL 304
Cdd:PRK06164 489 AACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
60-304 |
7.29e-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: 106.90 E-value: 7.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNITGH-TLLERYGMTE-IGMALSGPLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacs 135
Cdd:cd12117 251 LRELLTGGEVVSPPHVRRVLAACPGlRLVNGYGPTEnTTFTTSHVVTELDEVAGSIpiGRPIANTRVYVL---------- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 136 ytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTS 208
Cdd:cd12117 321 -------DEDGRPVPPG---VPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 209 vDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGhsLSHRELKEWARNVLAPYAVPSELVLV 288
Cdd:cd12117 391 -DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA--LDAAELRAFLRERLPAYMVPAAFVVL 467
|
250
....*....|....*.
gi 546232251 289 EEIPRNQMGKIDKKAL 304
Cdd:cd12117 468 DELPLTANGKVDRRAL 483
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
8-308 |
7.53e-26 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.14 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 8 QQVWEkFLSSEtpRINVFMAVPTIYTKLMEYYDRH-FTQPHaqdflravceekIRLMVSGSAALPLPVLEKWKNItGHTL 86
Cdd:PRK06018 258 ASVYE-LLDTE--KVTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAFEDM-GVEV 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 87 LERYGMTE---IGM--ALSGPLTTavrLPGSV--------GTPLPGVQVRIVsenpqreacsytihaegDERGTKVtPGF 153
Cdd:PRK06018 322 RHAWGMTEmspLGTlaALKPPFSK---LPGDArldvlqkqGYPPFGVEMKIT-----------------DDAGKEL-PWD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 154 EEKEGELLVRGPSVFREYWnkpEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHP 232
Cdd:PRK06018 381 GKTFGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVaTIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHP 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 233 SITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 308
Cdd:PRK06018 457 KVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
18-304 |
1.15e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 106.71 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMEYydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGm 97
Cdd:PRK07008 264 EAERVTFSAGVPTVWLGLLNH-----MREAGLRF------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMS- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 alsgPLTTAVRL-------PGSV--------GTPLPGVQVRIVSEnpqreacsytihaEGDErgtkvTPGFEEKEGELLV 162
Cdd:PRK07008 332 ----PLGTLCKLkwkhsqlPLDEqrkllekqGRVIYGVDMKIVGD-------------DGRE-----LPWDGKAFGDLQV 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 163 RGPSVFREYWNKPEETksafTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:PRK07008 390 RGPWVIDRYFRGDASP----LVDGWFPTGDVATIdADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA 464
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 242 VPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07008 465 CAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
61-304 |
1.49e-25 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 105.82 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 61 RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTE--IGMALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsyti 138
Cdd:cd17646 256 RRVFCSGEALPPELAARFLALPGAELHNLYGPTEaaIDVTHWPVRGPAETPSVPIGRPVPNTRLYVL------------- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 139 haegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDgWF-------KTGDTVVFK-DGQYWIRGRTSvD 210
Cdd:cd17646 323 ----DDALRPVPVGVP---GELYLGGVQLARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-D 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 211 IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS-LSHRELKEWARNVLAPYAVPSELVLVE 289
Cdd:cd17646 394 QVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLD 473
|
250
....*....|....*
gi 546232251 290 EIPRNQMGKIDKKAL 304
Cdd:cd17646 474 ALPLTANGKLDRAAL 488
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
40-299 |
1.56e-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: 106.51 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 40 DRH-----FTQPHAQDFLRAVCEEKIR------LMVSGSAALPL---PVLEKWKNITGH--TLLERYGMTEIGMALSGPL 103
Cdd:cd17634 323 DKHgvnilYTAPTAIRALMAAGDDAIEgtdrssLRILGSVGEPInpeAYEWYWKKIGKEkcPVVDTWWQTETGGFMITPL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 104 TTAVRL-PGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRG--PSVFREYWNKPEETKS 180
Cdd:cd17634 403 PGAIELkAGSATRPVFGVQPAVV-----------------DNEGHPQPGG---TEGNLVITDpwPGQTRTLFGDHERFEQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 181 AF--TLDGWFKTGDTV-VFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTL 257
Cdd:cd17634 463 TYfsTFKGMYFSGDGArRDEDGYYWITGR-SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVL 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 546232251 258 REGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd17634 542 NHGVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
21-304 |
1.71e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 105.85 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDRhftqPHAQDFLravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMals 100
Cdd:PRK13383 264 RADAFTAVPVVLARILELPPR----VRARNPL-----PQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGI--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 101 GPLTTAVRL---PGSVGTPLPGVQVRIVSEN--PQREACSYTIHAEGDERGTKVTPGfeekegellvRGPSVfreywnkp 175
Cdd:PRK13383 332 GALATPADLrdaPETVGKPVAGCPVRILDRNnrPVGPRVTGRIFVGGELAGTRYTDG----------GGKAV-------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 176 eetksaftLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 254
Cdd:PRK13383 394 --------VDGMTSTGDMGYLDNaGRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAF 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 546232251 255 VTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK13383 465 VVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
47-304 |
2.98e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 106.16 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 47 HAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmaLSGPLTtaVRLP---------------G 111
Cdd:PRK08633 893 HPLMF------ASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATE----TSPVAS--VNLPdvlaadfkrqtgskeG 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 112 SVGTPLPGVQVRIVseNPqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFT---LDGWF 188
Cdd:PRK08633 961 SVGMPLPGVAVRIV--DP--------------ETFEELPPG---EDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWY 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 189 KTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVS--ALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS- 264
Cdd:PRK08633 1022 VTGDKgHLDEDGFLTITDRYS-RFAKIGGEMVPlgAVEEELAKALGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEEl 1100
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 546232251 265 HRELKEwarNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK08633 1101 KRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
90-304 |
1.35e-24 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 102.77 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEigmalsgpltTA----VRLPG-------SVGTPLPGVQVRIvsenpqreaCSYTIhaegdergtkvtpgfeekeG 158
Cdd:PRK07445 261 YGMTE----------TAsqiaTLKPDdflagnnSSGQVLPHAQITI---------PANQT-------------------G 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 159 ELLVRGPSVFREYWNKPEETKSAFTLD--GWFKtgdtvvfKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PRK07445 303 NITIQAQSLALGYYPQILDSQGIFETDdlGYLD-------AQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGLVQD 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGhSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07445 375 VCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
60-304 |
1.91e-24 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 103.18 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAalPLPVLEKWKNITGHTLLERYGMTEIgmalSGPLTTAV------RLPGSVGTPLPgvqvrivsenpQREA 133
Cdd:PLN03102 303 VHVLTGGSP--PPAALVKKVQRLGFQVMHAYGLTEA----TGPVLFCEwqdewnRLPENQQMELK-----------ARQG 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 134 CSYTIHAEGDERGTKV---TPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRtSV 209
Cdd:PLN03102 366 VSILGLADVDVKNKETqesVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVgVIHPDGHVEIKDR-SK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 210 DIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS----------LSHRELKEWARNVLAPY 279
Cdd:PLN03102 444 DIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPHF 523
|
250 260
....*....|....*....|....*
gi 546232251 280 AVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PLN03102 524 MCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
28-304 |
2.74e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.78 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 28 VPTIYTKLMeyYDRHFTqphaqdflrAVCEEKIRLMV-SGSAALPLPVleKWKNITGHTLLERYGMTEIGmalsgplTTA 106
Cdd:PRK05857 267 VPTLLSKLV--SELKSA---------NATVPSLRLVGyGGSRAIAADV--RFIEATGVRTAQVYGLSETG-------CTA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 107 VRLP-----------GSVGTPLPGVQVRIVSENPqreacsytihaegderGTKVTPGFEEKE--GELLVRGPSVFREYWN 173
Cdd:PRK05857 327 LCLPtddgsivkieaGAVGRPYPGVDVYLAATDG----------------IGPTAPGAGPSAsfGTLWIKSPANMLGYWN 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 174 KPEETKSAFtLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV- 251
Cdd:PRK05857 391 NPERTAEVL-IDGWVNTGDLLERReDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVg 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 252 TAVVTLREGHSLSHRELKewaRNVLAPY-------AVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK05857 469 LAVVASAELDESAARALK---HTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
83-306 |
4.00e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 102.03 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 83 GHTLLERYGMTEIGMALSGPLTTAvrlPGSVGTPLPGVqvRIVseNPQ-REACSYtihAEGDERGTKVTPgfEEKEGELL 161
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVREPGTP---PGSIGRGAPGV--AIY--NPEtLTECAV---ARFDAHGALLNA--DEAIGELV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 162 VR-GPSVFREYWNKPEETKSAFTlDGWFKTGDtVVFKDGQYWI--RGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK13388 356 NTaGAGFFEGYYNNPEATAERMR-HGMYWSGD-LAYRDADGWIyfAGRTA-DWMRVDGENLSAAPIERILLRHPAINRVA 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK13388 433 VYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
52-273 |
1.04e-23 |
|
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: 100.75 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 52 LRAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEI--GMALSGP--LTTavrlpGSVGTPLPGVQVRIVSE 127
Cdd:cd17639 244 VRAALGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETcaGGTVQDPgdLET-----GRVGPPLPCCEIKLVDW 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 128 npqreacsytihAEGDERGTKVTPgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGR 206
Cdd:cd17639 318 ------------EEGGYSTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFhPDGTLKIIDR 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 207 TSvDIIKT--GGYkvSALE-VEWHLLAHPSITDVAVIGVPDMTwgqRVTAVVTLREGHslshreLKEWAR 273
Cdd:cd17639 381 KK-DLVKLqnGEY--IALEkLESIYRSNPLVNNICVYADPDKS---YPVAIVVPNEKH------LTKLAE 438
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
143-304 |
4.62e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 98.91 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 143 DERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSA 221
Cdd:PRK10946 369 DADGNPLPQG---EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIdPDGYITVVGREK-DQINRGGEKIAA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 222 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARNV-LAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:PRK10946 445 EEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE--PLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVD 522
|
....
gi 546232251 301 KKAL 304
Cdd:PRK10946 523 KKQL 526
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
82-305 |
8.55e-23 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 98.04 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 82 TGHTLLER---------YGMTEIGMALSG-PLTTAV-----RLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERG 146
Cdd:PRK04813 276 TAKKLLERfpsatiyntYGPTEATVAVTSiEITDEMldqykRLP--IGYAKPDSPLLII-----------------DEEG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 147 TKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAF-TLDGW--FKTGDTVVFKDGQYWIRGRtsVDI-IKTGGYKVSAL 222
Cdd:PRK04813 337 TKLPDG---EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLEDGLLFYQGR--IDFqIKLNGYRIELE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 223 EVEWHLLAHPSItDVAVIgVPDMTwGQRVT---AVVTLREGH-----SLSHrELKEWARNVLAPYAVPSELVLVEEIPRN 294
Cdd:PRK04813 412 EIEQNLRQSSYV-ESAVV-VPYNK-DHKVQyliAYVVPKEEDferefELTK-AIKKELKERLMEYMIPRKFIYRDSLPLT 487
|
250
....*....|.
gi 546232251 295 QMGKIDKKALI 305
Cdd:PRK04813 488 PNGKIDRKALI 498
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
83-304 |
1.58e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 97.44 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 83 GHTLLERYGMTEIGMALSGPLTTAvrlPGSVGTPLPGVQVRivseNPQ-REACSytiHAEGDERGtkVTPGfEEKEGELL 161
Cdd:PRK07867 290 GCVVVDGFGSTEGGVAITRTPDTP---PGALGPLPPGVAIV----DPDtGTECP---PAEDADGR--LLNA-DEAIGELV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 162 -VRGPSVFREYWNKPEETkSAFTLDGWFKTGDtVVFKD--GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:PRK07867 357 nTAGPGGFEGYYNDPEAD-AERMRGGVYWSGD-LAYRDadGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVA 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK07867 434 VYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
112-304 |
1.88e-22 |
|
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: 96.62 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 112 SVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW---- 187
Cdd:cd12115 269 SIGRPLANTQAYVL-----------------DRALQPVPLGVP---GELYIGGAGVARGYLGRPGLTAERFLPDPFgpga 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 188 --FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS 264
Cdd:cd12115 329 rlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGL 407
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 546232251 265 HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12115 408 VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
60-304 |
3.74e-22 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 96.45 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAalPLPVLEKWKNITGHTLLERYGMTEIgmalSGPLTTAVRLPGSVGTPlPGVQVRIVSenpqREACSYtIH 139
Cdd:PLN02479 313 VHVMTAGAA--PPPSVLFAMSEKGFRVTHTYGLSET----YGPSTVCAWKPEWDSLP-PEEQARLNA----RQGVRY-IG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 140 AEG----DERGTKVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVV-FKDGQYWIRGRtSVDIIKT 214
Cdd:PLN02479 381 LEGldvvDTKTMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFA-NGWFHSGDLGVkHPDGYIEIKDR-SKDIIIS 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 215 GGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH-----RELKEWARNVLAPYAVPSELVLvE 289
Cdd:PLN02479 459 GGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDeaalaEDIMKFCRERLPAYWVPKSVVF-G 537
|
250
....*....|....*
gi 546232251 290 EIPRNQMGKIDKKAL 304
Cdd:PLN02479 538 PLPKTATGKIQKHVL 552
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
59-192 |
4.13e-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: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEI--GMALSGPlttAVRLPGSVGTPLPGVQVRIVSEnPQREacsY 136
Cdd:cd05927 275 NVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP---GDTSVGHVGGPLPCAEVKLVDV-PEMN---Y 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 137 tiHAEGdergtkvtpgfEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 192
Cdd:cd05927 348 --DAKD-----------PNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
18-304 |
5.30e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 95.85 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRAVCEekirlmvsgsAALPLPVLEKWKNIT--GHTLLERYGMTEI 95
Cdd:PRK13390 239 ERYRITVTQMVPTMFVRLLKLDADVRTR-YDVSSLRAVIH----------AAAPCPVDVKHAMIDwlGPIVYEYYSSTEA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 96 -GMALsgpLTTAVRL--PGSVGTPLPGvqvrivsenpqreacsyTIHAEGDErgtkvtpGFEEKEGEL----LVRGPSVF 168
Cdd:PRK13390 308 hGMTF---IDSPDWLahPGSVGRSVLG-----------------DLHICDDD-------GNELPAGRIgtvyFERDRLPF 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 169 ReYWNKPEETKSA------FtldgWFKTGDT-VVFKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:PRK13390 361 R-YLNDPEKTAAAqhpahpF----WTTVGDLgSVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVIG 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 242 VPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK13390 435 VPDPEMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
61-304 |
8.30e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 94.72 E-value: 8.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 61 RLMVSGsAALPLPVLEKWKNITGHtLLERYGMTEIG-MALSGPLTTavrlPGSVGTPLPGVQVRIVSEnpqreacsytih 139
Cdd:PRK08308 216 AVMTSG-TPLPEAWFYKLRERTTY-MMQQYGCSEAGcVSICPDMKS----HLDLGNPLPHVSVSAGSD------------ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 140 aegdergtkvtpgfEEKEGELLVRgpsvfreywnkpEETKSAFTLD-GWFKTGDTVVFkdgqywiRGRTSvDIIKTGGYK 218
Cdd:PRK08308 278 --------------ENAPEEIVVK------------MGDKEIFTKDlGYKSERGTLHF-------MGRMD-DVINVSGLN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 219 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRegHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:PRK08308 324 VYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGK 401
|
....*.
gi 546232251 299 IDKKAL 304
Cdd:PRK08308 402 VSRKLL 407
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
60-304 |
1.86e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 94.71 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVSENpqreacsyti 138
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVGQTFVSNRVDEWR-LGTLGRVLPPYEIRVVAPD---------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 139 haegderGTKVTPGFEekeGELLVRGPSVFREYWNKPEetkSAFTLDGWFKTGDTVVFkDGQYWIR-GRTSVDIIKTGGY 217
Cdd:PRK06060 331 -------GTTAGPGVE---GDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCI-DSDGWVTyRCRADDTEVIGGV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 218 KVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNV---LAPYAVPSELVLVEEIPRN 294
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLlnrLSAFKVPHRFAVVDRLPRT 476
|
250
....*....|
gi 546232251 295 QMGKIDKKAL 304
Cdd:PRK06060 477 PNGKLVRGAL 486
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
21-304 |
1.86e-21 |
|
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: 94.92 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYydrhftQPHAQDFLRavceekiRLMVSGSAaLPLPVLEKWKNITGHT-LLERYGMTE--IGm 97
Cdd:COG1020 708 RVTVLNLTPSLLRALLDA------APEALPSLR-------LVLVGGEA-LPPELVRRWRARLPGArLVNLYGPTEttVD- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 ALSGPLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKP 175
Cdd:COG1020 773 STYYEVTPPDADGGSVpiGRPIANTRVYVL-----------------DAHLQPVPVGVP---GELYIGGAGLARGYLNRP 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 176 EETKSAF-----TLDG--WFKTGD--------TVVF---KDGQYWIRG-RtsvdiIKTGgykvsalEVEWHLLAHPSITD 236
Cdd:COG1020 833 ELTAERFvadpfGFPGarLYRTGDlarwlpdgNLEFlgrADDQVKIRGfR-----IELG-------EIEAALLQHPGVRE 900
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:COG1020 901 AVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
90-225 |
1.93e-21 |
|
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: 94.27 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEI--GMALSGPLTTAVRLPG----SVGTPLPGVQVRIVSENpqreacsytihaegdergTKVTPgfEEKEGELLVR 163
Cdd:cd05906 327 FGMTETcsGVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDE------------------GQLLP--EGEVGRLQVR 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546232251 164 GPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVE 225
Cdd:cd05906 387 GPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIE 447
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
60-304 |
2.37e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 93.89 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAAL----------PLPvlekwknitGHTLLERYGMTEIGMALSGPLTTA-----VRlPGSVGTPLPGVQVRI 124
Cdd:PLN02246 300 IRMVLSGAAPLgkeledafraKLP---------NAVLGQGYGMTEAGPVLAMCLAFAkepfpVK-SGSCGTVVRNAELKI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 125 VseNPqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWI 203
Cdd:PLN02246 370 V--DP--------------ETGASLPRN---QPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIgYIDDDDELFI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 204 RGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPS 283
Cdd:PLN02246 431 VDRLK-ELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIH 509
|
250 260
....*....|....*....|.
gi 546232251 284 ELVLVEEIPRNQMGKIDKKAL 304
Cdd:PLN02246 510 KVFFVDSIPKAPSGKILRKDL 530
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
59-304 |
2.37e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 94.28 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVSGSAALPLPVLEKWKN-ITGHTLLERYGMTE---IGMALSGPLT-TAVRLPGSVGTPLPGVQVRIVseNPqrea 133
Cdd:PLN02330 304 KLQAIMTAAAPLAPELLTAFEAkFPGVQVQEAYGLTEhscITLTHGDPEKgHGIAKKNSVGFILPNLEVKFI--DP---- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 134 csytihaEGDERGTKVTPGfeekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDII 212
Cdd:PLN02330 378 -------DTGRSLPKNTPG------ELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIgYIDDDGDIFIVDRIK-ELI 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 213 KTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIP 292
Cdd:PLN02330 444 KYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIP 523
|
250
....*....|..
gi 546232251 293 RNQMGKIDKKAL 304
Cdd:PLN02330 524 KSLSGKIMRRLL 535
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
5-304 |
2.97e-21 |
|
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: 93.30 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 5 FSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravceEKIRLMVSGSAALPLpvleKWKNitgh 84
Cdd:cd17650 172 LDPAALYDLILKS---RITLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKA----QDFK---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 85 TLLER----------YGMTEIGMALSGPLTTAVRLPGS----VGTPLPGVQVRIVSE--NPQREACSytihaegdergtk 148
Cdd:cd17650 230 TLAARfgqgmriinsYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDErlQPQPVGVA------------- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 149 vtpgfeekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSA 221
Cdd:cd17650 297 ---------GELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 222 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRegHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 301
Cdd:cd17650 367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
...
gi 546232251 302 KAL 304
Cdd:cd17650 445 RAL 447
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
223-298 |
4.72e-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: 84.90 E-value: 4.72e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 223 EVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGK 298
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
68-304 |
6.13e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 92.83 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 68 AALPLPVLEKWKNIT--GHTLLERYGMTEigmalsGPLTTAVRL------PGSVGTPLPGVqVRIVsenpqreacsytih 139
Cdd:PRK13391 283 AAAPCPPQVKEQMIDwwGPIIHEYYAATE------GLGFTACDSeewlahPGTVGRAMFGD-LHIL-------------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 140 aegDERGTKVTPGfeeKEGELLVRGPSVFrEYWNKPEETKSAFTLDG-WFKTGDT-VVFKDGQYWIRGRTSVDIIkTGGY 217
Cdd:PRK13391 342 ---DDDGAELPPG---EPGTIWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIgYVDEDGYLYLTDRAAFMII-SGGV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 218 KVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRN 294
Cdd:PRK13391 414 NIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRL 493
|
250
....*....|
gi 546232251 295 QMGKIDKKAL 304
Cdd:PRK13391 494 PTGKLYKRLL 503
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
22-306 |
3.10e-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: 90.45 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 22 INVFMAVPTIYTKLmeyydrhftqpHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTEIGMALSG 101
Cdd:cd17653 190 VDALMSTPSILSTL-----------SPQDFPN------LKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 102 PLTTAVRlPGSVGTPLPGVQVRIVSENPQreacsytihaegdergtkvtPGFEEKEGELLVRGPSVFREYWNKPEETKSA 181
Cdd:cd17653 251 TELLPGQ-PVTIGKPIPNSTCYILDADLQ--------------------PVPEGVVGEICISGVQVARGYLGNPALTASK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 182 FTLDGW------FKTGDTVVF-KDGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLA-HPSITDVAVIGVpdmtwGQRVTA 253
Cdd:cd17653 310 FVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQsQPEVTQAAAIVV-----NGRLVA 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 546232251 254 VVTlreGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:cd17653 384 FVT---PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
60-309 |
4.17e-20 |
|
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: 90.29 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWknITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVqVRIVS-ENPQREAcsyti 138
Cdd:cd05918 217 LRTLVLGGEALTQSDVDTW--ADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDpDNHDRLV----- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 139 haegdERGTkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFTLD-GW------------FKTGD--------TVVF- 196
Cdd:cd05918 289 -----PIGA---------VGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDlvrynpdgSLEYv 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 197 --KDGQYWIRG-RtsVDIiktggykvsaLEVEWHLLAHPSITDVAVIGV---PDMTWGQRVTAVVTLREGHSLSH----- 265
Cdd:cd05918 355 grKDTQVKIRGqR--VEL----------GEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGdgdsl 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 266 ------------RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHFH 309
Cdd:cd05918 423 flepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
58-241 |
4.63e-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: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 58 EKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEiGMALSGPLTTAVRLPGSVGTPLPGVQVRIvsenpqreacsyt 137
Cdd:cd05932 275 DQCRLAGCGSAPVPPALLEWYRSL-GLNILEAYGMTE-NFAYSHLNYPGRDKIGTVGNAGPGVEVRI------------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 138 ihaegdergtkvtpgfeEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTG- 215
Cdd:cd05932 340 -----------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKgELDADGNLTITGRVK-DIFKTSk 401
|
170 180
....*....|....*....|....*.
gi 546232251 216 GYKVSALEVEWHLLAHPSITDVAVIG 241
Cdd:cd05932 402 GKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
21-304 |
4.23e-19 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 87.65 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 21 RINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRavceekirlmVSGSAALPL-PVLEKW-KNITGHT---LLERYGMTEI 95
Cdd:PLN02654 369 KVTIFYTAPTLVRSLMRDGDEYVTR-HSRKSLR----------VLGSVGEPInPSAWRWfFNVVGDSrcpISDTWWQTET 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 96 GMALSGPLTTA-VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTpgfEEKEGELLVRG--PSVFREYW 172
Cdd:PLN02654 438 GGFMITPLPGAwPQKPGSATFPFFGVQPVIV-----------------DEKGKEIE---GECSGYLCVKKswPGAFRTLY 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 173 NKPE--ETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ 249
Cdd:PLN02654 498 GDHEryETTYFKPFAGYYFSGDGCSRdKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQ 576
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 250 RVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PLN02654 577 GIYAFVTLVEGVPYSeelRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
22-239 |
6.45e-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: 86.17 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 22 INVFMAVPTIYtklmeyydRHFTQPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALS 100
Cdd:TIGR01733 213 VTVLNLTPSLL--------ALLAAALPPALAS------LRLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWST 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 101 GPLTTAVRLPG----SVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPE 176
Cdd:TIGR01733 279 ATLVDPDDAPRespvPIGRPLANTRLYVL-----------------DDDLRPVPVG---VVGELYIGGPGVARGYLNRPE 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546232251 177 ETKSAFTLDG--------WFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAV 239
Cdd:TIGR01733 339 LTAERFVPDPfaggdgarLYRTGDLVRYlPDGNLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
18-304 |
7.92e-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: 86.56 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYTKLMEYYDRHFTQPHAqdfLRAVceekirlMVSG---SAALPLPVLEKWKNITGHTLlerYGMTE 94
Cdd:cd12114 214 ERHGVTLWNSVPALLEMLLDVLEAAQALLPS---LRLV-------LLSGdwiPLDLPARLRALAPDARLISL---GGATE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 95 IGM-ALSGPLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREY 171
Cdd:cd12114 281 ASIwSIYHPIDEVPPDWRSIpyGRPLANQRYRVL-----------------DPRGRDCPDWVP---GELWIGGRGVALGY 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 172 WNKPEETKSAF----TLDGWFKTGDTVVFK-DGQYWIRGRtsVDI-IKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 245
Cdd:cd12114 341 LGDPELTAARFvthpDGERLYRTGDLGRYRpDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 246 TWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd12114 419 GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
58-304 |
3.19e-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: 84.79 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 58 EKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGMTEIGMALS----GPLTTAVRLPGSVGTPLPGVQVRIVSENPQr 131
Cdd:cd17644 224 SSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAATvcrlTQLTERNITSVPIGRPIANTQVYILDENLQ- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 132 eacsytihaegdergtKVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW--------FKTGDTVVF-KDGQYW 202
Cdd:cd17644 303 ----------------PVPVGVP---GELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYlPDGNIE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 203 IRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVP 282
Cdd:cd17644 364 YLGRID-NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIP 442
|
250 260
....*....|....*....|..
gi 546232251 283 SELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17644 443 SAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
83-304 |
1.03e-17 |
|
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: 82.99 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 83 GHTLLERYGMTEIG-MALSGPLTTA-VRLPgsVGTPLPGVQVRIVSEnpqreacsytihaegderGTKVTPgfEEKEGEL 160
Cdd:cd17645 234 GYKLVNNYGPTENTvVATSFEIDKPyANIP--IGKPIDNTRVYILDE------------------ALQLQP--IGVAGEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 161 LVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS 233
Cdd:cd17645 292 CIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPL 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546232251 234 ITDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17645 371 IELAAVLAKEDADGRKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3-307 |
6.36e-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: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 3 PEFSPQQVWEKFlssETPRINVFMAVPTIYtklmeyydRHFTQphaQDFLRAvcEEKIRLMVSGSAALPLPVLEKWKNIT 82
Cdd:cd05974 161 ARFDAKRVLAAL---VRYGVTTLCAPPTVW--------RMLIQ---QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAW 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 83 GHTLLERYGMTEIgMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENpqreacsytihaegdergtkvtpGFEEKEGELLV 162
Cdd:cd05974 225 GLTIRDGYGQTET-TALVGNSPGQPVKAGSMGRPLPGYRVALLDPD-----------------------GAPATEGEVAL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 163 -----RGPSVFREYWNKPEETKSAFTlDGWFKTGDtVVFK--DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 235
Cdd:cd05974 281 dlgdtRPVGLMKGYAGDPDKTAHAMR-GGYYRTGD-IAMRdeDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVA 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 236 DVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVeEIPRNQMGKIDKKALIRH 307
Cdd:cd05974 358 EAAVVPSPDPVRLSVPKAFIVLRAGYEPSPetaLEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-304 |
7.71e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.36 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 42 HFTQPHAQDFLRAVCEEKIR---LMVSGSAALPLPVLEKWKNIT-GHTLLERYGMTEIGMALS-GPLTTAVRLPGSV--G 114
Cdd:PRK12467 752 KIVPSHLQALLQASRVALPRpqrALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVStYELSDEERDFGNVpiG 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 115 TPLPGVQVRIV--SENPqreacsytihaegdergtkVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW----- 187
Cdd:PRK12467 832 QPLANLGLYILdhYLNP-------------------VPVGVV---GELYIGGAGLARGYHRRPALTAERFVPDPFgadgg 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 188 --FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS 264
Cdd:PRK12467 890 rlYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAE 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 546232251 265 HR----ELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12467 969 HQatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
46-299 |
1.08e-16 |
|
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: 80.23 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 46 PHAQDFLRAvcEEKIRLMVSGSAALPLPvLEKWKNITGHTLLERY------GMTEI-GMALSGPLTTAVRlPGSVGTPLP 118
Cdd:cd05968 345 PRGDAPVNA--HDLSSLRVLGSTGEPWN-PEPWNWLFETVGKGRNpiinysGGTEIsGGILGNVLIKPIK-PSSFNGPVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 119 GVQVRIVsenpqreacsytihaegDERGTKVTPgfeeKEGELLVRGP--SVFREYWNKPEETKSAF--TLDGWFKTGDTV 194
Cdd:cd05968 421 GMKADVL-----------------DESGKPARP----EVGELVLLAPwpGMTRGFWRDEDRYLETYwsRFDNVWVHGDFA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 195 VF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKE 270
Cdd:cd05968 480 YYdEEGYFYILGR-SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELME 558
|
250 260
....*....|....*....|....*....
gi 546232251 271 WARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:cd05968 559 RVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
47-300 |
4.35e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 78.85 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 47 HAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG--MALSGPLTTAvrlPGSVGTPLPGVQVRI 124
Cdd:PRK06814 902 HPYDFRS------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApvIALNTPMHNK---AGTVGRLLPGIEYRL 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 125 VsenpqreacsytihaegdergtKVtPGFEEKeGELLVRGPSVFREYW--NKP---EETKsaftlDGWFKTGDTVVF-KD 198
Cdd:PRK06814 973 E----------------------PV-PGIDEG-GRLFVRGPNVMLGYLraENPgvlEPPA-----DGWYDTGDIVTIdEE 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 199 GQYWIRGRTSvDIIKTGGYKVSALEVE------WHLLAHpsitdvAVIGVPDMTWGQRVtavVTLREGHSLSHRELKEWA 272
Cdd:PRK06814 1024 GFITIKGRAK-RFAKIAGEMISLAAVEelaaelWPDALH------AAVSIPDARKGERI---ILLTTASDATRAAFLAHA 1093
|
250 260
....*....|....*....|....*....
gi 546232251 273 RNVLAP-YAVPSELVLVEEIPRNQMGKID 300
Cdd:PRK06814 1094 KAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
5-291 |
5.87e-16 |
|
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: 78.23 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 5 FSPQQVWEKFLS------SETPRINVFMAvpTIYTKL-MEYYDRHF--TQPHAQDFLRAVCEEKI--------------R 61
Cdd:cd17641 250 LLPPRVWEGIAAdvrarmMDATPFKRFMF--ELGMKLgLRALDRGKrgRPVSLWLRLASWLADALlfrplrdrlgfsrlR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 62 LMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIvsenpqreacsytihae 141
Cdd:cd17641 328 SAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVD-PDTVGVPFPGTEVRI----------------- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 142 gdergtkvtpgfeEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTG-GYKV 219
Cdd:cd17641 389 -------------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAK-DVGTTSdGTRF 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546232251 220 SALEVEWHLLAHPSITDVAVIGVPDmtwgQRVTAVVTLReghslsHRELKEWARNVLAPYAVPSELVLVEEI 291
Cdd:cd17641 455 SPQFIENKLKFSPYIAEAVVLGAGR----PYLTAFICID------YAIVGKWAEQRGIAFTTYTDLASRPEV 516
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
62-299 |
7.61e-16 |
|
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: 77.66 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 62 LMVSGSAALPLPVLEkwknitghtLLERYGMTEIGMALSGPLTTAVRLPgSVGTPLPGVQVRIVSENPQREAcsytihAE 141
Cdd:cd05931 316 LFVSGGPPGTGPVVL---------RVDRDALAGRAVAVAADDPAARELV-SCGRPLPDQEVRIVDPETGREL------PD 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 142 GDErgtkvtpgfeekeGELLVRGPSVFREYWNKPEETKSAFTL------DGWFKTGDTVVFKDGQYWIRGRTSvDIIKTG 215
Cdd:cd05931 380 GEV-------------GEIWVRGPSVASGYWGRPEATAETFGAlaatdeGGWLRTGDLGFLHDGELYITGRLK-DLIIVR 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 216 GYKVSALEVEWHL-LAHPSI--TDVAVIGVPDmtwGQRVTAVVTLREGHSLSHRELKEWARNVLApyAV-------PSEL 285
Cdd:cd05931 446 GRNHYPQDIEATAeEAHPALrpGCVAAFSVPD---DGEERLVVVAEVERGADPADLAAIAAAIRA--AVarehgvaPADV 520
|
250
....*....|....*.
gi 546232251 286 VLVE--EIPRNQMGKI 299
Cdd:cd05931 521 VLVRpgSIPRTSSGKI 536
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
24-241 |
9.13e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.78 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 24 VFMAVPTIYTKLMEYYDRhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWK----NITGH--TLLERYGMTEigm 97
Cdd:PRK12582 319 VYGNVPAGYAMLAEAMEK-------DDALRRSFFKNLRLMAYGGATLSDDLYERMQalavRTTGHriPFYTGYGATE--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 alSGPLTTAV----RLPGSVGTPLPGVQVRIVsenPQreacsytihaegderGTKVtpgfeekegELLVRGPSVFREYWN 173
Cdd:PRK12582 389 --TAPTTTGThwdtERVGLIGLPLPGVELKLA---PV---------------GDKY---------EVRVKGPNVTPGYHK 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 174 KPEETKSAFTLDGWFKTGDTVVFKDGQYWIR-----GRTSVDIIKTGGYKVSALEVEWHLLA--HPSITDVAVIG 241
Cdd:PRK12582 440 DPELTAAAFDEEGFYRLGDAARFVDPDDPEKglifdGRVAEDFKLSTGTWVSVGTLRPDAVAacSPVIHDAVVAG 514
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
53-206 |
4.47e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 75.78 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 53 RAVCEEKIRLMVSGSAALPLPVLEkWKNITGHTLLERYGMTEI----GMALSGPLTtavrlPGSVGTPLPGVQVRIVsen 128
Cdd:PTZ00216 423 RAVLGGRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTETvccgGIQRTGDLE-----PNAVGQLLKGVEMKLL--- 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 129 pqreacsytihaEGDERGTKVTPgfeEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGR 206
Cdd:PTZ00216 494 ------------DTEEYKHTDTP---EPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIaANGTLRIIGR 557
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
59-192 |
5.39e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 75.14 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGpLTTAVRLPGSVGTPLPGVQVRIVSEnPQREacsYTI 138
Cdd:PLN02736 377 RVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG-MDEGDNLSGHVGSPNPACEVKLVDV-PEMN---YTS 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 546232251 139 HAEGDERGtkvtpgfeekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 192
Cdd:PLN02736 452 EDQPYPRG------------EICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
73-304 |
1.25e-14 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 73.97 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 73 PVLEKWKNITGHTLLERYGMTEIGM-ALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREACSYTihaegdergtkvtp 151
Cdd:cd17648 222 PVFEKLRSRFAGLIINAYGPTETTVtNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV-------------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 152 gfeekeGELLVRGPSVFREYWNKPEETKSAF----------TLDG----WFKTGDTVVFK-DGQYWIRGRTSVDIiKTGG 216
Cdd:cd17648 288 ------GELYLGGDGVARGYLNRPELTAERFlpnpfqteqeRARGrnarLYKTGDLVRWLpSGELEYLGRNDFQV-KIRG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 217 YKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ--RVTAVV---TLREGHsLSHRELKEWARNVLAPYAVPSELVLVEEI 291
Cdd:cd17648 361 QRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVgyyLPEPGH-VPESDLLSFLRAKLPRYMVPARLVRLEGI 439
|
250
....*....|...
gi 546232251 292 PRNQMGKIDKKAL 304
Cdd:cd17648 440 PVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-306 |
1.54e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.61 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWknITGHTLLERYGMTEIGM-ALSGPLTTAVRLPGSVGTPLPGVQVRIVSENpqreacsyti 138
Cdd:PRK12316 3313 LKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATItVTHWQCVEEGKDAVPIGRPIANRACYILDGS---------- 3380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 139 haegdergtkVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSVDI 211
Cdd:PRK12316 3381 ----------LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQV 3450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 212 iKTGGYKVSALEVEWHLLAHPSITDVAVIGVPdmtwGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEI 291
Cdd:PRK12316 3451 -KIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERM 3525
|
250
....*....|....*
gi 546232251 292 PRNQMGKIDKKALIR 306
Cdd:PRK12316 3526 PLTPNGKLDRKALPR 3540
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
29-277 |
1.79e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 73.76 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 29 PTIYtklmeyydrhFTQPHAQDFLRAVCEE----------KIRLMVSGSAALPLPVLEKWKNITGHTLLER------YGM 92
Cdd:PRK08180 305 PTVY----------FNVPKGWEMLVPALERdaalrrrffsRLKLLFYAGAALSQDVWDRLDRVAEATCGERirmmtgLGM 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 93 TEigmalSGPLTT-----AVRlPGSVGTPLPGVQVRIVsenPQreacsytihaegderGTKVtpgfeekegELLVRGPSV 167
Cdd:PRK08180 375 TE-----TAPSATfttgpLSR-AGNIGLPAPGCEVKLV---PV---------------GGKL---------EVRVKGPNV 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 168 FREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIR-----GRTSVDIIKTGGYKVSALEVEWHLLAH--PSITDVAVI 240
Cdd:PRK08180 422 TPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPADPERglmfdGRIAEDFKLSSGTWVSVGPLRARAVSAgaPLVQDVVIT 501
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 546232251 241 G----------VPDMTWGQRVTAvvtLREGHS----LSHRELKEWARNVLA 277
Cdd:PRK08180 502 GhdrdeigllvFPNLDACRRLAG---LLADASlaevLAHPAVRAAFRERLA 549
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
160-304 |
2.30e-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: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 160 LLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVA 238
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIaVWDEEGYVEIKDR-LKDLIKSGGEWISSVDLENALMGHPKVKEAA 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 239 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd05915 442 VVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-306 |
2.90e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 45 QPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEK-WKNITGHTLLERYGMTEigmALSGPLTTAVRLPGSVGTPLPGVQVR 123
Cdd:PRK12316 2248 QQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTE---AVVTPLLWKCRPQDPCGAAYVPIGRA 2324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 124 IvsenpqreacsytihaeGDERGTKVTPGFE----EKEGELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGD 192
Cdd:PRK12316 2325 L-----------------GNRRAYILDADLNllapGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGD 2387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 193 TVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELKE 270
Cdd:PRK12316 2388 LARYRaDGVVEYLGR--IDhQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRA 2464
|
250 260 270
....*....|....*....|....*....|....*.
gi 546232251 271 WARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 306
Cdd:PRK12316 2465 WLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
42-304 |
1.12e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 42 HFTQPHAQDF----LRAVCEeKIRLMVSGSAALPLP----VLEKWKNITGHTlleRYGMTEIGMALSG---PLTTAVRLP 110
Cdd:PRK05691 1369 HFVPPLLQLFidepLAAACT-SLRRLFSGGEALPAElrnrVLQRLPQVQLHN---RYGPTETAINVTHwqcQAEDGERSP 1444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 111 gsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW--- 187
Cdd:PRK05691 1445 --IGRPLGNVLCRVL-----------------DAELNLLPPGVA---GELCIGGAGLARGYLGRPALTAERFVPDPLged 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 188 ----FKTGDTVVFK-DGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLAHPSITDVAVIgVPDMTWGQRVTAVVTLREGHS 262
Cdd:PRK05691 1503 garlYRTGDRARWNaDGALEYLGRLDQQV-KLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQE 1580
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 546232251 263 LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK05691 1581 AEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
155-304 |
1.50e-13 |
|
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: 70.54 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 155 EKEGELLVRGP----SVFREYWNKPEETKSAFTL------DGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALE 223
Cdd:cd05937 297 GEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQdADGRWYFLDRLG-DTFRWKSENVSTTE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 224 VEWHLLAHPSITDVAVIGV--PDMTwGQRVTAVVTLREGHS----LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMG 297
Cdd:cd05937 376 VADVLGAHPDIAEANVYGVkvPGHD-GRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNH 454
|
....*..
gi 546232251 298 KIDKKAL 304
Cdd:cd05937 455 KQQKGVL 461
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-304 |
2.06e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 10 VWEKFLSSETPRiNVFMAVPTIYT---KLMEYYDR------HFTQPHAQDFLR----AVCEEkIRLMVSGSAALPLPVLE 76
Cdd:PRK12316 711 VWEFFWPLMSGA-RLVVAAPGDHRdpaKLVELINRegvdtlHFVPSMLQAFLQdedvASCTS-LRRIVCSGEALPADAQE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 77 K--WKNITGHtLLERYGMTEIGMALSgpLTTAVRLPG---SVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTP 151
Cdd:PRK12316 789 QvfAKLPQAG-LYNLYGPTEAAIDVT--HWTCVEEGGdsvPIGRPIANLACYIL-----------------DANLEPVPV 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 152 GFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEV 224
Cdd:PRK12316 849 GVL---GELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEI 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 225 EWHLLAHPSITDVAVIGVPdmtwGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12316 925 EARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-304 |
2.91e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.37 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 45 QPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEK-WKNITGHTLLERYGMTEIGM------ALSGPLTTAVRLPgsVGTPL 117
Cdd:PRK12316 4796 QQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVtvllwkARDGDACGAAYMP--IGTPL 4873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 118 PGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKT 190
Cdd:PRK12316 4874 GNRSGYVL-----------------DGQLNPLPVG---VAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRT 4933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 191 GDTVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV-------TAVVTLREGH 261
Cdd:PRK12316 4934 GDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVgyvvpqdPALADADEAQ 5011
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 546232251 262 SLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12316 5012 AELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
85-298 |
2.96e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 70.03 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 85 TLLERYGMTEIGMALSGPLTTAVRlpgsVGTPLPGVQVRIVSENPQreacsytihaegdergtkVTPgfEEKEGELLVRG 164
Cdd:PRK09192 363 DRLEYQGKAVAPGAETRRVRTFVN----CGKALPGHEIEIRNEAGM------------------PLP--ERVVGHICVRG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 165 PSVFREYWNKpEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT--DVAVIGV 242
Cdd:PRK09192 419 PSLMSGYFRD-EESQDVLAADGWLDTGDLGYLLDGYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSI 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 546232251 243 PDMTwGQRVTAVVTLREGHSLSHRELK-EWARNVLAPYAVPSELVLV--EEIPRNQMGK 298
Cdd:PRK09192 497 AQEN-GEKIVLLVQCRISDEERRGQLIhALAALVRSEFGVEAAVELVppHSLPRTSSGK 554
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
158-304 |
5.01e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.80 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHL 228
Cdd:PRK12467 3436 GELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARL 3513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 229 LAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLShRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK12467 3514 LQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWR-ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
158-304 |
8.07e-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: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLA 230
Cdd:cd17656 328 GELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLN 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 231 HPSITDVAVIGVPDMTWGQRVTA-VVTLREghsLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 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 |
4.24e-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: 66.30 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 24 VFMAVPTIYTKLMEYYDRhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNI----TGH--TLLERYGMTEigm 97
Cdd:cd05921 263 VYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALavatVGEriPMMAGLGATE--- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 98 alSGPLTTAVRLP----GSVGTPLPGVQVRIVSEnpqreacsytihaegderGTKVtpgfeekegELLVRGPSVFREYWN 173
Cdd:cd05921 333 --TAPTATFTHWPtersGLIGLPAPGTELKLVPS------------------GGKY---------EVRVKGPNVTPGYWR 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 174 KPEETKSAFTLDGWFKTGDTVVFKD------GQYWiRGRTSVDIIKTGGYKVS--ALEVEWHLLAHPSITDVAVIG---- 241
Cdd:cd05921 384 QPELTAQAFDEEGFYCLGDAAKLADpddpakGLVF-DGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGedra 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 546232251 242 ------VPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLA 277
Cdd:cd05921 463 evgalvFPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLA 504
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
90-285 |
4.26e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 66.43 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEigMAlSgplT-TAVR---LPGsVGTPLPGVQVRIVsenpqreacsytihaegdergtkvtpgfeekEGELLVRGP 165
Cdd:PRK09029 271 YGLTE--MA-S---TvCAKRadgLAG-VGSPLPGREVKLV-------------------------------DGEIWLRGA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 166 SVFREYWNKPEETksafTL---DGWFKTGDTVVFKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITDVAVIGV 242
Cdd:PRK09029 313 SLALGYWRQGQLV----PLvndEGWFATRDRGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQHPLVQQVFVVPV 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 546232251 243 PDMTWGQRVTAVVtlrEGHSLSHRE-LKEWARNVLA----P---YAVPSEL 285
Cdd:PRK09029 388 ADAEFGQRPVAVV---ESDSEAAVVnLAEWLQDKLArfqqPvayYLLPPEL 435
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
60-273 |
5.29e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.08 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNITGHT--LLERYGMTE------IGM--ALSGplTTAVRLPGS---VGTPLPGVQVRI-- 124
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAMLPPDaeILTPYGATEalpissIESreILFA--TRAATDNGAgicVGRPVDGVEVRIia 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 125 VSENPqreacsytIHAEGDERgtKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFKD-G 199
Cdd:PRK09274 368 ISDAP--------IPEWDDAL--RLATG---EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqG 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 200 QYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTwGQRVTAVVTLREGHSLS----HRELKEWAR 273
Cdd:PRK09274 435 RLWFCGRKA-HRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSksalYQELRALAA 510
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
158-304 |
7.98e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.35 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTV-VFKDGQYWIRGRtsVD-IIKTGGYKVSALEVEWHL 228
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLArRRSDGVLEYVGR--IDhQVKIRGYRIELGEIEARL 4144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 229 LAHPSITDVAViGVPDMTWGQRVTAVVTLREGhSLSHREL----KEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK05691 4145 HEQAEVREAAV-AVQEGVNGKHLVGYLVPHQT-VLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
59-192 |
2.12e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 64.48 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmALSGPLTTAVR---LPGSVGTPLPGVQVRIVSenpqreacs 135
Cdd:PLN02861 384 RVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTE---SCGGCFTSIANvfsMVGTVGVPMTTIEARLES--------- 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 546232251 136 ytIHAEGDERGTKVtpgfeeKEGELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGD 192
Cdd:PLN02861 452 --VPEMGYDALSDV------PRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGD 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
158-304 |
3.41e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRTSVDIiKTGGYKVSALEVEWHLL 229
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQV-KIRGFRIELGEIESRLL 2611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 230 AHPSITDVAVIGVpDMTWGQR-----VTAVVTLREGHSLSHRE-LKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKA 303
Cdd:PRK05691 2612 EHPAVREAVVLAL-DTPSGKQlagylVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRA 2690
|
.
gi 546232251 304 L 304
Cdd:PRK05691 2691 L 2691
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
52-290 |
4.19e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 63.60 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 52 LRAVCEEKIRLMVSGSAALPlPVLEKWKNIT-GHTLLERYGMTEI--GMALSGPLTTAVrlpGSVGTPLPgvqvrivsen 128
Cdd:PLN02387 414 IRAVLGGRIRFMLSGGAPLS-GDTQRFINIClGAPIGQGYGLTETcaGATFSEWDDTSV---GRVGPPLP---------- 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 129 pqreaCSYTIHAEGDERGTKVT----PgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFK-DG 199
Cdd:PLN02387 480 -----CCYVKLVSWEEGGYLISdkpmP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHpDG 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 200 QYWIRGRTSvDIIKT--GGYkVSALEVEWHLLAHPSITDVAVIGVPDMTWGqrVTAVVTlreghslSHRELKEWARNVLA 277
Cdd:PLN02387 550 CLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSVSPYVDNIMVHADPFHSYC--VALVVP-------SQQALEKWAKKAGI 618
|
250
....*....|...
gi 546232251 278 PYAVPSELVLVEE 290
Cdd:PLN02387 619 DYSNFAELCEKEE 631
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-279 |
6.11e-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: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNITGHT--LLERYGMTE---IGMALSGPLTTAVRLPGS------VGTPLPGVQVRIVsen 128
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLSDEaeILTPYGATEalpVSSIGSRELLATTTAATSggagtcVGRPIPGVRVRII--- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 129 pqrEACSYTIHAEGDERgtKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFKD-GQYWI 203
Cdd:cd05910 278 ---EIDDEPIAEWDDTL--ELPRG---EIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWF 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 204 RGRTSVDIIKTGGyKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPY 279
Cdd:cd05910 350 CGRKAHRVITTGG-TLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
86-225 |
1.24e-10 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 61.99 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 86 LLERYGMTEIgmalSGPLTT----AVRLpGSVGTPLPGVQVRIVSENpqreacsytihAEGDergtkvtpgfeekeGELL 161
Cdd:cd05933 347 IMELYGMSET----SGPHTIsnpqAYRL-LSCGKALPGCKTKIHNPD-----------ADGI--------------GEIC 396
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546232251 162 VRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSVDIIKTGGYKVSALEVE 225
Cdd:cd05933 397 FWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLgKLDEDGFLYITGRIKELIITAGGENVPPVPIE 461
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
110-304 |
1.27e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 61.89 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 110 PGSVGTPLPGVQVRIVSENPqreacsytihaegderGTKVTPGfeEKeGELLVRGP-------SVFRE-------YWnkp 175
Cdd:PRK10524 410 LGSPGVPMYGYNVKLLNEVT----------------GEPCGPN--EK-GVLVIEGPlppgcmqTVWGDddrfvktYW--- 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 176 eetkSAF------TLDgWfktgdTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ 249
Cdd:PRK10524 468 ----SLFgrqvysTFD-W-----GIRDADGYYFILGRTD-DVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQ 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546232251 250 RVTAVVTLREGHSLSHREL-----KEWARNV---LAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK10524 537 VAVAFVVPKDSDSLADREArlaleKEIMALVdsqLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
112-244 |
2.75e-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: 60.97 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 112 SVGTPLPGVQVRIVSENPQREACSYTIHAEgdERGTKVTPGfeekegellvrgpsvfreYWNKPEETKSAFTLDGWFKTG 191
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQ--IRGKNVTPG------------------YYNNPEATAKVFTDDGWLKTG 374
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 192 DTVVFKDGQYWIRGRTSvDIIKTGGYKV-------SALEVEWHLLAHpsitdVAVIGVPD 244
Cdd:cd05908 375 DLGFIRNGRLVITGREK-DIIFVNGQNVyphdierIAEELEGVELGR-----VVACGVNN 428
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
43-304 |
7.21e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 60.06 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 43 FTQPHAQDFLRAVCEEKIRLMVSGSAaLPLPVLEKWKNITGHTLLERYGMTEIGMALS-----GPLTTAVR-LPGSVGTP 116
Cdd:PRK10252 703 FVASLTPEGARQSCASLRQVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVDVSwypafGEELAAVRgSSVPIGYP 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 117 LPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW------FKT 190
Cdd:PRK10252 782 VWNTGLRIL-----------------DARMRPVPPGVA---GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRT 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 191 GDTVVFK-DGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVA----VIGVPDMTWG--QRVTAVVTLREGHSL 263
Cdd:PRK10252 842 GDVARWLdDGAVEYLGR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGdaRQLVGYLVSQSGLPL 920
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 546232251 264 SHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PRK10252 921 DTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
18-304 |
8.52e-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: 59.41 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 18 ETPRINVFMAVPTIYtklmeyydRHFTQPHAQDFLRAVcEEKIRLMVSGSAALP-LPVLEKWKNITGHT-LLERYGMTEI 95
Cdd:cd17654 207 KRHRITVLQATPTLF--------RRFGSQSIKSTVLSA-TSSLRVLALGGEPFPsLVILSSWRGKGNRTrIFNIYGITEV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 96 GMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQreacsytihaegdergtkvtpgfeEKEGELLVRGPS---VFREYW 172
Cdd:cd17654 278 SCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGS------------------------EGTGQVFLGGLNrvcILDDEV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 173 NKPEETksaftldgWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVigvpdmTW--GQR 250
Cdd:cd17654 334 TVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV------TLsdQQR 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 546232251 251 VTAVVTLREGHSLSHRELKewaRNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17654 399 LIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| 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 546232251 158 GELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV-VFKDG 199
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVqINKNG 584
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
90-299 |
3.17e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 57.83 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEIGMA-------LSGPLTTavrlpgsVGTPLPGVQVRIVSEnpqreacsytihaEGDERGtkvtpgfEEKEGEL-- 160
Cdd:PTZ00237 412 YGQTEIGITylycyghINIPYNA-------TGVPSIFIKPSILSE-------------DGKELN-------VNEIGEVaf 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 161 -LVRGPSVFREYWNKPEETKSAFT-LDGWFKTGDtVVFKD--GQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITD 236
Cdd:PTZ00237 465 kLPMPPSFATTFYKNDEKFKQLFSkFPGYYNSGD-LGFKDenGYYTIVSR-SDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 237 VAVIGVPDMTWGQRVTAVVTLREGHSLSH-------RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 299
Cdd:PTZ00237 543 CCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnklkNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
39-300 |
5.63e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 57.03 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 39 YDRhFTQPHaqDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLP 118
Cdd:PRK08043 469 YAR-FANPY--DFAR------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAK-PGTVGRILP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 119 GVQVRIVSenpqreacsytihaegdergtkvTPGFEEKeGELLVRGPSVFREYW--NKPE--ETKSAFTLDG-----WFK 189
Cdd:PRK08043 539 GMDARLLS-----------------------VPGIEQG-GRLQLKGPNIMNGYLrvEKPGvlEVPTAENARGemergWYD 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 190 TGDTVVFKDGQY-WIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQrvtAVVTLREGHSLSHREL 268
Cdd:PRK08043 595 TGDIVRFDEQGFvQIQGRAK-RFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELTREKL 670
|
250 260 270
....*....|....*....|....*....|...
gi 546232251 269 KEWARNVLAP-YAVPSELVLVEEIPRNQMGKID 300
Cdd:PRK08043 671 QQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
60-192 |
1.21e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 56.18 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 60 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSEnPQREAcsytih 139
Cdd:PLN02614 388 VRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESV-PEMEY------ 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 546232251 140 aegDERGTkvTPgfeekEGELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGD 192
Cdd:PLN02614 461 ---DALAS--TP-----RGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGD 502
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
12-192 |
2.24e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 52.12 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 12 EKFLSSETP-RINVFMAvptIYTKLMEYYDRHFTQPHAQ---DFL-----RAVCEEKIRLMVSGSAALPLPVLEKWKNIT 82
Cdd:PLN02430 331 QKALQELNPrRRLIFNA---LYKYKLAWMNRGYSHKKASpmaDFLafrkvKAKLGGRLRLLISGGAPLSTEIEEFLRVTS 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 83 GHTLLERYGMTEIgmalSGPLTTA----VRLPGSVGTPLPGVQVRIvSENPQREacsytihaegdergtkVTPGFEEKEG 158
Cdd:PLN02430 408 CAFVVQGYGLTET----LGPTTLGfpdeMCMLGTVGAPAVYNELRL-EEVPEMG----------------YDPLGEPPRG 466
|
170 180 190
....*....|....*....|....*....|....
gi 546232251 159 ELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD 192
Cdd:PLN02430 467 EICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGD 499
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
59-291 |
4.71e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.03 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 59 KIRLMVsGSAALPlPVLEKWKNITG-HTLLERYGMTE--IGmalsgpLTTAVRLPGSVG-TPLPGV-QVRIV-----SEN 128
Cdd:PRK08279 315 RLRLMI-GNGLRP-DIWDEFQQRFGiPRILEFYAASEgnVG------FINVFNFDGTVGrVPLWLAhPYAIVkydvdTGE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 129 PQREAcsytihaegDERGTKVTPGfeekE-GELLVR-GPSVFREYWNKPEETKS-----AFTL-DGWFKTGDtVVFKDGQ 200
Cdd:PRK08279 387 PVRDA---------DGRCIKVKPG----EvGLLIGRiTDRGPFDGYTDPEASEKkilrdVFKKgDAWFNTGD-LMRDDGF 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 201 YWIRgrtSVDII------KtgGYKVSALEVEWHLLAHPSITDVAVIGV--PDMTwGQRVTAVVTLREGHSLSHRELKEWA 272
Cdd:PRK08279 453 GHAQ---FVDRLgdtfrwK--GENVATTEVENALSGFPGVEEAVVYGVevPGTD-GRAGMAAIVLADGAEFDLAALAAHL 526
|
250
....*....|....*....
gi 546232251 273 RNVLAPYAVPSELVLVEEI 291
Cdd:PRK08279 527 YERLPAYAVPLFVRLVPEL 545
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
143-299 |
1.44e-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: 49.58 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 143 DERGTKVTpgfEEKeGELLVRG--PSVFREYWNKPEETK--SAF--TLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTG 215
Cdd:cd05943 439 DEEGKPVW---GEK-GELVCTKpfPSMPVGFWNDPDGSRyrAAYfaKYPGVWAHGDWIEItPRGGVVILGR-SDGTLNPG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 216 GYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIP 292
Cdd:cd05943 514 GVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDIP 593
|
....*..
gi 546232251 293 RNQMGKI 299
Cdd:cd05943 594 RTLSGKK 600
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-206 |
1.64e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.78 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 112 SVGTPLPGVQVRIVseNPQreacsyTIHAEGDERgtkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFT-LDG--WF 188
Cdd:PRK05691 371 SCGRSQPGHAVLIV--DPQ------SLEVLGDNR-----------VGEIWASGPSIAHGYWRNPEASAKTFVeHDGrtWL 431
|
90
....*....|....*...
gi 546232251 189 KTGDTVVFKDGQYWIRGR 206
Cdd:PRK05691 432 RTGDLGFLRDGELFVTGR 449
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
56-223 |
2.11e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.04 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 56 CEEKIRLMVSGSAALPLPVLEKWKNITGH-TLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSEnpqreac 134
Cdd:PRK06334 297 CLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSE------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 135 sytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKpEETKSAFTLDG--WFKTGDT-VVFKDGQYWIRGRTSvDI 211
Cdd:PRK06334 370 ---------ETKVPVSSG---ETGLVLTRGTSLFSGYLGE-DFGQGFVELGGetWYVTGDLgYVDRHGELFLKGRLS-RF 435
|
170
....*....|....
gi 546232251 212 IKTGGYKVS--ALE 223
Cdd:PRK06334 436 VKIGAEMVSleALE 449
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
158-304 |
2.51e-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: 48.67 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFKD-------GQYWIRGRTSV--------------------- 209
Cdd:cd17647 316 GEIYVRAGGLAEGYRGLPELNKEKF-VNNWFVEPDHWNYLDkdnnepwRQFWLGPRDRLyrtgdlgrylpngdceccgra 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 210 -DIIKTGGYKVSALEVEWHLLAHPSI---------------TDVAVIgVPDM----TWGQRVTA----------VVTLRE 259
Cdd:cd17647 395 dDQVKIRGFRIELGEIDTHISQHPLVrenitlvrrdkdeepTLVSYI-VPRFdkpdDESFAQEDvpkevstdpiVKGLIG 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 546232251 260 GHSLSHrELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:cd17647 474 YRKLIK-DIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
106-206 |
7.22e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 106 AVRLPGSVGTPLPGVQ------VRIVSENPQREACSYTIhaegdergtkvtpgfeekeGELLVRGPSVFREYWNKPEETK 179
Cdd:PRK05850 359 AKRCETGGGTPLVSYGsprsptVRIVDPDTCIECPAGTV-------------------GEIWVHGDNVAAGYWQKPEETE 419
|
90 100 110
....*....|....*....|....*....|....*...
gi 546232251 180 SAF----------TLDG-WFKTGDTVVFKDGQYWIRGR 206
Cdd:PRK05850 420 RTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGR 457
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
158-206 |
8.33e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 47.03 E-value: 8.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546232251 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 |
9.13e-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: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 85 TLLERYGMTE--IGmalsgpLTTAVRLPGSVG---------TPLPGVQVRIVSENPQREACSYTIhaegdergtKVTPGf 153
Cdd:cd05940 222 RIAEFYAATEgnSG------FINFFGKPGAIGrnpsllrkvAPLALVKYDLESGEPIRDAEGRCI---------KVPRG- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 154 eeKEGELLVR--GPSVFREYWNKPEETKSAFTL-----DGWFKTGDTVVFKDGQYW-IRGRTSvDIIKTGGYKVSALEVE 225
Cdd:cd05940 286 --EPGLLISRinPLEPFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWyFVDRLG-DTFRWKGENVSTTEVA 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546232251 226 WHLLAHPSITDVAVIGV--PDmTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEI 291
Cdd:cd05940 363 AVLGAFPGVEEANVYGVqvPG-TDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEM 429
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-282 |
4.69e-05 |
|
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: 44.59 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 87 LERYGMTEIGMALsgplTTAVRLPGSVG---------TPLPGVQVRIVSENPQREACSYTIHAEGDERGTKVTPgfeeke 157
Cdd:cd05938 286 REFYGSTEGNIGF----FNYTGKIGAVGrvsylykllFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAK------ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 gellVRGPSVFREYWNKPEETKSAF------TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLA 230
Cdd:cd05938 356 ----ITQQSPFLGYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQdQQNFLYFHDRVG-DTFRWKGENVATTEVADVLGL 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 546232251 231 HPSITDVAVIGVPDMTWGQRV-TAVVTLREGHSLSHRELKEWARNVLAPYAVP 282
Cdd:cd05938 431 LDFLQEVNVYGVTVPGHEGRIgMAAVKLKPGHEFDGKKLYQHVREYLPAYARP 483
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
158-292 |
4.94e-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: 44.75 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 158 GELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV--VFKDGQYWIRGRTSVDIIKTGGY-KVSALEVEWhlLAHPSI 234
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMaeLGPDRLVYVDRRNNVLKLSQGEFvTVARLEAVF--AASPLV 513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 235 TDVAVIG-----------VPdmtwGQRVTAVVTLREGHSLSHRELKEWAR-NVLAPYAVPSElVLVEEIP 292
Cdd:cd17632 514 RQIFVYGnserayllavvVP----TQDALAGEDTARLRAALAESLQRIAReAGLQSYEIPRD-FLIETEP 578
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
158-206 |
7.18e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.35 E-value: 7.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546232251 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 |
9.62e-05 |
|
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: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 169 REYWNKPEetksaftlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI------------- 234
Cdd:TIGR03443 669 REFWLGPR--------DRLYRTGDLGRYlPDGNVECCGRAD-DQVKIRGFRIELGEIDTHLSQHPLVrenvtlvrrdkde 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 235 --TDVAVIgVPDMTWGQRVTA------------VVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 300
Cdd:TIGR03443 740 epTLVSYI-VPQDKSDELEEFksevddeessdpVVKGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVD 818
|
....
gi 546232251 301 KKAL 304
Cdd:TIGR03443 819 KPAL 822
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
112-225 |
1.37e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 43.45 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 112 SVGTPLPGVQVRIVSENPQREacsytihaegDERGTkvtpgfeekeGELLVRGPSVFREYWNkPEETKSAFTLDGWFKTG 191
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVL----------PPRGV----------GVIELRGESVTPGYLT-MDGFIPAQDADGWLDTG 419
|
90 100 110
....*....|....*....|....*....|....*
gi 546232251 192 DTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVE 225
Cdd:PRK07768 420 DLGYLTEeGEVVVCGRVK-DVIIMAGRNIYPTDIE 453
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
90-225 |
3.32e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.06 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 90 YGMTEIGMALSGPL--------------TTAVRLPGSVGTPLPGVQVRIvsenpqreacsytihAEGDERGTKVTPGFee 155
Cdd:PRK05851 310 YGLAESTCAVTVPVpgiglrvdevttddGSGARRHAVLGNPIPGMEVRI---------------SPGDGAAGVAGREI-- 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 156 keGELLVRGPSVFREYWNKPeetksAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVE 225
Cdd:PRK05851 373 --GEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIE 434
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
191-304 |
3.94e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 38.64 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546232251 191 GDTVVFKDGQYWIRGRTSVDIIKTGGYKVSALEVEWHLL-AHPSITDVAVIGVPDMTWG-QRVTAVVT---LREGHSLS- 264
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGpELLVIFLVlgeEKKGFDQAr 441
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 546232251 265 ----HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 304
Cdd:PLN03051 442 pealQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVL 485
|
|
| |
