|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
6-465 |
2.34e-161 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 462.34 E-value: 2.34e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVGTPVS 85
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 86 GTETTGagapgggnegegsgnvlvgygtqapparrrrvrppaapgaapgpVREERPLAAGAGAGAGTVNGVGAGVDDGHG 165
Cdd:PRK11856 84 AAAAAE--------------------------------------------AAPEAPAPEPAPAAAAAAAAAPAAAAAPAA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 166 RRAdgPVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEHAVRAGAPAAATTTATTATTRTATTRtttraSGTRVP 245
Cdd:PRK11856 120 PAA--AAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAAE-----GEERVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 246 LKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMNEAGgPKISLLALLARICTAALARFPELNSTVDMDAreIV 325
Cdd:PRK11856 193 LSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIG-VKLTVTDFLIKAVALALKKFPELNASWDDDA--IV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 326 RLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGSTPIINHPE 405
Cdd:PRK11856 270 LKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPE 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 406 AAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PRK11856 350 VAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
257-465 |
3.05e-87 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 265.56 E-value: 3.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 257 LSRSRREIPDATCWVDADATELMHARVRMNEAG---GPKISLLALLARICTAALARFPELNSTVDMDAREIVRLDEVHLG 333
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 334 FAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGR 413
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 414 IVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-465 |
6.42e-66 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 221.29 E-value: 6.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 2 AQVLEFKLPDLGeGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVG 81
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 82 TPVSGTETTGAGAPGGGNEGEGsgnvlvgygtqapparrrrvrppaapgaapgpvREERPLAAGAGAGAGTVNGVGAGVD 161
Cdd:TIGR01348 193 GSTPATAPAPASAQPAAQSPAA---------------------------------TQPEPAAAPAAAKAQAPAPQQAGTQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 162 DghgrraDGPVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEHAVRAGAPAAATTTATTATTRTATT---RTTTR 238
Cdd:TIGR01348 240 N------PAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALpwpNVDFS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 239 ASGT--RVPLKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMN---EAGGPKISLLALLARICTAALARFPEL 313
Cdd:TIGR01348 314 KFGEveEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNaavEKEGVKLTVLHILMKAVAAALKKFPKF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 314 NSTVDMDAREIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFG 393
Cdd:TIGR01348 394 NASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIG 473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 394 VDGSTPIINHPEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:TIGR01348 474 GTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
6-79 |
1.42e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 107.46 E-value: 1.42e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVA 79
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-78 |
1.20e-26 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 102.10 E-value: 1.20e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTV 78
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
6-465 |
2.34e-161 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 462.34 E-value: 2.34e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVGTPVS 85
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 86 GTETTGagapgggnegegsgnvlvgygtqapparrrrvrppaapgaapgpVREERPLAAGAGAGAGTVNGVGAGVDDGHG 165
Cdd:PRK11856 84 AAAAAE--------------------------------------------AAPEAPAPEPAPAAAAAAAAAPAAAAAPAA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 166 RRAdgPVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEHAVRAGAPAAATTTATTATTRTATTRtttraSGTRVP 245
Cdd:PRK11856 120 PAA--AAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAAE-----GEERVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 246 LKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMNEAGgPKISLLALLARICTAALARFPELNSTVDMDAreIV 325
Cdd:PRK11856 193 LSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIG-VKLTVTDFLIKAVALALKKFPELNASWDDDA--IV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 326 RLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGSTPIINHPE 405
Cdd:PRK11856 270 LKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPE 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 406 AAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PRK11856 350 VAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-465 |
3.97e-102 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 315.61 E-value: 3.97e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 2 AQVLEFKLPDLGEgLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVG 81
Cdd:PRK11855 117 GGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 82 TPVSGTETTGAGAPGGgnegegsgnvlvgygtqapparrrrvrppaapgaapgpvrEERPLAAGAGAGAGTVNGVGAGVD 161
Cdd:PRK11855 196 AAAPAAAAAPAAAAPA----------------------------------------AAAAAAPAPAPAAAAAPAAAAPAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 162 DGhgrrADGPVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVE------HAVRAGAPAAATTTATTATTRTATTRT 235
Cdd:PRK11855 236 AA----APGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQafvkgaMSAAAAAAAAAAAAGGGGLGLLPWPKV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 236 TTRASGT--RVPLKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMN---EAGGPKISLLALLARICTAALARF 310
Cdd:PRK11855 312 DFSKFGEieTKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKkeaEKAGVKLTMLPFFIKAVVAALKEF 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 311 PELNSTVDMDAREIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYG 390
Cdd:PRK11855 392 PVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLG 471
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1900756291 391 VFGVDGSTPIINHPEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PRK11855 472 GIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
257-465 |
3.05e-87 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 265.56 E-value: 3.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 257 LSRSRREIPDATCWVDADATELMHARVRMNEAG---GPKISLLALLARICTAALARFPELNSTVDMDAREIVRLDEVHLG 333
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 334 FAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGR 413
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 414 IVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-465 |
6.42e-66 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 221.29 E-value: 6.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 2 AQVLEFKLPDLGeGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVG 81
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 82 TPVSGTETTGAGAPGGGNEGEGsgnvlvgygtqapparrrrvrppaapgaapgpvREERPLAAGAGAGAGTVNGVGAGVD 161
Cdd:TIGR01348 193 GSTPATAPAPASAQPAAQSPAA---------------------------------TQPEPAAAPAAAKAQAPAPQQAGTQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 162 DghgrraDGPVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEHAVRAGAPAAATTTATTATTRTATT---RTTTR 238
Cdd:TIGR01348 240 N------PAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALpwpNVDFS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 239 ASGT--RVPLKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMN---EAGGPKISLLALLARICTAALARFPEL 313
Cdd:TIGR01348 314 KFGEveEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNaavEKEGVKLTVLHILMKAVAAALKKFPKF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 314 NSTVDMDAREIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFG 393
Cdd:TIGR01348 394 NASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIG 473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 394 VDGSTPIINHPEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:TIGR01348 474 GTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-459 |
3.65e-65 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 221.03 E-value: 3.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 2 AQVLEFKLPDLGegLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVG 81
Cdd:PRK11854 204 AGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 82 tpvsgtettgagapgggnegegsgnvlvgyGTQAPPARRRRVRPPAAPGAAPGPVREERPLAAGAGAGAGTVNGVgagvd 161
Cdd:PRK11854 282 ------------------------------GAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDA----- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 162 dghgrradgpVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEHAVRAGAPAAATTTATTATTRTATTRTTTRA-- 239
Cdd:PRK11854 327 ----------YVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGGPGLLPWPKvd 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 240 ------SGTrVPLKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMN-----EAGGPKISLLALLARICTAALA 308
Cdd:PRK11854 397 fskfgeIEE-VELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNaeaekRKLGVKITPLVFIMKAVAAALE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 309 RFPELNSTVDMDAREIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNN 388
Cdd:PRK11854 476 QMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISS 555
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 389 YGVFGVDGSTPIINHPEAAMLGVGRIVPKPwVHEG-ELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVE 459
Cdd:PRK11854 556 IGGLGTTHFTPIVNAPEVAILGVSKSAMEP-VWNGkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-465 |
4.81e-64 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 212.29 E-value: 4.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVGTPVS 85
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 86 GTETTGAGApgggnegegsgnvlvgygtqapparrrrvrppaapgaapgpvrEERPLAAGAGAGAGTVNGVGAgvddghg 165
Cdd:TIGR01347 82 AAPPAKSGE-------------------------------------------EKEETPAASAAAAPTAAANRP------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 166 rradgpvaVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEhavraGAPAAATTTATTATTRTATTRTTTRASGTRVP 245
Cdd:TIGR01347 112 --------SLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDII-----KKTEAPASAQPPAAAAAAAAPAAATRPEERVK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 246 LKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMNEA----GGPKISLLALLARICTAALARFPELNSTVDMDa 321
Cdd:TIGR01347 179 MTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEfekkHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 322 rEIVRLDEVHLGFAAQTERGLVVPVVkgahtRDAESLS-----AEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDG 396
Cdd:TIGR01347 258 -DIVYKDYYDISVAVSTDRGLVVPVV-----RNADRMSfadieKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLM 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900756291 397 STPIINHPEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:TIGR01347 332 STPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
7-465 |
3.38e-59 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 199.95 E-value: 3.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 7 FKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVGtpvsg 86
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 87 tettgagapgggnegegsgnvlvgygtqapparrrrvrppaapgaAPGPVREERPLAAGAgagagTVNGVGAGVDDGHGR 166
Cdd:PLN02528 76 ---------------------------------------------DSQHLRSDSLLLPTD-----SSNIVSLAESDERGS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 167 RADGPVAviSPLVRRLARQNGLDLRELPGSGPDGLITRADV-------EHAVRAGAPAAATTTATTATTRTATTRTTTRA 239
Cdd:PLN02528 106 NLSGVLS--TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlkyaaqkGVVKDSSSAEEATIAEQEEFSTSVSTPTEQSY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 240 SGTRVPLKGVRGAVADKLSRSRR--------EIPdatcwVDAdATELMHARVRMNEAGGPKISLLALLARICTAALARFP 311
Cdd:PLN02528 184 EDKTIPLRGFQRAMVKTMTAAAKvphfhyveEIN-----VDA-LVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYP 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 312 ELNSTVDMDAREIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGV 391
Cdd:PLN02528 258 LLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGA 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1900756291 392 FGVDGSTPIINHPEAAMLGVGRI--VPKPwVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PLN02528 338 IGGKFGSPVLNLPEVAIIALGRIqkVPRF-VDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
6-465 |
1.50e-58 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 198.13 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTelpvgspllTVAVGtpvs 85
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD---------TVTVG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 86 gtettgagapgggnegegsgNVLVGYGTQAPPARRRRVRPPAAPGAAPGPVREERPLaagagagagtvngvgagvddghg 165
Cdd:PRK05704 71 --------------------QVLGRIDEGAAAGAAAAAAAAAAAAAAAPAQAQAAAA----------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 166 rrADGPVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEhavRAGAPAAATTTATTATTRTATTRTTTRASGTRVP 245
Cdd:PRK05704 108 --AEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVL---AALAAAAAAPAAPAAAAPAAAPAPLGARPEERVP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 246 LKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMNEA----GGPKISLLALLARICTAALARFPELNSTVDMDa 321
Cdd:PRK05704 183 MTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAfekkHGVKLGFMSFFVKAVVEALKRYPEVNASIDGD- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 322 rEIVRLDEVHLGFAAQTERGLVVPVVkgahtRDAESLS-----AEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDG 396
Cdd:PRK05704 262 -DIVYHNYYDIGIAVGTPRGLVVPVL-----RDADQLSfaeieKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLM 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900756291 397 STPIINHPEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PRK05704 336 STPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
8-465 |
2.00e-53 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 184.89 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 8 KLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVGtpvsgt 87
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTG------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 88 ettgagapgggnegegsgnvlvGYGTQAPPARRRRVRPPAAPGAAPGPVREERPlaagagagagtvngvgagvddghGRR 167
Cdd:PTZ00144 122 ----------------------GAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPE-----------------------PPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 168 ADGPVAviSPLVRRLARQNGldlrelPGSGPDGLITRADVEhavragapaaatttattattrtattrtttrasgTRVPLK 247
Cdd:PTZ00144 157 ASKPTP--PAAAKPPEPAPA------AKPPPTPVARADPRE---------------------------------TRVPMS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 248 GVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMNEAG----GPKISLLALLARICTAALARFPELNSTVDMDarE 323
Cdd:PTZ00144 196 RMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFqkkhGVKLGFMSAFVKASTIALKKMPIVNAYIDGD--E 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 324 IVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGSTPIINH 403
Cdd:PTZ00144 274 IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINP 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 404 PEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PTZ00144 354 PQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-460 |
5.19e-52 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 184.83 E-value: 5.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVAVGTPVS 85
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 86 GTETTGAGAPGGGNEGEGSGNVlvgygtqapparrrrvrppaapgAAPGPVREERPLAAGAGAGAGTVNGVGAGVDDGHG 165
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEPAPDP-----------------------AARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 166 rradgpVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADV--------EHAVRAGAPAAATTTATTATTRTATTRTTT 237
Cdd:TIGR02927 265 ------GPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVlaaakaaeEARAAAAAPAAAAAPAAPAAAAKPAEPDTA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 238 RASGTRVPLKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVR----MNEAGGPKISLLALLARICTAALARFPEL 313
Cdd:TIGR02927 339 KLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndFLEKNGVNLTFLPFFVQAVTEALKAHPNV 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 314 NSTVDMDAREIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFG 393
Cdd:TIGR02927 419 NASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGG 498
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 394 VDGSTPIINHPEAAMLGVGRIVPKPWVHEGE-----LAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQ 460
Cdd:TIGR02927 499 ALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
173-464 |
2.91e-47 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 165.35 E-value: 2.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 173 AVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEH------AVRAGAPAAATTTATTATTRTATTRTTTRASGTRVPL 246
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENfikslkSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKREKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 247 KGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMNEA----GGPKISLLALLARICTAALARFPELNSTVDMDAR 322
Cdd:PRK11857 82 APIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlktEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 323 EIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGSTPIIN 402
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900756291 403 HPEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVL 464
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
175-465 |
5.67e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 157.76 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 175 ISPLVRRLARQNGLDLRELPGSGPDGLITRADVEHAVRAGAPAAATTTATTATTRTATTRTTTRASGT-RVPLKGVRGAV 253
Cdd:PRK14843 51 ISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPYGEIeRIPMTPMRKVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 254 ADKLSRSRREIPDATCWVDADATELMHARVRM----NEAGGPKISLLALLARICTAALARFPELNSTVDMDAREIVRLDE 329
Cdd:PRK14843 131 AQRMVESYLTAPTFTLNYEVDMTEMLALRKKVlepiMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 330 VHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGSTPIINHPEAAML 409
Cdd:PRK14843 211 VNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAIL 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1900756291 410 GVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PRK14843 291 GVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-465 |
2.27e-40 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 151.93 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTA-RYGDEGTELPVGSplltvAVGTPV 84
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKiVKGDGAKEIKVGE-----VIAITV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 85 SGTETTGAgapgggnegegsgnvLVGYGTQAPPARRRRVRPPAAPGAAPGPVREERPLAAGAGAGAGTVNgvgagvddgh 164
Cdd:PLN02744 189 EEEEDIGK---------------FKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPP---------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 165 grrADGPVAVISPLVRRLARQNGLDLRELPGSGPDGLITRADVEhavragapAAATTTATTATTRTATTRTTTRASGTRV 244
Cdd:PLN02744 244 ---SSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIE--------DYLASGGKGATAPPSTDSKAPALDYTDI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 245 PLKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMN----EAGGPKISLLALLARICTAALARFPELNSTVDMD 320
Cdd:PLN02744 313 PNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 321 AreIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNY-GVFGVDGSTP 399
Cdd:PLN02744 393 Y--IRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCA 470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 400 IINHPEAAMLGVG----RIVPKPWVHEGELAVRQVVQLSftFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PLN02744 471 IINPPQSAILAVGsaekRVIPGSGPDQYNFASFMSVTLS--CDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
243-465 |
6.42e-36 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 138.35 E-value: 6.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 243 RVPLKGVRGAVADKLSRSRREIPDATCWVDADATELMHARVRMNEA----GGPKISLLALLARICTAALARFPELNSTVD 318
Cdd:PLN02226 236 RVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfyekHGVKLGLMSGFIKAAVSALQHQPVVNAVID 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 319 MDarEIVRLDEVHLGFAAQTERGLVVPVVKGAHTRDAESLSAEFARLTEAARTGTLTPADLTGGTFTLNNYGVFGVDGST 398
Cdd:PLN02226 316 GD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLIST 393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1900756291 399 PIINHPEAAMLGVGRIVPKPWVHEGELAVRQVVQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 465
Cdd:PLN02226 394 PIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
6-79 |
1.42e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 107.46 E-value: 1.42e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVA 79
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-78 |
1.20e-26 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 102.10 E-value: 1.20e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTV 78
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
242-454 |
1.14e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 89.18 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 242 TRVPLKGVRGAVADKLSRSRrEIPDATCWVDADATELMHARVRMNE----AGGPKISLLALLARICTAALARFPELNSTV 317
Cdd:PRK12270 116 EVTPLRGAAAAVAKNMDASL-EVPTATSVRAVPAKLLIDNRIVINNhlkrTRGGKVSFTHLIGYALVQALKAFPNMNRHY 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900756291 318 DM-DAR-EIVRLDEVHLGFAAQTE-----RGLVVPVVKGAHTRD-AESLSAeFARLTEAARTGTLTPADLTGGTFTLNNY 389
Cdd:PRK12270 195 AEvDGKpTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDfAQFWAA-YEDIVRRARDGKLTADDFQGTTISLTNP 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900756291 390 GVFGVDGSTPIINHPEAAMLGVGRIV-PKPWvhEG-------ELAVRQVVQLSFTFDHRVCDGGTAGGFLRYV 454
Cdd:PRK12270 274 GGIGTVHSVPRLMKGQGAIIGVGAMEyPAEF--QGaseerlaELGISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
6-78 |
7.92e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 71.86 E-value: 7.92e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900756291 6 EFKLPDLGEGLTEAeIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTV 78
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
6-79 |
3.20e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 70.74 E-value: 3.20e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTVA 79
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVA 77
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-76 |
7.76e-13 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 70.42 E-value: 7.76e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1900756291 1 MAQvlEFKLPDLGegLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLL 76
Cdd:PRK11854 1 MAI--EIKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIM 72
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
175-208 |
3.69e-12 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 60.39 E-value: 3.69e-12
10 20 30
....*....|....*....|....*....|....
gi 1900756291 175 ISPLVRRLARQNGLDLRELPGSGPDGLITRADVE 208
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
9-75 |
4.43e-09 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 52.83 E-value: 4.43e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1900756291 9 LPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPL 75
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL 70
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
21-78 |
2.23e-07 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 47.80 E-value: 2.23e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1900756291 21 IVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTV 78
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-78 |
3.24e-05 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 43.73 E-value: 3.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1900756291 25 LVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTV 78
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
6-84 |
4.80e-04 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 42.60 E-value: 4.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900756291 6 EFKLPDLGEGLTEAEIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTElpvgspllTVAVGTPV 84
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTE--------GVKVNTPI 74
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
21-78 |
5.55e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 42.52 E-value: 5.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1900756291 21 IVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLLTV 78
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
25-61 |
1.61e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 38.57 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1900756291 25 LVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTAR 61
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
10-76 |
3.05e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 38.30 E-value: 3.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900756291 10 PDLGEGLTEA----EIVRWLVQVGDVVAVDQPVVEVETAKAMVEVPCPYGGVVTARYGDEGTELPVGSPLL 76
Cdd:PRK05641 80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| |
