|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
6-505 |
1.34e-157 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 454.25 E-value: 1.34e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGSPST 85
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 86 APDdadtdrppegqgraarsdggpaaergatvrreetpesgetagetagetsgnvlvgygtgapaarrrrvrpsvyAATA 165
Cdd:PRK11856 84 AAA-------------------------------------------------------------------------AAEA 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 166 QTSAPTPAPGRPGQVPARAGATDSAVAEEWEGPVAVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGleeda 245
Cdd:PRK11856 91 APEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAA----- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 246 ESVAASAPPlggpavggrPGPVAQPVQAAPEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMnata 325
Cdd:PRK11856 166 AAPAAAAAA---------AAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL---- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 326 dGGSAPKVSVLALLARICTAALSRFPELNSAVDTEAreVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRL 405
Cdd:PRK11856 233 -KAIGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 406 TEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGA 485
Cdd:PRK11856 310 AEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGA 389
|
490 500
....*....|....*....|
gi 1751404400 486 TAGGFLRYVADCVEQPALLL 505
Cdd:PRK11856 390 DAARFLKALKELLENPALLL 409
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
293-505 |
1.31e-84 |
|
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: 260.17 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 293 LSRSRREIPDATCWVDADATELMAARAAMNATAdGGSAPKVSVLALLARICTAALSRFPELNSAVDTEAREVVRLPAVHL 372
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDA-ADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 373 GFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVG 452
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751404400 453 RIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVEQPALLL 505
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-505 |
5.80e-73 |
|
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: 240.93 E-value: 5.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGlTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGSPST 85
Cdd:TIGR01348 2 EIKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 86 APDDADTDRPPE----GQGRAARSDGGPAAERGATVRREETPESGE-----------TAGETAGE--------------- 135
Cdd:TIGR01348 81 AQAEAKKEAAPAptagAPAPAAQAQAAPAAGQSSGVQEVTVPDIGDiekvtvievlvKVGDTVSAdqslitlesdkasme 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 136 ---------------------TSGNVLVGYGTGAPAARRRRVRPSVYAATAQTSAPTPAPGRPGQVPARAGATDSAVAEE 194
Cdd:TIGR01348 161 vpapasgvvksvkvkvgdsvpTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 195 wEGPVAVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGLEEDAESVAASApplGGPAVGGRPGPVAQpVQAA 274
Cdd:TIGR01348 241 -PAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASA---AGGAPGALPWPNVD-FSKF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 275 PEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATADGGSApKVSVLALLARICTAALSRFPELN 354
Cdd:TIGR01348 316 GEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGV-KLTVLHILMKAVAAALKKFPKFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 355 SAVDTEAREVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYGVFGV 434
Cdd:TIGR01348 395 ASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751404400 435 DGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVEQPALLL 505
Cdd:TIGR01348 475 TAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 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: 107.85 E-value: 1.42e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVA 79
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-78 |
2.41e-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: 101.71 E-value: 2.41e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTV 78
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
6-505 |
1.34e-157 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 454.25 E-value: 1.34e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGSPST 85
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 86 APDdadtdrppegqgraarsdggpaaergatvrreetpesgetagetagetsgnvlvgygtgapaarrrrvrpsvyAATA 165
Cdd:PRK11856 84 AAA-------------------------------------------------------------------------AAEA 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 166 QTSAPTPAPGRPGQVPARAGATDSAVAEEWEGPVAVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGleeda 245
Cdd:PRK11856 91 APEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAA----- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 246 ESVAASAPPlggpavggrPGPVAQPVQAAPEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMnata 325
Cdd:PRK11856 166 AAPAAAAAA---------AAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL---- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 326 dGGSAPKVSVLALLARICTAALSRFPELNSAVDTEAreVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRL 405
Cdd:PRK11856 233 -KAIGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 406 TEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGA 485
Cdd:PRK11856 310 AEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGA 389
|
490 500
....*....|....*....|
gi 1751404400 486 TAGGFLRYVADCVEQPALLL 505
Cdd:PRK11856 390 DAARFLKALKELLENPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
6-505 |
6.82e-108 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 331.79 E-value: 6.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEgLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGS--- 82
Cdd:PRK11855 4 EFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGaaa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 83 --------PSTAPDDADTDRPPEGQGRAARSDGGPAAER---------------------GATVRREET----------- 122
Cdd:PRK11855 83 aaaapaaaAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEvkvpdigeiteveviewlvkvGDTVEEDQSlitvetdkatm 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 123 ----PESGETA------GETAGEtsGNVLVGYGTGAPAARRRRVRPSVYAATAQTSAPTPAPGRPGQVPARAGATDSAva 192
Cdd:PRK11855 163 eipsPVAGVVKeikvkvGDKVSV--GSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAA-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 193 eewEGPVAVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGLEEDAESVAASAPPLGGPAVGGRPGPVAQPVQ 272
Cdd:PRK11855 239 ---PGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 273 aAPEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMA--ARAAMNATADGgsaPKVSVLALLARICTAALSRF 350
Cdd:PRK11855 316 -FGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEAlrKQLKKEAEKAG---VKLTMLPFFIKAVVAALKEF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 351 PELNSAVDTEAREVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYG 430
Cdd:PRK11855 392 PVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLG 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751404400 431 VFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVEQPALLL 505
Cdd:PRK11855 472 GIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
293-505 |
1.31e-84 |
|
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: 260.17 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 293 LSRSRREIPDATCWVDADATELMAARAAMNATAdGGSAPKVSVLALLARICTAALSRFPELNSAVDTEAREVVRLPAVHL 372
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDA-ADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 373 GFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVG 452
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751404400 453 RIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVEQPALLL 505
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-499 |
1.37e-76 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 252.62 E-value: 1.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 2 ARVLEFKLPDLGegLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAV- 80
Cdd:PRK11854 103 AAAKDVHVPDIG--SDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVa 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 81 GSPSTAPDDADTDRPPEGQGRAARSD--------GGPAAE-------RGATVRREE---TPESGETAGETAGETSGNVL- 141
Cdd:PRK11854 181 GEAPAAAPAAAEAAAPAAAPAAAAGVkdvnvpdiGGDEVEvtevmvkVGDKVEAEQsliTVEGDKASMEVPAPFAGTVKe 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 142 --------VGYGTGAPAARRRRVRPSVYAATAQTSAPTPAPGRPGQVPARAGATDSAVAEEWE-GPVAVISPLVRKLARR 212
Cdd:PRK11854 261 ikvnvgdkVKTGSLIMRFEVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAEnDAYVHATPLVRRLARE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 213 HGLDLRQITGSGREGLILRADVESAIKGLEEDAESvAASAPPLGGPAVGGRPGPVAQPVQAApEGERIALRGVRGAVADK 292
Cdd:PRK11854 341 FGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEA-APAAAAAGGGGPGLLPWPKVDFSKFG-EIEEVELGRIQKISGAN 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 293 LSRSRREIPDATCWVDADATELMA---ARAAMNATADGGSapKVSVLALLARICTAALSRFPELNSAVDTEAREVVRLPA 369
Cdd:PRK11854 419 LHRNWVMIPHVTQFDKADITELEAfrkQQNAEAEKRKLGV--KITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKY 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 370 VHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAML 449
Cdd:PRK11854 497 VNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAIL 576
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1751404400 450 GVGRIVAKPwVHEG-ELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVE 499
Cdd:PRK11854 577 GVSKSAMEP-VWNGkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-505 |
5.80e-73 |
|
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: 240.93 E-value: 5.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGlTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGSPST 85
Cdd:TIGR01348 2 EIKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 86 APDDADTDRPPE----GQGRAARSDGGPAAERGATVRREETPESGE-----------TAGETAGE--------------- 135
Cdd:TIGR01348 81 AQAEAKKEAAPAptagAPAPAAQAQAAPAAGQSSGVQEVTVPDIGDiekvtvievlvKVGDTVSAdqslitlesdkasme 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 136 ---------------------TSGNVLVGYGTGAPAARRRRVRPSVYAATAQTSAPTPAPGRPGQVPARAGATDSAVAEE 194
Cdd:TIGR01348 161 vpapasgvvksvkvkvgdsvpTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 195 wEGPVAVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGLEEDAESVAASApplGGPAVGGRPGPVAQpVQAA 274
Cdd:TIGR01348 241 -PAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASA---AGGAPGALPWPNVD-FSKF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 275 PEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATADGGSApKVSVLALLARICTAALSRFPELN 354
Cdd:TIGR01348 316 GEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGV-KLTVLHILMKAVAAALKKFPKFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 355 SAVDTEAREVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYGVFGV 434
Cdd:TIGR01348 395 ASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751404400 435 DGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVEQPALLL 505
Cdd:TIGR01348 475 TAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-500 |
2.01e-62 |
|
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: 213.72 E-value: 2.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLltVAVGSPST 85
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVL--AIIGDANA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 86 APDDADTDRPPegqgraARSDGGPaaergatvrrEETPESGETAGetagetsgnvlvgygtgapaarrrrvrpsvyAATA 165
Cdd:TIGR02927 206 APAEPAEEEAP------APSEAGS----------EPAPDPAARAP-------------------------------HAAP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 166 QTSAPTPAPGRPGQVPARAGATDSAvaeewegPVAVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGLEEDA 245
Cdd:TIGR02927 239 DPPAPAPAPAKTAAPAAAAPVSSGD-------SGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEAR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 246 ESVAASAPPlGGPAVGGRPGPVAQPVQAAPEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATA 325
Cdd:TIGR02927 312 AAAAAPAAA-AAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDF 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 326 DGGSAPKVSVLALLARICTAALSRFPELNSAVDTEAREVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRL 405
Cdd:TIGR02927 391 LEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 406 TEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGE-----LAVRQVVQLSLTFDHR 480
Cdd:TIGR02927 471 AARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHR 550
|
490 500
....*....|....*....|
gi 1751404400 481 VCDGATAGGFLRYVADCVEQ 500
Cdd:TIGR02927 551 LVDGADAGRFLTTIKKRLEE 570
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-505 |
4.84e-62 |
|
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: 208.05 E-value: 4.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGSpst 85
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 86 apddadtdrppegqgraarsDGGPAAERGATVRREETPesgetagetagetsgnvlvgygtgapaarrrrvrpsvyaATA 165
Cdd:TIGR01347 79 --------------------DATAAPPAKSGEEKEETP---------------------------------------AAS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 166 QTSAPTPAPGRPgqvparagatdsavaeewegpvaVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAikgleedA 245
Cdd:TIGR01347 100 AAAAPTAAANRP-----------------------SLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKK-------T 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 246 ESVAASAPPLGGPAVggrpgpvAQPVQAAPEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATA 325
Cdd:TIGR01347 150 EAPASAQPPAAAAAA-------AAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEF 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 326 DGGSAPKVSVLALLARICTAALSRFPELNSAVDTEarEVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRL 405
Cdd:TIGR01347 223 EKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 406 TEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGA 485
Cdd:TIGR01347 301 GKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGK 380
|
490 500
....*....|....*....|
gi 1751404400 486 TAGGFLRYVADCVEQPALLL 505
Cdd:TIGR01347 381 EAVTFLVTIKELLEDPRRLL 400
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
6-505 |
5.78e-59 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 200.06 E-value: 5.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSelpvgapllTVAVGspst 85
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD---------TVTVG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 86 apddadtdrppegQGRAARSDGGPAAergatvrreetpesgetagetagetsgnvlvgygtgapaarrrrvrpSVYAATA 165
Cdd:PRK05704 71 -------------QVLGRIDEGAAAG-----------------------------------------------AAAAAAA 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 166 QTSAPTPAPGRPGQVPARAGATDSAvaeewegpvaviSPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKgleedA 245
Cdd:PRK05704 91 AAAAAAAAPAQAQAAAAAEQSNDAL------------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALA-----A 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 246 ESVAASAPPLGGPAvggrpgPVAQPVQAAPEgERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATA 325
Cdd:PRK05704 154 AAAAPAAPAAAAPA------AAPAPLGARPE-ERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAF 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 326 DGGSAPKVSVLALLARICTAALSRFPELNSAVDTEarEVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRL 405
Cdd:PRK05704 227 EKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAEL 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 406 TEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGA 485
Cdd:PRK05704 305 AKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGK 384
|
490 500
....*....|....*....|
gi 1751404400 486 TAGGFLRYVADCVEQPALLL 505
Cdd:PRK05704 385 EAVGFLVTIKELLEDPERLL 404
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-505 |
1.71e-58 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 199.63 E-value: 1.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSE-LPVGAPLlTVAVGSPS 84
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPI-AVLVEEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 85 TAPDdADTDRPPEGQGRAArsdggpaaergatvrreetPESGETAgetagetsgnvlvgygtgapaarrrrvrpsvyaAT 164
Cdd:TIGR01349 80 DVAD-AFKNYKLESSASPA-------------------PKPSEIA---------------------------------PT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 165 AQTSAPTPAPGRPGQVPARAGATDSAVAEEwEGPVAViSPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGLEED 244
Cdd:TIGR01349 107 APPSAPKPSPAPQKQSPEPSSPAPLSDKES-GDRIFA-SPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPAS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 245 A-ESVAASAPPLGGPAVGGRPGpvaqpvqaapEGERIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNA 323
Cdd:TIGR01349 185 AnQQAAATTPATYPAAAPVSTG----------SYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 324 TADGGSapKVSVLALLARICTAALSRFPELNSAVDTEAreVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIG 403
Cdd:TIGR01349 255 MASEVY--KLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 404 RLTEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGE---LAVRQVVQLSLTFDHR 480
Cdd:TIGR01349 331 DLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHR 410
|
490 500
....*....|....*....|....*
gi 1751404400 481 VCDGATAGGFLRYVADCVEQPALLL 505
Cdd:TIGR01349 411 VIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
7-508 |
2.36e-57 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 196.09 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 7 FKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGspsta 86
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 87 pdDADTDRPPEGQGRAARSDGGPAAErgatvrreetpesgetaGETAGETSGNVLVgygtgapaarrrrvrpsvyaataq 166
Cdd:PLN02528 76 --DSQHLRSDSLLLPTDSSNIVSLAE-----------------SDERGSNLSGVLS------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 167 tsaptpapgrpgqvparagatdsavaeewegpvaviSPLVRKLARRHGLDLRQITGSGREGLILRADV--ESAIKGLEED 244
Cdd:PLN02528 113 ------------------------------------TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlkYAAQKGVVKD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 245 AESVAASAPPlggpAVGGRPGPVAQPVQAAPEGERIALRGVRGAVADKLSRSRReIPDATcWVDADATELMAARAAMNAT 324
Cdd:PLN02528 157 SSSAEEATIA----EQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAK-VPHFH-YVEEINVDALVELKASFQE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 325 ADGGSAPKVSVLALLARICTAALSRFPELNSAVDTEAREVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGR 404
Cdd:PLN02528 231 NNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 405 LTEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKP-WVHEGELAVRQVVQLSLTFDHRVCD 483
Cdd:PLN02528 311 LQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVYPASIMTVTIGADHRVLD 390
|
490 500
....*....|....*....|....*
gi 1751404400 484 GATAGGFLRYVADCVEQPALLLRTL 508
Cdd:PLN02528 391 GATVARFCNEWKSYVEKPELLMLHM 415
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
8-505 |
4.04e-56 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 192.98 E-value: 4.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 8 KLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVAVGspstap 87
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTG------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 88 ddadtDRPPEGQGRAARSDGGPAAERGATVRREETPEsgetagetagetsgnvlvgygtgapaarrrrvrpsvyaaTAQT 167
Cdd:PTZ00144 122 -----GAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPE---------------------------------------PPAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 168 SAPTPAPgrpgqvparagatdsavaeewegpvavisplvrklarrhgldlrqitgsgreglilradvesaikglEEDAES 247
Cdd:PTZ00144 158 SKPTPPA-------------------------------------------------------------------AAKPPE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 248 VAASAPPlggpavggrpgpVAQPVQAAPEGE-RIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATAD 326
Cdd:PTZ00144 171 PAPAAKP------------PPTPVARADPREtRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 327 GGSAPKVSVLALLARICTAALSRFPELNSAVDTEarEVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLT 406
Cdd:PTZ00144 239 KKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD--EIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 407 EAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGAT 486
Cdd:PTZ00144 317 EKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRD 396
|
490
....*....|....*....
gi 1751404400 487 AGGFLRYVADCVEQPALLL 505
Cdd:PTZ00144 397 AVTFLKKIKDLIEDPARML 415
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
200-504 |
3.22e-52 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 179.22 E-value: 3.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 200 AVISPLVRKLARRHGLDLRQITGSGREGLILRADVESAIKGLEE-DAESVAASAPPLGGPAvgGRPGPVAQPVQAAPEGE 278
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSaPTPAEAASVSSAQQAA--KTAAPAAAPPKLEGKRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 279 RIAlrGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATADGGSAPKVSVLALLARICTAALSRFPELNSAVD 358
Cdd:PRK11857 80 KVA--PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 359 TEAREVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYGVFGVDGST 438
Cdd:PRK11857 158 EATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751404400 439 PIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVEQPALL 504
Cdd:PRK11857 238 PVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
202-505 |
1.41e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 160.07 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 202 ISPLVRKLARRHGLDLRQITGSGREGLILRADVesaIKGLEEDAESvaasaPPLGGPAVGGRPGPVAQPVQAAPEGERIA 281
Cdd:PRK14843 51 ISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDV---LALLPENIEN-----DSIKSPAQIEKVEEVPDNVTPYGEIERIP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 282 LRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATADGGSAPKVSVLALLARICTAALSRFPELNSAVDTEA 361
Cdd:PRK14843 123 MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 362 REVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPII 441
Cdd:PRK14843 203 KTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPII 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751404400 442 NHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVADCVEQPALLL 505
Cdd:PRK14843 283 NQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-505 |
3.47e-43 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 160.79 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGS-ELPVGApllTVAVgsps 84
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkEIKVGE---VIAI---- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 85 TAPDDADTDRppeGQGRAARSDGGPAAERGAtvrrEETPESGETAGETagetsgnvlvgygtgapaarrrrvrpsvyaat 164
Cdd:PLN02744 187 TVEEEEDIGK---FKDYKPSSSAAPAAPKAK----PSPPPPKEEEVEK-------------------------------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 165 aQTSAPTPAPGRPGQVPARAGATDSavaeewegpvaviSPLVRKLARRHGLDLRQITGSGREGLILRADVES--AIKGLE 242
Cdd:PLN02744 228 -PASSPEPKASKPSAPPSSGDRIFA-------------SPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDylASGGKG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 243 EDAE-SVAASAPPLGGPAVggrpgPVAQpvqaapegerialrgVRGAVADKLSRSRREIPDATCWVDADATELMAARAAM 321
Cdd:PLN02744 294 ATAPpSTDSKAPALDYTDI-----PNTQ---------------IRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 322 NATADGGSAPKVSVLALLARICTAALSRFPELNSA-VDTEAREvvrLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGA 400
Cdd:PLN02744 354 NSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSwTDDYIRQ---YHNVNINVAVQTENGLYVPVVKDADKKGLSTIAE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 401 EIGRLTEAARTGKLTPAQLTGGTFTLNNY-GVFGVDGSTPIINHPEAAMLGVG----RIVakPWVHEGELAVRQVVQLSL 475
Cdd:PLN02744 431 EVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGsaekRVI--PGSGPDQYNFASFMSVTL 508
|
490 500 510
....*....|....*....|....*....|
gi 1751404400 476 TFDHRVCDGATAGGFLRYVADCVEQPALLL 505
Cdd:PLN02744 509 SCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
264-505 |
3.55e-31 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 125.64 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 264 PGPVAQPVQAAPEGE--------RIALRGVRGAVADKLSRSRREIPDATCWVDADATELMAARAAMNATADGGSAPKVSV 335
Cdd:PLN02226 213 PSSPPPPKQSAKEPQlppkererRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 336 LALLARICTAALSRFPELNSAVDTEarEVVRLPAVHLGFAAQTERGLMVPVVRDAHSRNTESIGAEIGRLTEAARTGKLT 415
Cdd:PLN02226 293 MSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTIS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 416 PAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIVAKPWVHEGELAVRQVVQLSLTFDHRVCDGATAGGFLRYVA 495
Cdd:PLN02226 371 IDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVK 450
|
250
....*....|
gi 1751404400 496 DCVEQPALLL 505
Cdd:PLN02226 451 DVVEDPQRLL 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: 107.85 E-value: 1.42e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTVA 79
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-78 |
2.41e-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: 101.71 E-value: 2.41e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTV 78
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
245-494 |
1.29e-17 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 86.48 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 245 AESVAASAPPLGGPAVGGRPGPVAQPVQAAPEGERIALRGVRGAVADKLSRSRrEIPDATCwVDADATELMAARAAM--- 321
Cdd:PRK12270 83 PPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASL-EVPTATS-VRAVPAKLLIDNRIVinn 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 322 -NATADGGsapKVSVLALLARICTAALSRFPELNSAVDTEA--REVVRLPAVHLGFAAQTE-----RGLMVPVVRDAHSR 393
Cdd:PRK12270 161 hLKRTRGG---KVSFTHLIGYALVQALKAFPNMNRHYAEVDgkPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 394 N-TESIGA--EIGRlteAARTGKLTPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGVGRIvAKPWVHEG------- 463
Cdd:PRK12270 238 DfAQFWAAyeDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerla 313
|
250 260 270
....*....|....*....|....*....|.
gi 1751404400 464 ELAVRQVVQLSLTFDHRVCDGATAGGFLRYV 494
Cdd:PRK12270 314 ELGISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
6-78 |
2.21e-15 |
|
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: 70.71 E-value: 2.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751404400 6 EFKLPDLGEGLTEAeIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTV 78
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
3-133 |
6.50e-15 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 76.14 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 3 RVLEFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLltvAVGS 82
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL---AVVA 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751404400 83 PSTAPDDADTDRPPEGQGRAARsDGGPAAERGATVRREETP-------ESGETAGETA 133
Cdd:PRK14875 78 DAEVSDAEIDAFIAPFARRFAP-EGIDEEDAGPAPRKARIGgrtvrylRLGEGDGTPV 134
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
202-235 |
1.97e-10 |
|
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: 55.77 E-value: 1.97e-10
10 20 30
....*....|....*....|....*....|....
gi 1751404400 202 ISPLVRKLARRHGLDLRQITGSGREGLILRADVE 235
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
9-75 |
2.85e-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: 53.60 E-value: 2.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751404400 9 LPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPL 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 |
5.59e-08 |
|
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: 49.72 E-value: 5.59e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751404400 21 IVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTV 78
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-78 |
9.49e-06 |
|
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: 45.27 E-value: 9.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1751404400 25 LVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTV 78
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
6-135 |
3.91e-05 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 46.06 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751404400 6 EFKLPDLGEGLTEAEIVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSE-LPVGAPLLTV------ 78
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVLleeges 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751404400 79 ------AVGSPSTAPDDADTDRPPEGQGRAARSDGGPAAERGATVRREETPESGETAGETAGE 135
Cdd:PRK11892 84 asdagaAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMTVRE 146
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
21-78 |
6.77e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 42.14 E-value: 6.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751404400 21 IVRWLVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTARFGEEGSELPVGAPLLTV 78
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
25-61 |
1.09e-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: 38.95 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1751404400 25 LVEVGDVVTIDQPVVEVETAKAMVEVPCPYGGVVTAR 61
Cdd:COG0509 44 LPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEV 80
|
|
| |
