NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2058207303|ref|XP_041976451|]
View 

lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial [Aricia agestis]

Protein Classification

lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex( domain architecture ID 1003376)

lipoamide acyltransferase component (E2) of branched-chain alpha-keto acid dehydrogenase complex that catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2)

CATH:  3.30.559.10
EC:  2.3.1.168
Gene Ontology:  GO:0043754|GO:0016407|GO:0031625|GO:0031405|GO:0009083

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02528 super family cl33511
2-oxoisovalerate dehydrogenase E2 component
 57-458 2.29e-163

2-oxoisovalerate dehydrogenase E2 component


The actual alignment was detected with superfamily member PLN02528:

Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 467.27  E-value: 2.29e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  57 FKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEE 136
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 137 ESPSPKDEKIETNADAKTESIAQRTK---VLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHL----------NM 203
Cdd:PLN02528   81 RSDSLLLPTDSSNIVSLAESDERGSNlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgvvkdssSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 204 SSDNSNIVPEPSQIKAATVETVAEDKTVPITGFTKAMVKSMTEAMKIPHFGYCDEYDVTKLVESRENLKVLAQKQGVKLT 283
Cdd:PLN02528  161 EEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 284 YMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQL 363
Cdd:PLN02528  241 FLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 364 SLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDAAGNLVKAHILTVSWSADHRVVDGVTMARFSNQ 443
Cdd:PLN02528  321 NPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNE 400

                         410
                  ....*....|....*
gi 2058207303 444 LKAYLENPYKMLLDL 458
Cdd:PLN02528  401 WKSYVEKPELLMLHM 415
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 57-458 2.29e-163

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 467.27  E-value: 2.29e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  57 FKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEE 136
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 137 ESPSPKDEKIETNADAKTESIAQRTK---VLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHL----------NM 203
Cdd:PLN02528   81 RSDSLLLPTDSSNIVSLAESDERGSNlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgvvkdssSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 204 SSDNSNIVPEPSQIKAATVETVAEDKTVPITGFTKAMVKSMTEAMKIPHFGYCDEYDVTKLVESRENLKVLAQKQGVKLT 283
Cdd:PLN02528  161 EEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 284 YMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQL 363
Cdd:PLN02528  241 FLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 364 SLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDAAGNLVKAHILTVSWSADHRVVDGVTMARFSNQ 443
Cdd:PLN02528  321 NPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNE 400

                         410
                  ....*....|....*
gi 2058207303 444 LKAYLENPYKMLLDL 458
Cdd:PLN02528  401 WKSYVEKPELLMLHM 415
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 240-455 2.23e-94

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: 283.67  E-value: 2.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 240 MVKSMTEamkIPHFGYCDEYDVTKLVESRENLKVLAQKQGVKLTYMPIIVKAASQSLTAYPILNSSLDSACENITYKSSH 319
Cdd:pfam00198   1 MTESKQT---IPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 320 NIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGA 399
Cdd:pfam00198  78 NIGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2058207303 400 LGKIQVLPRFdAAGNLVKAHILTVSWSADHRVVDGVTMARFSNQLKAYLENPYKML 455
Cdd:pfam00198 158 VGRIRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-456 5.11e-82

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: 263.27  E-value: 5.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  58 KLSDIGeGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEEE 137
Cdd:TIGR01348 120 TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPAT 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 138 SPSPKDEKIETNADAKTESIAQRTKVLT---------------------TPAVRRIAAQFKVDLSTVNATGKNGRLLKED 196
Cdd:TIGR01348 199 APAPASAQPAAQSPAATQPEPAAAPAAAkaqapapqqagtqnpakvdhaAPAVRRLAREFGVDLSAVKGTGIKGRILRED 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 197 LLSHLNMSSDNS------------NIVPEPSqikaATVETVAEDKTVPITGFTKAMVKSMTEA-MKIPHFGYCDEYDVTK 263
Cdd:TIGR01348 279 VQRFVKEPSVRAqaaaasaaggapGALPWPN----VDFSKFGEVEEVDMSRIRKISGANLTRNwTMIPHVTHFDKADITE 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 264 LVESRENLKVLAQKQGVKLTYMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKS 343
Cdd:TIGR01348 355 MEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKG 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 344 IIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDAAgNLVKAHILTV 423
Cdd:TIGR01348 435 ITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGK-EFEPRLMLPL 513

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2058207303 424 SWSADHRVVDGVTMARFSNQLKAYLENPYKMLL 456
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 55-128 1.18e-24

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: 96.70  E-value: 1.18e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2058207303  55 VPFKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDI 128
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 54-128 7.31e-21

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: 86.27  E-value: 7.31e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058207303  54 IVPFKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDI 128
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 57-458 2.29e-163

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 467.27  E-value: 2.29e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  57 FKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEE 136
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 137 ESPSPKDEKIETNADAKTESIAQRTK---VLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHL----------NM 203
Cdd:PLN02528   81 RSDSLLLPTDSSNIVSLAESDERGSNlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgvvkdssSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 204 SSDNSNIVPEPSQIKAATVETVAEDKTVPITGFTKAMVKSMTEAMKIPHFGYCDEYDVTKLVESRENLKVLAQKQGVKLT 283
Cdd:PLN02528  161 EEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 284 YMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQL 363
Cdd:PLN02528  241 FLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 364 SLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDAAGNLVKAHILTVSWSADHRVVDGVTMARFSNQ 443
Cdd:PLN02528  321 NPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNE 400

                         410
                  ....*....|....*
gi 2058207303 444 LKAYLENPYKMLLDL 458
Cdd:PLN02528  401 WKSYVEKPELLMLHM 415
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 54-456 6.91e-147

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 430.01  E-value: 6.91e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  54 IVPFKLSDIGEgIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDS 133
Cdd:PRK11855  119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 134 -------------GEEESPSPKDEKIETNADAKT---ESIAQRTKVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDL 197
Cdd:PRK11855  198 apaaaaapaaaapAAAAAAAPAPAPAAAAAPAAAapaAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDV 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 198 LSHLN--MSSDNSNIVPEP---------SQIKAATVETVAEDKTVPITGFTKAMVKSMTEA-MKIPHFGYCDEYDVTKLV 265
Cdd:PRK11855  278 QAFVKgaMSAAAAAAAAAAaagggglglLPWPKVDFSKFGEIETKPLSRIKKISAANLHRSwVTIPHVTQFDEADITDLE 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 266 ESRENLKVLAQKQGVKLTYMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSII 345
Cdd:PRK11855  358 ALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLL 437

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 346 EIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPrFDAAGNLVKAHILTVSW 425
Cdd:PRK11855  438 EIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDGKEFVPRLMLPLSL 516

                         410       420       430
                  ....*....|....*....|....*....|.
gi 2058207303 426 SADHRVVDGVTMARFSNQLKAYLENPYKMLL 456
Cdd:PRK11855  517 SYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 57-457 9.28e-130

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 381.45  E-value: 9.28e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  57 FKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGE- 135
Cdd:PRK11856    5 FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEa 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 136 -------------EESPSPKDEKIETNADAKTESIAQRTKVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHLN 202
Cdd:PRK11856   85 aaaaeaapeapapEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 203 MSSDNSniVPEPSQIKAATVETVAEDKTVPITGFTKAMVKSMTEA-MKIPHFGYCDEYDVTKLVESRENLKvlaqKQGVK 281
Cdd:PRK11856  165 AAAPAA--AAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTALLALRKQLK----AIGVK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 282 LTYMPIIVKAASQSLTAYPILNSSLDSacENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKG 361
Cdd:PRK11856  239 LTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREG 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 362 QLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDaAGNLVKAHILTVSWSADHRVVDGVTMARFS 441
Cdd:PRK11856  317 KLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV-DGEIVVRKVMPLSLSFDHRVIDGADAARFL 395

                         410
                  ....*....|....*.
gi 2058207303 442 NQLKAYLENPYKMLLD 457
Cdd:PRK11856  396 KALKELLENPALLLLE 411
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 240-455 2.23e-94

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: 283.67  E-value: 2.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 240 MVKSMTEamkIPHFGYCDEYDVTKLVESRENLKVLAQKQGVKLTYMPIIVKAASQSLTAYPILNSSLDSACENITYKSSH 319
Cdd:pfam00198   1 MTESKQT---IPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 320 NIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGA 399
Cdd:pfam00198  78 NIGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2058207303 400 LGKIQVLPRFdAAGNLVKAHILTVSWSADHRVVDGVTMARFSNQLKAYLENPYKML 455
Cdd:pfam00198 158 VGRIRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 61-450 7.49e-85

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 273.03  E-value: 7.49e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  61 DIGEGikEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEEESPS 140
Cdd:PRK11854  213 DIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPA 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 141 PKDEKIET---------------NADAKTESIAQRTKVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHLN--- 202
Cdd:PRK11854  291 KQEAAAPApaaakaeapaaapaaKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKdav 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 203 -------MSSDNSNIVPEPSQIKAATVETVAEDKTVPITGFTKAMVKSMTEA-MKIPHFGYCDEYDVTKLVESRENLKVL 274
Cdd:PRK11854  371 kraeaapAAAAAGGGGPGLLPWPKVDFSKFGEIEEVELGRIQKISGANLHRNwVMIPHVTQFDKADITELEAFRKQQNAE 450

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 275 AQKQ--GVKLTYMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELN 352
Cdd:PRK11854  451 AEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELM 530

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 353 SLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDAAgNLVKAHILTVSWSADHRVV 432
Cdd:PRK11854  531 DISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGK-EFAPRLMLPLSLSYDHRVI 609

                         410
                  ....*....|....*...
gi 2058207303 433 DGVTMARFSNQLKAYLEN 450
Cdd:PRK11854  610 DGADGARFITIINDRLSD 627
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-456 5.11e-82

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: 263.27  E-value: 5.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  58 KLSDIGeGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEEE 137
Cdd:TIGR01348 120 TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPAT 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 138 SPSPKDEKIETNADAKTESIAQRTKVLT---------------------TPAVRRIAAQFKVDLSTVNATGKNGRLLKED 196
Cdd:TIGR01348 199 APAPASAQPAAQSPAATQPEPAAAPAAAkaqapapqqagtqnpakvdhaAPAVRRLAREFGVDLSAVKGTGIKGRILRED 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 197 LLSHLNMSSDNS------------NIVPEPSqikaATVETVAEDKTVPITGFTKAMVKSMTEA-MKIPHFGYCDEYDVTK 263
Cdd:TIGR01348 279 VQRFVKEPSVRAqaaaasaaggapGALPWPN----VDFSKFGEVEEVDMSRIRKISGANLTRNwTMIPHVTHFDKADITE 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 264 LVESRENLKVLAQKQGVKLTYMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKS 343
Cdd:TIGR01348 355 MEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKG 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 344 IIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDAAgNLVKAHILTV 423
Cdd:TIGR01348 435 ITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGK-EFEPRLMLPL 513

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2058207303 424 SWSADHRVVDGVTMARFSNQLKAYLENPYKMLL 456
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 58-458 2.11e-73

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: 236.55  E-value: 2.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  58 KLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEEE 137
Cdd:TIGR01347   4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 138 SPS---PKDEKIETNADAKTESIAQRTKVLTtPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHLnmSSDNSNIVPEP 214
Cdd:TIGR01347  84 PPAksgEEKEETPAASAAAAPTAAANRPSLS-PAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKT--EAPASAQPPAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 215 SQIKAATVETVAEDKTVPITGFTKAMVKSMTE-----AMkIPHFgycDEYDVTKLVESRENLKVLAQKQ-GVKLTYMPII 288
Cdd:TIGR01347 161 AAAAAAPAAATRPEERVKMTRLRQRIAERLKEaqnstAM-LTTF---NEVDMSAVMELRKRYKEEFEKKhGVKLGFMSFF 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 289 VKAASQSLTAYPILNSSLDSacENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQLSLSDL 368
Cdd:TIGR01347 237 VKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDM 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 369 SGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPrFDAAGNLVKAHILTVSWSADHRVVDGVTMARFSNQLKAYL 448
Cdd:TIGR01347 315 TGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELL 393

                         410
                  ....*....|
gi 2058207303 449 ENPYKMLLDL 458
Cdd:TIGR01347 394 EDPRRLLLDL 403
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 56-449 2.74e-70

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: 233.37  E-value: 2.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  56 PFKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDIN-----V 130
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGdanaaP 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 131 EDSGEEESPSPKDEKIETNAD-------------------AKTESIAQRTKVLT-------TPAVRRIAAQFKVDLSTVN 184
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEPAPDpaaraphaapdppapapapAKTAAPAAAAPVSSgdsgpyvTPLVRKLAKDKGVDLSTVK 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 185 ATGKNGRLLKEDLLSHLNMSSD------NSNIVPEPSQIKAATvETVAEDKTvPITGFTKAM-------VKSMTEAMKI- 250
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAAKAAEEaraaaaAPAAAAAPAAPAAAA-KPAEPDTA-KLRGTTQKMnrirqitADKTIESLQTs 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 251 PHFGYCDEYDVTKLVESRENLKV-LAQKQGVKLTYMPIIVKAASQSLTAYPILNSSLDSACENITYKSSHNIGVAMDTPN 329
Cdd:TIGR02927 366 AQLTQVHEVDMTRVAALRARAKNdFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPR 445

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 330 GLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRF 409
Cdd:TIGR02927 446 GLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRV 525

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2058207303 410 --DAAGNLVKA--HILTVSWSADHRVVDGVTMARFSNQLKAYLE 449
Cdd:TIGR02927 526 ikDEDGGESIAirSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
54-458 7.70e-69

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 224.71  E-value: 7.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  54 IVPfklsDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDS 133
Cdd:PRK05704    6 KVP----TLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 134 G--EEESPSPKDEKIETNADAKTESIAQRTKVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHLnmsSDNSNIV 211
Cdd:PRK05704   82 AgaAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAAL---AAAAAAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 212 PEPSQIKAATVETVAEDKT---VPITGFTKAMVKSMTE-----AMkIPHFgycDEYDVTKLVESRENLKVLAQKQ-GVKL 282
Cdd:PRK05704  159 AAPAAAAPAAAPAPLGARPeerVPMTRLRKTIAERLLEaqnttAM-LTTF---NEVDMTPVMDLRKQYKDAFEKKhGVKL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 283 TYMPIIVKAASQSLTAYPILNSSLDSacENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQ 362
Cdd:PRK05704  235 GFMSFFVKAVVEALKRYPEVNASIDG--DDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGK 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 363 LSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIgaLG--KIQVLPrfdAA--GNLVKAHILTVSWSADHRVVDG---- 434
Cdd:PRK05704  313 LSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAI--LGmhKIKERP---VAvnGQIVIRPMMYLALSYDHRIIDGkeav 387

                         410       420
                  ....*....|....*....|....*..
gi 2058207303 435 ---VTMarfsnqlKAYLENPYKMLLDL 458
Cdd:PRK05704  388 gflVTI-------KELLEDPERLLLDL 407
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 29-458 3.22e-67

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 220.71  E-value: 3.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  29 NVSSRIQKNHDIGLRCIHSTSILNK-IVPFKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGT 107
Cdd:PTZ00144   18 KGMFRRFSLRKLQPACSAHFSKSYFsIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 108 VTRLYHQVDQTALVGHPLVDInvedsgeEESPSPKDEKIETNADAKTESIAQRTKVLTTPAVRRIAAQFKVDLSTVNAtg 187
Cdd:PTZ00144   98 ITKIFAEEGDTVEVGAPLSEI-------DTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKP-- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 188 kngrllkedllshlnmssdnsnivPEPSQIKAATVETVAED----KTVPITgftkAMVKSMTEAMK--------IPHFGY 255
Cdd:PTZ00144  169 ------------------------PEPAPAAKPPPTPVARAdpreTRVPMS----RMRQRIAERLKasqntcamLTTFNE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 256 CDeydVTKLVESRENLKVLAQKQ-GVKLTYMPIIVKAASQSLTAYPILNSSLDSACenITYKSSHNIGVAMDTPNGLVVP 334
Cdd:PTZ00144  221 CD---MSALMELRKEYKDDFQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVP 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 335 VIKNVQNKSIIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIgaLGKIQVLPRFDAAGN 414
Cdd:PTZ00144  296 VIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAI--LGMHAIKKRPVVVGN 373

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2058207303 415 LVKAH-ILTVSWSADHRVVDGVTMARFSNQLKAYLENPYKMLLDL 458
Cdd:PTZ00144  374 EIVIRpIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 74-456 6.97e-63

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: 210.04  E-value: 6.97e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  74 WFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTR-LYHQVDQTALVGHPLV--------------DINVEDSGEEES 138
Cdd:TIGR01349  19 WLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKiLVPEGTKDVPVNKPIAvlveekedvadafkNYKLESSASPAP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 139 -PSPKDEKIETNADAKTESIAQRT----------------KVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHL 201
Cdd:TIGR01349  99 kPSEIAPTAPPSAPKPSPAPQKQSpepsspaplsdkesgdRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 202 NMSSDNSNIVPE---PSQIKAATVETVAEDKTVPITGFTKAMVKSMTEAMK-IPHFGYCDEYDVTKLVESRENLKVLAQK 277
Cdd:TIGR01349 179 PQSPASANQQAAattPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVSIECNVDKLLALRKELNAMASE 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 278 QgVKLTYMPIIVKAASQSLTAYPILNSSLDSacENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDK 357
Cdd:TIGR01349 259 V-YKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKR 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 358 GSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALG--KIQVLPRFDAAGNLVKAHILTVSWSADHRVVDGV 435
Cdd:TIGR01349 336 ARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGavEDVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGA 415

                         410       420
                  ....*....|....*....|.
gi 2058207303 436 TMARFSNQLKAYLENPYKMLL 456
Cdd:TIGR01349 416 VGAEFLKSFKKYLENPIEMLL 436
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 162-451 6.66e-58

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 193.09  E-value: 6.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 162 KVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLL----SHLNMSSDNSNIVPEPSQIKAATVETVA-----EDKTVP 232
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVEnfikSLKSAPTPAEAASVSSAQQAAKTAAPAAappklEGKREK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 233 ITGFTKAMVKSMTEAMK-IPHFGYCDEYDVTKLVESRENLKVLAQK-QGVKLTYMPIIVKAASQSLTAYPILNSSLDSAC 310
Cdd:PRK11857   81 VAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKDPVLKtEGVKLTFLPFIAKAILIALKEFPIFAAKYDEAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 311 ENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPII 390
Cdd:PRK11857  161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2058207303 391 FPPQVSIGALGKIQVLPRFDaAGNLVKAHILTVSWSADHRVVDGVTMARFSNQLKAYLENP 451
Cdd:PRK11857  241 NYPELAIAGVGAIIDKAIVK-NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 74-456 6.88e-49

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 175.04  E-value: 6.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  74 WFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTAL-VGHpLVDINVEDSGE----------------- 135
Cdd:PLN02744  132 WLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIkVGE-VIAITVEEEEDigkfkdykpsssaapaa 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 136 ----EESPSPKDEKIETNADA------KTESIAQR-TKVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHLnmS 204
Cdd:PLN02744  211 pkakPSPPPPKEEEVEKPASSpepkasKPSAPPSSgDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYL--A 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 205 SDNSNIVPEPSQIKAATvetvAEDKT-VPITGFTKAMVKSMTEAMK-IPHFGYCDEYDVTKLVESRENLKVLAQKQGVK- 281
Cdd:PLN02744  289 SGGKGATAPPSTDSKAP----ALDYTdIPNTQIRKVTASRLLQSKQtIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKk 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 282 LTYMPIIVKAASQSLTAYPILNSSLDSacENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKG 361
Cdd:PLN02744  365 ISVNDLVIKAAALALRKVPQCNSSWTD--DYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKAREN 442

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 362 QLSLSDLSGGTFTISNIGivGGTYTK---PIIFPPQVSIGALGKIQ--VLPRfDAAGNLVKAHILTVSWSADHRVVDGVT 436
Cdd:PLN02744  443 SLKPEDYEGGTFTVSNLG--GPFGIKqfcAIINPPQSAILAVGSAEkrVIPG-SGPDQYNFASFMSVTLSCDHRVIDGAI 519

                         410       420
                  ....*....|....*....|
gi 2058207303 437 MARFSNQLKAYLENPYKMLL 456
Cdd:PLN02744  520 GAEWLKAFKGYIENPESMLL 539
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 47-458 8.73e-42

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 154.53  E-value: 8.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  47 STSILNKIVPfklsDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLV 126
Cdd:PLN02226   88 SGDTVEAVVP----HMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 127 DINV-EDSGEEESPSPK-DEKIETNADAKTESiAQRTKVLTTPAVRRIAAQfkvdlstvnatgkngrllkedllshlnms 204
Cdd:PLN02226  164 IISKsEDAASQVTPSQKiPETTDPKPSPPAED-KQKPKVESAPVAEKPKAP----------------------------- 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 205 sdnSNIVPEPSQIKAATVETVAEDKTVPITGFTKAMVKSMTEAMK-IPHFGYCDEYDVTKLVESRENLK-VLAQKQGVKL 282
Cdd:PLN02226  214 ---SSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNtFALLTTFNEVDMTNLMKLRSQYKdAFYEKHGVKL 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 283 TYMPIIVKAASQSLTAYPILNSSLDSacENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQ 362
Cdd:PLN02226  291 GLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGT 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 363 LSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFdAAGNLVKAHILTVSWSADHRVVDGVTMARFSN 442
Cdd:PLN02226  369 ISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTYDHRLIDGREAVYFLR 447

                         410
                  ....*....|....*.
gi 2058207303 443 QLKAYLENPYKMLLDL 458
Cdd:PLN02226  448 RVKDVVEDPQRLLLDI 463
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 155-456 2.32e-37

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 139.66  E-value: 2.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 155 ESIAQRTKVLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLLSHLNMSSDNSNIVPEPSQIKAATVETVA----EDKT 230
Cdd:PRK14843   41 ETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVtpygEIER 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 231 VPITGFTKAMVKSMTEA-MKIPHFGYCDEYDVTKLVESREN-LKVLAQKQGVKLTYMPIIVKAASQSLTAYPILNSSLDS 308
Cdd:PRK14843  121 IPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303 309 ACENITYKSSHNIGVAMDTPNGLVVPVIKNVQNKSIIEIAKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKP 388
Cdd:PRK14843  201 DGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGP 280

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2058207303 389 IIFPPQVSIGALGKIQVLPRFdAAGNLVKAHILTVSWSADHRVVDGVTMARFSNQLKAYLENPYKMLL 456
Cdd:PRK14843  281 IINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 55-128 1.18e-24

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: 96.70  E-value: 1.18e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2058207303  55 VPFKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDI 128
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 54-128 7.31e-21

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: 86.27  E-value: 7.31e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058207303  54 IVPFKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDI 128
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 55-128 6.20e-17

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: 74.94  E-value: 6.20e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2058207303  55 VPFKLSDIGEGIKEVVVkEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDI 128
Cdd:pfam00364   1 TEIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 163-198 2.24e-11

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: 58.08  E-value: 2.24e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2058207303 163 VLTTPAVRRIAAQFKVDLSTVNATGKNGRLLKEDLL 198
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 212-440 5.36e-11

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 64.91  E-value: 5.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  212 PEPSQIKAATVETVAEDKTVPITGFTKAMVKSMTEAMKIPhfgycdeydvT---------KLVEsrENLKV----LAQKQ 278
Cdd:PRK12270    99 PPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------TatsvravpaKLLI--DNRIVinnhLKRTR 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  279 GVKLTYMPIIVKAASQSLTAYPILNSSLDSacenITYKSSH------NIGVAMDT--PNG---LVVPVIKNVQNKSIIEI 347
Cdd:PRK12270   167 GGKVSFTHLIGYALVQALKAFPNMNRHYAE----VDGKPTLvtpahvNLGLAIDLpkKDGsrqLVVPAIKGAETMDFAQF 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  348 AKELNSLQDKGSKGQLSLSDLSGGTFTISNIGIVGGTYTKPIIFPPQVSIGALGKIQVLPRFDAAGNLVKAH-----ILT 422
Cdd:PRK12270   243 WAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAElgiskVMT 322

                          250
                   ....*....|....*...
gi 2058207303  423 VSWSADHRVVDGVTMARF 440
Cdd:PRK12270   323 LTSTYDHRIIQGAESGEF 340
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 58-158 8.35e-09

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 57.70  E-value: 8.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  58 KLSDIGEGikEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDINVEDSGEEE 137
Cdd:PRK11854    6 KVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAADA 83

                          90       100
                  ....*....|....*....|.
gi 2058207303 138 SPSPKDEKIETNADAKTESIA 158
Cdd:PRK11854   84 APAQAEEKKEAAPAAAPAAAA 104
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 59-128 2.85e-07

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: 47.82  E-value: 2.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  59 LSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDI 128
Cdd:cd06663     4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 54-169 1.17e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 50.33  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058207303  54 IVPFKLSDIGEGIKEVVVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPL-------- 125
Cdd:PRK14875    2 ITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLavvadaev 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2058207303 126 --VDI----------NVEDSGEEESPSPKDEKIETnaDAKTESIAQRTKVLTTPAV 169
Cdd:PRK14875   82 sdAEIdafiapfarrFAPEGIDEEDAGPAPRKARI--GGRTVRYLRLGEGDGTPVV 135
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 70-128 5.67e-05

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: 40.86  E-value: 5.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2058207303  70 VVKEWFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRLYHQVDQTALVGHPLVDI 128
Cdd:cd06850     9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 74-111 1.79e-03

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 40.67  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2058207303  74 WFVKEGDKVQQFDNICEVQSDKATVTITSRYDGTVTRL 111
Cdd:PRK11892   22 WLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI 59
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH