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Conserved domains on  [gi|1622825563|ref|XP_028700317|]
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lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial isoform X4 [Macaca mulatta]

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

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List of domain hits

 Name Accession Description Interval E-value
PLN02528 super family cl33511
2-oxoisovalerate dehydrogenase E2 component
 87-502 1.21e-180

2-oxoisovalerate dehydrogenase E2 component


The actual alignment was detected with superfamily member PLN02528:

Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 512.73  E-value: 1.21e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  87 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 166
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 167 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 241
Cdd:PLN02528   81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 242 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 321
Cdd:PLN02528  160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 322 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 401
Cdd:PLN02528  236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 402 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 481
Cdd:PLN02528  316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395

                         410       420
                  ....*....|....*....|.
gi 1622825563 482 RFSNLWKSYLENPAFMLLDLK 502
Cdd:PLN02528  396 RFCNEWKSYVEKPELLMLHMR 416
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 87-502 1.21e-180

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 512.73  E-value: 1.21e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  87 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 166
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 167 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 241
Cdd:PLN02528   81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 242 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 321
Cdd:PLN02528  160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 322 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 401
Cdd:PLN02528  236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 402 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 481
Cdd:PLN02528  316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395

                         410       420
                  ....*....|....*....|.
gi 1622825563 482 RFSNLWKSYLENPAFMLLDLK 502
Cdd:PLN02528  396 RFCNEWKSYVEKPELLMLHMR 416
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 287-498 4.18e-97

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: 292.14  E-value: 4.18e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 287 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 365
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 366 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGS 445
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622825563 446 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 498
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 78-499 1.29e-74

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: 245.17  E-value: 1.29e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  78 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 157
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 158 IETEALKDSEEDVVE-------------------------TPAVSHDEHTHQEIKGRKtlATPAVRRLAMENNIKLSEVV 212
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGTQNPAKVDH--AAPAVRRLAREFGVDLSAVK 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 213 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 291
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 292 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 371
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 372 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIgaLGSIKAI-- 449
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622825563 450 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 499
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 85-158 4.19e-25

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: 98.25  E-value: 4.19e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825563  85 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 158
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 85-158 1.88e-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: 88.20  E-value: 1.88e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825563  85 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 158
Cdd:COG0508     3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 87-502 1.21e-180

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 512.73  E-value: 1.21e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  87 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 166
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 167 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 241
Cdd:PLN02528   81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 242 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 321
Cdd:PLN02528  160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 322 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 401
Cdd:PLN02528  236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 402 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 481
Cdd:PLN02528  316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395

                         410       420
                  ....*....|....*....|.
gi 1622825563 482 RFSNLWKSYLENPAFMLLDLK 502
Cdd:PLN02528  396 RFCNEWKSYVEKPELLMLHMR 416
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 75-499 1.30e-157

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 458.90  E-value: 1.30e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  75 KTTAALRGQVVQFKLSDIGEgIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKP 154
Cdd:PRK11855  110 AAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 155 LVDIETEALKDSEEDVVETPAVSHDEHTHQE------------------IKGRKTLATPAVRRLAMENNIKLSEVVGSGK 216
Cdd:PRK11855  189 LVVIEVAAAAPAAAAAPAAAAPAAAAAAAPApapaaaaapaaaapaaaaAPGKAPHASPAVRRLARELGVDLSQVKGTGK 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 217 DGRILKEDILNYLEkqtGAILPPSPKAEIMPPPPKPKDMTIPIPVskpPVFT--GKDKTEPIKGFQKAMVKTMSAAL-KI 293
Cdd:PRK11855  269 KGRITKEDVQAFVK---GAMSAAAAAAAAAAAAGGGGLGLLPWPK---VDFSkfGEIETKPLSRIKKISAANLHRSWvTI 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 294 PHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQG 373
Cdd:PRK11855  343 PHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNG 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 374 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPrFN 453
Cdd:PRK11855  423 LVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VW 501

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1622825563 454 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 499
Cdd:PRK11855  502 DGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 84-500 3.09e-133

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 391.85  E-value: 3.09e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  84 VVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE-- 161
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEge 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 162 --------------ALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 227
Cdd:PRK11856   82 aeaaaaaeaapeapAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 228 YLEKQTGAILPPSPKaeimppppkpkdmtipiPVSKPPVFTGKDKTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTE 306
Cdd:PRK11856  162 AAAAAAPAAAAAAAA-----------------AAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTA 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 307 LVKLREELKPIAfargIKLSFMPFFLKAVSLGLLQFPILNASVDEncQNITYKASHNIGIAMDTEQGLIVPNVKNVQICS 386
Cdd:PRK11856  225 LLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKS 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 387 IFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNV 466
Cdd:PRK11856  299 LFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPL 377

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1622825563 467 SWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD 500
Cdd:PRK11856  378 SLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 287-498 4.18e-97

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: 292.14  E-value: 4.18e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 287 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 365
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 366 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGS 445
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622825563 446 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 498
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 82-493 9.18e-84

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 271.49  E-value: 9.18e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  82 GQVVQFKLSDIGEGirEVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE 161
Cdd:PRK11854  204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 162 --------ALKDSEEDV---------VETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKED 224
Cdd:PRK11854  282 gaapaaapAKQEAAAPApaaakaeapAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 225 ILNYLEK-----QTGAILPPSPKAEIMPpppkpkdmtIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAAL-KIPHFGY 298
Cdd:PRK11854  362 VQAYVKDavkraEAAPAAAAAGGGGPGL---------LPWPKVDFSKF-GEIEEVELGRIQKISGANLHRNWvMIPHVTQ 431

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 299 CDEVDLTELVKLREELKPIAFAR--GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIV 376
Cdd:PRK11854  432 FDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVV 511

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 377 PNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKg 456
Cdd:PRK11854  512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGK- 590

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1622825563 457 EVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLEN 493
Cdd:PRK11854  591 EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 78-499 1.29e-74

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: 245.17  E-value: 1.29e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  78 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 157
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 158 IETEALKDSEEDVVE-------------------------TPAVSHDEHTHQEIKGRKtlATPAVRRLAMENNIKLSEVV 212
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGTQNPAKVDH--AAPAVRRLAREFGVDLSAVK 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 213 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 291
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 292 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 371
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 372 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIgaLGSIKAI-- 449
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622825563 450 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 499
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 85-501 3.87e-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: 236.94  E-value: 3.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  85 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALK 164
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 165 D------SEEDVVETPAVShdEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILP 238
Cdd:TIGR01347  81 TaappakSGEEKEETPAAS--AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 239 PSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKGFQKAMVKTM-----SAALkIPHFgycDEVDLTELVKLREE 313
Cdd:TIGR01347 159 AAAAAA-----------------AAPAAATRPEERVKMTRLRQRIAERLkeaqnSTAM-LTTF---NEVDMSAVMELRKR 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 314 LKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIAT 392
Cdd:TIGR01347 218 YKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 393 ELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRfnqkgeVYKAQIVN-----VS 467
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV------AVNGQIEIrpmmyLA 369

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1622825563 468 WSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 501
Cdd:TIGR01347 370 LSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 190-494 2.46e-69

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 223.90  E-value: 2.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 190 KTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAilpPSPKAEIMPPPPKPKDMTiPIPVSKPPVFTG 269
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT-AAPAAAPPKLEG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 270 KdkTEPIKGFQKAMVKTMSAALK-IPHFGYCDEVDLTELVKLREELK-PIAFARGIKLSFMPFFLKAVSLGLLQFPILNA 347
Cdd:PRK11857   77 K--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 348 SVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGT 427
Cdd:PRK11857  155 KYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825563 428 YTKPVILPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENP 494
Cdd:PRK11857  235 YGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
88-501 1.26e-68

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 225.48  E-value: 1.26e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  88 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEA----L 163
Cdd:PRK05704    6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAaagaA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 164 KDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKA 243
Cdd:PRK05704   86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 244 eimppppkpkdmtipiPVSKPPVFTGK-DKTEPIKGFQK-------------AMVKTmsaalkiphFgycDEVDLTELVK 309
Cdd:PRK05704  166 ----------------PAAAPAPLGARpEERVPMTRLRKtiaerlleaqnttAMLTT---------F---NEVDMTPVMD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 310 LREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIF 388
Cdd:PRK05704  218 LRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFA 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 389 DIATELNRLQKLGSVGQLSTTDLTGGTFTLSNigsiGGTY----TKPVILPPEVAIgaLG--SIKAIPRfnqkgeVYKAQ 462
Cdd:PRK05704  296 EIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERPV------AVNGQ 363

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622825563 463 IVN-----VSWSADHRVIDGA-------TMsrfsnlwKSYLENPAFMLLDL 501
Cdd:PRK05704  364 IVIrpmmyLALSYDHRIIDGKeavgflvTI-------KELLEDPERLLLDL 407
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 82-496 2.48e-65

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: 221.42  E-value: 2.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  82 GQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI--- 158
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgda 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 159 --------ETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLA----------------------TPAVRRLAMENNIKL 208
Cdd:TIGR02927 204 naapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVDL 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 209 SEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKAeimppppKPKDMTIPIPVSKPP-VFTGK--DKTEPIKGFQKAMVK 285
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPA-------AAAAPAAPAAAAKPAePDTAKlrGTTQKMNRIRQITAD 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 286 TMSAALKI-PHFGYCDEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHN 363
Cdd:TIGR02927 357 KTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEH 436

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 364 IGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGAL 443
Cdd:TIGR02927 437 VGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGT 516

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825563 444 GSIKAIPRF---NQKGEVYKA-QIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAF 496
Cdd:TIGR02927 517 GAIVKRPRVikdEDGGESIAIrSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 96-499 1.93e-61

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: 207.34  E-value: 1.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  96 IREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY--NLDDIAyVGKPLV-------DIET------ 160
Cdd:TIGR01349  11 MTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVpeGTKDVP-VNKPIAvlveekeDVADafknyk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 161 ------EALKDSEE--------------DVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRI 220
Cdd:TIGR01349  90 lessasPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 221 LKEDILNYLEKQTgAILPPSPKAEIMPPPPKPkdmtipipvskPPVFTGKDKTEPIKGFQKAMVKTMSAALK-IPHFGYC 299
Cdd:TIGR01349 170 VKKDIESFVPQSP-ASANQQAAATTPATYPAA-----------APVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 300 DEVDLTELVKLREELKPIAFARgIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNV 379
Cdd:TIGR01349 238 IECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVATPDGLITPIV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 380 KNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSI--KAIPRFNQKGE 457
Cdd:TIGR01349 315 RNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVDNDEEKG 394

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1622825563 458 VYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 499
Cdd:TIGR01349 395 FAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 88-501 7.43e-60

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 202.61  E-value: 7.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  88 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSE 167
Cdd:PTZ00144   48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 168 EdvVETPAVSHDEHTHQEIKGRKTLATPAvrrlamennIKLSEVVGSGKDgrilkedilnylEKQTGAILPPSPKAEImp 247
Cdd:PTZ00144  128 A--PAAAAAAKAEKTTPEKPKAAAPTPEP---------PAASKPTPPAAA------------KPPEPAPAAKPPPTPV-- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 248 pppkpkDMTIPIPVSKPPVFTGKDKTEPIKGFQK--AMVKTMsaalkiphfgycDEVDLTELVKLREELKPIAFAR-GIK 324
Cdd:PTZ00144  183 ------ARADPRETRVPMSRMRQRIAERLKASQNtcAMLTTF------------NECDMSALMELRKEYKDDFQKKhGVK 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 325 LSFMPFFLKAVSLGLLQFPILNASVDENCqnITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVG 404
Cdd:PTZ00144  245 LGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNN 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 405 QLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIK--AIPRFNQkgeVYKAQIVNVSWSADHRVIDGATMSR 482
Cdd:PTZ00144  323 KLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKkrPVVVGNE---IVIRPIMYLALTYDHRLIDGRDAVT 399

                         410
                  ....*....|....*....
gi 1622825563 483 FSNLWKSYLENPAFMLLDL 501
Cdd:PTZ00144  400 FLKKIKDLIEDPARMLLDL 418
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 98-499 5.21e-46

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 168.49  E-value: 5.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  98 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY------------------NLDDIAYVG--KPLVD 157
Cdd:PLN02744  126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKgdgakeikvgeviaitveEEEDIGKFKdyKPSSS 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 158 IETEALKDSE------EDVVETPAVSHDEHTHQE----IKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 227
Cdd:PLN02744  206 AAPAAPKAKPsppppkEEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIED 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 228 YLEKQ-TGAILPPSPKAEIMPPPPkpkdmtIPIPVSKPPVFTGKdktepikgfqkamvKTMSAALKIPHFGYCDEVDLTE 306
Cdd:PLN02744  286 YLASGgKGATAPPSTDSKAPALDY------TDIPNTQIRKVTAS--------------RLLQSKQTIPHYYLTVDTRVDK 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 307 LVKLREELKPIAFARGIK-LSFMPFFLKAVSLGLLQFPILNAS-VDE---NCQNItykashNIGIAMDTEQGLIVPNVKN 381
Cdd:PLN02744  346 LMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDDyirQYHNV------NINVAVQTENGLYVPVVKD 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 382 VQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGS-IGGTYTKPVILPPEVAIGALGSI--KAIPRfNQKGEV 458
Cdd:PLN02744  420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAekRVIPG-SGPDQY 498

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1622825563 459 YKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 499
Cdd:PLN02744  499 NFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 194-499 5.18e-37

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 139.66  E-value: 5.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 194 TPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYL--EKQTGAILPPSPKAEIMPpppkpkdmtipIPVSKPPvfTGKD 271
Cdd:PRK14843   52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLpeNIENDSIKSPAQIEKVEE-----------VPDNVTP--YGEI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 272 KTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREE-LKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASV 349
Cdd:PRK14843  119 ERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 350 DENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYT 429
Cdd:PRK14843  199 TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSF 278

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 430 KPVILPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 499
Cdd:PRK14843  279 GPIINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 64-501 2.31e-36

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 140.28  E-value: 2.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  64 SFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY 143
Cdd:PLN02226   71 SLVSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 144 NLDDIAYVGKPLVDIETEALKDSE----EDVVETPAVSHDEHTHQEIKGRKTLATPAvrrlamenniklsevvgsgkdgr 219
Cdd:PLN02226  151 KEGDTVEPGTKVAIISKSEDAASQvtpsQKIPETTDPKPSPPAEDKQKPKVESAPVA----------------------- 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 220 ilkedilnylEKQTGAILPPSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKgfQKAMVKTMSAALKIPHFGYC 299
Cdd:PLN02226  208 ----------EKPKAPSSPPPPKQS-----------------AKEPQLPPKERERRVP--MTRLRKRVATRLKDSQNTFA 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 300 -----DEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQG 373
Cdd:PLN02226  259 llttfNEVDMTNLMKLRSQYKDAFYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKG 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563 374 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFn 453
Cdd:PLN02226  337 LVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV- 415

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1622825563 454 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 501
Cdd:PLN02226  416 VGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 85-158 4.19e-25

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: 98.25  E-value: 4.19e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825563  85 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 158
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 85-158 1.88e-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: 88.20  E-value: 1.88e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825563  85 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 158
Cdd:COG0508     3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 85-158 1.09e-20

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: 85.73  E-value: 1.09e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825563  85 VQFKLSDIGEGIREVtVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 158
Cdd:pfam00364   1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 192-226 2.09e-14

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: 66.94  E-value: 2.09e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622825563 192 LATPAVRRLAMENNIKLSEVVGSGKDGRILKEDIL 226
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 258-483 1.06e-11

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 67.61  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  258 PIPVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPhfgycdevdlTEL------VKLREELKPI-----AFARGIKLS 326
Cdd:PRK12270   102 AAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------TATsvravpAKLLIDNRIVinnhlKRTRGGKVS 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  327 FMPFFLKAVSLGLLQFPILNASVDE--NCQNITYKASHNIGIAMDTEQ-----GLIVPNVKNVQICSIFDIATELNRLQK 399
Cdd:PRK12270   172 FTHLIGYALVQALKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVR 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  400 LGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKGEVYKAQ-----IVNVSWSADHRV 474
Cdd:PRK12270   252 RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAElgiskVMTLTSTYDHRI 331


                   ....*....
gi 1622825563  475 IDGATMSRF 483
Cdd:PRK12270   332 IQGAESGEF 340
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 93-238 3.39e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 61.50  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  93 GEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVe 172
Cdd:PRK14875   11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEIDAF- 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825563 173 tpavshdehthqeikgrktlATPAVRRLAMEnNIKLSEVVGSGKDGRILKEDIlNYLEKQTGAILP 238
Cdd:PRK14875   90 --------------------IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 89-158 3.88e-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: 53.21  E-value: 3.88e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825563  89 LSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 158
Cdd:cd06663     4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 100-158 1.05e-04

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: 40.48  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825563 100 TVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 158
Cdd:cd06850     9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 98-141 2.12e-03

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 40.67  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622825563  98 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKL 141
Cdd:PRK11892   16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI 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.
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