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Conserved domains on  [gi|1716950954|ref|NP_001358971|]
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dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial isoform 13 [Homo sapiens]

Protein Classification

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase( domain architecture ID 11492247)

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (E2) ; the pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle

CATH:  2.40.50.100
EC:  2.3.1.12
Gene Ontology:  GO:0045254|GO:0016746

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 67-493 0e+00

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: 649.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  67 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 146
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 147 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 222
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 223 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 299
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 300 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 379
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 380 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 458
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716950954 459 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 67-493 0e+00

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: 649.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  67 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 146
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 147 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 222
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 223 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 299
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 300 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 379
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 380 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 458
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716950954 459 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 58-493 2.34e-173

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 498.61  E-value: 2.34e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  58 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 137
Cdd:PLN02744  106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 138 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 217
Cdd:PLN02744  186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 218 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSID 297
Cdd:PLN02744  266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVD 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 298 VNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 375
Cdd:PLN02744  341 TRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 376 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 454
Cdd:PLN02744  421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1716950954 455 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PLN02744  501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 282-492 2.14e-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: 284.82  E-value: 2.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 282 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 358
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 359 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 438
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716950954 439 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 492
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 65-139 9.85e-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: 97.09  E-value: 9.85e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716950954  65 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 139
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 66-140 3.55e-20

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: 84.35  E-value: 3.55e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716950954  66 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 140
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 67-493 0e+00

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: 649.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  67 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 146
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 147 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 222
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 223 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 299
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 300 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 379
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 380 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 458
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716950954 459 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 58-493 2.34e-173

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 498.61  E-value: 2.34e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  58 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 137
Cdd:PLN02744  106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 138 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 217
Cdd:PLN02744  186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 218 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSID 297
Cdd:PLN02744  266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVD 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 298 VNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 375
Cdd:PLN02744  341 TRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 376 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 454
Cdd:PLN02744  421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1716950954 455 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PLN02744  501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 66-493 6.32e-152

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 439.23  E-value: 6.32e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  66 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKEAD 145
Cdd:PRK11856    4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 146 ISAFADYRPTEVTDLKPQVPPPtpppvaavpptpqPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTG 225
Cdd:PRK11856   83 EAAAAAEAAPEAPAPEPAPAAA-------------AAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 226 PDGRITKKDIDSFVPSKVAPAPAAVVPPTGPgmAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLL 305
Cdd:PRK11856  150 PGGRITKEDVEAAAAAAAPAAAAAAAAAAAP--PAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 306 VRKELNKILEgrsKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAN 385
Cdd:PRK11856  228 LRKQLKAIGV---KLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAR 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 386 DVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCD 465
Cdd:PRK11856  305 EIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE--IVVRKVMPLSLSFD 382

                         410       420
                  ....*....|....*....|....*...
gi 1716950954 466 HRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PRK11856  383 HRVIDGADAARFLKALKELLENPALLLL 410
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 282-492 2.14e-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: 284.82  E-value: 2.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 282 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 358
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 359 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 438
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716950954 439 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 492
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 79-493 1.97e-83

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 267.84  E-value: 1.97e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  79 GTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEGYLAKILVPEGTRdVPLGTPLcIIVEKEADISAFADYRPTE 156
Cdd:PRK11855  133 VEVIEWLVKVGDTVEEDQSLITVETDKATM--EIpsPVAGVVKEIKVKVGDK-VSVGSLL-VVIEVAAAAPAAAAAPAAA 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 157 VTDLKPQVPPPTPPPVaavpptpqplAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDID 236
Cdd:PRK11855  209 APAAAAAAAPAPAPAA----------AAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQ 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 237 SFV-----PSKVAPAPAAVVPPTGPGMAPVPTGVFTD------IPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLL 305
Cdd:PRK11855  279 AFVkgamsAAAAAAAAAAAAGGGGLGLLPWPKVDFSKfgeietKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 306 VRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT---VIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVE 381
Cdd:PRK11855  359 LRKQLKKEAEKAGvKLTMLPFFIKAVVAALKEFPVFNASLDEDgdeLTYKKYF-NIGFAVDTPNGLVVPVIKDVDKKSLL 437

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 382 TIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVT 461
Cdd:PRK11855  438 EIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMK--PVWDGKEFVPRLMLPLS 515

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1716950954 462 LSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PRK11855  516 LSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 67-493 4.25e-76

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: 244.64  E-value: 4.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  67 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEkeadi 146
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEE----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 147 SAFADYRPTEVTDLKPqvppptpppvaavpptpqplAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGP 226
Cdd:TIGR01347  77 GNDATAAPPAKSGEEK--------------------EETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 227 DGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPvpTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLV 306
Cdd:TIGR01347 137 TGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAA--TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMEL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 307 RKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIA 384
Cdd:TIGR01347 215 RKRYKEEFEKKHgvKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIE 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 385 NDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVpADNEKgFDVASMMSVTLSC 464
Cdd:TIGR01347 295 KEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQ-IEIRPMMYLALSY 372

                         410       420
                  ....*....|....*....|....*....
gi 1716950954 465 DHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:TIGR01347 373 DHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
67-493 1.72e-68

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 224.71  E-value: 1.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  67 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEGYLAKILVPEGTrDVPLGTPLCIIVEKEA 144
Cdd:PRK05704    5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVL--EVpaPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 145 DISAFADYRPTEvtdlkpqvppptpppvaavpptPQPLAPTPSAPCPATPAGPKGrvfVSPLAKKLAVEKGIDLTQVKGT 224
Cdd:PRK05704   82 AGAAAAAAAAAA----------------------AAAAAPAQAQAAAAAEQSNDA---LSPAARKLAAENGLDASAVKGT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 225 GPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIphyylSI-----DVN 299
Cdd:PRK05704  137 GKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTT-----AMlttfnEVD 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 300 MGEVLLVRKELNKILEGR--SKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHI 377
Cdd:PRK05704  212 MTPVMDLRKQYKDAFEKKhgVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQ 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 378 KGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASM 457
Cdd:PRK05704  292 LSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ--IVIRPM 369

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1716950954 458 MSVTLSCDHRVVDG--AVGaqWLAEFRKYLEKPITMLL 493
Cdd:PRK05704  370 MYLALSYDHRIIDGkeAVG--FLVTIKELLEDPERLLL 405
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 69-493 1.30e-62

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 209.92  E-value: 1.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  69 LPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIvekeaDISA 148
Cdd:PTZ00144   49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEI-----DTGG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 149 FADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPkgrvfvSPLAKKLAvekgidlTQVKGTGPDG 228
Cdd:PTZ00144  123 APPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEP------APAAKPPP-------TPVARADPRE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 229 ritkkdidsfvpskvapapaavvpptgpgmapvptgvfTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRK 308
Cdd:PTZ00144  190 --------------------------------------TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 309 ELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAND 386
Cdd:PTZ00144  232 EYKDDFQKKHgvKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 387 VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCDH 466
Cdd:PTZ00144  312 LADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE--IVIRPIMYLALTYDH 389

                         410       420
                  ....*....|....*....|....*..
gi 1716950954 467 RVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PTZ00144  390 RLIDGRDAVTFLKKIKDLIEDPARMLL 416
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 79-493 6.45e-62

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 213.33  E-value: 6.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  79 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTpLCIIVEKEADISAFAdyrPTEVT 158
Cdd:PRK11854  219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAAPAAA---PAKQE 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 159 DLKPQVPPPTPPPVAAvpptpqplAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSF 238
Cdd:PRK11854  294 AAAPAPAAAKAEAPAA--------APAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 239 V----PSKVAPAPAAVVPPTGPGMAPVPT------GVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRK 308
Cdd:PRK11854  366 VkdavKRAEAAPAAAAAGGGGPGLLPWPKvdfskfGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRK 445

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 309 ELNKILEGRS---KISVNDFIIKASALACLKVPEANSSWMD---TVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVET 382
Cdd:PRK11854  446 QQNAEAEKRKlgvKITPLVFIMKAVAAALEQMPRFNSSLSEdgqRLTLKKYV-NIGIAVDTPNGLVVPVFKDVNKKGIIE 524

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 383 IANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVTL 462
Cdd:PRK11854  525 LSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAME--PVWNGKEFAPRLMLPLSL 602

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1716950954 463 SCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PRK11854  603 SYDHRVIDGADGARFITIINDRLSDIRRLVL 633
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 55-486 1.06e-58

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: 203.32  E-value: 1.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  55 QAPGSSYPPH------MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEgTR 128
Cdd:TIGR02927 111 EAPAPAAPQAggsgeaTEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DD 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 129 DVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPK----GRVFVS 204
Cdd:TIGR02927 190 TVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVssgdSGPYVT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 205 PLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSfvPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIP-------------I 271
Cdd:TIGR02927 270 PLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLA--AAKAAEEARAAAAAPAAAAAPAAPAAAAKPAepdtaklrgttqkM 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 272 SNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTV- 348
Cdd:TIGR02927 348 NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNgvNLTFLPFFVQAVTEALKAHPNVNASYNAETk 427

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 349 -IRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIIN 427
Cdd:TIGR02927 428 eVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILN 507

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716950954 428 PPQACILAIGASEDKLVPADNEKGFDVASMMSVT---LSCDHRVVDGAVGAQWLAEFRKYLE 486
Cdd:TIGR02927 508 PPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCylpLTYDHRLVDGADAGRFLTTIKKRLE 569
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 87-493 1.95e-58

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: 202.03  E-value: 1.95e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  87 KVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPp 166
Cdd:TIGR01348 138 KVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAAT- 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 167 ptpppvaavpptpQPLAPTPSAPCPATPAGPKGR--------VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSF 238
Cdd:TIGR01348 216 -------------QPEPAAAPAAAKAQAPAPQQAgtqnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRF 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 239 VPSKVAPAPAAVVPPTG--PGMAPVPTGVFT------DIPISNIRRVIAQRLMQSKQTIPH--YYLSIDVNMGEVLLVRK 308
Cdd:TIGR01348 283 VKEPSVRAQAAAASAAGgaPGALPWPNVDFSkfgeveEVDMSRIRKISGANLTRNWTMIPHvtHFDKADITEMEAFRKQQ 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 309 ELNKILEGrSKISVNDFIIKASALACLKVPEANSSWM---DTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIAN 385
Cdd:TIGR01348 363 NAAVEKEG-VKLTVLHILMKAVAAALKKFPKFNASLDlggEQLILKKYV-NIGVAVDTPNGLLVPVIKDVDRKGITELAL 440

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 386 DVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILaiGASEDKLVPADNEKGFDVASMMSVTLSCD 465
Cdd:TIGR01348 441 ELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAIL--GVSKSGMEPVWNGKEFEPRLMLPLSLSYD 518

                         410       420
                  ....*....|....*....|....*...
gi 1716950954 466 HRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:TIGR01348 519 HRVIDGADAARFTTYICESLADIRRLLL 546
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 201-493 1.08e-57

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 194.74  E-value: 1.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 201 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP-SKVAPAPAAVVPPTGPGMAP---VPTGVFTDIPISNIRR 276
Cdd:PRK14843   49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPeNIENDSIKSPAQIEKVEEVPdnvTPYGEIERIPMTPMRK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 277 VIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGR-SKISVNDFIIKASALACLKVPEANSSWMD---TVIRQ 351
Cdd:PRK14843  129 VIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATgKKTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIITH 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 352 NHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQA 431
Cdd:PRK14843  209 NYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716950954 432 CILAIGASEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PRK14843  288 AILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 83-493 2.24e-51

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 179.92  E-value: 2.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  83 RWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGtrD-VPLGTPLC-IIVEKEADISAFADYRPTEVTDL 160
Cdd:PLN02528   17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG--DiVKVGETLLkIMVEDSQHLRSDSLLLPTDSSNI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 161 KpqvppptpppvaavpptpqplaptpSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP 240
Cdd:PLN02528   95 V-------------------------SLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 241 SK-VAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIA----QRLMQSKQT----IPHYYLSIDVNMGEVLLVRKELN 311
Cdd:PLN02528  150 QKgVVKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPlrgfQRAMVKTMTaaakVPHFHYVEEINVDALVELKASFQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 312 KI-LEGRSKISVNDFIIKASALACLKVPEANSSW----MDTVIRQNHvvDVSVAVSTPAGLITPIVFNAHIKGVETIAND 386
Cdd:PLN02528  230 ENnTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHGLVVPNIKNVQSLSLLEITKE 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 387 VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDklVPADNEKGFDV-ASMMSVTLSCD 465
Cdd:PLN02528  308 LSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTIGAD 385

                         410       420
                  ....*....|....*....|....*...
gi 1716950954 466 HRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PLN02528  386 HRVLDGATVARFCNEWKSYVEKPELLML 413
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 200-488 9.53e-41

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 148.40  E-value: 9.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 200 RVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV------PSKVAPAPAAVVPPTGPGMAPVPTGVFTDI---P 270
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGkreK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 271 ISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGRS-KISVNDFIIKASALACLKVP-------EAN 341
Cdd:PRK11857   81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSvKDPVLKTEGvKLTFLPFIAKAILIALKEFPifaakydEAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 342 SSwmdtvIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKN 421
Cdd:PRK11857  161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716950954 422 FSAIINPPQACILAIGASEDKlvpADNEKGFDVAS-MMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKP 488
Cdd:PRK11857  236 GVPVINYPELAIAGVGAIIDK---AIVKNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 66-204 1.14e-29

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 121.18  E-value: 1.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  66 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEAD 145
Cdd:PRK11892    4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1716950954 146 ISAFADyRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVS 204
Cdd:PRK11892   84 ASDAGA-APAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVT 141
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 65-493 1.04e-28

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 118.32  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  65 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPlGTPLCIIVEKEA 144
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEP-GTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 145 DISAFA-DYRPTEVTDLKPQVPPPTPPPVAAVPPtpqPLAPTPSAPCPATPAgpkgrvfvsplakklavekgidltqvKG 223
Cdd:PLN02226  171 AASQVTpSQKIPETTDPKPSPPAEDKQKPKVESA---PVAEKPKAPSSPPPP--------------------------KQ 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 224 TGPDGRITKKDIDSFVPskvapapaavvpptgpgmapvptgvftdipISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEV 303
Cdd:PLN02226  222 SAKEPQLPPKERERRVP------------------------------MTRLRKRVATRLKDSQNTFALLTTFNEVDMTNL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 304 LLVRKEL-NKILEGRS-KISVNDFIIKASALACLKVPEANSSW-MDTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGV 380
Cdd:PLN02226  272 MKLRSQYkDAFYEKHGvKLGLMSGFIKAAVSALQHQPVVNAVIdGDDIIYRDYV-DISIAVGTSKGLVVPVIRGADKMNF 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954 381 ETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGAsedkLVPADNEKGFDVA--SMM 458
Cdd:PLN02226  351 AEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHS----IVSRPMVVGGSVVprPMM 426

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716950954 459 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 493
Cdd:PLN02226  427 YVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 65-139 9.85e-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: 97.09  E-value: 9.85e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716950954  65 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 139
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 66-139 6.01e-24

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: 94.82  E-value: 6.01e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716950954  66 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 139
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 66-140 3.55e-20

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: 84.35  E-value: 3.55e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716950954  66 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 140
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 201-236 2.72e-15

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: 69.25  E-value: 2.72e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1716950954 201 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDID 236
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 67-151 6.60e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 73.05  E-value: 6.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  67 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIVEKE--- 143
Cdd:PRK14875    5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEvsd 83


                  ....*...
gi 1716950954 144 ADISAFAD 151
Cdd:PRK14875   84 AEIDAFIA 91
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 66-139 1.68e-11

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: 59.92  E-value: 1.68e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716950954  66 QVLLPALSPTMTMGTVQrWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 139
Cdd:pfam00364   2 EIKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 375-485 7.36e-07

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 52.20  E-value: 7.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716950954  375 AHIKGVETIA--------NDVVSlatKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA-------- 438
Cdd:PRK12270   229 PAIKGAETMDfaqfwaayEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefq 305

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1716950954  439 --SEDKLvpadNEKGfdVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYL 485
Cdd:PRK12270   306 gaSEERL----AELG--ISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 79-139 1.03e-03

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: 37.40  E-value: 1.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1716950954  79 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 139
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
 
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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