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Conserved domains on  [gi|221316669|ref|NP_001137469|]
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2-oxoglutarate dehydrogenase-like, mitochondrial isoform c [Homo sapiens]

Protein Classification

2-oxoglutarate dehydrogenase subunit E1( domain architecture ID 11484076)

2-oxoglutarate dehydrogenase subunit E1 catalyzes the decarboxylation of 2-oxoglutarate and the formation of TPP-hydroxysuccinate

EC:  1.2.4.2
Gene Ontology:  GO:0004591

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
SucA super family cl43187
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes ...
1-793 0e+00

2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes [Energy production and conversion]; 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes is part of the Pathway/BioSystem: TCA cycle


The actual alignment was detected with superfamily member COG0567:

Pssm-ID: 440333 [Multi-domain]  Cd Length: 935  Bit Score: 1174.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   1 MFINDVEQCQWIRQKFETP-GVMQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMG 79
Cdd:COG0567  170 MHISDPEEKRWIQERLESTrNRPSFSAEEKKRILEKLTAAEGFEKFLHTKYVGQKRFSLEGGESLIPALDELIERAGELG 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  80 IENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAADEGSGDVKYHLGmYHerINRVT-NRNITLSLVANPSHLEAV 158
Cdd:COG0567  250 VKEIVIGMAHRGRLNVLVNILGKPPRDIFSEFEGKSAEDVLGSGDVKYHLG-FS--SDVETpGGKVHLSLAFNPSHLEIV 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 159 DPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:COG0567  327 NPVVEGSVRARQDRRGDTDRDKVLPILIHGDAAFAGQGVVYETLNMSQLRGYRTGGTIHIVINNQIGFTTSPRDARSSTY 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:COG0567  407 CTDVAKMVQAPIFHVNGDDPEAVVFVARLALDYRQKFKKDVVIDLVCYRRHGHNEGDEPAFTQPLMYKKIKKHPTTREIY 486
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSKDKKILhIKHWLDSPWPGFFNVDGEpkSMTCPATGIPEDMLTHIGSV 398
Cdd:COG0567  487 ADKLVAEGVITAEEADEMVDEYRAALDEGFEVVKEYKPN-KADWLEGDWSPYRRLGED--WDDPVDTGVPLEKLKELGEK 563
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 399 ASSVPlEDFKIHTGLSRILRGRADM-TKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEvDRRT 477
Cdd:COG0567  564 LTTLP-EGFKLHPKVEKILEDRRKMaEGEKPLDWGMAEALAYASLLDEGYPVRLSGQDSGRGTFSHRHAVLHDQK-TGET 641
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 478 CVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLL 557
Cdd:COG0567  642 YVPLNHLSEGQARFEVYNSLLSEEAVLGFEYGYALAEPNTLVIWEAQFGDFANGAQVVIDQFISSGESKWGRLSGLVMLL 721
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 558 PHGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTPK 637
Cdd:COG0567  722 PHGYEGQGPEHSSARLERFLQLCAED-------------------NMQVCNPTTPAQYFHLLRRQMKRPFRKPLIVMTPK 782
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 638 SLLRHPEAKSSFDQMVSGtSFQRVIPEDGAAarAPEQVQRLIFCTGKVYYDLVKERSSQDLEEkVAITRLEQISPFPFDL 717
Cdd:COG0567  783 SLLRHKLAVSSLEELAEG-SFQEVIDDTDEL--DPKKVKRVVLCSGKVYYDLLEERRERGRDD-VAIVRIEQLYPFPEEE 858
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221316669 718 IKQEAEKYPGA-ELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFNL 793
Cdd:COG0567  859 LAAELAKYPNAkEVVWCQEEPKNMGAWYFIQHRLEEVLPKGQRLRYAGRPASASPATGYMSVHKAEQKALVEEALGI 935
 
Name Accession Description Interval E-value
SucA COG0567
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes ...
1-793 0e+00

2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes [Energy production and conversion]; 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440333 [Multi-domain]  Cd Length: 935  Bit Score: 1174.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   1 MFINDVEQCQWIRQKFETP-GVMQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMG 79
Cdd:COG0567  170 MHISDPEEKRWIQERLESTrNRPSFSAEEKKRILEKLTAAEGFEKFLHTKYVGQKRFSLEGGESLIPALDELIERAGELG 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  80 IENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAADEGSGDVKYHLGmYHerINRVT-NRNITLSLVANPSHLEAV 158
Cdd:COG0567  250 VKEIVIGMAHRGRLNVLVNILGKPPRDIFSEFEGKSAEDVLGSGDVKYHLG-FS--SDVETpGGKVHLSLAFNPSHLEIV 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 159 DPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:COG0567  327 NPVVEGSVRARQDRRGDTDRDKVLPILIHGDAAFAGQGVVYETLNMSQLRGYRTGGTIHIVINNQIGFTTSPRDARSSTY 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:COG0567  407 CTDVAKMVQAPIFHVNGDDPEAVVFVARLALDYRQKFKKDVVIDLVCYRRHGHNEGDEPAFTQPLMYKKIKKHPTTREIY 486
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSKDKKILhIKHWLDSPWPGFFNVDGEpkSMTCPATGIPEDMLTHIGSV 398
Cdd:COG0567  487 ADKLVAEGVITAEEADEMVDEYRAALDEGFEVVKEYKPN-KADWLEGDWSPYRRLGED--WDDPVDTGVPLEKLKELGEK 563
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 399 ASSVPlEDFKIHTGLSRILRGRADM-TKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEvDRRT 477
Cdd:COG0567  564 LTTLP-EGFKLHPKVEKILEDRRKMaEGEKPLDWGMAEALAYASLLDEGYPVRLSGQDSGRGTFSHRHAVLHDQK-TGET 641
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 478 CVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLL 557
Cdd:COG0567  642 YVPLNHLSEGQARFEVYNSLLSEEAVLGFEYGYALAEPNTLVIWEAQFGDFANGAQVVIDQFISSGESKWGRLSGLVMLL 721
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 558 PHGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTPK 637
Cdd:COG0567  722 PHGYEGQGPEHSSARLERFLQLCAED-------------------NMQVCNPTTPAQYFHLLRRQMKRPFRKPLIVMTPK 782
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 638 SLLRHPEAKSSFDQMVSGtSFQRVIPEDGAAarAPEQVQRLIFCTGKVYYDLVKERSSQDLEEkVAITRLEQISPFPFDL 717
Cdd:COG0567  783 SLLRHKLAVSSLEELAEG-SFQEVIDDTDEL--DPKKVKRVVLCSGKVYYDLLEERRERGRDD-VAIVRIEQLYPFPEEE 858
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221316669 718 IKQEAEKYPGA-ELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFNL 793
Cdd:COG0567  859 LAAELAKYPNAkEVVWCQEEPKNMGAWYFIQHRLEEVLPKGQRLRYAGRPASASPATGYMSVHKAEQKALVEEALGI 935
sucA PRK09404
2-oxoglutarate dehydrogenase E1 component; Reviewed
1-792 0e+00

2-oxoglutarate dehydrogenase E1 component; Reviewed


Pssm-ID: 236499 [Multi-domain]  Cd Length: 924  Bit Score: 1145.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   1 MFINDVEQCQWIRQKFETPGVmQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGI 80
Cdd:PRK09404 164 MHISDPEERRWLQQRIESGRP-SFSAEEKKAILERLTAAEGFERFLHTKFVGQKRFSLEGGESLIPMLDEIIRRAGKLGV 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  81 ENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAAD-EGSGDVKYHLGMYHERinRVTNRNITLSLVANPSHLEAVD 159
Cdd:PRK09404 243 KEIVIGMAHRGRLNVLVNVLGKPPRDLFAEFEGKHGPDEvLGSGDVKYHLGFSSDR--ETDGGEVHLSLAFNPSHLEIVN 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 160 PVVQGKTKAEQFYRGDAQG-KKVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:PRK09404 321 PVVEGSVRARQDRRGDGQDrKKVLPILIHGDAAFAGQGVVAETLNLSQLRGYRTGGTIHIVINNQIGFTTSPPDDRSTPY 400
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:PRK09404 401 CTDVAKMVQAPIFHVNGDDPEAVVFATRLALEYRQKFKKDVVIDLVCYRRHGHNEGDEPSFTQPLMYKKIKKHPTTRELY 480
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSKDKKilhIKHWLDSPWPGFFNVDGEPKsmtcPATGIPEDMLTHIGSV 398
Cdd:PRK09404 481 ADKLVAEGVITEEEADEMVNEYRDALDAGFEVVKEWR---PADWLAGDWSPYLGHEWDDP----VDTGVPLERLKELAEK 553
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 399 ASSVPlEDFKIHTGLSRILRGRADM-TKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEvDRRT 477
Cdd:PRK09404 554 LTTVP-EGFKVHPKVKKILEDRREMaEGEKPIDWGMAEALAFASLLDEGYPVRLSGQDSGRGTFSHRHAVLHDQK-TGET 631
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 478 CVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLL 557
Cdd:PRK09404 632 YIPLNHLSEGQASFEVYDSPLSEEAVLGFEYGYSTAEPNTLVIWEAQFGDFANGAQVVIDQFISSGEQKWGRLSGLVMLL 711
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 558 PHGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTPK 637
Cdd:PRK09404 712 PHGYEGQGPEHSSARLERFLQLCAED-------------------NMQVCNPTTPAQYFHLLRRQALRPFRKPLVVMTPK 772
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 638 SLLRHPEAKSSFDQMVSGtSFQRVIPEDGAAarAPEQVQRLIFCTGKVYYDLVKERSSQDLEEkVAITRLEQISPFPFDL 717
Cdd:PRK09404 773 SLLRHPLAVSSLEELAEG-SFQPVIGDIDEL--DPKKVKRVVLCSGKVYYDLLEARRKRGIDD-VAIVRIEQLYPFPHEE 848
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221316669 718 IKQEAEKYPGA-ELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFN 792
Cdd:PRK09404 849 LAAELAKYPNAkEVVWCQEEPKNQGAWYFIQHHLEEVLPEGQKLRYAGRPASASPAVGYMSLHKKQQEALVEDALG 924
2oxo_dh_E1 TIGR00239
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists ...
1-791 0e+00

2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists of this thiamine pyrophosphate-binding subunit (E1), dihydrolipoamide succinyltransferase (E2), and lipoamide dehydrogenase (E3). The E1 ortholog from Corynebacterium glutamicum is unusual in having an N-terminal extension that resembles the dihydrolipoamide succinyltransferase (E2) component of 2-oxoglutarate dehydrogenase. [Energy metabolism, TCA cycle]


Pssm-ID: 161785 [Multi-domain]  Cd Length: 929  Bit Score: 881.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669    1 MFINDVEQCQWIRQKFETPGVMQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGI 80
Cdd:TIGR00239 163 MHITSTEEKRWLQQRIESGERAQFNSEEKKRFLSRLTAAEGFERFLGAKFPGAKRFSLEGLDALVPMLKEIIRHSVNSGT 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   81 ENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAAD-EGSGDVKYHLGMYHERINrVTNRNITLSLVANPSHLEAVD 159
Cdd:TIGR00239 243 RDVVLGMAHRGRLNVLVNVLGKPPEDIFSEFAGKHKSHLpDGTGDVKYHMGRFSSDFT-TDGKLVHLALAFNPSHLEIVS 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  160 PVVQGKTKAEQFYRGDAQGK-KVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:TIGR00239 322 PVVIGSTRARLDRLNDSPEStKVLAILIHGDAAFAGQGVVQETLNMSKLRGYSVGGTIHIIINNQIGFTTNPLDARSTPY 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:TIGR00239 402 CSDLAKMIQAPIFHVNADDPEAVAFATRLAVEYRNTFKRDVFIDLVGYRRHGHNEADEPSATQPLMYQKIKKHPTPRKVY 481
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAygrskDKKILHIKHWLDSPWPGFFNVDgEPKSMTCPaTGIPEDMLTHIGSV 398
Cdd:TIGR00239 482 ADKLVSEGVATEEDVTEMVNLYRDALEAA-----DCVVPSWREMNTASFTWSPELN-HEWDEEYP-NKVEMKRLQELAKR 554
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  399 ASSVPlEDFKIHTGLSRIL--RGRADMTKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEvDRR 476
Cdd:TIGR00239 555 ISEVP-EGVEMHSRVAKIYfdRTKAMAAGEKLFDWGGAENLAFATLVDDGIPVRLSGEDSERGTFFQRHAVLHDQS-NGS 632
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  477 TCVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLL 556
Cdd:TIGR00239 633 TYTPLQHLHNGQGAFRVWNSVLSEESVLGFEYGYATTSPRTLVIWEAQFGDFANGAQVVIDQFISSGEQKWGQMSGLVML 712
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  557 LPHGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTP 636
Cdd:TIGR00239 713 LPHGYEGQGPEHSSGRLERFLQLAAEQ-------------------NMQVCVPTTPAQVFHILRRQALRGMRRPLVVMSP 773
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  637 KSLLRHPEAKSSFDQMVSGTsFQRVIP--EDGAAARAPEQVQRLIFCTGKVYYDLVKERSSqDLEEKVAITRLEQISPFP 714
Cdd:TIGR00239 774 KSLLRHPLAVSSLEELAEGT-FQPVIGeiEESGLSLDPEGVKRLVLCSGKVYYDLHEQRRK-NGQKDVAIVRIEQLYPFP 851
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221316669  715 FDLIKQEAEKYPG-AELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAF 791
Cdd:TIGR00239 852 HKAVKEVLQQYPNlKEIVWCQEEPLNMGAWYYSQPHLREVIPEGVSVRYAGRPASASPAVGYMSLHQKQQQDLLNDAL 929
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
42-305 0e+00

Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle.


Pssm-ID: 238974 [Multi-domain]  Cd Length: 265  Bit Score: 520.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  42 FEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGIENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAAD-- 119
Cdd:cd02016    1 FEQFLATKFPGQKRFGLEGAESLIPALDELIDRAAELGVEEVVIGMAHRGRLNVLANVLGKPLEQIFSEFEGKSEFPEdd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 120 EGSGDVKYHLGMYHERINRVtNRNITLSLVANPSHLEAVDPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVY 199
Cdd:cd02016   81 EGSGDVKYHLGYSSDRKTPS-GKKVHLSLAPNPSHLEAVNPVVMGKTRAKQDYRGDGERDKVLPILIHGDAAFAGQGVVY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 200 ETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDV 279
Cdd:cd02016  160 ETLNLSNLPGYTTGGTIHIVVNNQIGFTTDPRDSRSSPYCTDVAKMIGAPIFHVNGDDPEAVVRATRLALEYRQKFKKDV 239
                        250       260
                 ....*....|....*....|....*.
gi 221316669 280 VVDLVCYRRRGHNEMDEPMFTQPLMY 305
Cdd:cd02016  240 VIDLVCYRRHGHNELDEPSFTQPLMY 265
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
34-360 5.91e-92

Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.


Pssm-ID: 395548 [Multi-domain]  Cd Length: 300  Bit Score: 290.77  E-value: 5.91e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   34 ARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGiENVIlgMPHRGRLNVLANVIRkdLEQIFCQFDP 113
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPG-DYII--PGYRDHGNLLARGLS--LEEIFAELYG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  114 KLEaadEGSGDVKYhlGMYHERINRVTNRNITLSLVAnpshleavdPVVQGKTKAEQFyrgdaQGKKVMSILVHGDAAfA 193
Cdd:pfam00676  76 RVA---KGKGGSMH--GYYGAKGNRFYGGNGILGAQV---------PLGAGIALAAKY-----RGKKEVAITLYGDGA-A 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  194 GQGVVYETFHLSDLPSYTTngtVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRN 273
Cdd:pfam00676 136 NQGDFFEGLNFAALWKLPV---IFVCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERAR 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  274 TFNKDVVVDLVCYRRRGHNEMDEPMFTQ-PLMYKQIHRQVPVLKKYADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSK 352
Cdd:pfam00676 213 TGKGPFLIELVTYRYGGHSMSDDPSTYRtRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAE 292

                  ....*...
gi 221316669  353 DKKILHIK 360
Cdd:pfam00676 293 SAPEPHPE 300
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
495-641 8.55e-24

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 97.56  E-value: 8.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   495 NSSLSEYGVLGFELGYAMAspnALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVrhngiVLLLPHGMEGM-GPEHSSARP 573
Cdd:smart00861  19 DTGIAEQAMVGFAAGLALH---GLRPVVEIFFTFFDRAKDQIRSAGASGNVPVV-----FRHDGGGGVGEdGPTHHSIED 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221316669   574 E-RFLQMsnddsdaypaftkdfevsqlydCNWIVVNCSTPANYFHVLRRQILLPfRKPLIIFTPKSLLR 641
Cdd:smart00861  91 EaLLRAI----------------------PGLKVVAPSDPAEAKGLLRAAIRDD-GPVVIRLERKSLYR 136
 
Name Accession Description Interval E-value
SucA COG0567
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes ...
1-793 0e+00

2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes [Energy production and conversion]; 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440333 [Multi-domain]  Cd Length: 935  Bit Score: 1174.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   1 MFINDVEQCQWIRQKFETP-GVMQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMG 79
Cdd:COG0567  170 MHISDPEEKRWIQERLESTrNRPSFSAEEKKRILEKLTAAEGFEKFLHTKYVGQKRFSLEGGESLIPALDELIERAGELG 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  80 IENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAADEGSGDVKYHLGmYHerINRVT-NRNITLSLVANPSHLEAV 158
Cdd:COG0567  250 VKEIVIGMAHRGRLNVLVNILGKPPRDIFSEFEGKSAEDVLGSGDVKYHLG-FS--SDVETpGGKVHLSLAFNPSHLEIV 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 159 DPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:COG0567  327 NPVVEGSVRARQDRRGDTDRDKVLPILIHGDAAFAGQGVVYETLNMSQLRGYRTGGTIHIVINNQIGFTTSPRDARSSTY 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:COG0567  407 CTDVAKMVQAPIFHVNGDDPEAVVFVARLALDYRQKFKKDVVIDLVCYRRHGHNEGDEPAFTQPLMYKKIKKHPTTREIY 486
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSKDKKILhIKHWLDSPWPGFFNVDGEpkSMTCPATGIPEDMLTHIGSV 398
Cdd:COG0567  487 ADKLVAEGVITAEEADEMVDEYRAALDEGFEVVKEYKPN-KADWLEGDWSPYRRLGED--WDDPVDTGVPLEKLKELGEK 563
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 399 ASSVPlEDFKIHTGLSRILRGRADM-TKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEvDRRT 477
Cdd:COG0567  564 LTTLP-EGFKLHPKVEKILEDRRKMaEGEKPLDWGMAEALAYASLLDEGYPVRLSGQDSGRGTFSHRHAVLHDQK-TGET 641
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 478 CVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLL 557
Cdd:COG0567  642 YVPLNHLSEGQARFEVYNSLLSEEAVLGFEYGYALAEPNTLVIWEAQFGDFANGAQVVIDQFISSGESKWGRLSGLVMLL 721
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 558 PHGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTPK 637
Cdd:COG0567  722 PHGYEGQGPEHSSARLERFLQLCAED-------------------NMQVCNPTTPAQYFHLLRRQMKRPFRKPLIVMTPK 782
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 638 SLLRHPEAKSSFDQMVSGtSFQRVIPEDGAAarAPEQVQRLIFCTGKVYYDLVKERSSQDLEEkVAITRLEQISPFPFDL 717
Cdd:COG0567  783 SLLRHKLAVSSLEELAEG-SFQEVIDDTDEL--DPKKVKRVVLCSGKVYYDLLEERRERGRDD-VAIVRIEQLYPFPEEE 858
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221316669 718 IKQEAEKYPGA-ELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFNL 793
Cdd:COG0567  859 LAAELAKYPNAkEVVWCQEEPKNMGAWYFIQHRLEEVLPKGQRLRYAGRPASASPATGYMSVHKAEQKALVEEALGI 935
sucA PRK09404
2-oxoglutarate dehydrogenase E1 component; Reviewed
1-792 0e+00

2-oxoglutarate dehydrogenase E1 component; Reviewed


Pssm-ID: 236499 [Multi-domain]  Cd Length: 924  Bit Score: 1145.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   1 MFINDVEQCQWIRQKFETPGVmQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGI 80
Cdd:PRK09404 164 MHISDPEERRWLQQRIESGRP-SFSAEEKKAILERLTAAEGFERFLHTKFVGQKRFSLEGGESLIPMLDEIIRRAGKLGV 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  81 ENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAAD-EGSGDVKYHLGMYHERinRVTNRNITLSLVANPSHLEAVD 159
Cdd:PRK09404 243 KEIVIGMAHRGRLNVLVNVLGKPPRDLFAEFEGKHGPDEvLGSGDVKYHLGFSSDR--ETDGGEVHLSLAFNPSHLEIVN 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 160 PVVQGKTKAEQFYRGDAQG-KKVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:PRK09404 321 PVVEGSVRARQDRRGDGQDrKKVLPILIHGDAAFAGQGVVAETLNLSQLRGYRTGGTIHIVINNQIGFTTSPPDDRSTPY 400
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:PRK09404 401 CTDVAKMVQAPIFHVNGDDPEAVVFATRLALEYRQKFKKDVVIDLVCYRRHGHNEGDEPSFTQPLMYKKIKKHPTTRELY 480
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSKDKKilhIKHWLDSPWPGFFNVDGEPKsmtcPATGIPEDMLTHIGSV 398
Cdd:PRK09404 481 ADKLVAEGVITEEEADEMVNEYRDALDAGFEVVKEWR---PADWLAGDWSPYLGHEWDDP----VDTGVPLERLKELAEK 553
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 399 ASSVPlEDFKIHTGLSRILRGRADM-TKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEvDRRT 477
Cdd:PRK09404 554 LTTVP-EGFKVHPKVKKILEDRREMaEGEKPIDWGMAEALAFASLLDEGYPVRLSGQDSGRGTFSHRHAVLHDQK-TGET 631
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 478 CVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLL 557
Cdd:PRK09404 632 YIPLNHLSEGQASFEVYDSPLSEEAVLGFEYGYSTAEPNTLVIWEAQFGDFANGAQVVIDQFISSGEQKWGRLSGLVMLL 711
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 558 PHGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTPK 637
Cdd:PRK09404 712 PHGYEGQGPEHSSARLERFLQLCAED-------------------NMQVCNPTTPAQYFHLLRRQALRPFRKPLVVMTPK 772
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 638 SLLRHPEAKSSFDQMVSGtSFQRVIPEDGAAarAPEQVQRLIFCTGKVYYDLVKERSSQDLEEkVAITRLEQISPFPFDL 717
Cdd:PRK09404 773 SLLRHPLAVSSLEELAEG-SFQPVIGDIDEL--DPKKVKRVVLCSGKVYYDLLEARRKRGIDD-VAIVRIEQLYPFPHEE 848
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221316669 718 IKQEAEKYPGA-ELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFN 792
Cdd:PRK09404 849 LAAELAKYPNAkEVVWCQEEPKNQGAWYFIQHHLEEVLPEGQKLRYAGRPASASPAVGYMSLHKKQQEALVEDALG 924
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
1-791 0e+00

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 954.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669    1 MFINDVEQCQWIRQKFETPGVmQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGI 80
Cdd:PRK12270  468 MHIQDPEQRRWLQERVERPHE-KPTREEQKRILSKLNAAEAFETFLQTKYVGQKRFSLEGGESLIPLLDAVLDQAAEHGL 546
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   81 ENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLE-AADEGSGDVKYHLGMYHERInRVTNRNITLSLVANPSHLEAVD 159
Cdd:PRK12270  547 DEVVIGMAHRGRLNVLANIVGKPYSQIFREFEGNLDpRSAQGSGDVKYHLGAEGTFT-QMFGDEIKVSLAANPSHLEAVD 625
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  160 PVVQGKTKAEQFYRGD-AQGKKVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:PRK12270  626 PVLEGIVRAKQDRLDKgEEGFTVLPILLHGDAAFAGQGVVAETLNLSQLRGYRTGGTIHIVVNNQVGFTTAPESSRSSEY 705
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:PRK12270  706 ATDVAKMIQAPIFHVNGDDPEAVVRVARLAFEYRQRFHKDVVIDLVCYRRRGHNEGDDPSMTQPLMYDLIDAKRSVRKLY 785
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSKDKKilhikhwlDSPWPGFFNVDGEPKSMTCPATGIPEDMLTHIGSV 398
Cdd:PRK12270  786 TEALIGRGDITVEEAEQALRDYQGQLERVFNEVREAE--------KKPPEPPESVESDQGPPAGVDTAVSAEVLERIGDA 857
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  399 ASSVPlEDFKIHTGLSRILRGRADMTKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEVDRRTC 478
Cdd:PRK12270  858 HVNLP-EGFTVHPKLKPLLEKRREMAREGGIDWAFGELLAFGSLLLEGTPVRLSGQDSRRGTFSQRHAVLIDRETGEEYT 936
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  479 vPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLLP 558
Cdd:PRK12270  937 -PLQNLSDDQGKFLVYDSLLSEYAAMGFEYGYSVERPDALVLWEAQFGDFANGAQTIIDEFISSGEAKWGQRSGVVLLLP 1015
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  559 HGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTPKS 638
Cdd:PRK12270 1016 HGYEGQGPDHSSARIERFLQLCAEG-------------------NMTVAQPSTPANYFHLLRRQALSGPRRPLVVFTPKS 1076
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  639 LLRHPEAKSSFDQMVSGTsFQRVIPEDGAAarAPEQVQRLIFCTGKVYYDLVKERSSQDLEEkVAITRLEQISPFPFDLI 718
Cdd:PRK12270 1077 MLRLKAAVSDVEDFTEGK-FRPVIDDPTVD--DGAKVRRVLLCSGKLYYDLAARREKDGRDD-TAIVRVEQLYPLPRAEL 1152
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221316669  719 KQEAEKYPGA-ELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAF 791
Cdd:PRK12270 1153 REALARYPNAtEVVWVQEEPANQGAWPFMALNLPELLPDGRRLRRVSRPASASPATGSAKVHAVEQQELLDEAF 1226
2oxo_dh_E1 TIGR00239
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists ...
1-791 0e+00

2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists of this thiamine pyrophosphate-binding subunit (E1), dihydrolipoamide succinyltransferase (E2), and lipoamide dehydrogenase (E3). The E1 ortholog from Corynebacterium glutamicum is unusual in having an N-terminal extension that resembles the dihydrolipoamide succinyltransferase (E2) component of 2-oxoglutarate dehydrogenase. [Energy metabolism, TCA cycle]


Pssm-ID: 161785 [Multi-domain]  Cd Length: 929  Bit Score: 881.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669    1 MFINDVEQCQWIRQKFETPGVMQFSSEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGI 80
Cdd:TIGR00239 163 MHITSTEEKRWLQQRIESGERAQFNSEEKKRFLSRLTAAEGFERFLGAKFPGAKRFSLEGLDALVPMLKEIIRHSVNSGT 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   81 ENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAAD-EGSGDVKYHLGMYHERINrVTNRNITLSLVANPSHLEAVD 159
Cdd:TIGR00239 243 RDVVLGMAHRGRLNVLVNVLGKPPEDIFSEFAGKHKSHLpDGTGDVKYHMGRFSSDFT-TDGKLVHLALAFNPSHLEIVS 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  160 PVVQGKTKAEQFYRGDAQGK-KVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPY 238
Cdd:TIGR00239 322 PVVIGSTRARLDRLNDSPEStKVLAILIHGDAAFAGQGVVQETLNMSKLRGYSVGGTIHIIINNQIGFTTNPLDARSTPY 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  239 PTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKY 318
Cdd:TIGR00239 402 CSDLAKMIQAPIFHVNADDPEAVAFATRLAVEYRNTFKRDVFIDLVGYRRHGHNEADEPSATQPLMYQKIKKHPTPRKVY 481
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  319 ADKLIAEGTVTLQEFEEEIAKYDRICEEAygrskDKKILHIKHWLDSPWPGFFNVDgEPKSMTCPaTGIPEDMLTHIGSV 398
Cdd:TIGR00239 482 ADKLVSEGVATEEDVTEMVNLYRDALEAA-----DCVVPSWREMNTASFTWSPELN-HEWDEEYP-NKVEMKRLQELAKR 554
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  399 ASSVPlEDFKIHTGLSRIL--RGRADMTKNRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEvDRR 476
Cdd:TIGR00239 555 ISEVP-EGVEMHSRVAKIYfdRTKAMAAGEKLFDWGGAENLAFATLVDDGIPVRLSGEDSERGTFFQRHAVLHDQS-NGS 632
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  477 TCVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLL 556
Cdd:TIGR00239 633 TYTPLQHLHNGQGAFRVWNSVLSEESVLGFEYGYATTSPRTLVIWEAQFGDFANGAQVVIDQFISSGEQKWGQMSGLVML 712
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  557 LPHGMEGMGPEHSSARPERFLQMSNDDsdaypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTP 636
Cdd:TIGR00239 713 LPHGYEGQGPEHSSGRLERFLQLAAEQ-------------------NMQVCVPTTPAQVFHILRRQALRGMRRPLVVMSP 773
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  637 KSLLRHPEAKSSFDQMVSGTsFQRVIP--EDGAAARAPEQVQRLIFCTGKVYYDLVKERSSqDLEEKVAITRLEQISPFP 714
Cdd:TIGR00239 774 KSLLRHPLAVSSLEELAEGT-FQPVIGeiEESGLSLDPEGVKRLVLCSGKVYYDLHEQRRK-NGQKDVAIVRIEQLYPFP 851
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221316669  715 FDLIKQEAEKYPG-AELAWCQEEHKNMGYYDYISPRFMTILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAF 791
Cdd:TIGR00239 852 HKAVKEVLQQYPNlKEIVWCQEEPLNMGAWYYSQPHLREVIPEGVSVRYAGRPASASPAVGYMSLHQKQQQDLLNDAL 929
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
42-305 0e+00

Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle.


Pssm-ID: 238974 [Multi-domain]  Cd Length: 265  Bit Score: 520.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  42 FEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGIENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAAD-- 119
Cdd:cd02016    1 FEQFLATKFPGQKRFGLEGAESLIPALDELIDRAAELGVEEVVIGMAHRGRLNVLANVLGKPLEQIFSEFEGKSEFPEdd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 120 EGSGDVKYHLGMYHERINRVtNRNITLSLVANPSHLEAVDPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVY 199
Cdd:cd02016   81 EGSGDVKYHLGYSSDRKTPS-GKKVHLSLAPNPSHLEAVNPVVMGKTRAKQDYRGDGERDKVLPILIHGDAAFAGQGVVY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 200 ETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDV 279
Cdd:cd02016  160 ETLNLSNLPGYTTGGTIHIVVNNQIGFTTDPRDSRSSPYCTDVAKMIGAPIFHVNGDDPEAVVRATRLALEYRQKFKKDV 239
                        250       260
                 ....*....|....*....|....*.
gi 221316669 280 VVDLVCYRRRGHNEMDEPMFTQPLMY 305
Cdd:cd02016  240 VIDLVCYRRHGHNELDEPSFTQPLMY 265
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
34-360 5.91e-92

Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.


Pssm-ID: 395548 [Multi-domain]  Cd Length: 300  Bit Score: 290.77  E-value: 5.91e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   34 ARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGiENVIlgMPHRGRLNVLANVIRkdLEQIFCQFDP 113
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPG-DYII--PGYRDHGNLLARGLS--LEEIFAELYG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  114 KLEaadEGSGDVKYhlGMYHERINRVTNRNITLSLVAnpshleavdPVVQGKTKAEQFyrgdaQGKKVMSILVHGDAAfA 193
Cdd:pfam00676  76 RVA---KGKGGSMH--GYYGAKGNRFYGGNGILGAQV---------PLGAGIALAAKY-----RGKKEVAITLYGDGA-A 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  194 GQGVVYETFHLSDLPSYTTngtVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRN 273
Cdd:pfam00676 136 NQGDFFEGLNFAALWKLPV---IFVCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERAR 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  274 TFNKDVVVDLVCYRRRGHNEMDEPMFTQ-PLMYKQIHRQVPVLKKYADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSK 352
Cdd:pfam00676 213 TGKGPFLIELVTYRYGGHSMSDDPSTYRtRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAE 292

                  ....*...
gi 221316669  353 DKKILHIK 360
Cdd:pfam00676 293 SAPEPHPE 300
OxoGdeHyase_C pfam16870
2-oxoglutarate dehydrogenase C-terminal; OxoGdeHyase_C is a family found immediately ...
646-791 3.63e-73

2-oxoglutarate dehydrogenase C-terminal; OxoGdeHyase_C is a family found immediately C-terminal to Transket_pyr, pfam02779. It is found at the C-terminus of 2-oxoglutarate dehydrogenase.


Pssm-ID: 465289 [Multi-domain]  Cd Length: 147  Bit Score: 235.03  E-value: 3.63e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  646 KSSFDQMVSGTSFQRVIPEDGAAArAPEQVQRLIFCTGKVYYDLVKERSSQDLEEKVAITRLEQISPFPFDLIKQEAEKY 725
Cdd:pfam16870   1 RSSLEEFTPGTHFQRVIPDPEPLV-DPEKVKRVVLCSGKVYYDLLKEREERGGIKDVAIVRIEQLYPFPFDLLKEELDKY 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221316669  726 PGA-ELAWCQEEHKNMGYYDYISPRFMTILRRA-RPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAF 791
Cdd:pfam16870  80 PNAaEIVWCQEEPKNQGAWSFVQPRLETVLNETgHRLRYAGRPPSASPATGSKSVHLAEQEALLDDAF 147
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
427-641 3.51e-56

Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.


Pssm-ID: 460692 [Multi-domain]  Cd Length: 174  Bit Score: 190.45  E-value: 3.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  427 RTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQEVDRrtcvpmnhlwpdqapytVCNSSLSEYGVLGF 506
Cdd:pfam02779   1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQGAGR-----------------VIDTGIAEQAMVGF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669  507 ELGYAMASPNaLVLWEAQFGDFHNtaqcIIDQFISTGQAKWVRHNG-IVLLLPHGMEGMGPEHSSARPERFLQMSNddsd 585
Cdd:pfam02779  64 ANGMALHGPL-LPPVEATFSDFLN----RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIP---- 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 221316669  586 aypaftkdfevsqlydcNWIVVNCSTPANYFHVLRRQILLPFRKPLIIFTPKSLLR 641
Cdd:pfam02779 135 -----------------GLKVVRPSDAAETKGLLRAAIRRDGRKPVVLRLPRQLLR 173
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
495-641 8.55e-24

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 97.56  E-value: 8.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669   495 NSSLSEYGVLGFELGYAMAspnALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVrhngiVLLLPHGMEGM-GPEHSSARP 573
Cdd:smart00861  19 DTGIAEQAMVGFAAGLALH---GLRPVVEIFFTFFDRAKDQIRSAGASGNVPVV-----FRHDGGGGVGEdGPTHHSIED 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221316669   574 E-RFLQMsnddsdaypaftkdfevsqlydCNWIVVNCSTPANYFHVLRRQILLPfRKPLIIFTPKSLLR 641
Cdd:smart00861  91 EaLLRAI----------------------PGLKVVAPSDPAEAKGLLRAAIRDD-GPVVIRLERKSLYR 136
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
177-347 1.60e-10

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 62.90  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 177 QGKKVMSILVHGDAAfAGQGVVYETFHLS---DLPsyttngTVHVVVNNQIGFTTdPRmARSSPYPTDVARVVNA--PIF 251
Cdd:cd02000  123 RGEDRVAVCFFGDGA-TNEGDFHEALNFAalwKLP------VIFVCENNGYAIST-PT-SRQTAGTSIADRAAAYgiPGI 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 252 HVNADDPEAVIYVCSVAAEW-RNTfNKDVVVDLVCYRRRGHNEMDEPMftqplMYK-----QIHRQVPVLKKYADKLIAE 325
Cdd:cd02000  194 RVDGNDVLAVYEAAKEAVERaRAG-GGPTLIEAVTYRLGGHSTSDDPS-----RYRtkeevEEWKKRDPILRLRKYLIEA 267
                        170       180
                 ....*....|....*....|....*.
gi 221316669 326 GTVT---LQEFEEEIAKY-DRICEEA 347
Cdd:cd02000  268 GILTeeeLAAIEAEVKAEvEEAVEFA 293
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
188-395 8.25e-06

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 48.60  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 188 GDAAfAGQGVVYETFHLS---DLPsyttngTVHVVVNNQIGFTTdPRmARSSPYPTDVARVV--NAPIFHVNADDPEAVI 262
Cdd:COG1071  157 GDGA-TSEGDFHEALNFAavwKLP------VVFVCENNGYAIST-PV-ERQTAVETIADRAAgyGIPGVRVDGNDVLAVY 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 263 YVCSVAAEW-RNTfNKDVVVDLVCYRRRGHNEMDEPMftqplMYK-----QIHRQVPVLKKYADKLIAEGTVTlQEFEEE 336
Cdd:COG1071  228 AAVKEAVERaRAG-EGPTLIEAKTYRLGGHSTSDDPT-----RYRtkeevEEWRERDPIERLRAYLLEEGLLT-EEELEA 300
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316669 337 I-AKYDRICEEAygrskdkkilhIKHWLDSPWPGffnvdgepksmtcpatgiPEDMLTHI 395
Cdd:COG1071  301 IeAEAKAEVEEA-----------VEFAEASPEPD------------------PEELFDDV 331
 
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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