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UniProtKB/Swiss-Prot entry P23129


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODO1_BACSU
Primary accession number P23129
Secondary accession numbers O68261 Q45642
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on August 31, 2004 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 75)
Name and origin of the protein
Protein name 2-oxoglutarate dehydrogenase E1 component
Synonyms EC 1.2.4.2
Alpha-ketoglutarate dehydrogenase
Gene name
Name: odhA
Synonyms: citK
OrderedLocusNames: BSU19370
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
DOI=10.1007/BF00283849; PubMed=1508153 [NCBI, ExPASy, EBI, Israel, Japan]
Resnekov O., Melin L., Carlsson P., Mannerloev M., von Gabain A., Hederstedt L.;
"Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex.";
Mol. Gen. Genet. 234:285-296(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
SEQUENCE REVISION.
DOI=10.1101/gr.9.11.1116; PubMed=10568751 [NCBI, ExPASy, EBI, Israel, Japan]
Medigue C., Rose M., Viari A., Danchin A.;
"Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence.";
Genome Res. 9:1116-1127(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270.
STRAIN=168;
DOI=10.1093/dnares/5.3.195; PubMed=9734814 [NCBI, ExPASy, EBI, Israel, Japan]
Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D., Park S.-H.;
"Sequence analysis of the Bacillus subtilis 168 chromosome region between the sspC and odhA loci (184 degrees-180 degrees).";
DNA Res. 5:195-201(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 649-941.
STRAIN=168;
PubMed=2500417 [NCBI, ExPASy, EBI, Israel, Japan]
Carlsson P., Hederstedt L.;
"Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively.";
J. Bacteriol. 171:3667-3672(1989).
Comments
  • FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • SUBUNIT: Homodimer.
  • SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X54805; CAA38576.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99114; CAB13829.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026147; AAC17864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27141; AAA22628.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S25295; A32879.
RefSeq NP_389819.2; -.
3D structure databases
ModBase P23129.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1937-MON; -.
Organism-specific databases
SubtiList BG10272; odhA. [Micado]
Ontologies
GO
GO:0004591; Molecular function: oxoglutarate dehydrogenase (succinyl-transferring) activity (inferred from electronic annotation from HAMAP).
GO:0030976; Molecular function: thiamin pyrophosphate binding (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01169; -; 1.
PBIL [Tree]
InterPro IPR011603; 2oxoglutarate_DHase_E1.
IPR001017; DHase_E1.
IPR005475; Transketo_Cen_R.
Graphical view of domain structure.
PANTHER PTHR23152; 2oxoglutarate_DH_E1; 1.
Pfam PF00676; E1_dh; 1.
PF02779; Transket_pyr; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000157; Oxoglu_dh_E1; 1.
TIGRFAMs TIGR00239; 2oxo_dh_E1; 1.
ProtoNet P23129.
Genome annotation databases
GeneID 939507; -.
GenomeReviews AL009126_GR; BSU19370.
KEGG bsu:BSU19370; -.
Phylogenomic databases
HOGENOM P23129; -.
Genome annotation databases
CMR P23129; BSU19370.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   941  941     2-oxoglutarate dehydrogenase E1 component. PRO_0000162169
CONFLICT   35    35        Y -> N (in Ref. 4; AAC17864). 
CONFLICT   110   110        L -> S (in Ref. 4; AAC17864). 
CONFLICT   133   133        P -> L (in Ref. 4; AAC17864). 
CONFLICT   231   231        I -> T (in Ref. 4; AAC17864). 
CONFLICT   834   834        S -> D (in Ref. 5; AAA22628). 
CONFLICT   924   941        VHKKEQERIVSDSLTRKN -> EFIKKNRNVLYLIA (in Ref. 1; CAA38576). 
Sequence information
Length: 941 AA [This is the length of the unprocessed precursor] Molecular weight: 105740 Da [This is the MW of the unprocessed precursor] CRC64: 6B2D1CE12572E7C4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFQNSMKQRM NWEDFYGPNL GYALELYDQY TQDPYSIDPD LKEMFDELGA PPSDIKEASG 

        70         80         90        100        110        120 
TKEKGRVTAD LIQKIASAVR LAEDIRTYGH LNASVNPLRK DEKKSELFPL SDYGLTEEEI 

       130        140        150        160        170        180 
KAIPASVICK DAPKNISNGL EAIQYLRNTY KRTISFEFDH VHDFKEREWL TRKIESGELF 

       190        200        210        220        230        240 
QKNSAEKLSA VLERLTEVEG FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKSGTT 

       250        260        270        280        290        300 
SVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPRSLVPS EDPLESATDG RGMSNTIWGR 

       310        320        330        340        350        360 
IGSFKTLKQN QPALPLANNP SHLEFINPIV EGSTRAAQET RTQSGYPVQD ETKSLAILIH 

       370        380        390        400        410        420 
GDAAFPGEGI VAETLNLSSL KGYQVGGAIH IIANNMIGFT TESAESRSTK YASDLAKGYE 

       430        440        450        460        470        480 
IPIVHVNADD PEACLSAVKF AVEYRKTFNK DFLIDLIGYR RYGHNEMDEP STTQPMLYDA 

       490        500        510        520        530        540 
VRKHPTSNKF SLKKLVKEGV VTEEVVQNIE KSVTKRIEVA IQKVPSKKEH TACEIELPEP 

       550        560        570        580        590        600 
VSNGFPDVDT SIHFHVLRKL NGELITGESF MFSQAKAHFR KTAKAFDDDR KVEWSLAESL 

       610        620        630        640        650        660 
AFASILKDGT PIRLTGQDSE RGTFAQRNLV LHDSETGKEF VPLHHLSDCS TSFAVHNSPL 

       670        680        690        700        710        720 
SEGSVLGFEY GYNVHSPETL VLWEAQYGDF ANAAQVYFDQ FISAGRAKWG QKSGLVMLLP 

       730        740        750        760        770        780 
HGYEGQGPEH SSGRIERFLQ LAAENNWTVA NLTSAAQYFH ILRRQAKMLL REEIRPLVIM 

       790        800        810        820        830        840 
TPKSLLRNPN TVSEVQELSE SRFQPVYEQS GLSHDYEKVT RLVLSSGKVS IDISVHFNKL 

       850        860        870        880        890        900 
EDGKEWLHIA RIEQLYPFPA KGVKELFAKL PNLKEIVWVQ EEPQNMGAWG YISPYLTEIA 

       910        920        930        940 
PEGVSVQYIG RRRRSSPAEG DPTVHKKEQE RIVSDSLTRK N 

P23129 in FASTA format

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