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P23129

- ODO1_BACSU

UniProt

P23129 - ODO1_BACSU

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

    Cofactori

    Thiamine pyrophosphate.

    GO - Molecular functioni

    1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
    2. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW
    2. tricarboxylic acid cycle Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciBSUB:BSU19370-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase
    Gene namesi
    Name:odhA
    Synonyms:citK
    Ordered Locus Names:BSU19370
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU19370. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9449442-oxoglutarate dehydrogenase E1 componentPRO_0000162169Add
    BLAST

    Proteomic databases

    PaxDbiP23129.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi224308.BSU19370.

    Structurei

    3D structure databases

    ProteinModelPortaliP23129.
    SMRiP23129. Positions 71-943.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259588.
    KOiK00164.
    OrthoDBiEOG6V1M1F.
    PhylomeDBiP23129.

    Family and domain databases

    Gene3Di3.40.50.970. 2 hits.
    HAMAPiMF_01169. SucA_OdhA.
    InterProiIPR011603. 2oxoglutarate_DH_E1.
    IPR023784. 2oxoglutarate_DH_E1_bac.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view]
    PANTHERiPTHR23152. PTHR23152. 1 hit.
    PfamiPF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 2 hits.
    TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P23129-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFQNSMKQRM NWEDFYGPNL GYALELYDQY TQDPNSIDPD LKEMFDELGA    50
    PPSDIKEASG TKEKGRVTAD LIQKIASAVR LAEDIRTYGH LNASVNPLRK 100
    DEKKSELFPL SDYGLTEEEI KAIPASVICK DAPKNISNGL EAIQYLRNTY 150
    KRTISFEFDH VHDFKEREWL TRKIESGELF QKNSAEKLSA VLERLTEVEG 200
    FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKSGTT SVNIGMAHRG 250
    RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSIGISYG WTGDVKYHLG 300
    ANRELQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQSGYPVQ 350
    DETKSLAILI HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF 400
    TTESAESRST KYASDLAKGY EIPIVHVNAD DPEACLSAVK FAVEYRKTFN 450
    KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD AVRKHPTVKQ IFAEKLVKEG 500
    VVTEEVVQNI EKSVTKRIED AYQKVPSKKE HTACEIELPE PVSNGFPDVD 550
    TSIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA 600
    ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG KEFVPLHHLS 650
    DCSTSFAVHN SPLSEGSVLG FEYGYNVHSP ETLVLWEAQY GDFANAAQVY 700
    FDQFISAGRA KWGQKSGLVM LLPHGYEGQG PEHSSGRIER FLQLAAENNW 750
    TVANLTSAAQ YFHILRRQAK MLLREEIRPL VIMTPKSLLR NPNTVSEVQE 800
    LSESRFQPVY EQSGLSHDYE KVTRLVLSSG KVSIDISDHF NKLEDGKEWL 850
    HIARIEQLYP FPAKGVKELF AKLPNLKEIV WVQEEPQNMG AWGYISPYLT 900
    EIAPEGVSVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN 944
    Length:944
    Mass (Da):106,278
    Last modified:July 28, 2009 - v3
    Checksum:iDCBC7B28C44A9CC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351N → Y in CAA38576. (PubMed:1508153)Curated
    Sequence conflicti110 – 1101L → S in AAC17864. (PubMed:9734814)Curated
    Sequence conflicti133 – 1331P → L in AAC17864. (PubMed:9734814)Curated
    Sequence conflicti231 – 2311I → T in AAC17864. (PubMed:9734814)Curated
    Sequence conflicti275 – 2773NKD → RS in CAA38576. (PubMed:1508153)Curated
    Sequence conflicti283 – 31634GSIGI…SARIT → DPLESATDGRGMSNTIWGRI GSFKTLKQNQPALP in CAA38576. (PubMed:1508153)CuratedAdd
    BLAST
    Sequence conflicti488 – 4947VKQIFAE → SNKFSLK in CAA38576. (PubMed:1508153)Curated
    Sequence conflicti520 – 5223DAY → VAI in CAA38576. (PubMed:1508153)Curated
    Sequence conflicti554 – 5563DFD → HFH in CAA38576. (PubMed:1508153)Curated
    Sequence conflicti567 – 5693NWP → TG in CAA38576. (PubMed:1508153)Curated
    Sequence conflicti573 – 58513NVFGK…ILERR → MFSQAKAHFRKT in CAA38576. (PubMed:1508153)CuratedAdd
    BLAST
    Sequence conflicti837 – 8382SD → DV in AAA22628. (PubMed:2500417)Curated
    Sequence conflicti838 – 8381D → V in CAA38576. (PubMed:1508153)Curated
    Sequence conflicti927 – 94418VHKKE…LTRKN → EFIKKNRNVLYLIA in CAA38576. (PubMed:1508153)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54805 Genomic DNA. Translation: CAA38576.1.
    AL009126 Genomic DNA. Translation: CAB13829.3.
    AF026147 Genomic DNA. Translation: AAC17864.1.
    M27141 Genomic DNA. Translation: AAA22628.1.
    PIRiS25295. A32879.
    RefSeqiNP_389819.3. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13829; CAB13829; BSU19370.
    GeneIDi939507.
    KEGGibsu:BSU19370.
    PATRICi18975725. VBIBacSub10457_2053.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54805 Genomic DNA. Translation: CAA38576.1 .
    AL009126 Genomic DNA. Translation: CAB13829.3 .
    AF026147 Genomic DNA. Translation: AAC17864.1 .
    M27141 Genomic DNA. Translation: AAA22628.1 .
    PIRi S25295. A32879.
    RefSeqi NP_389819.3. NC_000964.3.

    3D structure databases

    ProteinModelPortali P23129.
    SMRi P23129. Positions 71-943.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU19370.

    Proteomic databases

    PaxDbi P23129.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13829 ; CAB13829 ; BSU19370 .
    GeneIDi 939507.
    KEGGi bsu:BSU19370.
    PATRICi 18975725. VBIBacSub10457_2053.

    Organism-specific databases

    GenoListi BSU19370. [Micado ]

    Phylogenomic databases

    eggNOGi COG0567.
    HOGENOMi HOG000259588.
    KOi K00164.
    OrthoDBi EOG6V1M1F.
    PhylomeDBi P23129.

    Enzyme and pathway databases

    BioCyci BSUB:BSU19370-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.970. 2 hits.
    HAMAPi MF_01169. SucA_OdhA.
    InterProi IPR011603. 2oxoglutarate_DH_E1.
    IPR023784. 2oxoglutarate_DH_E1_bac.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view ]
    PANTHERi PTHR23152. PTHR23152. 1 hit.
    Pfami PF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex."
      Resnekov O., Melin L., Carlsson P., Mannerloev M., von Gabain A., Hederstedt L.
      Mol. Gen. Genet. 234:285-296(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      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.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence."
      Medigue C., Rose M., Viari A., Danchin A.
      Genome Res. 9:1116-1127(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "Sequence analysis of the Bacillus subtilis 168 chromosome region between the sspC and odhA loci (184 degrees-180 degrees)."
      Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D., Park S.-H.
      DNA Res. 5:195-201(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270.
      Strain: 168.
    6. "Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively."
      Carlsson P., Hederstedt L.
      J. Bacteriol. 171:3667-3672(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-944.
      Strain: 168.

    Entry informationi

    Entry nameiODO1_BACSU
    AccessioniPrimary (citable) accession number: P23129
    Secondary accession number(s): O68261, Q45642
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 113 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3