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Q81TK1

- ODO1_BACAN

UniProt

Q81TK1 - ODO1_BACAN

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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).UniRule annotation

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.UniRule annotation

    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

    BioCyciANTHRA:ODHA-MONOMER.
    BANT260799:GJAJ-1251-MONOMER.
    BANT261594:GJ7F-1307-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase E1 componentUniRule annotation (EC:1.2.4.2UniRule annotation)
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenaseUniRule annotation
    Gene namesi
    Name:odhAUniRule annotation
    Ordered Locus Names:BA_1270, GBAA_1270, BAS1177
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9559552-oxoglutarate dehydrogenase E1 componentPRO_0000162161Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ81TK1. 5 interactions.
    STRINGi198094.BA_1270.

    Structurei

    3D structure databases

    ProteinModelPortaliQ81TK1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259588.
    KOiK00164.
    OMAiNEEERRW.
    OrthoDBiEOG6V1M1F.

    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.

    Q81TK1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRKNTTTNP WAKFHGPNLG YVIEQYDLYV TGAGSVDPEL QELFEIFGAP    50
    SFQDDVVTGD NTATHFSPQN TGNIEKILKV VQLVEQIRSF GHTLAHINPM 100
    EDAANGQSLL EKAMNELSDA DLKAIPAKTV WQDAPEGIHT ALDVIHRLKE 150
    VYTQSLAYEF SHIQDSEERA WLHQMVESNS LRQPLSNKKR TALLKRLTAV 200
    EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EIVLEGAKNG VEDVMIGMAH 250
    RGRLSVLAHV LEKPYSHMFA EFKHAKIEGA VANSGWTGDV KYHLGREQVV 300
    SNEEVSTRVT LANNPSHLEF VNPVVEGFAR AAQENRKKSG LPEQDTSKSF 350
    VILVHGDAAF PGQGIVSETL NLSRLNAYQT GGTIHVIANN AVGFTTDSYD 400
    SRSTKYSSDL AKGFDIPIVH VNADDPEACL AAANLAIQYR MLFKKDFLID 450
    LIGYRRYGHN EMDDPAVTQP QVYKKIKNHP TVRAIYADQL QAAGVLNADE 500
    IETITQFTQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG IQPIDTGVEL 550
    DSLRAINEGL LSWPEGFNVY PKVKKILERR KDALEENGKI EWALAESLAF 600
    ASILQEGTPI RLTGQDSQRG TFAHRHIVLH DTDTNETYSP LHRLPNINAS 650
    FSVHNSPLSE AAVVGYEYGY NVFAPETLVM WEAQYGDFSN TAQALFDQYV 700
    SAGRAKWGQK SGLVLLLPHG YEGQGPEHSS ARPERFLQLA AENNWTVANL 750
    TSAAQYFHIL RRQASILGTE AVRPLVLMTP KSLLRHPLTL STANQLSEGR 800
    FQPALEQENL GTKPNKVKRL VLSTGKMAID LAAEIESGRH EYNLDEIHIV 850
    RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA 900
    GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVSHALDVK YNFRQDKLEI 950
    EVFSN 955
    Length:955
    Mass (Da):106,519
    Last modified:June 1, 2003 - v1
    Checksum:i0A7BEDB8CE00E280
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25228.1.
    AE017334 Genomic DNA. Translation: AAT30361.1.
    AE017225 Genomic DNA. Translation: AAT53498.1.
    RefSeqiNP_843742.1. NC_003997.3.
    YP_017886.1. NC_007530.2.
    YP_027447.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP25228; AAP25228; BA_1270.
    AAT30361; AAT30361; GBAA_1270.
    AAT53498; AAT53498; BAS1177.
    GeneIDi1086638.
    2816661.
    2848680.
    KEGGiban:BA_1270.
    bar:GBAA_1270.
    bat:BAS1177.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25228.1 .
    AE017334 Genomic DNA. Translation: AAT30361.1 .
    AE017225 Genomic DNA. Translation: AAT53498.1 .
    RefSeqi NP_843742.1. NC_003997.3.
    YP_017886.1. NC_007530.2.
    YP_027447.1. NC_005945.1.

    3D structure databases

    ProteinModelPortali Q81TK1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q81TK1. 5 interactions.
    STRINGi 198094.BA_1270.

    Protocols and materials databases

    DNASUi 1086638.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP25228 ; AAP25228 ; BA_1270 .
    AAT30361 ; AAT30361 ; GBAA_1270 .
    AAT53498 ; AAT53498 ; BAS1177 .
    GeneIDi 1086638.
    2816661.
    2848680.
    KEGGi ban:BA_1270.
    bar:GBAA_1270.
    bat:BAS1177.

    Phylogenomic databases

    eggNOGi COG0567.
    HOGENOMi HOG000259588.
    KOi K00164.
    OMAi NEEERRW.
    OrthoDBi EOG6V1M1F.

    Enzyme and pathway databases

    BioCyci ANTHRA:ODHA-MONOMER.
    BANT260799:GJAJ-1251-MONOMER.
    BANT261594:GJ7F-1307-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. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
      Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
      , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
      Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames / isolate Porton.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames ancestor.
    3. "Complete genome sequence of Bacillus anthracis Sterne."
      Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sterne.

    Entry informationi

    Entry nameiODO1_BACAN
    AccessioniPrimary (citable) accession number: Q81TK1
    Secondary accession number(s): Q6I1T3, Q6KVM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3