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Q6ABX8

- ODPB_LEIXX

UniProt

Q6ABX8 - ODPB_LEIXX

Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

    Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

    Cofactori

    Thiamine pyrophosphate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731Thiamine pyrophosphateBy similarity

    GO - Molecular functioni

    1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciLXYL281090:GH0X-2350-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
    Gene namesi
    Name:pdhB
    Ordered Locus Names:Lxx25060
    OrganismiLeifsonia xyli subsp. xyli (strain CTCB07)
    Taxonomic identifieri281090 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia
    ProteomesiUP000001306: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 337337Pyruvate dehydrogenase E1 component subunit betaPRO_0000232457Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.By similarity

    Protein-protein interaction databases

    STRINGi281090.Lxx25060.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ABX8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG0022.
    HOGENOMiHOG000281451.
    KOiK00162.
    OMAiEMHEEST.
    OrthoDBiEOG6JQH4C.

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProiIPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view]
    PfamiPF02779. Transket_pyr. 1 hit.
    PF02780. Transketolase_C. 1 hit.
    [Graphical view]
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 1 hit.
    SSF52922. SSF52922. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6ABX8-1 [UniParc]FASTAAdd to Basket

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    MERAPALAEP EPRVQSLPMV KALNAGLRQA LVADPKVLIL GEDVGPLGGV    50
    FRVTEGLQSE FGASRVVDTP LAEAGIVGTA IGLAMRGYRP VVEIQFNGFV 100
    FPGFDQITTQ LAKMANRHSG AVSMPVVIRI PHGGHIGAVE HHQEAPEAYF 150
    AHTAGLRIVA PSTPHDAYWM IQEAIASDDP VIFFEPMSRY WPKGEVDTLE 200
    NPLPLHASRI VRSGTDATIV AWAGMVPVAL RAAEIAAEEG RSLEVVDLRS 250
    LAPIDYAPVL RSVQKTGRLV VAQEAPGIVS VGSEVAAVVG EKAFYSLEAP 300
    VLRVAGFDTP FPPAKLESLY LPDADRILEV VDRSLAY 337
    Length:337
    Mass (Da):36,087
    Last modified:September 13, 2004 - v1
    Checksum:i2B45A895DC8D84E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016822 Genomic DNA. Translation: AAT90114.1.
    RefSeqiYP_063219.1. NC_006087.1.

    Genome annotation databases

    EnsemblBacteriaiAAT90114; AAT90114; Lxx25060.
    GeneIDi2940400.
    KEGGilxx:Lxx25060.
    PATRICi22338782. VBILeiXyl11655_2623.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016822 Genomic DNA. Translation: AAT90114.1 .
    RefSeqi YP_063219.1. NC_006087.1.

    3D structure databases

    ProteinModelPortali Q6ABX8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 281090.Lxx25060.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT90114 ; AAT90114 ; Lxx25060 .
    GeneIDi 2940400.
    KEGGi lxx:Lxx25060.
    PATRICi 22338782. VBILeiXyl11655_2623.

    Phylogenomic databases

    eggNOGi COG0022.
    HOGENOMi HOG000281451.
    KOi K00162.
    OMAi EMHEEST.
    OrthoDBi EOG6JQH4C.

    Enzyme and pathway databases

    BioCyci LXYL281090:GH0X-2350-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProi IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view ]
    Pfami PF02779. Transket_pyr. 1 hit.
    PF02780. Transketolase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 1 hit.
    SSF52922. SSF52922. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CTCB07.

    Entry informationi

    Entry nameiODPB_LEIXX
    AccessioniPrimary (citable) accession number: Q6ABX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 59 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

    External Data

    Dasty 3