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P49432

- ODPB_RAT

UniProt

P49432 - ODPB_RAT

Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

Pdhb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.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 sitei89 – 891Thiamine pyrophosphateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: RGD
    2. glucose metabolic process Source: UniProtKB-KW
    3. tricarboxylic acid cycle Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Enzyme and pathway databases

    ReactomeiREACT_203088. Pyruvate metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1)
    Short name:
    PDHE1-B
    Gene namesi
    Name:Pdhb
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi1359146. Pdhb.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: RGD
    3. pyruvate dehydrogenase complex Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
    BLAST
    Chaini31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020459Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671PhosphotyrosineBy similarity
    Modified residuei354 – 3541N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP49432.
    PRIDEiP49432.

    2D gel databases

    UCD-2DPAGEP49432.
    World-2DPAGE0004:P49432.

    PTM databases

    PhosphoSiteiP49432.

    Expressioni

    Gene expression databases

    GenevestigatoriP49432.

    Interactioni

    Subunit structurei

    Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules By similarity.By similarity

    Protein-protein interaction databases

    IntActiP49432. 2 interactions.
    MINTiMINT-4592348.
    STRINGi10116.ENSRNOP00000010545.

    Structurei

    3D structure databases

    ProteinModelPortaliP49432.
    SMRiP49432. Positions 30-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0022.
    GeneTreeiENSGT00530000063423.
    HOGENOMiHOG000281450.
    HOVERGENiHBG000917.
    InParanoidiP49432.
    KOiK00162.
    OMAiNVKVPMV.
    OrthoDBiEOG7KSX8S.
    PhylomeDBiP49432.
    TreeFamiTF105674.

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProiIPR027110. PDHB.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view]
    PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P49432-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD    50
    EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA 100
    MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSAGLQPV PIVFRGPNGA 150
    SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDDNPVVML 200
    ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV AHSRPVGHCL 250
    EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG 300
    VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII 350
    FAIKKTLNI 359
    Length:359
    Mass (Da):38,982
    Last modified:January 9, 2007 - v2
    Checksum:i1B942D0A68C86D51
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31A → G(PubMed:2025639)Curated
    Sequence conflicti11 – 155PLRQA → LCGRL(PubMed:2025639)Curated
    Sequence conflicti22 – 221R → L(PubMed:2025639)Curated
    Sequence conflicti25 – 251R → C(PubMed:2025639)Curated
    Sequence conflicti238 – 2381T → N(PubMed:2025639)Curated
    Sequence conflicti241 – 2422AH → CY(PubMed:2025639)Curated
    Sequence conflicti259 – 2591E → G(PubMed:2025639)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC079137 mRNA. Translation: AAH79137.1.
    PIRiS15892.
    RefSeqiNP_001007621.1. NM_001007620.1.
    XP_006251816.1. XM_006251754.1.
    UniGeneiRn.102424.

    Genome annotation databases

    EnsembliENSRNOT00000010545; ENSRNOP00000010545; ENSRNOG00000007895.
    GeneIDi289950.
    KEGGirno:289950.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC079137 mRNA. Translation: AAH79137.1 .
    PIRi S15892.
    RefSeqi NP_001007621.1. NM_001007620.1.
    XP_006251816.1. XM_006251754.1.
    UniGenei Rn.102424.

    3D structure databases

    ProteinModelPortali P49432.
    SMRi P49432. Positions 30-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P49432. 2 interactions.
    MINTi MINT-4592348.
    STRINGi 10116.ENSRNOP00000010545.

    PTM databases

    PhosphoSitei P49432.

    2D gel databases

    UCD-2DPAGE P49432.
    World-2DPAGE 0004:P49432.

    Proteomic databases

    PaxDbi P49432.
    PRIDEi P49432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000010545 ; ENSRNOP00000010545 ; ENSRNOG00000007895 .
    GeneIDi 289950.
    KEGGi rno:289950.

    Organism-specific databases

    CTDi 5162.
    RGDi 1359146. Pdhb.

    Phylogenomic databases

    eggNOGi COG0022.
    GeneTreei ENSGT00530000063423.
    HOGENOMi HOG000281450.
    HOVERGENi HBG000917.
    InParanoidi P49432.
    KOi K00162.
    OMAi NVKVPMV.
    OrthoDBi EOG7KSX8S.
    PhylomeDBi P49432.
    TreeFami TF105674.

    Enzyme and pathway databases

    Reactomei REACT_203088. Pyruvate metabolism.

    Miscellaneous databases

    NextBioi 630523.
    PROi P49432.

    Gene expression databases

    Genevestigatori P49432.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProi IPR027110. PDHB.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view ]
    PANTHERi PTHR11624:SF56. PTHR11624:SF56. 1 hit.
    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. "The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase."
      Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T.
      Biochim. Biophys. Acta 1089:1-7(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    3. Dunn M.J.
      Submitted (MAR-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 31-38.
      Tissue: Heart.
    4. Lubec G., Afjehi-Sadat L., Diao W.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 286-324, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.

    Entry informationi

    Entry nameiODPB_RAT
    AccessioniPrimary (citable) accession number: P49432
    Secondary accession number(s): Q6AY95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    External Data

    Dasty 3