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A7MB35

- ODPA_BOVIN

UniProt

A7MB35 - ODPA_BOVIN

Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (02 Oct 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

    Enzyme regulationi

    Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
    2. glucose metabolic process Source: UniProtKB-KW
    3. glycolytic process Source: InterPro
    4. 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_204177. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_226374. Pyruvate metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC:1.2.4.1)
    Alternative name(s):
    PDHE1-A type I
    Gene namesi
    Name:PDHA1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome X

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionBy similarityAdd
    BLAST
    Chaini30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialPRO_0000329312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631N6-acetyllysine; alternateBy similarity
    Modified residuei63 – 631N6-succinyllysine; alternateBy similarity
    Modified residuei232 – 2321Phosphoserine; by PDK1By similarity
    Modified residuei244 – 2441N6-acetyllysine; alternateBy similarity
    Modified residuei244 – 2441N6-succinyllysine; alternateBy similarity
    Modified residuei267 – 2671N6-acetyllysineBy similarity
    Modified residuei277 – 2771N6-succinyllysineBy similarity
    Modified residuei293 – 2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
    Modified residuei295 – 2951PhosphoserineBy similarity
    Modified residuei300 – 3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
    Modified residuei301 – 3011PhosphotyrosineBy similarity
    Modified residuei313 – 3131N6-acetyllysine; alternateBy similarity
    Modified residuei313 – 3131N6-succinyllysine; alternateBy similarity
    Modified residuei321 – 3211N6-acetyllysineBy similarity
    Modified residuei336 – 3361N6-acetyllysineBy similarity
    Modified residuei385 – 3851N6-succinyllysineBy similarity

    Post-translational modificationi

    Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation By similarity.By similarity
    Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiA7MB35.
    PRIDEiA7MB35.

    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

    STRINGi9913.ENSBTAP00000052439.

    Structurei

    3D structure databases

    ProteinModelPortaliA7MB35.
    SMRiA7MB35. Positions 30-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1071.
    GeneTreeiENSGT00530000063174.
    HOGENOMiHOG000281336.
    HOVERGENiHBG001863.
    InParanoidiA7MB35.
    KOiK00161.
    OMAiRGPNQWI.
    OrthoDBiEOG73JKVQ.
    TreeFamiTF300742.

    Family and domain databases

    Gene3Di3.40.50.970. 1 hit.
    InterProiIPR001017. DH_E1.
    IPR017597. Pyrv_DH_E1_asu_subgrp-y.
    IPR029061. THDP-binding.
    [Graphical view]
    PfamiPF00676. E1_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 1 hit.
    TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A7MB35-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKMLAAVSR VLSGVAQKPA SRVLVASRHF ANDATFEIKK CDLHRLEEGP    50
    PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC 100
    CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RRGGCAKGKG 150
    GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN 200
    QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP 250
    GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 300
    YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA 350
    QFATADPEPP LEELGYHIYC NDPPFEVRGA NQWIKFKSIS 390
    Length:390
    Mass (Da):43,388
    Last modified:October 2, 2007 - v1
    Checksum:i1297C2B1960BBEDF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC151313 mRNA. Translation: AAI51314.1.
    RefSeqiNP_001094516.1. NM_001101046.2.
    UniGeneiBt.19415.

    Genome annotation databases

    EnsembliENSBTAT00000057115; ENSBTAP00000052439; ENSBTAG00000019852.
    GeneIDi407109.
    KEGGibta:407109.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC151313 mRNA. Translation: AAI51314.1 .
    RefSeqi NP_001094516.1. NM_001101046.2.
    UniGenei Bt.19415.

    3D structure databases

    ProteinModelPortali A7MB35.
    SMRi A7MB35. Positions 30-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000052439.

    Proteomic databases

    PaxDbi A7MB35.
    PRIDEi A7MB35.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000057115 ; ENSBTAP00000052439 ; ENSBTAG00000019852 .
    GeneIDi 407109.
    KEGGi bta:407109.

    Organism-specific databases

    CTDi 5160.

    Phylogenomic databases

    eggNOGi COG1071.
    GeneTreei ENSGT00530000063174.
    HOGENOMi HOG000281336.
    HOVERGENi HBG001863.
    InParanoidi A7MB35.
    KOi K00161.
    OMAi RGPNQWI.
    OrthoDBi EOG73JKVQ.
    TreeFami TF300742.

    Enzyme and pathway databases

    Reactomei REACT_204177. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_226374. Pyruvate metabolism.

    Miscellaneous databases

    NextBioi 20818379.

    Family and domain databases

    Gene3Di 3.40.50.970. 1 hit.
    InterProi IPR001017. DH_E1.
    IPR017597. Pyrv_DH_E1_asu_subgrp-y.
    IPR029061. THDP-binding.
    [Graphical view ]
    Pfami PF00676. E1_dh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 1 hit.
    TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Hypothalamus.

    Entry informationi

    Entry nameiODPA_BOVIN
    AccessioniPrimary (citable) accession number: A7MB35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    External Data

    Dasty 3