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Q8HXW9

- ODPA_MACFA

UniProt

Q8HXW9 - ODPA_MACFA

Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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

    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
    ORF Names:QccE-20080
    OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
    Taxonomic identifieri9541 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

    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_0000020441Add
    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 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

    PRIDEiQ8HXW9.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliQ8HXW9.
    SMRiQ8HXW9. Positions 29-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG001863.

    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.

    Q8HXW9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP    50
    PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC 100
    CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG 150
    GSTHMYAKNF YRGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAD 200
    QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP 250
    GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 300
    YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA 350
    QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 390
    Length:390
    Mass (Da):43,366
    Last modified:March 1, 2003 - v1
    Checksum:i420CE38364BDB33C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB083322 mRNA. Translation: BAC20601.1.
    UniGeneiMfa.1100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB083322 mRNA. Translation: BAC20601.1 .
    UniGenei Mfa.1100.

    3D structure databases

    ProteinModelPortali Q8HXW9.
    SMRi Q8HXW9. Positions 29-390.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q8HXW9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG001863.

    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. "Isolation and characterization of cDNA for macaque neurological disease genes."
      Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiODPA_MACFA
    AccessioniPrimary (citable) accession number: Q8HXW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program