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P29804

- ODPA_PIG

UniProt

P29804 - ODPA_PIG

Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      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.1 Publication

    Catalytic activityi

    Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.1 Publication

    Cofactori

    Thiamine pyrophosphate.1 Publication

    Enzyme regulationi

    Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.1 Publication

    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    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 peptidei‹1 – 28›28MitochondrionBy similarityAdd
    BLAST
    Chaini29 – 389361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialPRO_0000020443Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621N6-acetyllysine; alternateBy similarity
    Modified residuei62 – 621N6-succinyllysine; alternateBy similarity
    Modified residuei231 – 2311Phosphoserine; by PDK1By similarity
    Modified residuei243 – 2431N6-acetyllysine; alternateBy similarity
    Modified residuei243 – 2431N6-succinyllysine; alternateBy similarity
    Modified residuei276 – 2761N6-succinyllysineBy similarity
    Modified residuei292 – 2921Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
    Modified residuei294 – 2941PhosphoserineBy similarity
    Modified residuei299 – 2991Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
    Modified residuei300 – 3001PhosphotyrosineBy similarity
    Modified residuei312 – 3121N6-acetyllysine; alternateBy similarity
    Modified residuei312 – 3121N6-succinyllysine; alternateBy similarity
    Modified residuei320 – 3201N6-acetyllysineBy similarity
    Modified residuei335 – 3351N6-acetyllysineBy similarity
    Modified residuei384 – 3841N6-succinyllysineBy similarity

    Post-translational modificationi

    Phosphorylation at Ser-231, Ser-292 and Ser-299 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-292 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-231, Ser-292 and Ser-299, is required for reactivation.1 Publication
    Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP29804.

    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

    ProteinModelPortaliP29804.
    SMRiP29804. Positions 28-389.
    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: Fragment.

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

    P29804-1 [UniParc]FASTAAdd to Basket

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    GKMLAAVSRV LSGVAQKPAS RVLVASRTFA NDATFEIKKC DLHRLEEGPP    50
    VTTVLTREDG LKYYRMMQTV RRMELKADQL YKQKIIRGFC HLCDGQEACC 100
    VGLEAGINPT DHLITAYRAH GFTFTRGLSV REILAELTGR RGGCGKGKGG 150
    SMHMYAKNFY GGNGIVGAQV PLGAGIALAC KYNGKDEVCL TLYGDGAANQ 200
    GQIFEAYNMA ALWKLPCVFI CENNRYGMGT SVERAAASTD YYKRGDFIPG 250
    LRVDGMDILC VREATRFAAA YCRSGKGPIL MELQTYRYHG HSMSDPGVSY 300
    RTREEIQEVR SKSDPIMLLK DRMVNSNLAS VEELKEIDVE VRKEIEDAAQ 350
    FATADPEPPL EELGYHIYCN DPPFEVRGAN QWIKFKSIS 389
    Length:389
    Mass (Da):43,121
    Last modified:April 1, 1993 - v1
    Checksum:iE9C7DF85389A9A47
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52990 mRNA. Translation: CAA37180.1.
    PIRiS20813. DEPGPA.
    UniGeneiSsc.50287.
    Ssc.98154.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52990 mRNA. Translation: CAA37180.1 .
    PIRi S20813. DEPGPA.
    UniGenei Ssc.50287.
    Ssc.98154.

    3D structure databases

    ProteinModelPortali P29804.
    SMRi P29804. Positions 28-389.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P29804.

    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. "Characterisation of a cDNA for porcine PDH-E1 alpha and comparison with the human cDNA."
      Sermon K., Demeirleir L., Elpers I., Lissens W., Liebaers I.
      Nucleic Acids Res. 18:4925-4925(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Muscle.
    2. "Regulation of kinase reactions in pig heart pyruvate dehydrogenase complex."
      Kerbey A.L., Radcliffe P.M., Randle P.J., Sugden P.H.
      Biochem. J. 181:427-433(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, COFACTOR, PHOSPHORYLATION AT SER-231; SER-292 AND SER-299.

    Entry informationi

    Entry nameiODPA_PIG
    AccessioniPrimary (citable) accession number: P29804
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 81 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