Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A5A6L0

- ODPA_PANTR

UniProt

A5A6L0 - ODPA_PANTR

Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    OrganismiPan troglodytes (Chimpanzee)
    Taxonomic identifieri9598 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
    ProteomesiUP000002277: Unplaced

    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_0000297491Add
    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

    PRIDEiA5A6L0.

    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

    ProteinModelPortaliA5A6L0.
    SMRiA5A6L0. Positions 29-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1071.
    HOGENOMiHOG000281336.
    HOVERGENiHBG001863.
    InParanoidiA5A6L0.
    KOiK00161.

    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.

    A5A6L0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP    50
    PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC 100
    CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG 150
    GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN 200
    QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP 250
    GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSGPGVS 300
    YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA 350
    QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 390
    Length:390
    Mass (Da):43,238
    Last modified:June 12, 2007 - v1
    Checksum:i4F95746CBB792E78
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB222138 mRNA. Translation: BAF62383.1.
    RefSeqiNP_001104283.1. NM_001110813.1.
    UniGeneiPtr.3278.

    Genome annotation databases

    GeneIDi465525.
    KEGGiptr:465525.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB222138 mRNA. Translation: BAF62383.1 .
    RefSeqi NP_001104283.1. NM_001110813.1.
    UniGenei Ptr.3278.

    3D structure databases

    ProteinModelPortali A5A6L0.
    SMRi A5A6L0. Positions 29-390.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi A5A6L0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 465525.
    KEGGi ptr:465525.

    Organism-specific databases

    CTDi 5160.

    Phylogenomic databases

    eggNOGi COG1071.
    HOGENOMi HOG000281336.
    HOVERGENi HBG001863.
    InParanoidi A5A6L0.
    KOi K00161.

    Miscellaneous databases

    NextBioi 20843882.

    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. "Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome."
      Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.
      Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.

    Entry informationi

    Entry nameiODPA_PANTR
    AccessioniPrimary (citable) accession number: A5A6L0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 51 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