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)

P52903

- ODPA_SOLTU

UniProt

P52903 - ODPA_SOLTU

Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.

    Enzyme regulationi

    E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.By similarity

    GO - Molecular functioni

    1. cobalt ion binding Source: EnsemblPlants/Gramene
    2. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
    3. zinc ion binding Source: EnsemblPlants/Gramene

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW
    2. response to salt stress Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (EC:1.2.4.1)
    Short name:
    PDHE1-A
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EnsemblPlants/Gramene
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. nucleus Source: EnsemblPlants/Gramene

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2626Mitochondrion1 PublicationAdd
    BLAST
    Chaini27 – 391365Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020455Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    ProMEXiP52903.

    Interactioni

    Subunit structurei

    Tetramer of 2 alpha and 2 beta subunits.By similarity

    Protein-protein interaction databases

    IntActiP52903. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP52903.
    SMRiP52903. Positions 32-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    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.

    P52903-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSTSRAIN HIMKPLSAAV CATRRLSSDS TATITVETSL PFTSHNIDPP    50
    SRSVETSPKE LMTFFKDMTE MRRMEIAADS LYKAKLIRGF CHLYDGQEAV 100
    AVGMEAAITK KDCIITAYRD HCIFLGRGGT LVEAFAELMG RRDGCSRGKG 150
    GSMHFYKKES GFYGGHGIVG AQVPLGIGLA FAQKYKKEDY VTFAMYGDGA 200
    ANQGQLFEAL NMAALWDLPA ILVCENNHYG MGTAEWRAAK SPAYYKRGDY 250
    VPGLRVDGMD VFAVKQACTF AKQHALKNGP IILEMDTYRY HGHSMSDPGS 300
    TYRTRDEISG VRQERDPVER IRSLILAHNI ATEAELKDIE KENRKVVDEA 350
    IAKAKESPMP DPSELFTNVY VKGFGVEAYG ADRKELRATL P 391
    Length:391
    Mass (Da):43,228
    Last modified:October 1, 1996 - v1
    Checksum:iF9110B374B022F0D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z26949 mRNA. Translation: CAA81558.1.
    PIRiT07372.
    UniGeneiStu.18026.

    Genome annotation databases

    EnsemblPlantsiPGSC0003DMT400058223; PGSC0003DMT400058223; PGSC0003DMG400022607.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z26949 mRNA. Translation: CAA81558.1 .
    PIRi T07372.
    UniGenei Stu.18026.

    3D structure databases

    ProteinModelPortali P52903.
    SMRi P52903. Positions 32-379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P52903. 1 interaction.

    Proteomic databases

    ProMEXi P52903.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi PGSC0003DMT400058223 ; PGSC0003DMT400058223 ; PGSC0003DMG400022607 .

    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. "Mitochondrial pyruvate dehydrogenase. Molecular cloning of the E1 alpha subunit and expression analysis."
      Grof C.P., Winning B.M., Scaysbrook T.P., Hill S.A., Leaver C.J.
      Plant Physiol. 108:1623-1629(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Desiree.
      Tissue: Leaf.
    2. "Genome sequence and analysis of the tuber crop potato."
      The Potato Genome Sequencing Consortium
      Nature 475:189-195(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. DM1-3 516 R44.
    3. "Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato."
      Millar A.H., Knorpp C., Leaver C.J., Hill S.A.
      Biochem. J. 334:571-576(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-42.
      Strain: cv. Romano.
      Tissue: Tuber.

    Entry informationi

    Entry nameiODPA_SOLTU
    AccessioniPrimary (citable) accession number: P52903
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    External Data

    Dasty 3