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O13366

- ODPA_KLULA

UniProt

O13366 - ODPA_KLULA

Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene

PDA1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (27 Sep 2004)
      Previous versions | rss
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    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.By similarity

    Enzyme regulationi

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    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
    Gene namesi
    Name:PDA1
    Ordered Locus Names:KLLA0F12001g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome F

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 412Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020450
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Tetramer of 2 alpha and 2 beta subunits.By similarity

    Protein-protein interaction databases

    STRINGi28985.O13366.

    Structurei

    3D structure databases

    ProteinModelPortaliO13366.
    SMRiO13366. Positions 62-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1071.
    HOGENOMiHOG000281336.
    KOiK00161.
    OMAiRERTCHA.
    OrthoDBiEOG7QZGMC.

    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.

    O13366-1 [UniParc]FASTAAdd to Basket

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    MLSLKAQSSV VGKSSSLRLV RNFSKNVRAL SQVADETKPG DDDLVQIDLP    50
    ETSFEGYLLD VPELSYQTTK SNLLQMYKDM IIVRRMEMAC DALYKAKKIR 100
    GFCHSSVGQE AIAVGIENAI TKRDTVITSY RCHGFTYMRG AAVQAVLAEL 150
    MGRRTGVSFG KGGSMHLYAP GFYGGNGIVG AQVPLGAGLA FAHQYKHEDA 200
    CSFALYGDGA SNQGQVFESF NMAKLWNLPA VFCCENNKYG MGTAAARSSA 250
    MTEYFKRGQY IPGLKVNGMD ILAVYQASKF AKDWTVSGNG PIVLEYETYR 300
    YGGHSMSDPG TTYRTRDEIQ HMRSKNDPIA GLKMHLLELG IATEDEIKAY 350
    DKAARKYVDE QVELADAAPA PEAKMSILFE DVYVPGSETP TLRGRLQEDT 400
    WDFAKKSFAF RD 412
    Length:412
    Mass (Da):45,453
    Last modified:September 27, 2004 - v2
    Checksum:iCBCC8AB3DC4C7E96
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti275 – 2817YQASKFA → TKL in AAD03773. (PubMed:9884236)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023920 Genomic DNA. Translation: AAD03773.1.
    CR382126 Genomic DNA. Translation: CAG98332.1.
    RefSeqiXP_455624.1. XM_455624.1.

    Genome annotation databases

    GeneIDi2894999.
    KEGGikla:KLLA0F12001g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023920 Genomic DNA. Translation: AAD03773.1 .
    CR382126 Genomic DNA. Translation: CAG98332.1 .
    RefSeqi XP_455624.1. XM_455624.1.

    3D structure databases

    ProteinModelPortali O13366.
    SMRi O13366. Positions 62-397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.O13366.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2894999.
    KEGGi kla:KLLA0F12001g.

    Phylogenomic databases

    eggNOGi COG1071.
    HOGENOMi HOG000281336.
    KOi K00161.
    OMAi RERTCHA.
    OrthoDBi EOG7QZGMC.

    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. "Inactivation of the Kluyveromyces lactis KlPDA1 gene leads to loss of pyruvate dehydrogenase activity, impairs growth on glucose and triggers aerobic alcoholic fermentation."
      Zeeman A.-M., Luttik M.A.H., Thiele C., van Dijken J.P., Pronk J.T., Steensma H.Y.
      Microbiology 144:3437-3446(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC MYA-539 / JBD100.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

    Entry informationi

    Entry nameiODPA_KLULA
    AccessioniPrimary (citable) accession number: O13366
    Secondary accession number(s): Q6CKB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    External Data

    Dasty 3