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P16451

- ODPX_YEAST

UniProt

P16451 - ODPX_YEAST

Protein

Pyruvate dehydrogenase complex protein X component, mitochondrial

Gene

PDX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.

    GO - Molecular functioni

    1. structural molecule activity Source: SGD
    2. transferase activity, transferring acyl groups Source: InterPro

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:YGR193C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase complex protein X component, mitochondrial
    Alternative name(s):
    Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
    E3-binding protein
    Pyruvate dehydrogenase complex component E3BP
    Gene namesi
    Name:PDX1
    Ordered Locus Names:YGR193C
    ORF Names:G7579
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR193c.
    SGDiS000003425. PDX1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial pyruvate dehydrogenase complex Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
    BLAST
    Chaini31 – 410380Pyruvate dehydrogenase complex protein X component, mitochondrialPRO_0000020487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei73 – 731N6-lipoyllysineBy similarity

    Proteomic databases

    MaxQBiP16451.
    PaxDbiP16451.
    PeptideAtlasiP16451.

    Expressioni

    Gene expression databases

    GenevestigatoriP16451.

    Interactioni

    Subunit structurei

    Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.

    Protein-protein interaction databases

    BioGridi33446. 31 interactions.
    DIPiDIP-5550N.
    IntActiP16451. 8 interactions.
    MINTiMINT-508924.
    STRINGi4932.YGR193C.

    Structurei

    3D structure databases

    ProteinModelPortaliP16451.
    SMRiP16451. Positions 37-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 10775Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00750000118712.
    HOGENOMiHOG000246828.
    OMAiKWICERQ.
    OrthoDBiEOG7W41P8.

    Family and domain databases

    Gene3Di4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR000089. Biotin_lipoyl.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16451-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSAISKVST LKSCTRYLTK CNYHASAKLL AVKTFSMPAM SPTMEKGGIV    50
    SWKYKVGEPF SAGDVILEVE TDKSQIDVEA LDDGKLAKIL KDEGSKDVDV 100
    GEPIAYIADV DDDLATIKLP QEANTANAKS IEIKKPSADS TEATQQHLKK 150
    ATVTPIKTVD GSQANLEQTL LPSVSLLLAE NNISKQKALK EIAPSGSNGR 200
    LLKGDVLAYL GKIPQDSVNK VTEFIKKNER LDLSNIKPIQ LKPKIAEQAQ 250
    TKAADKPKIT PVEFEEQLVF HAPASIPFDK LSESLNSFMK EAYQFSHGTP 300
    LMDTNSKYFD PIFEDLVTLS PREPRFKFSY DLMQIPKANN MQDTYGQEDI 350
    FDLLTGSDAT ASSVRPVEKN LPEKNEYILA LNVSVNNKKF NDAEAKAKRF 400
    LDYVRELESF 410
    Length:410
    Mass (Da):45,362
    Last modified:August 1, 1990 - v1
    Checksum:i11649CA28C420CDF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti378 – 3781I → M in AAT93002. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28222 Genomic DNA. Translation: AAA34910.1.
    X82408 Genomic DNA. Translation: CAA57804.1.
    Z72978 Genomic DNA. Translation: CAA97219.1.
    AY692983 Genomic DNA. Translation: AAT93002.1.
    BK006941 Genomic DNA. Translation: DAA08286.1.
    PIRiA36183. DEBYPX.
    RefSeqiNP_011709.1. NM_001181322.1.

    Genome annotation databases

    EnsemblFungiiYGR193C; YGR193C; YGR193C.
    GeneIDi853107.
    KEGGisce:YGR193C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28222 Genomic DNA. Translation: AAA34910.1 .
    X82408 Genomic DNA. Translation: CAA57804.1 .
    Z72978 Genomic DNA. Translation: CAA97219.1 .
    AY692983 Genomic DNA. Translation: AAT93002.1 .
    BK006941 Genomic DNA. Translation: DAA08286.1 .
    PIRi A36183. DEBYPX.
    RefSeqi NP_011709.1. NM_001181322.1.

    3D structure databases

    ProteinModelPortali P16451.
    SMRi P16451. Positions 37-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33446. 31 interactions.
    DIPi DIP-5550N.
    IntActi P16451. 8 interactions.
    MINTi MINT-508924.
    STRINGi 4932.YGR193C.

    Proteomic databases

    MaxQBi P16451.
    PaxDbi P16451.
    PeptideAtlasi P16451.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR193C ; YGR193C ; YGR193C .
    GeneIDi 853107.
    KEGGi sce:YGR193C.

    Organism-specific databases

    CYGDi YGR193c.
    SGDi S000003425. PDX1.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00750000118712.
    HOGENOMi HOG000246828.
    OMAi KWICERQ.
    OrthoDBi EOG7W41P8.

    Enzyme and pathway databases

    BioCyci YEAST:YGR193C-MONOMER.

    Miscellaneous databases

    NextBioi 973115.

    Gene expression databases

    Genevestigatori P16451.

    Family and domain databases

    Gene3Di 4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR000089. Biotin_lipoyl.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae."
      Behal R.H., Browning K.S., Hall T.B., Reed L.J.
      Proc. Natl. Acad. Sci. U.S.A. 86:8732-8736(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-60 AND 192-206.
    2. "The complete sequence of a 9037 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII."
      Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.
      Yeast 11:587-591(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex."
      Lawson J.E., Behal R.H., Reed L.J.
      Biochemistry 30:2834-2839(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiODPX_YEAST
    AccessioniPrimary (citable) accession number: P16451
    Secondary accession number(s): D6VUX5, E9P906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 414 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3