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Protein

Phosphoglycerate mutase 1

Gene

GPM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.2 Publications

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.1 Publication

Enzyme regulationi

Inhibited by inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates.1 Publication

Kineticsi

kcat is 490 sec(-1) for the mutase reaction, 0.0074 sec(-1) for the synthase reaction and 0.0087 sec(-1) for the phosphatase reaction with 3-phosphoglycerate as substrate.1 Publication

  1. KM=740 µM for 3-phosphoglycerate2 Publications
  2. KM=8.1 µM for 2,3-bisphosphoglycerate (for mutase reaction)2 Publications
  3. KM=2.4 µM for 2,3-bisphosphoglycerate (for phosphatase reaction)2 Publications

    Pathway: glycolysis

    This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Glyceraldehyde-3-phosphate dehydrogenase 1 (TDH1), Glyceraldehyde-3-phosphate dehydrogenase 2 (TDH2), Glyceraldehyde-3-phosphate dehydrogenase 3 (TDH3)
    2. Phosphoglycerate kinase (PGK1)
    3. Phosphoglycerate mutase 2 (GPM2), Phosphoglycerate mutase 3 (GPM3), Phosphoglycerate mutase 1 (GPM1)
    4. Enolase 2 (ENO2), Enolase-related protein 2 (ERR2), Enolase-related protein 1 (ERR1), Enolase-related protein 3 (ERR3), Enolase 1 (ENO1)
    5. Pyruvate kinase 2 (PYK2), Pyruvate kinase 1 (CDC19)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei9 – 91Tele-phosphohistidine intermediate3 Publications
    Binding sitei60 – 601Substrate2 Publications
    Binding sitei98 – 981Substrate1 Publication
    Active sitei182 – 18211 Publication

    GO - Molecular functioni

    • phosphoglycerate mutase activity Source: SGD

    GO - Biological processi

    • gluconeogenesis Source: SGD
    • glycolytic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Glycolysis

    Enzyme and pathway databases

    BioCyciMetaCyc:YKL152C-MONOMER.
    YEAST:YKL152C-MONOMER.
    BRENDAi5.4.2.11. 984.
    ReactomeiREACT_275254. Glycolysis.
    REACT_286539. Gluconeogenesis.
    UniPathwayiUPA00109; UER00186.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate mutase 1 (EC:5.4.2.111 Publication)
    Short name:
    PGAM 1
    Alternative name(s):
    BPG-dependent PGAM 1
    MPGM 1
    Phosphoglyceromutase 1
    Gene namesi
    Name:GPM1
    Synonyms:GPM
    Ordered Locus Names:YKL152C
    ORF Names:YKL607
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XI

    Organism-specific databases

    EuPathDBiFungiDB:YKL152C.
    SGDiS000001635. GPM1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: SGD
    • mitochondrial intermembrane space Source: SGD
    • mitochondrion Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1691K → P: Causes dissociation of the homotetramer to dimers at low concentrations. 1 Publication
    Mutagenesisi182 – 1821H → A: Reduces kcat of the mutase reaction 10000-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 247246Phosphoglycerate mutase 1PRO_0000179839Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine1 Publication
    Modified residuei49 – 491Phosphotyrosine1 Publication
    Modified residuei116 – 1161Phosphoserine4 Publications
    Modified residuei127 – 1271Phosphoserine1 Publication
    Modified residuei128 – 1281Phosphoserine1 Publication
    Modified residuei185 – 1851Phosphoserine1 Publication
    Modified residuei197 – 1971Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP00950.
    PaxDbiP00950.
    PeptideAtlasiP00950.

    2D gel databases

    COMPLUYEAST-2DPAGEP00950.
    SWISS-2DPAGEP00950.

    Interactioni

    Subunit structurei

    Homotetramer: dimer of dimers.6 Publications

    Protein-protein interaction databases

    BioGridi33985. 57 interactions.
    DIPiDIP-6260N.
    IntActiP00950. 29 interactions.
    MINTiMINT-603921.
    STRINGi4932.YKL152C.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Helixi13 – 164Combined sources
    Helixi30 – 4516Combined sources
    Beta strandi51 – 555Combined sources
    Helixi59 – 7113Combined sources
    Beta strandi79 – 813Combined sources
    Helixi83 – 853Combined sources
    Helixi91 – 933Combined sources
    Helixi98 – 11518Combined sources
    Beta strandi116 – 1183Combined sources
    Beta strandi126 – 1305Combined sources
    Helixi136 – 1383Combined sources
    Helixi143 – 1453Combined sources
    Helixi152 – 16514Combined sources
    Helixi167 – 1726Combined sources
    Beta strandi177 – 1815Combined sources
    Helixi183 – 19412Combined sources
    Turni198 – 2003Combined sources
    Helixi201 – 2033Combined sources
    Beta strandi208 – 2103Combined sources
    Beta strandi212 – 2165Combined sources
    Turni218 – 2203Combined sources
    Beta strandi222 – 2243Combined sources
    Beta strandi227 – 2304Combined sources
    Turni231 – 2333Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQ3X-ray2.70A/B/C/D2-247[»]
    1BQ4X-ray2.50A/B/C/D2-247[»]
    1QHFX-ray1.70A/B2-241[»]
    3PGMX-ray2.80A/B2-247[»]
    4PGMX-ray2.30A/B/C/D2-247[»]
    5PGMX-ray2.12A/B/C/D/E/F/G/H2-247[»]
    ProteinModelPortaliP00950.
    SMRiP00950. Positions 2-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00950.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni8 – 158Substrate binding4 Publications
    Regioni21 – 222Substrate binding4 Publications
    Regioni87 – 904Substrate binding4 Publications
    Regioni114 – 1152Substrate binding3 Publications
    Regioni183 – 1842Substrate binding2 Publications

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi233 – 24210Ala-rich

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0588.
    GeneTreeiENSGT00390000016700.
    HOGENOMiHOG000221682.
    InParanoidiP00950.
    KOiK01834.
    OMAiLNKDRAR.
    OrthoDBiEOG7SXWF2.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    HAMAPiMF_01039. PGAM_GpmA.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view]
    PANTHERiPTHR11931. PTHR11931. 1 hit.
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    TIGRFAMsiTIGR01258. pgm_1. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00950-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPKLVLVRHG QSEWNEKNLF TGWVDVKLSA KGQQEAARAG ELLKEKKVYP
    60 70 80 90 100
    DVLYTSKLSR AIQTANIALE KADRLWIPVN RSWRLNERHY GDLQGKDKAE
    110 120 130 140 150
    TLKKFGEEKF NTYRRSFDVP PPPIDASSPF SQKGDERYKY VDPNVLPETE
    160 170 180 190 200
    SLALVIDRLL PYWQDVIAKD LLSGKTVMIA AHGNSLRGLV KHLEGISDAD
    210 220 230 240
    IAKLNIPTGI PLVFELDENL KPSKPSYYLD PEAAAAGAAA VANQGKK
    Length:247
    Mass (Da):27,609
    Last modified:January 23, 2007 - v3
    Checksum:i45E1A9CCDBDC104D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X06408 Genomic DNA. Translation: CAA29698.1.
    X58789 Genomic DNA. Translation: CAA41595.1.
    Z26877 Genomic DNA. Translation: CAA81501.1.
    Z28152 Genomic DNA. Translation: CAA81994.1.
    S57976 Genomic DNA. Translation: AAB26026.1. Different termination.
    BK006944 Genomic DNA. Translation: DAA09011.1.
    PIRiS00358. PMBYY.
    RefSeqiNP_012770.1. NM_001179718.1.

    Genome annotation databases

    EnsemblFungiiYKL152C; YKL152C; YKL152C.
    GeneIDi853705.
    KEGGisce:YKL152C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X06408 Genomic DNA. Translation: CAA29698.1.
    X58789 Genomic DNA. Translation: CAA41595.1.
    Z26877 Genomic DNA. Translation: CAA81501.1.
    Z28152 Genomic DNA. Translation: CAA81994.1.
    S57976 Genomic DNA. Translation: AAB26026.1. Different termination.
    BK006944 Genomic DNA. Translation: DAA09011.1.
    PIRiS00358. PMBYY.
    RefSeqiNP_012770.1. NM_001179718.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQ3X-ray2.70A/B/C/D2-247[»]
    1BQ4X-ray2.50A/B/C/D2-247[»]
    1QHFX-ray1.70A/B2-241[»]
    3PGMX-ray2.80A/B2-247[»]
    4PGMX-ray2.30A/B/C/D2-247[»]
    5PGMX-ray2.12A/B/C/D/E/F/G/H2-247[»]
    ProteinModelPortaliP00950.
    SMRiP00950. Positions 2-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33985. 57 interactions.
    DIPiDIP-6260N.
    IntActiP00950. 29 interactions.
    MINTiMINT-603921.
    STRINGi4932.YKL152C.

    2D gel databases

    COMPLUYEAST-2DPAGEP00950.
    SWISS-2DPAGEP00950.

    Proteomic databases

    MaxQBiP00950.
    PaxDbiP00950.
    PeptideAtlasiP00950.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYKL152C; YKL152C; YKL152C.
    GeneIDi853705.
    KEGGisce:YKL152C.

    Organism-specific databases

    EuPathDBiFungiDB:YKL152C.
    SGDiS000001635. GPM1.

    Phylogenomic databases

    eggNOGiCOG0588.
    GeneTreeiENSGT00390000016700.
    HOGENOMiHOG000221682.
    InParanoidiP00950.
    KOiK01834.
    OMAiLNKDRAR.
    OrthoDBiEOG7SXWF2.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00186.
    BioCyciMetaCyc:YKL152C-MONOMER.
    YEAST:YKL152C-MONOMER.
    BRENDAi5.4.2.11. 984.
    ReactomeiREACT_275254. Glycolysis.
    REACT_286539. Gluconeogenesis.

    Miscellaneous databases

    EvolutionaryTraceiP00950.
    NextBioi974701.
    PROiP00950.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    HAMAPiMF_01039. PGAM_GpmA.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view]
    PANTHERiPTHR11931. PTHR11931. 1 hit.
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    TIGRFAMsiTIGR01258. pgm_1. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The amino acid sequence of yeast phosphoglycerate mutase."
      Fothergill L.A., Harkins R.N.
      Proc. R. Soc. Lond., B, Biol. Sci. 215:19-44(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-247.
    2. "Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae."
      White M.F., Fothergill-Gilmore L.A.
      FEBS Lett. 229:383-387(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Sequence and localization of the gene encoding yeast phosphoglycerate mutase."
      Heinisch J.J., von Borstel R.C., Rodicio R.M.
      Curr. Genet. 20:167-171(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci of chromosome XI of Saccharomyces cerevisiae."
      Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.
      Yeast 10:S35-S40(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Transcriptional control of yeast phosphoglycerate mutase-encoding gene."
      Rodicio R., Heinisch J.J., Hollenberg C.P.
      Gene 125:125-133(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
    8. Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Strain: ATCC 26786 / X2180-1A.
    9. "Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins."
      Norbeck J., Blomberg A.
      Yeast 13:1519-1534(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 110-114 AND 204-217.
      Strain: ATCC 44827 / SKQ2N.
    10. "Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase. Investigation of the role of active-site His181."
      White M.F., Fothergill-Gilmore L.A.
      Eur. J. Biochem. 207:709-714(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-182, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Dissociation of the tetrameric phosphoglycerate mutase from yeast by a mutation in the subunit contact region."
      White M.F., Fothergill-Gilmore L.A., Kelly S.M., Price N.C.
      Biochem. J. 295:743-748(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-169, BIOPHYSICOCHEMICAL PROPERTIES.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. Cited for: SUBCELLULAR LOCATION.
    15. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    16. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-116 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-127 AND SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49; SER-116; SER-128 AND SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH 3-PHOSPHO-D-GLYCERATE, SUBUNIT, REACTION MECHANISM.
    23. "The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate mutase."
      Rigden D.J., Alexeev D., Phillips S.E.V.P., Fothergill-Gilmore L.A.
      J. Mol. Biol. 276:449-459(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT.
    24. "Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A."
      Crowhurst G.S., Dalby A.R., Isupov M.N., Campbell J.W., Littlechild J.A.
      Acta Crystallogr. D 55:1822-1826(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH 3-PHOSPHO-D-GLYCERATE, SUBUNIT, ACTIVE SITE.
    25. "Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism."
      Rigden D.J., Walter R.A., Phillips S.E., Fothergill-Gilmore L.A.
      J. Mol. Biol. 286:1507-1517(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
    26. "Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis."
      Rigden D.J., Walter R.A., Phillips S.E., Fothergill-Gilmore L.A.
      J. Mol. Biol. 289:691-699(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiPMG1_YEAST
    AccessioniPrimary (citable) accession number: P00950
    Secondary accession number(s): D6VX45, Q02117
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 175 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 172000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.