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P00950

- PMG1_YEAST

UniProt

P00950 - PMG1_YEAST

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Protein

Phosphoglycerate mutase 1

Gene
GPM1, GPM, YKL152C, YKL607
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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.

Catalytic activityi

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

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Tele-phosphohistidine intermediate1 Publication
Binding sitei15 – 1512-phospho-D-glycerate
Binding sitei60 – 6012-phospho-D-glycerate
Active sitei182 – 1821

GO - Molecular functioni

  1. phosphoglycerate mutase activity Source: SGD

GO - Biological processi

  1. gluconeogenesis Source: SGD
  2. 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.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase 1 (EC:5.4.2.11)
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: Chromosome XI

Organism-specific databases

SGDiS000001635. GPM1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. mitochondrial intermembrane space Source: SGD
  3. 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.
Mutagenesisi182 – 1821H → A: Reduces kcat of the mutase reaction 10000-fold.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine
Modified residuei49 – 491Phosphotyrosine
Modified residuei116 – 1161Phosphoserine
Modified residuei127 – 1271Phosphoserine
Modified residuei128 – 1281Phosphoserine
Modified residuei185 – 1851Phosphoserine
Modified residuei197 – 1971Phosphoserine

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00950.
PaxDbiP00950.
PeptideAtlasiP00950.

2D gel databases

COMPLUYEAST-2DPAGEP00950.
SWISS-2DPAGEP00950.

Expressioni

Gene expression databases

GenevestigatoriP00950.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi33985. 53 interactions.
DIPiDIP-6260N.
IntActiP00950. 23 interactions.
MINTiMINT-603921.
STRINGi4932.YKL152C.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00950.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 2222-phospho-D-glycerate binding
Regioni87 – 9042-phospho-D-glycerate binding
Regioni114 – 11522-phospho-D-glycerate bindingy By similarity

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0588.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
KOiK01834.
OMAiFPRTECL.
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

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MPKLVLVRHG QSEWNEKNLF TGWVDVKLSA KGQQEAARAG ELLKEKKVYP    50
DVLYTSKLSR AIQTANIALE KADRLWIPVN RSWRLNERHY GDLQGKDKAE 100
TLKKFGEEKF NTYRRSFDVP PPPIDASSPF SQKGDERYKY VDPNVLPETE 150
SLALVIDRLL PYWQDVIAKD LLSGKTVMIA AHGNSLRGLV KHLEGISDAD 200
IAKLNIPTGI PLVFELDENL KPSKPSYYLD PEAAAAGAAA VANQGKK 247
Length:247
Mass (Da):27,609
Last modified:January 23, 2007 - v3
Checksum:i45E1A9CCDBDC104D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S00358. PMBYY.
RefSeqi NP_012770.1. NM_001179718.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BQ3 X-ray 2.70 A/B/C/D 2-247 [» ]
1BQ4 X-ray 2.50 A/B/C/D 2-247 [» ]
1QHF X-ray 1.70 A/B 2-241 [» ]
3PGM X-ray 2.80 A/B 2-247 [» ]
4PGM X-ray 2.30 A/B/C/D 2-247 [» ]
5PGM X-ray 2.12 A/B/C/D/E/F/G/H 2-247 [» ]
ProteinModelPortali P00950.
SMRi P00950. Positions 2-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33985. 53 interactions.
DIPi DIP-6260N.
IntActi P00950. 23 interactions.
MINTi MINT-603921.
STRINGi 4932.YKL152C.

2D gel databases

COMPLUYEAST-2DPAGE P00950.
SWISS-2DPAGE P00950.

Proteomic databases

MaxQBi P00950.
PaxDbi P00950.
PeptideAtlasi P00950.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL152C ; YKL152C ; YKL152C .
GeneIDi 853705.
KEGGi sce:YKL152C.

Organism-specific databases

SGDi S000001635. GPM1.

Phylogenomic databases

eggNOGi COG0588.
GeneTreei ENSGT00390000016700.
HOGENOMi HOG000221682.
KOi K01834.
OMAi FPRTECL.
OrthoDBi EOG7SXWF2.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00186 .
BioCyci MetaCyc:YKL152C-MONOMER.
YEAST:YKL152C-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00950.
NextBioi 974701.
PROi P00950.

Gene expression databases

Genevestigatori P00950.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
HAMAPi MF_01039. PGAM_GpmA.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view ]
PANTHERi PTHR11931. PTHR11931. 1 hit.
Pfami PF00300. His_Phos_1. 1 hit.
[Graphical view ]
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
TIGRFAMsi TIGR01258. pgm_1. 1 hit.
PROSITEi PS00175. PG_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  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).
  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.

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: July 9, 2014
This is version 166 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.

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