Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00950 (PMG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate mutase 1

Short name=PGAM 1
EC=5.4.2.11
Alternative name(s):
BPG-dependent PGAM 1
MPGM 1
Phosphoglyceromutase 1
Gene names
Name:GPM1
Synonyms:GPM
Ordered Locus Names:YKL152C
ORF Names:YKL607
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. Ref.10

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039

Subunit structure

Homotetramer. Ref.11 Ref.24

Subcellular location

Cytoplasm. Mitochondrion intermembrane space Ref.12 Ref.14 Ref.19.

Miscellaneous

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

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Biophysicochemical properties

Kinetic parameters:

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.

KM=740 µM for 3-phosphoglycerate Ref.10 Ref.11

KM=8.1 µM for 2,3-bisphosphoglycerate (for mutase reaction)

KM=2.4 µM for 2,3-bisphosphoglycerate (for phosphatase reaction)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.8
Chain2 – 247246Phosphoglycerate mutase 1 HAMAP-Rule MF_01039
PRO_0000179839

Regions

Region21 – 2222-phospho-D-glycerate binding HAMAP-Rule MF_01039
Region87 – 9042-phospho-D-glycerate binding HAMAP-Rule MF_01039
Region114 – 11522-phospho-D-glycerate bindingy By similarity
Compositional bias233 – 24210Ala-rich HAMAP-Rule MF_01039

Sites

Active site91Tele-phosphohistidine intermediate Ref.24
Active site1821 Ref.24
Binding site1512-phospho-D-glycerate
Binding site6012-phospho-D-glycerate

Amino acid modifications

Modified residue121Phosphoserine Ref.16
Modified residue491Phosphotyrosine Ref.18
Modified residue1161Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18
Modified residue1271Phosphoserine Ref.17
Modified residue1281Phosphoserine Ref.18
Modified residue1851Phosphoserine Ref.16
Modified residue1971Phosphoserine Ref.17 Ref.18

Experimental info

Mutagenesis1691K → P: Causes dissociation of the homotetramer to dimers at low concentrations. Ref.11
Mutagenesis1821H → A: Reduces kcat of the mutase reaction 10000-fold. Ref.10

Secondary structure

................................................ 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00950 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 45E1A9CCDBDC104D

FASTA24727,609
        10         20         30         40         50         60 
MPKLVLVRHG QSEWNEKNLF TGWVDVKLSA KGQQEAARAG ELLKEKKVYP DVLYTSKLSR 

        70         80         90        100        110        120 
AIQTANIALE KADRLWIPVN RSWRLNERHY GDLQGKDKAE TLKKFGEEKF NTYRRSFDVP 

       130        140        150        160        170        180 
PPPIDASSPF SQKGDERYKY VDPNVLPETE SLALVIDRLL PYWQDVIAKD LLSGKTVMIA 

       190        200        210        220        230        240 
AHGNSLRGLV KHLEGISDAD IAKLNIPTGI PLVFELDENL KPSKPSYYLD PEAAAAGAAA 


VANQGKK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[13]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]"Enolase takes part in a macromolecular complex associated to mitochondria in yeast."
Brandina I., Graham J., Lemaitre-Guillier C., Entelis N., Krasheninnikov I., Sweetlove L., Tarassov I., Martin R.P.
Biochim. Biophys. Acta 1757:1217-1228(2006) [PubMed] [Europe PMC] [Abstract]
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]"Intermembrane space proteome of yeast mitochondria."
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.
Mol. Cell. Proteomics 11:1840-1852(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Structure and activity of phosphoglycerate mutase."
Winn S.I., Watson H.C., Harkins R.N., Fothergill L.A.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:121-130(1981) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRPMBYY. S00358.
RefSeqNP_012770.1. NM_001179718.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQ3X-ray2.70A/B/C/D2-247[»]
1BQ4X-ray2.50A/B/C/D2-247[»]
1QHFX-ray1.70A/B2-240[»]
3PGMX-ray2.80A/B2-247[»]
4PGMX-ray2.30A/B/C/D2-247[»]
5PGMX-ray2.12A/B/C/D/E/F/G/H2-246[»]
ProteinModelPortalP00950.
SMRP00950. Positions 2-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33985. 53 interactions.
DIPDIP-6260N.
IntActP00950. 23 interactions.
MINTMINT-603921.
STRING4932.YKL152C.

2D gel databases

COMPLUYEAST-2DPAGEP00950.
SWISS-2DPAGEP00950.

Proteomic databases

PaxDbP00950.
PeptideAtlasP00950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL152C; YKL152C; YKL152C.
GeneID853705.
KEGGsce:YKL152C.

Organism-specific databases

SGDS000001635. GPM1.

Phylogenomic databases

eggNOGCOG0588.
GeneTreeENSGT00390000016700.
HOGENOMHOG000221682.
KOK01834.
OMALNKDRAR.
OrthoDBEOG7SXWF2.

Enzyme and pathway databases

BioCycYEAST:YKL152C-MONOMER.
UniPathwayUPA00109; UER00186.

Gene expression databases

GenevestigatorP00950.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00950.
NextBio974701.
PROP00950.

Entry information

Entry namePMG1_YEAST
AccessionPrimary (citable) accession number: P00950
Secondary accession number(s): D6VX45, Q02117
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways