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P00950 (PMG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglycerate mutase 1

Short name=PGAM 1
EC=5.4.2.1
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.

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer.

Miscellaneous

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.8
Chain2 – 247246Phosphoglycerate mutase 1
PRO_0000179839

Regions

Compositional bias233 – 24210Ala-rich

Sites

Active site91Tele-phosphohistidine intermediate Ref.16
Active site1821
Site601Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue121Phosphoserine Ref.12
Modified residue1161Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14
Modified residue1271Phosphoserine Ref.13 Ref.14
Modified residue1281Phosphoserine Ref.12 Ref.13 Ref.14
Modified residue1311Phosphoserine Ref.14
Modified residue1851Phosphoserine Ref.12
Modified residue1971Phosphoserine Ref.13 Ref.14

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]"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].
[11]"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, MASS SPECTROMETRY.
Strain: ADR376.
[12]"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; SER-128 AND SER-185, MASS SPECTROMETRY.
[13]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-127; SER-128 AND SER-197, MASS SPECTROMETRY.
[14]"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; SER-128; SER-131 AND SER-197, MASS SPECTROMETRY.
[15]"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).
[16]"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).
+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...

Protein-protein interaction databases

DIPDIP-6260N.
IntActP00950. 18 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.
OMAGRKEACA.
OrthoDBEOG4X6GJK.

Enzyme and pathway databases

UniPathwayUPA00109; UER00186.

Gene expression databases

GenevestigatorP00950.
GermOnlineYKL152C. Saccharomyces cerevisiae.

Family and domain databases

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.

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 3, 2013
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XI

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families