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Protein

Phosphoglycerate mutase 2

Gene

GPM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Could be non-functional.

Catalytic activityi

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

Pathwayi: 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 3 (ERR3), Enolase-related protein 1 (ERR1), 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 sitei17 – 171Tele-phosphohistidine intermediateBy similarity
Binding sitei73 – 731SubstrateBy similarity
Active sitei126 – 1261Proton donor/acceptorBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Sitei242 – 2421Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciYEAST:G3O-29450-MONOMER.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase 2 (EC:5.4.2.11)
Short name:
PGAM 2
Alternative name(s):
BPG-dependent PGAM 2
MPGM 2
Phosphoglyceromutase 2
Gene namesi
Name:GPM2
Ordered Locus Names:YDL021W
ORF Names:D2835
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL021W.
SGDiS000002179. GPM2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 311311Phosphoglycerate mutase 2PRO_0000179840Add
BLAST

Proteomic databases

MaxQBiQ12008.
TopDownProteomicsiQ12008.

PTM databases

iPTMnetiQ12008.

Interactioni

Protein-protein interaction databases

BioGridi32034. 8 interactions.
IntActiQ12008. 2 interactions.
MINTiMINT-4478840.

Structurei

3D structure databases

ProteinModelPortaliQ12008.
SMRiQ12008. Positions 12-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 238Substrate bindingBy similarity
Regioni29 – 302Substrate bindingBy similarity
Regioni126 – 1294Substrate bindingBy similarity
Regioni153 – 1542Substrate bindingBy similarity
Regioni243 – 2442Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075884.
HOGENOMiHOG000221682.
InParanoidiQ12008.
KOiK01834.
OMAiERHYGSW.
OrthoDBiEOG71CFXN.

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. 2 hits.
PfamiPF00300. His_Phos_1. 2 hits.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 2 hits.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASTPSNVM TLFLLRHGQS ELNHENIFCG WIDAKLTEKG KEQARHSAEL
60 70 80 90 100
IEQYCKANNL RLPQIGYTSR LIRTQQTIET MCEEFKLKPQ LQVVYDFNKI
110 120 130 140 150
KLGDEFGSDD KDNMKIPILQ TWRLNERHYG SWQGQRKPNV LKEYGKDKYM
160 170 180 190 200
FIRRDYEGKP PPVDLDREMI QQENEKGSST GYEFKEPNRQ IKYELECSNH
210 220 230 240 250
DIVLPDSESL REVVYRLNPF LQNVILKLAN QYDESSCLIV GHGSSVRSLL
260 270 280 290 300
KILEGISDDD IKNVDIPNGI PLVVELDKNN GLKFIRKFYL DPESAKINAE
310
KVRNEGFIKN P
Length:311
Mass (Da):36,073
Last modified:November 1, 1997 - v1
Checksum:i1E53ECAAF06C932C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48432 Genomic DNA. Translation: CAA88338.1.
Z74069 Genomic DNA. Translation: CAA98580.1.
AY692876 Genomic DNA. Translation: AAT92895.1.
BK006938 Genomic DNA. Translation: DAA11829.1.
PIRiS52498.
RefSeqiNP_010263.1. NM_001180080.1.

Genome annotation databases

EnsemblFungiiYDL021W; YDL021W; YDL021W.
GeneIDi851541.
KEGGisce:YDL021W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48432 Genomic DNA. Translation: CAA88338.1.
Z74069 Genomic DNA. Translation: CAA98580.1.
AY692876 Genomic DNA. Translation: AAT92895.1.
BK006938 Genomic DNA. Translation: DAA11829.1.
PIRiS52498.
RefSeqiNP_010263.1. NM_001180080.1.

3D structure databases

ProteinModelPortaliQ12008.
SMRiQ12008. Positions 12-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32034. 8 interactions.
IntActiQ12008. 2 interactions.
MINTiMINT-4478840.

PTM databases

iPTMnetiQ12008.

Proteomic databases

MaxQBiQ12008.
TopDownProteomicsiQ12008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL021W; YDL021W; YDL021W.
GeneIDi851541.
KEGGisce:YDL021W.

Organism-specific databases

EuPathDBiFungiDB:YDL021W.
SGDiS000002179. GPM2.

Phylogenomic databases

GeneTreeiENSGT00550000075884.
HOGENOMiHOG000221682.
InParanoidiQ12008.
KOiK01834.
OMAiERHYGSW.
OrthoDBiEOG71CFXN.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciYEAST:G3O-29450-MONOMER.

Miscellaneous databases

PROiQ12008.

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. 2 hits.
PfamiPF00300. His_Phos_1. 2 hits.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 2 hits.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase."
    Heinisch J.J., Mueller S., Schlueter E., Jacoby J., Rodicio R.
    Yeast 14:203-213(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPMG2_YEAST
AccessioniPrimary (citable) accession number: Q12008
Secondary accession number(s): D6VRW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 141 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 2020 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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 one 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.