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Protein

Phosphoglycerate mutase 3

Gene

GPM3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei14 – 141Tele-phosphohistidine intermediateBy similarity
Binding sitei70 – 701SubstrateBy similarity
Active sitei120 – 1201Proton donor/acceptorBy similarity
Binding sitei131 – 1311SubstrateBy similarity
Sitei235 – 2351Transition 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-33467-MONOMER.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase 3 (EC:5.4.2.11)
Short name:
PGAM 3
Alternative name(s):
BPG-dependent PGAM 3
MPGM 3
Phosphoglyceromutase 3
Gene namesi
Name:GPM3
Ordered Locus Names:YOL056W
ORF Names:O1236
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL056W.
SGDiS000005417. GPM3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Phosphoglycerate mutase 3PRO_0000179841Add
BLAST

Proteomic databases

MaxQBiQ12326.
PeptideAtlasiQ12326.

Interactioni

Protein-protein interaction databases

BioGridi34345. 43 interactions.
DIPiDIP-4234N.
IntActiQ12326. 5 interactions.
MINTiMINT-520340.

Structurei

3D structure databases

ProteinModelPortaliQ12326.
SMRiQ12326. Positions 8-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 208Substrate bindingBy similarity
Regioni26 – 272Substrate bindingBy similarity
Regioni120 – 1234Substrate bindingBy similarity
Regioni147 – 1482Substrate bindingBy similarity
Regioni236 – 2372Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075884.
HOGENOMiHOG000221682.
InParanoidiQ12326.
KOiK01834.
OMAiFCGWIDI.
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. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12326-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVTDTFKLF ILRHGQSELN SENIFCGWID AQLTEKGKSQ ARHSAKLIKQ
60 70 80 90 100
FCDSNNISLP QIGYTSRLIR TQQTMDVILE ELGLKHTNYV ITTNTNIKEE
110 120 130 140 150
LQDTRFEGSM PVLQTWRLNE RHYGAWQGQR KPDILKEYGK EKYMYIRRDY
160 170 180 190 200
NGKPPKVNLN LEMVQEENDQ GSSTGYDFKE PNRHLKYGPE EKANERLPES
210 220 230 240 250
ESLCEVVVRL KPFLNNVVLS TANKISQESC VIVGHGSSVR SLLKVLEGIS
260 270 280 290 300
DEDIKDVDIP NGIPLVIELD RDNYSFVRKF YLDPESAKVN AQMVRDEGFE

KNP
Length:303
Mass (Da):34,863
Last modified:November 1, 1997 - v1
Checksum:i29C3FF3D28560914
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91067 Genomic DNA. Translation: CAA62530.1.
Z74798 Genomic DNA. Translation: CAA99064.1.
BK006948 Genomic DNA. Translation: DAA10727.1.
PIRiS61723.
RefSeqiNP_014585.1. NM_001183311.1.

Genome annotation databases

EnsemblFungiiYOL056W; YOL056W; YOL056W.
GeneIDi854098.
KEGGisce:YOL056W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91067 Genomic DNA. Translation: CAA62530.1.
Z74798 Genomic DNA. Translation: CAA99064.1.
BK006948 Genomic DNA. Translation: DAA10727.1.
PIRiS61723.
RefSeqiNP_014585.1. NM_001183311.1.

3D structure databases

ProteinModelPortaliQ12326.
SMRiQ12326. Positions 8-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34345. 43 interactions.
DIPiDIP-4234N.
IntActiQ12326. 5 interactions.
MINTiMINT-520340.

Proteomic databases

MaxQBiQ12326.
PeptideAtlasiQ12326.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL056W; YOL056W; YOL056W.
GeneIDi854098.
KEGGisce:YOL056W.

Organism-specific databases

EuPathDBiFungiDB:YOL056W.
SGDiS000005417. GPM3.

Phylogenomic databases

GeneTreeiENSGT00550000075884.
HOGENOMiHOG000221682.
InParanoidiQ12326.
KOiK01834.
OMAiFCGWIDI.
OrthoDBiEOG71CFXN.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciYEAST:G3O-33467-MONOMER.

Miscellaneous databases

NextBioi975767.
PROiQ12326.

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. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
    Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
    Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90843 / S288c / FY73.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPMG3_YEAST
AccessioniPrimary (citable) accession number: Q12326
Secondary accession number(s): D6W211
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 140 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 3730 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.