Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglycerate mutase

Gene

gpm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 2 (gpd3), Glyceraldehyde-3-phosphate dehydrogenase 1 (tdh1)
  2. Phosphoglycerate kinase (pgk1)
  3. Phosphoglycerate mutase (gpm1)
  4. Enolase 1-2 (eno102), Enolase 1-1 (eno101)
  5. Pyruvate kinase (pyk1)
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)DescriptionActionsGraphical viewLength
Active sitei15Tele-phosphohistidine intermediateBy similarity1
Binding sitei66SubstrateBy similarity1
Active sitei93Proton donor/acceptorBy similarity1
Binding sitei104SubstrateBy similarity1
Sitei163Transition state stabilizerBy similarity1

GO - Molecular functioni

  • 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: PomBase
  • phosphoglycerate mutase activity Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BRENDAi5.4.2.11. 5613.
ReactomeiR-SPO-6798695. Neutrophil degranulation.
R-SPO-70171. Glycolysis.
R-SPO-70263. Gluconeogenesis.
R-SPO-70326. Glucose metabolism.
SABIO-RKP36623.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase (EC:5.4.2.11)
Short name:
PGAM
Alternative name(s):
BPG-dependent PGAM
MPGM
Phosphoglyceromutase
Gene namesi
Name:gpm1
ORF Names:SPAC26F1.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC26F1.06.
PomBaseiSPAC26F1.06. gpm1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001798381 – 211Phosphoglycerate mutaseAdd BLAST211

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37Phosphothreonine1 Publication1
Modified residuei62Phosphoserine1 Publication1
Modified residuei96Phosphotyrosine1 Publication1
Modified residuei166Phosphoserine1 Publication1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36623.
PRIDEiP36623.

PTM databases

iPTMnetiP36623.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi278562. 3 interactors.
IntActiP36623. 1 interactor.
MINTiMINT-4689166.

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 12Combined sources4
Helixi19 – 23Combined sources5
Beta strandi28 – 30Combined sources3
Helixi36 – 52Combined sources17
Beta strandi57 – 64Combined sources8
Helixi65 – 78Combined sources14
Beta strandi83 – 89Combined sources7
Helixi97 – 99Combined sources3
Helixi104 – 120Combined sources17
Beta strandi121 – 124Combined sources4
Helixi133 – 148Combined sources16
Helixi151 – 154Combined sources4
Beta strandi158 – 162Combined sources5
Helixi164 – 175Combined sources12
Turni179 – 181Combined sources3
Beta strandi182 – 184Combined sources3
Beta strandi189 – 191Combined sources3
Beta strandi193 – 197Combined sources5
Beta strandi199 – 201Combined sources3
Beta strandi203 – 205Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FZTNMR-A1-211[»]
ProteinModelPortaliP36623.
SMRiP36623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36623.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 21Substrate bindingBy similarity8
Regioni27 – 28Substrate bindingBy similarity2
Regioni93 – 96Substrate bindingBy similarity4
Regioni120 – 121Substrate bindingBy similarity2
Regioni164 – 165Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000221682.
InParanoidiP36623.
KOiK01834.
OMAiVKNQGKK.
OrthoDBiEOG092C4JJL.
PhylomeDBiP36623.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA. 1 hit.
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. 2 hits.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTEAAPNLL VLTRHGESEW NKLNLFTGWK DPALSETGIK EAKLGGERLK
60 70 80 90 100
SRGYKFDIAF TSALQRAQKT CQIILEEVGE PNLETIKSEK LNERYYGDLQ
110 120 130 140 150
GLNKDDARKK WGAEQVQIWR RSYDIAPPNG ESLKDTAERV LPYYKSTIVP
160 170 180 190 200
HILKGEKVLI AAHGNSLRAL IMDLEGLTGD QIVKRELATG VPIVYHLDKD
210
GKYVSKELID N
Length:211
Mass (Da):23,765
Last modified:June 1, 1994 - v1
Checksum:i4B937820E2FA5C15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75385 mRNA. Translation: CAA53154.1.
CU329670 Genomic DNA. Translation: CAA97363.1.
PIRiS43369. S43214.
RefSeqiNP_594889.1. NM_001020318.2.

Genome annotation databases

EnsemblFungiiSPAC26F1.06.1; SPAC26F1.06.1:pep; SPAC26F1.06.
GeneIDi2542085.
KEGGispo:SPAC26F1.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75385 mRNA. Translation: CAA53154.1.
CU329670 Genomic DNA. Translation: CAA97363.1.
PIRiS43369. S43214.
RefSeqiNP_594889.1. NM_001020318.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FZTNMR-A1-211[»]
ProteinModelPortaliP36623.
SMRiP36623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278562. 3 interactors.
IntActiP36623. 1 interactor.
MINTiMINT-4689166.

PTM databases

iPTMnetiP36623.

Proteomic databases

MaxQBiP36623.
PRIDEiP36623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC26F1.06.1; SPAC26F1.06.1:pep; SPAC26F1.06.
GeneIDi2542085.
KEGGispo:SPAC26F1.06.

Organism-specific databases

EuPathDBiFungiDB:SPAC26F1.06.
PomBaseiSPAC26F1.06. gpm1.

Phylogenomic databases

HOGENOMiHOG000221682.
InParanoidiP36623.
KOiK01834.
OMAiVKNQGKK.
OrthoDBiEOG092C4JJL.
PhylomeDBiP36623.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BRENDAi5.4.2.11. 5613.
ReactomeiR-SPO-6798695. Neutrophil degranulation.
R-SPO-70171. Glycolysis.
R-SPO-70263. Gluconeogenesis.
R-SPO-70326. Glucose metabolism.
SABIO-RKP36623.

Miscellaneous databases

EvolutionaryTraceiP36623.
PROiP36623.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA. 1 hit.
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. 2 hits.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMGY_SCHPO
AccessioniPrimary (citable) accession number: P36623
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  4. SIMILARITY comments
    Index of protein domains and families

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.