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Protein

Phosphoglycerate mutase 1

Gene

Pgam1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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), but with a reduced activity.

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.By similarity
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei11Tele-phosphohistidine intermediateBy similarity1
Binding sitei62SubstrateBy similarity1
Active sitei89Proton donor/acceptorBy similarity1
Binding sitei100SubstrateBy similarity1
Sitei186Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase 1 (EC:5.4.2.11By similarity, EC:5.4.2.4By similarity)
Alternative name(s):
BPG-dependent PGAM 1
Phosphoglycerate mutase isozyme B
Short name:
PGAM-B
Gene namesi
Name:Pgam1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3312. Pgam1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • myelin sheath Source: Ensembl
  • nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001798282 – 254Phosphoglycerate mutase 1Add BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei26PhosphotyrosineCombined sources1
Modified residuei31PhosphoserineBy similarity1
Modified residuei106N6-acetyllysineBy similarity1
Modified residuei118PhosphoserineCombined sources1
Modified residuei251N6-acetyllysine; alternateBy similarity1
Modified residuei251N6-succinyllysine; alternateBy similarity1
Modified residuei253N6-acetyllysineBy similarity1
Modified residuei254N6-acetyllysineBy similarity1

Post-translational modificationi

Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP25113.
PRIDEiP25113.

2D gel databases

World-2DPAGE0004:P25113.

PTM databases

iPTMnetiP25113.
PhosphoSitePlusiP25113.

Expressioni

Gene expression databases

BgeeiENSRNOG00000050585.
GenevisibleiP25113. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi246778. 3 interactors.
STRINGi10116.ENSRNOP00000065690.

Structurei

3D structure databases

ProteinModelPortaliP25113.
SMRiP25113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 17Substrate bindingBy similarity8
Regioni23 – 24Substrate bindingBy similarity2
Regioni89 – 92Substrate bindingBy similarity4
Regioni116 – 117Substrate bindingBy similarity2
Regioni187 – 188Substrate bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi122 – 131Pro-rich10

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
GeneTreeiENSGT00390000016700.
HOVERGENiHBG027528.
InParanoidiP25113.
KOiK01834.
OMAiEIVHLWR.
OrthoDBiEOG091G0GIS.
PhylomeDBiP25113.

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. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25113-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY
60 70 80 90 100
EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK
110 120 130 140 150
AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL
160 170 180 190 200
PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL
210 220 230 240 250
SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR KAMEAVAAQG

KVKK
Length:254
Mass (Da):28,832
Last modified:January 23, 2007 - v4
Checksum:i6DC09A3BEBB22409
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55C → V in AAA41834 (PubMed:1533381).Curated1
Sequence conflicti99N → K in AAB19888 (PubMed:1832843).Curated1
Sequence conflicti180R → G in AAA41834 (PubMed:1533381).Curated1
Sequence conflicti184A → P in AAA41834 (PubMed:1533381).Curated1
Sequence conflicti190 – 191LR → YG in AAA41834 (PubMed:1533381).Curated2
Sequence conflicti232F → S in AAA41834 (PubMed:1533381).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76591 mRNA. Translation: AAA41834.1.
S63233 mRNA. Translation: AAB19888.2.
BC065582 mRNA. Translation: AAH65582.1.
RefSeqiNP_445742.2. NM_053290.2.
UniGeneiRn.1383.
Rn.145927.
Rn.154337.

Genome annotation databases

EnsembliENSRNOT00000071965; ENSRNOP00000065690; ENSRNOG00000050585.
GeneIDi24642.
KEGGirno:24642.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76591 mRNA. Translation: AAA41834.1.
S63233 mRNA. Translation: AAB19888.2.
BC065582 mRNA. Translation: AAH65582.1.
RefSeqiNP_445742.2. NM_053290.2.
UniGeneiRn.1383.
Rn.145927.
Rn.154337.

3D structure databases

ProteinModelPortaliP25113.
SMRiP25113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246778. 3 interactors.
STRINGi10116.ENSRNOP00000065690.

PTM databases

iPTMnetiP25113.
PhosphoSitePlusiP25113.

2D gel databases

World-2DPAGE0004:P25113.

Proteomic databases

PaxDbiP25113.
PRIDEiP25113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000071965; ENSRNOP00000065690; ENSRNOG00000050585.
GeneIDi24642.
KEGGirno:24642.

Organism-specific databases

CTDi5223.
RGDi3312. Pgam1.

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
GeneTreeiENSGT00390000016700.
HOVERGENiHBG027528.
InParanoidiP25113.
KOiK01834.
OMAiEIVHLWR.
OrthoDBiEOG091G0GIS.
PhylomeDBiP25113.

Miscellaneous databases

PROiP25113.

Gene expression databases

BgeeiENSRNOG00000050585.
GenevisibleiP25113. RN.

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. 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...

Entry informationi

Entry nameiPGAM1_RAT
AccessioniPrimary (citable) accession number: P25113
Secondary accession number(s): Q6P0K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.