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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) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediateBy similarity
Binding sitei62 – 621SubstrateBy similarity
Active sitei89 – 891Proton donor/acceptorBy similarity
Binding sitei100 – 1001SubstrateBy similarity
Sitei186 – 1861Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

ReactomeiR-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase 1 (EC:3.1.3.13, EC:5.4.2.11, EC:5.4.2.4)
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

  • nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 254253Phosphoglycerate mutase 1PRO_0000179828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei26 – 261PhosphotyrosineCombined sources
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei106 – 1061N6-acetyllysineBy similarity
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei251 – 2511N6-acetyllysine; alternateBy similarity
Modified residuei251 – 2511N6-succinyllysine; alternateBy similarity
Modified residuei253 – 2531N6-acetyllysineBy similarity
Modified residuei254 – 2541N6-acetyllysineBy similarity

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.
PhosphoSiteiP25113.

Expressioni

Gene expression databases

GenevisibleiP25113. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi246778. 3 interactions.
STRINGi10116.ENSRNOP00000065690.

Structurei

3D structure databases

ProteinModelPortaliP25113.
SMRiP25113. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 178Substrate bindingBy similarity
Regioni23 – 242Substrate bindingBy similarity
Regioni89 – 924Substrate bindingBy similarity
Regioni116 – 1172Substrate bindingBy similarity
Regioni187 – 1882Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 13110Pro-rich

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
GeneTreeiENSGT00390000016700.
HOVERGENiHBG027528.
InParanoidiP25113.
KOiK01834.
OMAiADDENWH.
OrthoDBiEOG7XM2ZV.
PhylomeDBiP25113.

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. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551C → V in AAA41834 (PubMed:1533381).Curated
Sequence conflicti99 – 991N → K in AAB19888 (PubMed:1832843).Curated
Sequence conflicti180 – 1801R → G in AAA41834 (PubMed:1533381).Curated
Sequence conflicti184 – 1841A → P in AAA41834 (PubMed:1533381).Curated
Sequence conflicti190 – 1912LR → YG in AAA41834 (PubMed:1533381).Curated
Sequence conflicti232 – 2321F → S in AAA41834 (PubMed:1533381).Curated

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. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246778. 3 interactions.
STRINGi10116.ENSRNOP00000065690.

PTM databases

iPTMnetiP25113.
PhosphoSiteiP25113.

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.
OMAiADDENWH.
OrthoDBiEOG7XM2ZV.
PhylomeDBiP25113.

Enzyme and pathway databases

ReactomeiR-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.

Miscellaneous databases

PROiP25113.

Gene expression databases

GenevisibleiP25113. RN.

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. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequencing of a cDNA encoding the B isozyme of rat phosphoglycerate mutase."
    Urena J.M., Grana X., de Lecea L., Ruiz P., Castella J., Carreras J., Pons G., Climent F.
    Gene 113:281-282(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA encoding type B subunit of rat phosphoglycerate mutase: its isolation and nucleotide sequence."
    Uchida K.
    Arch. Biochem. Biophys. 288:558-561(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-39; 47-62; 163-176 AND 222-240, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  5. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-23; TYR-26 AND SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: June 8, 2016
This is version 139 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.