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P16290 (PGAM2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate mutase 2

EC=3.1.3.13
EC=5.4.2.11
EC=5.4.2.4
Alternative name(s):
BPG-dependent PGAM 2
Muscle-specific phosphoglycerate mutase
Phosphoglycerate mutase isozyme M
Short name=PGAM-M
Gene names
Name:Pgam2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039

3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. HAMAP-Rule MF_01039

2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate. HAMAP-Rule MF_01039

Subunit structure

Homodimer.

Tissue specificity

In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 253253Phosphoglycerate mutase 2 HAMAP-Rule MF_01039
PRO_0000179831

Regions

Compositional bias122 – 1254Poly-Pro HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate
Active site1861
Site621Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Cross-link179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P16290 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 73F6118A1C73D545

FASTA25328,755
        10         20         30         40         50         60 
MATHRLVMVR HGESSWNQEN RFCGWFDAEL SEKGAEEAKR GATAIKDAKI EFDICYTSVL 

        70         80         90        100        110        120 
KRAIRTLWTI LDVTDQMWVP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD 

       130        140        150        160        170        180 
TPPPPMDEKH NYYASISKDR RYAGLKPEEL PTCESLKDTI ARALPFWNEE IAPKIKAGKR 

       190        200        210        220        230        240 
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NQELKPTKPM RFLGDEETVR 

       250 
KAMEAVAAQG KAK 

« Hide

References

[1]"Sequence of rat skeletal muscle phosphoglycerate mutase cDNA."
Castella-Escola J., Montoliu L., Pons G., Puigdomenech P., Cohen-Solal M., Carreras J., Rigau J., Climent F.
Biochem. Biophys. Res. Commun. 165:1345-1351(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"The gene encoding rat phosphoglycerate mutase subunit M: cloning and promoter analysis in skeletal muscle cells."
Ruiz-Lozano P., de Lecea L., Buesa C., Perez de la Osa P., Lepage D., Gualberto A., Walsh K., Pons G.
Gene 147:243-248(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31835 mRNA. Translation: AAA41835.1.
Z17319 Genomic DNA. Translation: CAA78967.1.
PIRPMRTYM. A33793.
RefSeqNP_059024.1. NM_017328.2.
UniGeneRn.9738.

3D structure databases

ProteinModelPortalP16290.
SMRP16290. Positions 2-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP16290. 7 interactions.
MINTMINT-4588391.
STRING10116.ENSRNOP00000018227.

PTM databases

PhosphoSiteP16290.

Proteomic databases

PaxDbP16290.
PRIDEP16290.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018227; ENSRNOP00000018227; ENSRNOG00000013532.
GeneID24959.
KEGGrno:24959.
UCSCRGD:3313. rat.

Organism-specific databases

CTD5224.
RGD3313. Pgam2.

Phylogenomic databases

eggNOGCOG0588.
GeneTreeENSGT00390000016700.
HOGENOMHOG000221682.
HOVERGENHBG027528.
InParanoidP16290.
KOK01834.
OMAWTILEGT.
OrthoDBEOG7XM2ZV.
PhylomeDBP16290.
TreeFamTF300007.

Enzyme and pathway databases

SABIO-RKP16290.

Gene expression databases

GenevestigatorP16290.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604991.
PROP16290.

Entry information

Entry namePGAM2_RAT
AccessionPrimary (citable) accession number: P16290
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families