[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(92)90408-H; PubMed=1533381 [NCBI, ExPASy, EBI, Israel, Japan] Urena J.M., Grana X., de Lecea L., Ruiz P., Castella J., Carreras J., Pons G., Climent F.; "Isolation and sequencing of a cDNA encoding the B isozyme of rat phosphoglycerate mutase."; Gene 113:281-282(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0003-9861(91)90235-B; PubMed=1832843 [NCBI, ExPASy, EBI, Israel, Japan] Uchida K.; "cDNA encoding type B subunit of rat phosphoglycerate mutase: its isolation and nucleotide sequence."; Arch. Biochem. Biophys. 288:558-561(1991).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PROTEIN SEQUENCE OF 11-39; 47-62; 163-176 AND 222-240, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q.; Submitted (APR-2007) to UniProtKB.
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS SPECTROMETRY. TISSUE=Kidney; DOI=10.1073/pnas.0600895103; PubMed=16641100 [NCBI, ExPASy, EBI, Israel, Japan] Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).

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.
CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H₂O = 3-phospho-D-glycerate + phosphate.
SUBUNIT: Homodimer.
TISSUE SPECIFICITY: In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.
SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M76591; AAA41834.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S63233; AAB19888.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065582; AAH65582.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_445742.1; -.

UniGene

Rn.1383

3D structure databases

HSSP

P31217; 1E58. [HSSP ENTRY / PDB]

P25113; 2-246.

PTM databases

P25113; -.

Organism-specific databases

RGD

3312; Pgam1.

Ontologies

GO:0004083;	Molecular function: bisphosphoglycerate 2-phosphatase activity (inferred from electronic annotation from EC).
GO:0004082;	Molecular function: bisphosphoglycerate mutase activity (inferred from electronic annotation from EC).
GO:0004619;	Molecular function: phosphoglycerate mutase activity (inferred from electronic annotation from EC).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001345; PG/BPGM_mutase.
IPR013078; PG_mutase.
IPR005952; Phosphogly_mut1.
Graphical view of domain structure.

PANTHER

PTHR11931; Phosphogly_mut1; 1.

Pfam

PF00300; PGAM; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01258; pgm_1; 1.

PROSITE

PS00175; PG_MUTASE; 1.

ProtoNet

P25113.

Genome annotation databases

GeneID

24642; -.

KEGG

rno:24642; -.

Phylogenomic databases

HOVERGEN

P25113; -.

Other

LinkHub

P25113; -.

NextBio

603944; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Direct protein sequencing; Glycolysis; Hydrolase; Isomerase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 254`	`253`	`Phosphoglycerate mutase 1.`	`PRO_0000179828`
`COMPBIAS`	`122 131`	`10`	`Pro-rich.`
`ACT_SITE`	`11 11`		`Tele-phosphohistidine intermediate.`
`ACT_SITE`	`186 186`
`SITE`	`62 62`	`1`	`Interaction with carboxyl group of phosphoglycerates.`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`14 14`		`Phosphoserine.`
`MOD_RES`	`26 26`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`118 118`		`Phosphoserine (By similarity).`
`CONFLICT`	`55 55`		`C -> V (in Ref. 1; AAA41834).`
`CONFLICT`	`99 99`		`N -> K (in Ref. 2; AAB19888).`
`CONFLICT`	`180 180`		`R -> G (in Ref. 1; AAA41834).`
`CONFLICT`	`184 184`		`A -> P (in Ref. 1; AAA41834).`
`CONFLICT`	`190 191`		`LR -> YG (in Ref. 1; AAA41834).`
`CONFLICT`	`232 232`		`F -> S (in Ref. 1; AAA41834).`

Sequence information

Length: 254 AA [This is the length of the unprocessed precursor]

Molecular weight: 28832 Da [This is the MW of the unprocessed precursor]

CRC64: 6DC09A3BEBB22409 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ 

        70         80         90        100        110        120 
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD 

       130        140        150        160        170        180 
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR 

       190        200        210        220        230        240 
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR 

       250 
KAMEAVAAQG KVKK

P25113 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools