[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(86)90181-2; PubMed=3023182 [NCBI, ExPASy, EBI, Israel, Japan] Yanagawa S., Hitomi K., Sasaki R., Chiba H.; "Isolation and characterization of cDNA encoding rabbit reticulocyte 2,3-bisphosphoglycerate synthase."; Gene 44:185-191(1986).

Comments

FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. Can also catalyze the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H₂O = 3-phospho-D-glycerate + phosphate.
SUBUNIT: Homodimer.
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

M15884; AAA31240.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A24973; PMRBBM.

NP_001075738.1; -.

3D structure databases

HSSP

P31217; 1E58. [HSSP ENTRY / PDB]

SMR

P07952; 2-256.

ModBase

P07952.

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.

Genome annotation databases

Ensembl

ENSOCUG00000003144; Oryctolagus cuniculus. [Contig view]

GeneID

100009096; -.

Phylogenomic databases

HOVERGEN

P07952; -.

Other

ProtoNet

P07952.

UniRef

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

Keywords

Glycolysis; Hydrolase; Isomerase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 259`	`258`	`Bisphosphoglycerate mutase.`	`PRO_0000179836`
`ACT_SITE`	`11 11`		`Tele-phosphohistidine intermediate.`
`ACT_SITE`	`188 188`
`SITE`	`62 62`	`1`	`Interaction with carboxyl group of phosphoglycerates.`

Sequence information

Length: 259 AA [This is the length of the unprocessed precursor]

Molecular weight: 30030 Da [This is the MW of the unprocessed precursor]

CRC64: 350A0290D24AE528 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL 

        70         80         90        100        110        120 
NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EKMALNHGEE QVRIWRRSYN 

       130        140        150        160        170        180 
VTPPPIEESH PYYHEIYSDR RYRVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG 

       190        200        210        220        230        240 
KTVLISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA 

       250 
IQAAIKKVED QGKVKRAEK

P07952 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