MF_01038

2,3-bisphosphoglycerate-independent phosphoglycerate mutase [gpmI]

HAMAP entry
Member databaseHAMAP
HAMAP typefamily
Short nameGpmI

Description
Imported from IPR005995

This 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM) is a metalloenzyme found particularly in eubacteria and higher plants. It is distantly related to archaeal iPGAM (
IPR004456
) and distinct from the unrelated cofactor-dependent PGAM. Activity has been demonstrated for proteins from a variety of organisms, including Pseudomonas syringae pv. tomato
[1]
, Bacillus subtilis
[2]
, Bacillus stearothermophilus
[3]
, maize
[4]
, castor bean
[5]
, and Trypanosoma brucei
[6]
. The structure of the B. stearothermophilus enzyme has two domains
[7]
. Residues 1-76 and 311-511 form the phosphatase domain, containing the active site residue and two metal-binding sites. This domain is similar to alkaline phosphatase and arylsulphatase, which are members of the SCOP alkaline phosphatase-like superfamily, but there is meagre sequence similarity outside of the metal-binding segments. Residues 77-310 form the phosphotransferase domain, which is poorly conserved (or perhaps unrelated) in the archaeal enzymes.

References
Imported from IPR005995

1.Isolation and sequence analysis of the Pseudomonas syringae pv. tomato gene encoding a 2,3-diphosphoglycerate-independent phosphoglyceromutase. Morris VL, Jackson DP, Grattan M, Ainsworth T, Cuppels DA. J. Bacteriol. 177, 1727-33, (1995). View articlePMID: 7896694

2.Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. Leyva-Vazquez MA, Setlow P. J. Bacteriol. 176, 3903-10, (1994). View articlePMID: 8021172

3.Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus. Chander M, Setlow P, Lamani E, Jedrzejas MJ. J. Struct. Biol. 126, 156-65, (1999). View articlePMID: 10388626

4.Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize. Possible relationship to the alkaline phosphatase family. Grana X, de Lecea L, el-Maghrabi MR, Urena JM, Caellas C, Carreras J, Puigdomenech P, Pilkis SJ, Climent F. J. Biol. Chem. 267, 12797-803, (1992). View articlePMID: 1535626

5.Higher-plant cofactor-independent phosphoglyceromutase: purification, molecular characterization and expression. Huang Y, Blakeley SD, McAleese SM, Fothergill-Gilmore LA, Dennis DT. Plant Mol. Biol. 23, 1039-53, (1993). View articlePMID: 8260624

6.Trypanosoma brucei contains a 2,3-bisphosphoglycerate independent phosphoglycerate mutase. Chevalier N, Rigden DJ, Van Roy J, Opperdoes FR, Michels PA. Eur. J. Biochem. 267, 1464-72, (2000). View articlePMID: 10691985

7.Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate. Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G. J. Biol. Chem. 275, 23146-53, (2000). View articlePMID: 10764795

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