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InterPro: IPR006124 Metalloenzyme

Protein matches Help

UniProtKB

Matches:

2371 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006124 Metalloenzyme

Secondary

IPR002599

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01676	Metalloenzyme	2371
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005995 Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent
IPR010045 Phosphopentomutase
IPR017849 Alkaline phosphatase-like, alpha/beta/alpha
IPR017850 Alkaline-phosphatase-like, core domain

GO Term annotation Help

Function

GO:0003824 catalytic activity
GO:0046872 metal ion binding

InterPro annotation

Entry Details in BioMart

Abstract

This domain unites alkaline phosphatase, N-acetylgalactosamine-4-sulphatase, and cerebroside sulphatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulphatases. This domain is also related to alkaline phosphatase IPR001952 [1]. The most conserved residues are probably involved in metal binding and catalysis.

Structural links Help

PDB - click here

SCOP: c.76.1.3 , c.76.1.5

CATH: 3.40.720.10

Database links Help

Enzyme: EC:5.4.2

PANDIT: PF01676

Blocks: IPB006124

Pfam Clan: CL0088.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006124

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O04499 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1

O57742 2,3-bisphosphoglycerate-independent phosphoglycerate mutase

P51379 2,3-bisphosphoglycerate-independent phosphoglycerate mutase

P74507 2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Q81X77 2,3-bisphosphoglycerate-independent phosphoglycerate mutase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005995	Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent
IPR011258	BPG-independent PGAM, N-terminal
IPR004456	Cofactor-independent phosphoglycerate mutase, archaeal
IPR019304	2,3-bisphosphoglycerate-independent phosphoglycerate mutase
IPR006124	Metalloenzyme
IPR017850	Alkaline-phosphatase-like, core domain
IPR017849	Alkaline phosphatase-like, alpha/beta/alpha
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Galperin MY, Bairoch A, Koonin EV. A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci. 7 1829-35 1998 [PubMed: 10082381] http://www.proteinscience.org/cgi/content/abstract/7/8/1829

Additional Reading Open in usermanual
	Rigden DJ, Lamani E, Mello LV, Littlejohn JE, Jedrzejas MJ. Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling. J. Mol. Biol. 328 2003 909-20 [PubMed: 12729763] http://dx.doi.org/10.1016/S0022-2836(03)00350-4
	Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G. Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate. J. Biol. Chem. 275 2000 23146-53 [PubMed: 10764795] http://dx.doi.org/10.1074/jbc.M002544200
	Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G. Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus. EMBO J. 19 2000 1419-31 [PubMed: 10747010] http://dx.doi.org/10.1093/emboj/19.7.1419

InterPro 23.1