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InterPro: IPR019796 Glucose-6-phosphate dehydrogenase, active site

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Matches:

1631 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
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Accession List
Matches in BioMart

Accession

IPR019796 Glc-6-P_DH_AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00069	G6P_DEHYDROGENASE	1631
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001282 Glucose-6-phosphate dehydrogenase
IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0006006 glucose metabolic process
GO:0055114 oxidation reduction

Function

GO:0004345 glucose-6-phosphate dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

Glucose-6-phosphate dehydrogenase (G6PD) [1] catalyses the first step in the pentose pathway, the reduction of glucose-6-phosphate to gluconolactone 6-phosphate. A lysine residue has been identified as a reactive nucleophile associated with the activity of the enzyme [2]. The sequence around this lysine is totally conserved from bacterial to mammalian G6PD's and is used as the pattern to identify the proteins associated with this entry.

Structural links Help

PDB - click here

SCOP: c.2.1.3 , d.81.1.5

CATH: 3.30.360.10

Database links Help

Enzyme: EC:1.1.1.49

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR019796

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P11412 Glucose-6-phosphate 1-dehydrogenase

P11413 Glucose-6-phosphate 1-dehydrogenase

P12646 Glucose-6-phosphate 1-dehydrogenase

Q00612 Glucose-6-phosphate 1-dehydrogenase X

Q27464 Glucose-6-phosphate 1-dehydrogenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016040	NAD(P)-binding domain
IPR001282	Glucose-6-phosphate dehydrogenase
IPR019796	Glucose-6-phosphate dehydrogenase, active site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Jeffery J, Persson B, Wood I, Bergman T, Jeffery R, Jornvall H. Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure. Eur. J. Biochem. 212 41-9 1993 [PubMed: 8444164] http://dx.doi.org/10.1111/j.1432-1033.1993.tb17630.x
2.	Camardella L, Caruso C, Rutigliano B, Romano M, Di Prisco G, Descalzi-Cancedda F. Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate. Eur. J. Biochem. 171 485-9 1988 [PubMed: 3126064] http://dx.doi.org/10.1111/j.1432-1033.1988.tb13815.x

Additional Reading Open in usermanual
	Au SW, Gover S, Lam VM, Adams MJ. Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency. Structure 8 2000 293-303 [PubMed: 10745013] http://dx.doi.org/10.1016/S0969-2126(00)00104-0
	Au SW, Naylor CE, Gover S, Vandeputte-Rutten L, Scopes DA, Mason PJ, Luzzatto L, Lam VM, Adams MJ. Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 55 1999 826-34 [PubMed: 10089300] http://dx.doi.org/10.1107/S0907444999000827
	Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ. Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase. Acta Crystallogr. D Biol. Crystallogr. 61 2005 495-504 [PubMed: 15858258] http://dx.doi.org/10.1107/S0907444905002350
	Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ. NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes. Acta Crystallogr. D Biol. Crystallogr. 57 2001 635-48 [PubMed: 11320304] http://dx.doi.org/10.1107/S0907444901003420
	Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR. An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme. Biochemistry 39 2000 15002-11 [PubMed: 11106478] http://dx.doi.org/10.1021/bi0014608

InterPro 23.1