EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR001282 Glucose-6-phosphate dehydrogenase

Protein matches Help

UniProtKB

Matches:

2424 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

IPR001282 Glc-6-P_DH

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00479	G6PD_N	2069
Pfam	PF02781	G6PD_C	2262
PIRSF	PIRSF000110	G6PD	1749
PRINTS	PR00079	G6PDHDRGNASE	2034
PANTHER	PTHR23429	G6PDH	2383
TIGRFAMs	TIGR00871	zwf	1772
Signatures in BioMart

InterPro Relationships Help

Contains

IPR016040 NAD(P)-binding domain
IPR019796 Glucose-6-phosphate dehydrogenase, active site

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 (EC:1.1.1.49) (G6PDH) is a ubiquitous protein, present in bacteria and all eukaryotic cell types [1]. The enzyme catalyses the the first step in the pentose pathway, i.e. the conversion of glucose-6-phosphate to gluconolactone 6-phosphate in the presence of NADP, producing NADPH. The ubiquitous expression of the enzyme gives it a major role in the production of NADPH for the many NADPH-mediated reductive processes in all cells [2]. Deficiency of G6PDH is a common genetic abnormality affecting millions of people worldwide. Many sequence variants, most caused by single point mutations, are known, exhibiting a wide variety of phenotypes [2].

Structural links Help

PDB - click here

SCOP: c.2.1.3 , d.81.1.5

CATH: 3.30.360.10 , 3.40.50.720

Database links Help

PDBe-motif: PS00069

Enzyme: EC:1.1.1.49

PROSITE doc: PDOC00067

PANDIT: PF00479 , PF02781

Blocks: IPB001282

Pfam Clan: CL0063.21

AC	CL0063.21
ID	NADP_Rossmann
DE	FAD/NAD(P)-binding Rossmann fold Superfamily
PF00044	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
PF00056	IPR001236	Lactate/malate dehydrogenase
PF00070	IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00106	IPR002198	Short-chain dehydrogenase/reductase SDR
PF00107	IPR013149	Alcohol dehydrogenase, zinc-binding
PF00208	IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
PF00479	IPR001282	Glucose-6-phosphate dehydrogenase
PF00670	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
PF00732	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
PF00743	IPR000960	Flavin-containing monooxygenase FMO
PF00890	IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00899	IPR000594	UBA/THIF-type NAD/FAD binding fold
PF00996	IPR018203	GDP dissociation inhibitor
PF01073	IPR002225	3-beta hydroxysteroid dehydrogenase/isomerase
PF01113	IPR000846	Dihydrodipicolinate reductase
PF01118	IPR000534	Semialdehyde dehydrogenase, NAD-binding
PF01134	IPR002218	Glucose-inhibited division protein A-related
PF01210	IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01225	IPR000713	Mur ligase, N-terminal
PF01232	IPR013131	Mannitol dehydrogenase, N-terminal
PF01262	IPR007698	Alanine dehydrogenase/PNT, C-terminal
PF01266	IPR006076	FAD dependent oxidoreductase
PF01370	IPR001509	NAD-dependent epimerase/dehydratase
PF01408	IPR000683	Oxidoreductase, N-terminal
PF01488	IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
PF01494	IPR002938	Monooxygenase, FAD-binding
PF01593	IPR002937	Amine oxidase
PF01946	IPR002922	Thiamine biosynthesis Thi4 protein
PF02153	IPR003099	Prephenate dehydrogenase
PF02254	IPR003148	Regulator of K+ conductance, N-terminal
PF02423	IPR003462	Ornithine cyclodeaminase/mu-crystallin
PF02558	IPR013332	Ketopantoate reductase ApbA/PanE, N-terminal
PF02629	IPR003781	CoA-binding
PF02670	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02719	IPR003869	Polysaccharide biosynthesis protein CapD-like
PF02737	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
PF02826	IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02882	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
PF03435	IPR005097	Saccharopine dehydrogenase
PF03446	IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
PF03447	IPR005106	Aspartate/homoserine dehydrogenase, NAD-binding
PF03486	IPR004792	HI0933-like protein
PF03721	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03807	IPR004455	NADP oxidoreductase, coenzyme F420-dependent
PF03949	IPR012302	Malic enzyme, NAD-binding
PF04321	IPR005913	dTDP-4-dehydrorhamnose reductase
PF04723	IPR006812	Glycine reductase complex selenoprotein A
PF04820	IPR006905	Tryptophan halogenase
PF05368	IPR008030	NmrA-like
PF05834	IPR008671	Lycopene beta/epsilon cyclase
PF06039	IPR006231	Malate:quinone-oxidoreductase
PF07157	IPR009826	DNA circulation, N-terminal
PF07991	IPR013116	Acetohydroxy acid isomeroreductase, catalytic
PF07992	IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07993	IPR013120	Male sterility, NAD-binding
PF07994	IPR002587	Myo-inositol-1-phosphate synthase
PF08491	IPR013698	Squalene epoxidase
PF08659	IPR013968	Polyketide synthase, KR
PF10727	IPR019665	Putative oxidoreductase/dehydrogenase, Rossmann-like domain

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001282

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

P97324 Glucose-6-phosphate 1-dehydrogenase 2

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.	Fouts D, Ganguly R, Gutierrez AG, Lucchesi JC, Manning JE. Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene. Gene 63 261-75 1988 [PubMed: 2838391] http://dx.doi.org/10.1016/0378-1119(88)90530-6
2.	Vulliamy TJ, D'Urso M, Battistuzzi G, Estrada M, Foulkes NS, Martini G, Calabro V, Poggi V, Giordano R, Town M. Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia. Proc. Natl. Acad. Sci. U.S.A. 85 5171-5 1988 [PubMed: 3393536] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=3393536

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
	Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry 37 1998 2759-67 [PubMed: 9485426] http://dx.doi.org/10.1021/bi972069y
	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