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InterPro: IPR006109 NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal

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2309 proteins

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Accession

IPR006109 NAD_Gly3P_DH_C

Secondary

IPR001652

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF07479	NAD_Gly3P_dh_C	2309
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013328 Dehydrogenase, multihelical

Found in

IPR006168 NAD-dependent glycerol-3-phosphate dehydrogenase
IPR017751 NAD-dependent glycerol-3-phosphate dehydrogenase, eukaryotic

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process
GO:0055114 oxidation reduction

Function

GO:0016614 oxidoreductase activity, acting on CH-OH group of donors

InterPro annotation

Entry Details in BioMart

Abstract

NAD-dependent glycerol-3-phosphate dehydrogenase (EC:1.1.1.8) (GPD) catalyzes the reversible reduction of dihydroxyacetone phosphate to glycerol-3-phosphate. It is a cytoplasmic protein, active as a homodimer [1], each monomer containing an N-terminal NAD binding site [2]. In insects, it acts in conjunction with a mitochondrial alpha-glycerophosphate oxidase in the alpha-glycerophosphate cycle, which is essential for the production of energy used in insect flight [1].

Structural links Help

PDB - click here

SCOP: a.100.1.6

CATH: 1.10.1040.10 , 3.40.50.720

Database links Help

Enzyme: EC:1.1.1.94

PANDIT: PF07479

Pfam Clan: CL0106.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006109

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P13706 Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic

P13707 Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic

P21695 Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic

P34517 Probable glycerol-3-phosphate dehydrogenase 2

P41911 Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006168	NAD-dependent glycerol-3-phosphate dehydrogenase
IPR008927	6-phosphogluconate dehydrogenase, C-terminal-like
IPR016040	NAD(P)-binding domain
IPR017751	NAD-dependent glycerol-3-phosphate dehydrogenase, eukaryotic
IPR013328	Dehydrogenase, multihelical
IPR006109	NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal
IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	von Kalm L, Weaver J, DeMarco J, MacIntyre RJ, Sullivan DT. Structural characterization of the alpha-glycerol-3-phosphate dehydrogenase-encoding gene of Drosophila melanogaster. Proc. Natl. Acad. Sci. U.S.A. 86 5020-4 1989 [PubMed: 2500660] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2500660
2.	Otto J, Argos P, Rossmann MG. Prediction of secondary structural elements in glycerol-3-phosphate dehydrogenase by comparison with other dehydrogenases. Eur. J. Biochem. 109 325-30 1980 [PubMed: 6773774] http://dx.doi.org/10.1111/j.1432-1033.1980.tb04798.x

Additional Reading Open in usermanual
	Choe J, Guerra D, Michels PA, Hol WG. Leishmania mexicana glycerol-3-phosphate dehydrogenase showed conformational changes upon binding a bi-substrate adduct. J. Mol. Biol. 329 2003 335-49 [PubMed: 12758080] http://dx.doi.org/10.1016/S0022-2836(03)00421-2
	Choe J, Suresh S, Wisedchaisri G, Kennedy KJ, Gelb MH, Hol WG. Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase. Chem. Biol. 9 2002 1189-97 [PubMed: 12445769] http://dx.doi.org/10.1016/S1074-5521(02)00243-0
	Suresh S, Turley S, Opperdoes FR, Michels PA, Hol WG. A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Structure 8 2000 541-52 [PubMed: 10801498] http://dx.doi.org/10.1016/S0969-2126(00)00135-0
	Sakasegawa S, Hagemeier CH, Thauer RK, Essen LO, Shima S. Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: a glycerol-3-phosphate dehydrogenase with an unusual NADP+ preference. Protein Sci. 13 2004 3161-71 [PubMed: 15557260] http://dx.doi.org/10.1110/ps.04980304
	Pahlman IL, Larsson C, Averet N, Bunoust O, Boubekeur S, Gustafsson L, Rigoulet M. Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J. Biol. Chem. 277 2002 27991-5 [PubMed: 12032156] http://dx.doi.org/10.1074/jbc.M204079200

InterPro 23.1