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InterPro: IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase

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2002 proteins

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Accession

IPR000447 FAD-dep_Gly3P_DH

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR01001	FADG3PDH	1977
PROSITE pattern	PS00977	FAD_G3PDH_1	1208
PROSITE pattern	PS00978	FAD_G3PDH_2	1102
Signatures in BioMart

InterPro Relationships Help

Parent

IPR006076 FAD dependent oxidoreductase

Found in

IPR017752 Anaerobic glycerol-3-phosphate dehydrogenase, A subunit

GO Term annotation Help

Process

GO:0006072 glycerol-3-phosphate metabolic process
GO:0055114 oxidation reduction

Function

GO:0004368 glycerol-3-phosphate dehydrogenase activity

Component

GO:0009331 glycerol-3-phosphate dehydrogenase complex

InterPro annotation

Entry Details in BioMart

Abstract

FAD-dependent glycerol-3-phosphate dehydrogenase (G3PDH; EC:1.1.99.5) catalyzes the conversion of glycerol-3-phosphate into dihydroxyacetone phosphate:

sn-glycerol-3-phosphate + acceptor = glycerone phosphate + reduced acceptor

Insulin exposure often stimulates G3PDH activity [1, 2], and thus is key to reducing the effects of the disease diabetes. In obese people, where insulin resistance has been demonstrated, the amount of G3PDH has been shown to be correspondingly lower than that in normal weight people [1]. In bacteria [3] it is associated with the utilization of glycerol coupled to respiration. In Escherichia coli and Haemophilus influenzae, two isozymes are known: one expressed under anaerobic conditions (gene glpA) and one in aerobic conditions (gene glpD). In eukaryotes, a mitochondrial form of GPD participates in the glycerol phosphate shuttle in conjunction with an NAD-dependent cytoplasmic GPD (EC:1.1.1.8) [4, 5]. This mechanism is responsible for the preservation of a redox balance [6, 7]. In this environment, the enzyme has been recorded to increase activity in the presence of calcium [8]. These enzymes are proteins of about 60 to 70 Kd which contain a probable FAD-binding domain in their N-terminal extremity. The mammalian enzyme differs from the bacterial or yeast proteins by having an EF-hand calcium-binding region (see PDOC00018) in its C-terminal extremity.

Database links Help

PDBe-motif: PS00977 , PS00978

Enzyme: EC:1.1.5.3

PROSITE doc: PDOC00753

Blocks: IPB000447

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000447

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P32191 Glycerol-3-phosphate dehydrogenase, mitochondrial

P43304 Glycerol-3-phosphate dehydrogenase, mitochondrial

P90795 Probable glycerol-3-phosphate dehydrogenase, mitochondrial

Q64521 Glycerol-3-phosphate dehydrogenase, mitochondrial

Q9SS48 Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006076	FAD dependent oxidoreductase
IPR011992	EF-hand-like domain
IPR018247	EF-Hand 1, calcium-binding site
IPR002048	Calcium-binding EF-hand
IPR018249	EF-HAND 2
IPR018248	EF-Hand domain
IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Tu KY, Ju HS, Pettit F, Shive W, Topek NH, Matthews R, Matthews K. Glycerol-3-phosphate dehydrogenase activity in human lymphocytes: effects of insulin, obesity and weight loss. Biochem. Biophys. Res. Commun. 207 183-90 1995 [PubMed: 7857262] http://dx.doi.org/10.1006/bbrc.1995.1170
2.	Koike G, Van Vooren P, Shiozawa M, Galli J, Li LS, Glaser A, Balasubramanyam A, Brown LJ, Luthman H, Szpirer C, MacDonald MJ, Jacob HJ. Genetic mapping and chromosome localization of the rat mitochondrial glycerol-3-phosphate dehydrogenase gene, a candidate for non-insulin-dependent diabetes mellitus. Genomics 38 96-9 1996 [PubMed: 8954787] http://dx.doi.org/10.1006/geno.1996.0599
3.	Austin D, Larson TJ. Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12. J. Bacteriol. 173 101-7 1991 [PubMed: 1987111] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1987111&action=stream&blobtype=pdf
4.	Ronnow B, Kielland-Brandt MC. GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae. Yeast 9 1121-30 1993 [PubMed: 8256521] http://dx.doi.org/10.1002/yea.320091013
5.	Brown LJ, MacDonald MJ, Lehn DA, Moran SM. Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence for EF-hand calcium-binding domains. J. Biol. Chem. 269 14363-6 1994 [PubMed: 8182039] http://intl.jbc.org/cgi/content/abstract/269/20/14363
6.	Dummler K, Muller S, Seitz HJ. Regulation of adenine nucleotide translocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues. Biochem. J. 317 ( Pt 3) 913-8 1996 [PubMed: 8760382] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8760382
7.	Larsson C, Pahlman IL, Ansell R, Rigoulet M, Adler L, Gustafsson L. The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae. Yeast 14 347-57 1998 [PubMed: 9559543] http://dx.doi.org/10.1002/(SICI)1097-0061(19980315)14:4<347::AID-YEA226>3.3.CO;2-0
8.	MacDonald MJ, Brown LJ. Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied. Arch. Biochem. Biophys. 326 79-84 1996 [PubMed: 8579375] http://dx.doi.org/10.1006/abbi.1996.0049

InterPro 23.1