PROSITE documentation PDOC00753
FAD-dependent glycerol-3-phosphate dehydrogenase signatures


FAD-dependent glycerol-3-phosphate dehydrogenase (EC (GPD) catalyzes the conversion of glycerol-3-phosphate into dihydroxyacetone phosphate. In bacteria [1] it is associated with the utilization of glycerol coupled to respiration. In Escherichia coli, 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 [2,3].

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.

We developed two signature patterns. One based on the first half of the FAD-binding domain and one which corresponds to a conserved region in the central part of these enzymes.

Expert(s) to contact by email:

Brown L.J.

Last update:

December 2004 / Pattern and text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

FAD_G3PDH_1, PS00977; FAD-dependent glycerol-3-phosphate dehydrogenase signature 1  (PATTERN)

FAD_G3PDH_2, PS00978; FAD-dependent glycerol-3-phosphate dehydrogenase signature 2  (PATTERN)


1AuthorsAustin D. Larson T.J.
TitleNucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12.
SourceJ. Bacteriol. 173:101-107(1991).
PubMed ID1987111

2AuthorsRoennow B. Kielland-Brandt M.C.
SourceYeast 9:1121-1130(1993).

3AuthorsBrown L.J. McDonald M.J. Lehn D.A. Moran S.M.
TitleSequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence for EF-hand calcium-binding domains.
SourceJ. Biol. Chem. 269:14363-14366(1994).
PubMed ID8182039

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