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sn-glycerol-3-phosphate dehydrogenase subunit A

sn-glycerol-3-phosphate dehydrogenase subunit A catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone using fumarate or nitrate as electron acceptor

Arch. IDVersionDate PublishedReview Level
1101427612016-08-19
curated
Arch. ID11014276
Version1
Date Published2016-08-19
Review Level
curated
Rossmann-fold NAD(P)(+)-binding proteins: A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.Rossmann-fold NAD(P)(+)-binding proteinsObsolete: This domain/cluster is obsoleteObsoleteFer2_BFD: BFD-like [2Fe-2S] binding domainFer2_BFD
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Sequences with this architecture
This architecture currently does not link to any protein sequence records.
Name, label and taxonomic scope
Taxonomic scopeNameLabel
All organismssn-glycerol-3-phosphate dehydrogenase subunit Asn-glycerol-3-phosphate dehydrogenase subunit A catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone using fumarate or nitrate as electron acceptor
Name, label and taxonomic scope
Tax. ExpAll organisms
Namesn-glycerol-3-phosphate dehydrogenase subunit A
Labelsn-glycerol-3-phosphate dehydrogenase subunit A catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone using fumarate or nitrate as electron acceptor
Supporting evidence
Comments
  • includes FAD-dependent glycerol-3-phosphate dehydrogenase; catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone using fumarate or nitrate as electron acceptor; also includes other FAD/NAD(P)-binding oxidoreductases
  • EC 1.1.5.3 (formerly EC 1.1.99.5)
  • sn-glycerol-3-phosphate dehydrogenase subunit A also known as glycerol-3-phosphate dehydrogenase; alpha-glycerophosphate dehydrogenase; anaerobic glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked L-glycerol-3-phosphate dehydrogenase; glycerol phosphate dehydrogenase; glycerol-3-phosphate CoQ reductase; glycerophosphate dehydrogenase; L-3-glycerophosphate-ubiquinone oxidoreductase; L-glycerophosphate dehydrogenase; mGPD; mitochondrial glycerol phosphate dehydrogenase; NAD+-independent glycerol phosphate dehydrogenase; pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase; sn-glycerol-3-phosphate dehydrogenase; sn-glycerol-3-phosphate:acceptor 2-oxidoreductase
E.C. Number
CDD
Protein Accession
  • KMY39857: glycerol-3-phosphate dehydrogenase [Aeromonas caviae]
  • EJM54118: NAD(FAD)-dependent dehydrogenase [Pseudomonas sp. GM48]
  • D4GQU6: RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A2; Short=G-3-P dehydrogenase A2; Short=G3PDH A2
Conserved domains in this architecture
AccessionShort nameTitle
cl21454Rossmann-fold NAD(P)(+)-binding proteinsA large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.
cl25187ObsoleteThis domain/cluster is obsolete
pfam04324Fer2_BFDBFD-like [2Fe-2S] binding domain

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