ID GPDA_DROAE Reviewed; 350 AA. AC Q27556; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 16-JUN-2009, entry version 63. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic; DE Short=GPDH-C; DE Short=GPD-C; DE EC=1.1.1.8; GN Name=Gpdh; OS Drosophila americana (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=40366; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96025618; PubMed=8522168; DOI=10.1007/BF01439583; RA Tominaga H., Narise S.; RT "Sequence evolution of the Gpdh gene in the Drosophila virilis species RT group."; RL Genetica 96:293-302(1995). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone CC phosphate + NADH. CC -!- PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D50089; BAA20286.1; -; Genomic_DNA. DR FlyBase; FBgn0015636; Dame\Gpdh. DR BRENDA; 1.1.1.8; 304551. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase (NAD+) a...; IEA:EC. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006168; NAD-dep_Gly3P_DH. DR InterPro; IPR017751; NAD-dep_Gly3P_DH_euk. DR InterPro; IPR011128; NAD-dep_Gly3P_DH_N. DR InterPro; IPR006109; NAD_Gly3P_DH_C. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR PANTHER; PTHR11728; NAD_Gly3P_DH; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR ProDom; PD001278; NAD_Gly3P_C; 1. DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Cytoplasm; NAD; Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 350 Glycerol-3-phosphate dehydrogenase FT [NAD+], cytoplasmic. FT /FTId=PRO_0000138072. FT NP_BIND 11 16 NAD (By similarity). FT REGION 270 271 Substrate binding (By similarity). FT ACT_SITE 206 206 Proton acceptor (By similarity). FT BINDING 98 98 NAD (By similarity). FT BINDING 121 121 NAD; via amide nitrogen (By similarity). FT BINDING 121 121 Substrate (By similarity). FT BINDING 155 155 NAD; via amide nitrogen (By similarity). FT BINDING 270 270 NAD (By similarity). FT BINDING 299 299 NAD (By similarity). SQ SEQUENCE 350 AA; 38323 MW; E23908D262F6D660 CRC64; MAEKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEEMIDGKK LTEIINETHE NVKYLKGHKL PTNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR DLFQANHFRV VVVEDAEAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEDLEK EMLNGQKLQG PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPKDLI DCIRNHPEHM //