ID   GPDA_DROVI              Reviewed;         353 AA.
AC   P07735; Q27634;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 76.
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 virilis (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Narise S., Tominaga H.;
RT   "Temperature-dependency differencies in GPDH allozmyes associated with
RT   a single base change in the coding region of the GPDH structural gene
RT   in Drosophila virilis.";
RL   Life Sci. Adv. (Genet.) 11:39-45(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92305069; PubMed=1610907; DOI=10.1016/0167-4781(92)90086-F;
RA   Tominaga H., Shiba T., Narise S.;
RT   "Structure of Drosophila virilis glycerol-3-phosphate dehydrogenase
RT   gene and a comparison with the Drosophila melanogaster gene.";
RL   Biochim. Biophys. Acta 1131:233-238(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-353.
RA   Arai K., Tominaga H., Yokote Y., Narise S.;
RT   "The complete amino-acid sequence of cytoplasmic glycerol-3-phosphate
RT   dehydrogenase from Drosophila virilis.";
RL   Biochim. Biophys. Acta 953:6-13(1988).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone
CC       phosphate + NADH.
CC   -!- PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; X59076; CAA41800.1; -; mRNA.
DR   EMBL; D10697; BAA01539.1; -; Genomic_DNA.
DR   PIR; A60985; A60985.
DR   PIR; B60985; B60985.
DR   PIR; JS0023; JS0023.
DR   PIR; S31790; S31790.
DR   FlyBase; FBgn0013081; Dvir\Gpdh.
DR   BRENDA; 1.1.1.8; 141708.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    353       Glycerol-3-phosphate dehydrogenase
FT                                [NAD+], cytoplasmic.
FT                                /FTId=PRO_0000138077.
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).
FT   MOD_RES       2      2       Blocked amino end (Ala).
FT   CONFLICT     15     15       W -> N (in Ref. 3; AA sequence).
FT   CONFLICT     35     35       E -> K (in Ref. 1; CAA41800).
SQ   SEQUENCE   353 AA;  38651 MW;  E18B4DF92303D8C2 CRC64;
     MAEKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEEMIDGKK LTEIINETHE
     NVKYLKGHKL PTNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI
     KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR
     DLFQANHFRV VVVEDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF
     VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEDLEK EMLNGQKLQG
     PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPKDLI DCIRNHPEHM QTL
//