ID GPDA_TRYBB Reviewed; 354 AA. AC P90593; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 25-NOV-2008, entry version 51. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal; DE EC=1.1.1.8; GN Name=GPD; OS Trypanosoma brucei brucei. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=427; RX MEDLINE=97077437; PubMed=8920004; DOI=10.1016/0166-6851(95)02556-1; RA Kohl L., Drmota T., Thi C.-D., Callens M., van Beeumen J., RA Opperdoes F.R., Michels P.A.M.; RT "Cloning and characterization of the NAD-linked glycerol-3-phosphate RT dehydrogenases of Trypanosoma brucei brucei and Leishmania mexicana RT mexicana and expression of the trypanosome enzyme in Escherichia RT coli."; RL Mol. Biochem. Parasitol. 76:159-173(1996). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone CC phosphate + NADH. CC -!- SUBCELLULAR LOCATION: Glycosome. 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; X89738; CAA61890.1; -; Genomic_DNA. DR PIR; T48649; T48649. DR HSSP; P90551; 1EVY. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-KW. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase (NAD+) a...; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; 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; DHase_multihelical. DR InterPro; IPR016040; NAD(P)-bd. DR InterPro; IPR017751; NAD-dep_Gly3P_DH_euk. DR InterPro; IPR006168; NAD-dep_Gly3P_DHase. DR InterPro; IPR011128; NAD-dep_Gly3P_DHase_N. DR InterPro; IPR006109; NAD_Gly3P_DHase_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 PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Glycosome; NAD; Oxidoreductase. FT CHAIN 1 354 Glycerol-3-phosphate dehydrogenase FT [NAD+], glycosomal. FT /FTId=PRO_0000138083. FT NP_BIND 15 20 NAD (By similarity). FT REGION 267 268 Substrate binding (By similarity). FT MOTIF 352 354 Microbody targeting signal (Potential). FT ACT_SITE 203 203 Proton acceptor (By similarity). FT BINDING 90 90 NAD (By similarity). FT BINDING 118 118 NAD; via amide nitrogen (By similarity). FT BINDING 118 118 Substrate (By similarity). FT BINDING 150 150 NAD; via amide nitrogen (By similarity). FT BINDING 267 267 NAD (By similarity). FT BINDING 293 293 NAD (By similarity). SQ SEQUENCE 354 AA; 37783 MW; 12CE19AEDA9E4EC9 CRC64; MVSGVTYLKR GAVFGSGAFG TALACVLAKK CESVSVWHMN ANEARVVNQK HENVYFLPGA PLPANLTFTA DAEECAKGAE IVLFVIPTQF LRGFLQKNSH ILRNHVVSRN VPVVMCSKGI ERSSLLFPAQ ILEEFLPNYP IGVIAGPSFA IEVAKGMLTN VCTAAADINM ARKIQRIMTT SDGSFRCWAT TDVIGCEIAS AMKNVLAIAS GALKGLGTEN NARAALISRG LLEIRDLTLA LGGTGEAVFG LPGLGDLLLT CSSELSRNFT VGMKLGQGIS LEEIKRTSKA VAEGVATAEP LERLAKKHNA DLPICHEVYN VLYANGCAKR SFKKLNSCKL ADEGLPALPR TSKM //