ID GPDA_LEIMA Reviewed; 367 AA. AC Q4QHG4; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal; DE EC=1.1.1.8; GN Name=GPD; ORFNames=LmjF10.0510; OS Leishmania major. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania. OX NCBI_TaxID=5664; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/IL/81/Friedlin; RX PubMed=16020728; DOI=10.1126/science.1112680; RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., RA Cadag E., Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., RA Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., RA Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., RA Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., RA Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., RA Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., RA Mottram J.C., Mueller-Auer S., Munden H., Nelson S., Norbertczak H., RA Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., RA Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., RA Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., RA Schaefer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., RA Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., RA Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., RA Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B.G., RA Myler P.J.; RT "The genome of the kinetoplastid parasite, Leishmania major."; RL Science 309:436-442(2005). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone CC phosphate + NADH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Glycosome (By similarity). 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; CT005249; CAJ02624.1; -; Genomic_DNA. DR RefSeq; XP_001681384.1; -. DR SMR; Q4QHG4; 11-358. DR GeneID; 5649653; -. DR KEGG; lma:LmjF10.0510; -. DR HOGENOM; Q4QHG4; -. DR OMA; Q4QHG4; WHIKEEE. DR BRENDA; 1.1.1.8; 19061. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell. 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: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; 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 PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Glycosome; NAD; Oxidoreductase. FT CHAIN 1 367 Glycerol-3-phosphate dehydrogenase FT [NAD+], glycosomal. FT /FTId=PRO_0000262291. FT NP_BIND 23 28 NAD (By similarity). FT REGION 275 276 Substrate binding (By similarity). FT MOTIF 365 367 Microbody targeting signal (Potential). FT ACT_SITE 211 211 Proton acceptor (Potential). FT BINDING 98 98 NAD (By similarity). FT BINDING 126 126 Substrate (By similarity). FT BINDING 158 158 NAD; via amide nitrogen (By similarity). FT BINDING 275 275 NAD (By similarity). FT BINDING 297 297 NAD; via amide nitrogen (By similarity). FT BINDING 301 301 NAD (By similarity). SQ SEQUENCE 367 AA; 39299 MW; 49F47113F30B5657 CRC64; MISTKRHINT NELLHLSKAV VFGSGAFGTA LAMVLSKKCR EVCVWHIKEE EARLVNEKRE NDLYLRGVQL ASNIIFTSDV DEAYKGAELI LFVIPTQFLR GFFQKSGGNL IAYAKARQVP VLVCTKGIER STLKFPAQIV GEFFPSNLLS VLAGPSFAIE VATGVFTCVS VASADINVAR RLQRIMTTGD RSFVCWATTD TVGCEVASAV KNVLAIGSGV ANGLGMGLNA RAALITRGLL EIRDLTAALG GDGSAIFGLA GFGDLQLTCS SELSRNFTVG KKLGKGLSLE EIQRTSKAVA EGVATAEPLV RLAQQLKVTM PLCQQIYEVV YKKKNPRAAI ADLLSCGLQD EGLPPLFKKS AATPSKL //