ID GPD2_SCHPO Reviewed; 373 AA. AC Q09845; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 16-JUN-2009, entry version 67. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD+] 2; DE EC=1.1.1.8; GN Name=gpd2; ORFNames=SPAC23D3.04c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96422483; PubMed=8825100; RX DOI=10.1111/j.1365-2958.1995.18050963.x; RA Ohmiya R., Yamada H., Nakashima K., Aiba H., Mizuno T.; RT "Osmoregulation of fission yeast: cloning of two distinct genes RT encoding glycerol-3-phosphate dehydrogenase, one of which is RT responsible for osmotolerance for growth."; RL Mol. Microbiol. 18:963-973(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS RP SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone CC phosphate + NADH. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). 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; D50797; BAA09425.1; -; Genomic_DNA. DR EMBL; CU329670; CAA91239.1; -; Genomic_DNA. DR PIR; JC6053; JC6053. DR RefSeq; NP_594542.1; -. DR GeneID; 2541502; -. DR KEGG; spo:SPAC23D3.04c; -. DR NMPDR; fig|4896.1.peg.4512; -. DR GeneDB_Spombe; SPAC23D3.04c; -. DR OMA; Q09845; THENVKY. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-002639-MON; -. DR BRENDA; 1.1.1.8; 653. DR ArrayExpress; Q09845; -. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase (NAD+) a...; IMP:GeneDB_SPombe. 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:0006114; P:glycerol biosynthetic process; IMP:GeneDB_SPombe. 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 Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein. FT CHAIN 1 373 Glycerol-3-phosphate dehydrogenase [NAD+] FT 2. FT /FTId=PRO_0000138096. FT NP_BIND 31 36 NAD (By similarity). FT REGION 300 301 Substrate binding (By similarity). FT ACT_SITE 236 236 Proton acceptor (By similarity). FT BINDING 123 123 NAD (By similarity). FT BINDING 146 146 NAD; via amide nitrogen (By similarity). FT BINDING 146 146 Substrate (By similarity). FT BINDING 179 179 NAD; via amide nitrogen (By similarity). FT BINDING 300 300 NAD (By similarity). FT BINDING 329 329 NAD (By similarity). FT MOD_RES 15 15 Phosphoserine. SQ SEQUENCE 373 AA; 40874 MW; 7C3AFBC3DFFB470E CRC64; MTVAALNKLS ALSGSIQKSF SPKLISVGII GSGNWGTAIA KICGENAKAH PDIFHPQVHM WMYEEKIQHE GKECNLTEVF NTTHENVKYL KGIKCPSNVF ANPDIRDVGS RSDILVWVLP HQFVVRICNQ LKGCLKKDAV AISCIKGVSV TKDRVRLFSD IIEENTGMYC GVLSGANIAS EVAQEKFCET TIGYLPNSSV NPRYTPKTIQ ALFNRPYFRV NIVEDVPGVA LGGALKNIVA VAAGIIDGLE LGDNTKSAVM RIGLLEMQKF GRMFFDCKPL TMSEESCGIA DLITTCLGGR NHKCAVAFVK TGKPMHVVEQ ELLDGQKLQG AATAKEVYEF LDNQNKVSEF PLFTAVYRIV YEGLPPNKLL EAI //