GPD2_SCHPO
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 03-AUG-2022, entry version 155.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 2;
DE EC=1.1.1.8;
GN Name=gpd2; ORFNames=SPAC23D3.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8825100; 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 encoding
RT glycerol-3-phosphate dehydrogenase, one of which is responsible for
RT osmotolerance for growth.";
RL Mol. Microbiol. 18:963-973(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA 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 IDENTIFICATION BY
RP MASS 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:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; D50797; BAA09425.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91239.1; -; Genomic_DNA.
DR PIR; JC6053; JC6053.
DR RefSeq; NP_594542.1; NM_001019971.2.
DR AlphaFoldDB; Q09845; -.
DR SMR; Q09845; -.
DR BioGRID; 278004; 14.
DR STRING; 4896.SPAC23D3.04c.1; -.
DR iPTMnet; Q09845; -.
DR MaxQB; Q09845; -.
DR PaxDb; Q09845; -.
DR PRIDE; Q09845; -.
DR EnsemblFungi; SPAC23D3.04c.1; SPAC23D3.04c.1:pep; SPAC23D3.04c.
DR GeneID; 2541502; -.
DR KEGG; spo:SPAC23D3.04c; -.
DR PomBase; SPAC23D3.04c; gpd2.
DR VEuPathDB; FungiDB:SPAC23D3.04c; -.
DR eggNOG; KOG2711; Eukaryota.
DR HOGENOM; CLU_033449_2_2_1; -.
DR InParanoid; Q09845; -.
DR OMA; NRMFGNM; -.
DR PhylomeDB; Q09845; -.
DR Reactome; R-SPO-1483166; Synthesis of PA.
DR PRO; PR:Q09845; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; ISO:PomBase.
DR GO; GO:0051287; F:NAD binding; IC:PomBase.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0006114; P:glycerol biosynthetic process; IMP:PomBase.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IC:PomBase.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006116; P:NADH oxidation; ISO:PomBase.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..373
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 2"
FT /id="PRO_0000138096"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 31..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 300..301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
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
