GPD1_SCHPO
ID GPD1_SCHPO Reviewed; 385 AA.
AC P21696; O94310; P78927;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1;
DE EC=1.1.1.8 {ECO:0000305|PubMed:8825100};
DE AltName: Full=GPDH-C;
DE Short=GPD-C;
GN Name=gpd1; ORFNames=SPBC215.05;
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=2263480; DOI=10.1093/nar/18.23.7145;
RA Pidoux A.L., Fawell E.H., Armstrong J.;
RT "Glycerol-3-phosphate dehydrogenase homologue from Schizosaccharomyces
RT pombe.";
RL Nucleic Acids Res. 18:7145-7145(1990).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77, AND CATALYTIC ACTIVITY.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 AND THR-382, AND
RP IDENTIFICATION BY 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; Evidence={ECO:0000305|PubMed:8825100};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; X56162; CAA39630.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22119.1; -; Genomic_DNA.
DR EMBL; D50796; BAA09424.1; -; Genomic_DNA.
DR PIR; T39895; T39895.
DR RefSeq; NP_596682.1; NM_001022605.2.
DR AlphaFoldDB; P21696; -.
DR SMR; P21696; -.
DR BioGRID; 276983; 50.
DR STRING; 4896.SPBC215.05.1; -.
DR iPTMnet; P21696; -.
DR SwissPalm; P21696; -.
DR MaxQB; P21696; -.
DR PaxDb; P21696; -.
DR PRIDE; P21696; -.
DR EnsemblFungi; SPBC215.05.1; SPBC215.05.1:pep; SPBC215.05.
DR GeneID; 2540455; -.
DR KEGG; spo:SPBC215.05; -.
DR PomBase; SPBC215.05; gpd1.
DR VEuPathDB; FungiDB:SPBC215.05; -.
DR eggNOG; KOG2711; Eukaryota.
DR HOGENOM; CLU_033449_2_2_1; -.
DR InParanoid; P21696; -.
DR OMA; FIHKVCD; -.
DR PhylomeDB; P21696; -.
DR Reactome; R-SPO-1483166; Synthesis of PA.
DR PRO; PR:P21696; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IMP:PomBase.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEP:PomBase.
DR GO; GO:0009992; P:cellular water homeostasis; IEP:PomBase.
DR GO; GO:0006114; P:glycerol biosynthetic process; IMP:PomBase.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006116; P:NADH oxidation; ISO:PomBase.
DR GO; GO:0031137; P:regulation of conjugation with cellular fusion; IMP: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..385
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1"
FT /id="PRO_0000138095"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 29..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 296..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 382
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 54..56
FT /note="SKV -> GKG (in Ref. 1; CAA39630)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..127
FT /note="CD -> WH (in Ref. 1; CAA39630)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="Missing (in Ref. 1; CAA39630)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="R -> S (in Ref. 1; CAA39630)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="F -> S (in Ref. 1; CAA39630)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41995 MW; 8061C294196516E1 CRC64;
MSGYGQQGVS AANIDSIRPK KRLSIGVVGS GNWGTAIAKI CGENARAHGH HFRSKVRMWV
FEEEIEYKGE KRKLTEVFNE AHENVKYLPG IECPPNVIAV PDVREVARRA DILVFVVPHQ
FIERVCDQMV GLIRPGAVGI SCIKGVAVSK EGVRLYSEVI SEKLGIYCGV LSGANVANEV
AREQFCETTI GFNPPNEVDI PREQIAAVFD RPYFSVVSVD DVAGVALGGA LKNVVAMAVG
FADGLEWGGN TKAAIMRRGL LEMQKFATTF FDSDPRTMVE QSCGIADLVT SCLGGRNNRC
AEAFVKTGKS LETLEKELLG GQLLQGAATS KDVHEFLLTK DMVKDFPLFT AVYNISYEDM
DPKDLIIVLQ PLKEDSENEG GTETE
