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Database: UniProt
Entry: P87228
LinkDB: P87228
Original site: P87228 
ID   SERA_SCHPO              Reviewed;         466 AA.
AC   P87228; O59798;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JAN-2019, entry version 141.
DE   RecName: Full=Putative D-3-phosphoglycerate dehydrogenase;
DE            Short=3-PGDH;
DE            EC=1.1.1.95;
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000305};
DE            EC=1.1.1.399 {ECO:0000250|UniProtKB:P40054};
GN   ORFNames=SPCC364.07, SPCC4G3.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
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.,
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-258, 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   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-
CC       glycerate to 3-phosphonooxypyruvate, the first step of the
CC       phosphorylated L-serine biosynthesis pathway. Also catalyzes the
CC       reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
CC       {ECO:0000250|UniProtKB:P40054}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.399;
CC         Evidence={ECO:0000250|UniProtKB:P40054};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; CU329672; CAB09778.1; -; Genomic_DNA.
DR   PIR; T41375; T41375.
DR   RefSeq; NP_587837.1; NM_001022830.2.
DR   ProteinModelPortal; P87228; -.
DR   SMR; P87228; -.
DR   BioGrid; 276053; 9.
DR   STRING; 4896.SPCC364.07.1; -.
DR   iPTMnet; P87228; -.
DR   MaxQB; P87228; -.
DR   PaxDb; P87228; -.
DR   PRIDE; P87228; -.
DR   EnsemblFungi; SPCC364.07.1; SPCC364.07.1:pep; SPCC364.07.
DR   GeneID; 2539490; -.
DR   KEGG; spo:SPCC364.07; -.
DR   EuPathDB; FungiDB:SPCC364.07; -.
DR   PomBase; SPCC364.07; -.
DR   HOGENOM; HOG000136696; -.
DR   InParanoid; P87228; -.
DR   KO; K00058; -.
DR   OMA; YHAIGIR; -.
DR   PhylomeDB; P87228; -.
DR   Reactome; R-SPO-977347; Serine biosynthesis.
DR   UniPathway; UPA00135; UER00196.
DR   PRO; PR:P87228; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; ISS:PomBase.
DR   GO; GO:0006564; P:L-serine biosynthetic process; ISS:PomBase.
DR   GO; GO:0009070; P:serine family amino acid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029015; PGDH_2.
DR   PANTHER; PTHR10996:SF165; PTHR10996:SF165; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; NAD; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Serine biosynthesis.
FT   CHAIN         1    466       Putative D-3-phosphoglycerate
FT                                dehydrogenase.
FT                                /FTId=PRO_0000076017.
FT   DOMAIN      396    466       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     205    206       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     282    284       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     344    347       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    284    284       {ECO:0000250}.
FT   ACT_SITE    313    313       {ECO:0000250}.
FT   ACT_SITE    344    344       Proton donor. {ECO:0000250}.
FT   BINDING     225    225       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     308    308       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   MOD_RES      87     87       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     258    258       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
SQ   SEQUENCE   466 AA;  50883 MW;  1E6EA04BF137C628 CRC64;
     MDIKGGRRGN VEDSLNKLSL SPPDNNSSFL SNHFQVRKSY SQAPARTLKP FASEDIKILL
     LENVNQSALS NLKDEGYQVE FLKTSMSEDD LVEKIKGVHA IGIRSKTRLT RRVLEAADSL
     IVIGCFCIGT NQVDLDFAAE RGIAVFNSPY ANSRSVAELV IGYIISLARQ VGDRSLELHR
     GEWNKVSSGC WEIRGKTLGI IGYGHIGSQL SVLAEAMGLH VVYYDILPIM PLGSAKQLSS
     LPELLHRADF VSLHVPASPE TKNMISSKEF AAMKEGSYLI NASRGTVVDI PALVDASKSG
     KIAGAAIDVY PSEPAGNGKD KFVDSLNSWT SELTHCKNII LTPHIGGSTE EAQYNIGIEV
     SEALTRYINE GNSIGAVNFP EVSLRSLTEA DRNAARVLFV HRNVPGVLRQ VNELFIDHNI
     KSQFSDSRGD IAYLVADISD CTPGSLEALH QKLESLPCKI NTRLLY
//
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