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Database: UniProt
Entry: P40054
LinkDB: P40054
Original site: P40054 
ID   SERA_YEAST              Reviewed;         469 AA.
AC   P40054; D3DLY8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   13-FEB-2019, entry version 183.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase 1;
DE            Short=3-PGDH 1;
DE            EC=1.1.1.95;
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000305};
DE            EC=1.1.1.399 {ECO:0000269|PubMed:26774271};
GN   Name=SER3; OrderedLocusNames=YER081W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 201388 / BY4741;
RX   PubMed=26774271; DOI=10.1074/jbc.M115.704494;
RA   Becker-Kettern J., Paczia N., Conrotte J.F., Kay D.P., Guignard C.,
RA   Jung P.P., Linster C.L.;
RT   "Saccharomyces cerevisiae forms D-2-hydroxyglutarate and couples its
RT   degradation to D-lactate formation via a cytosolic transhydrogenase.";
RL   J. Biol. Chem. 291:6036-6058(2016).
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:0000269|PubMed:26774271}.
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:0000269|PubMed:26774271};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=49 uM for 2-oxoglutarate {ECO:0000269|PubMed:26774271};
CC         Note=kcat is 0.2 sec(-1) for 2-oxoglutarate reduction.
CC         {ECO:0000269|PubMed:26774271};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- INTERACTION:
CC       P40510:SER33; NbExp=3; IntAct=EBI-16961, EBI-16821;
CC   -!- MISCELLANEOUS: Present with 7670 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; U18839; AAB64636.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07742.1; -; Genomic_DNA.
DR   PIR; S50584; S50584.
DR   RefSeq; NP_011004.3; NM_001178972.3.
DR   ProteinModelPortal; P40054; -.
DR   SMR; P40054; -.
DR   BioGrid; 36826; 70.
DR   DIP; DIP-5336N; -.
DR   IntAct; P40054; 7.
DR   MINT; P40054; -.
DR   STRING; 4932.YER081W; -.
DR   MoonDB; P40054; Predicted.
DR   iPTMnet; P40054; -.
DR   MaxQB; P40054; -.
DR   PaxDb; P40054; -.
DR   PRIDE; P40054; -.
DR   EnsemblFungi; YER081W_mRNA; YER081W_mRNA; YER081W.
DR   GeneID; 856814; -.
DR   KEGG; sce:YER081W; -.
DR   EuPathDB; FungiDB:YER081W; -.
DR   SGD; S000000883; SER3.
DR   GeneTree; ENSGT00940000176610; -.
DR   HOGENOM; HOG000136696; -.
DR   InParanoid; P40054; -.
DR   KO; K00058; -.
DR   OMA; YHAIGIR; -.
DR   BioCyc; YEAST:YER081W-MONOMER; -.
DR   Reactome; R-SCE-977347; Serine biosynthesis.
DR   UniPathway; UPA00135; UER00196.
DR   PRO; PR:P40054; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0061759; F:alpha-ketoglutarate reductase activity; IDA:SGD.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IMP:SGD.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009070; P:serine family amino acid biosynthetic process; IMP:SGD.
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    469       D-3-phosphoglycerate dehydrogenase 1.
FT                                /FTId=PRO_0000076018.
FT   DOMAIN      399    469       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     208    209       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     285    287       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     347    350       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    287    287       {ECO:0000250}.
FT   ACT_SITE    316    316       {ECO:0000250}.
FT   ACT_SITE    347    347       Proton donor. {ECO:0000250}.
FT   BINDING     228    228       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     311    311       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   MOD_RES      22     22       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MOD_RES      29     29       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P40510}.
FT   MOD_RES      33     33       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P40510}.
SQ   SEQUENCE   469 AA;  51193 MW;  E1E69070BF41A87C CRC64;
     MTSIDINNLQ NTFQQAMNMS GSPGAVCTSP TQSFMNTVPQ RLNAVKHPKI LKPFSTGDMK
     ILLLENVNQT AITIFEEQGY QVEFYKSSLP EEELIEKIKD VHAIGIRSKT RLTSNVLQHA
     KNLVCIGCFC IGTNQVDLDY ATSRGIAVFN SPFSNSRSVA ELVIAEIISL ARQLGDRSIE
     LHTGTWNKVA ARCWEVRGKT LGIIGYGHIG SQLSVLAEAM GLHVLYYDIV TIMALGTARQ
     VSTLDELLNK SDFVTLHVPA TPETEKMLSA PQFAAMKDGA YVINASRGTV VDIPSLIQAV
     KANKIAGAAL DVYPHEPAKN GEGSFNDELN SWTSELVSLP NIILTPHIGG STEEAQSSIG
     IEVATALSKY INEGNSVGSV NFPEVALKSL SYDQENTVRV LYIHQNVPGV LKTVNDILSN
     HNIEKQFSDS NGEIAYLMAD ISSVDQSDIK DIYEQLNQTS AKISIRLLY
//
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