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Database: UniProt
Entry: P40510
LinkDB: P40510
Original site: P40510 
ID   SER33_YEAST             Reviewed;         469 AA.
AC   P40510; D6VVL0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   01-MAY-2013, entry version 124.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase 2;
DE            Short=3-PGDH 2;
DE            EC=1.1.1.95;
GN   Name=SER33; OrderedLocusNames=YIL074C;
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 204511 / S288c / AB972;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
RA   Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
RA   Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
RA   Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RG   Saccharomyces Genome Database;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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 MASS
RP   SPECTROMETRY.
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-28; SER-29 AND
RP   THR-31, AND MASS SPECTROMETRY.
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).
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3-
CC       phosphonooxypyruvate + NADH.
CC   -!- CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate +
CC       NADH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-16821, EBI-16821;
CC       P40054:SER3; NbExp=4; IntAct=EBI-16821, EBI-16961;
CC   -!- MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 ACT domain.
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DR   EMBL; Z37997; CAA86096.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08476.1; -; Genomic_DNA.
DR   PIR; S48370; S48370.
DR   RefSeq; NP_012191.1; NM_001179424.1.
DR   ProteinModelPortal; P40510; -.
DR   SMR; P40510; 59-469.
DR   DIP; DIP-4483N; -.
DR   IntAct; P40510; 5.
DR   MINT; MINT-404061; -.
DR   PaxDb; P40510; -.
DR   PeptideAtlas; P40510; -.
DR   PRIDE; P40510; -.
DR   EnsemblFungi; YIL074C; YIL074C; YIL074C.
DR   GeneID; 854736; -.
DR   KEGG; sce:YIL074C; -.
DR   CYGD; YIL074c; -.
DR   SGD; S000001336; SER33.
DR   eggNOG; COG0111; -.
DR   GeneTree; ENSGT00530000063021; -.
DR   HOGENOM; HOG000136696; -.
DR   KO; K00058; -.
DR   OMA; NLVVIGC; -.
DR   OrthoDB; EOG4NGKWJ; -.
DR   UniPathway; UPA00135; UER00196.
DR   NextBio; 977440; -.
DR   ArrayExpress; P40510; -.
DR   Genevestigator; P40510; -.
DR   GermOnline; YIL074C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; 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   Gene3D; 3.40.50.720; -; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 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 2.
FT                                /FTId=PRO_0000076019.
FT   DOMAIN      398    468       ACT.
FT   NP_BIND     208    209       NAD (By similarity).
FT   NP_BIND     285    287       NAD (By similarity).
FT   NP_BIND     347    350       NAD (By similarity).
FT   ACT_SITE    287    287       By similarity.
FT   ACT_SITE    316    316       By similarity.
FT   ACT_SITE    347    347       Proton donor (By similarity).
FT   BINDING     228    228       NAD (By similarity).
FT   BINDING     311    311       NAD (By similarity).
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      28     28       Phosphothreonine.
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES      31     31       Phosphothreonine.
SQ   SEQUENCE   469 AA;  51188 MW;  23C59BAEA9FEDB36 CRC64;
     MSYSAADNLQ DSFQRAMNFS GSPGAVSTSP TQSFMNTLPR RVSITKQPKA LKPFSTGDMN
     ILLLENVNAT AIKIFKDQGY QVEFHKSSLP EDELIEKIKD VHAIGIRSKT RLTEKILQHA
     RNLVCIGCFC IGTNQVDLKY AASKGIAVFN SPFSNSRSVA ELVIGEIISL ARQLGDRSIE
     LHTGTWNKVA ARCWEVRGKT LGIIGYGHIG SQLSVLAEAM GLHVLYYDIV TIMALGTARQ
     VSTLDELLNK SDFVTLHVPA TPETEKMLSA PQFAAMKDGA YVINASRGTV VDIPSLIQAV
     KANKIAGAAL DVYPHEPAKN GEGSFNDELN SWTSELVSLP NIILTPHIGG STEEAQSSIG
     IEVATALSKY INEGNSVGSV NFPEVSLKSL DYDQENTVRV LYIHRNVPGV LKTVNDILSD
     HNIEKQFSDS HGEIAYLMAD ISSVNQSEIK DIYEKLNQTS AKVSIRLLY
//
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