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Database: UniProt
Entry: P0A9T3
LinkDB: P0A9T3
Original site: P0A9T3 
ID   SERA_SHIFL              Reviewed;         410 AA.
AC   P0A9T3; P08328; Q47633;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JAN-2019, entry version 104.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=PGDH;
DE            EC=1.1.1.95 {ECO:0000250|UniProtKB:P0A9T0};
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000250|UniProtKB:P0A9T0};
DE            EC=1.1.1.399 {ECO:0000250|UniProtKB:P0A9T0};
GN   Name=serA; OrderedLocusNames=SF2898, S3098;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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:P0A9T0}.
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         Evidence={ECO:0000250|UniProtKB:P0A9T0};
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:P0A9T0};
CC   -!- ACTIVITY REGULATION: In bacteria displays feedback inhibition by
CC       L-serine. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AE005674; AAN44382.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18204.1; -; Genomic_DNA.
DR   RefSeq; NP_708675.1; NC_004337.2.
DR   RefSeq; WP_001151604.1; NZ_UIQL01000025.1.
DR   ProteinModelPortal; P0A9T3; -.
DR   SMR; P0A9T3; -.
DR   EnsemblBacteria; AAN44382; AAN44382; SF2898.
DR   EnsemblBacteria; AAP18204; AAP18204; S3098.
DR   GeneID; 1025927; -.
DR   KEGG; sfl:SF2898; -.
DR   KEGG; sfx:S3098; -.
DR   PATRIC; fig|198214.7.peg.3447; -.
DR   eggNOG; ENOG4108JQ1; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136696; -.
DR   KO; K00058; -.
DR   OMA; YHAIGIR; -.
DR   OrthoDB; 1638924at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
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   Pfam; PF01842; ACT; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; NAD; Oxidoreductase;
KW   Reference proteome; Serine biosynthesis.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    410       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076006.
FT   DOMAIN      339    410       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     161    162       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     238    240       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     292    295       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    240    240       {ECO:0000250}.
FT   ACT_SITE    269    269       {ECO:0000250}.
FT   ACT_SITE    292    292       Proton donor. {ECO:0000250}.
FT   BINDING     181    181       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     264    264       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
SQ   SEQUENCE   410 AA;  44176 MW;  61EF5EFC304DF6F0 CRC64;
     MAKVSLEKDK IKFLLVEGVH QKALESLRAA GYTNIEFHKG ALDDEQLKES IRDAHFIGLR
     SRTHLTEDVI NAAEKLVAIG CFCIGTNQVD LDAAAKRGIP VFNAPFSNTR SVAELVIGEL
     LLLLRGVPEA NAKAHRGVWN KLAAGSFEAR GKKLGIIGYG HIGTQLGILA ESLGMYVYFY
     DIENKLPLGN ATQVQHLSDL LNMSDVVSLH VPENPSTKNM MGAKEISLMK PGSLLINASR
     GTVVDIPALC DALASKHLAG AAIDVFPTEP ATNSDPFTSP LCEFDNVLLT PHIGGSTQEA
     QENIGLEVAG KLIKYSDNGS TLSAVNFPEV SLPLHGGRRL MHIHENRPGV LTALNKIFAE
     QGVNIAAQYL QTSAQMGYVV IDIEADEDVA EKALQAMKAI PGTIRARLLY
//
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