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Database: UniProt
Entry: P0A9T1
LinkDB: P0A9T1
Original site: P0A9T1 
ID   SERA_ECOL6              Reviewed;         410 AA.
AC   P0A9T1; P08328; Q47633;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-SEP-2014, entry version 70.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=PGDH;
DE            EC=1.1.1.95;
GN   Name=serA; OrderedLocusNames=c3494;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3-
CC       phosphonooxypyruvate + NADH.
CC   -!- CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate +
CC       NADH.
CC   -!- ENZYME REGULATION: In bacteria displays feedback inhibition by L-
CC       serine (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SUBUNIT: Homotetramer (By similarity).
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; AE014075; AAN81942.1; -; Genomic_DNA.
DR   RefSeq; NP_755369.1; NC_004431.1.
DR   ProteinModelPortal; P0A9T1; -.
DR   STRING; 199310.c3494; -.
DR   PRIDE; P0A9T1; -.
DR   EnsemblBacteria; AAN81942; AAN81942; c3494.
DR   GeneID; 1039390; -.
DR   KEGG; ecc:c3494; -.
DR   PATRIC; 18284808; VBIEscCol75197_3289.
DR   HOGENOM; HOG000136696; -.
DR   KO; K00058; -.
DR   OMA; KFVKYSD; -.
DR   OrthoDB; EOG6VXFC3; -.
DR   BioCyc; ECOL199310:C3494-MONOMER; -.
DR   SABIO-RK; P0A9T1; -.
DR   UniPathway; UPA00135; UER00196.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
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   Gene3D; 3.40.50.720; -; 2.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR029015; PGDH_2.
DR   PANTHER; PTHR10996:SF18; PTHR10996:SF18; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 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   Serine biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    410       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076001.
FT   DOMAIN      339    410       ACT.
FT   NP_BIND     161    162       NAD (By similarity).
FT   NP_BIND     238    240       NAD (By similarity).
FT   NP_BIND     292    295       NAD (By similarity).
FT   ACT_SITE    240    240       By similarity.
FT   ACT_SITE    269    269       By similarity.
FT   ACT_SITE    292    292       Proton donor (By similarity).
FT   BINDING     181    181       NAD (By similarity).
FT   BINDING     264    264       NAD (By similarity).
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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