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 01-MAY-2013, entry version 63.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AE014075; AAN81942.1; -; Genomic_DNA.
DR RefSeq; NP_755369.1; NC_004431.1.
DR ProteinModelPortal; P0A9T1; -.
DR SMR; P0A9T1; 5-410.
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; RGGWLKS; -.
DR ProtClustDB; PRK11790; -.
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: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_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 Pfam; PF01842; 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 338 409 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
//
