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Database: UniProt
Entry: P43885
LinkDB: P43885
Original site: P43885 
ID   SERA_HAEIN              Reviewed;         410 AA.
AC   P43885;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   05-DEC-2018, entry version 133.
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=HI_0465;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; L42023; AAC22124.1; -; Genomic_DNA.
DR   PIR; C64070; C64070.
DR   RefSeq; NP_438626.1; NC_000907.1.
DR   RefSeq; WP_005693698.1; NC_000907.1.
DR   ProteinModelPortal; P43885; -.
DR   SMR; P43885; -.
DR   STRING; 71421.HI0465; -.
DR   PRIDE; P43885; -.
DR   EnsemblBacteria; AAC22124; AAC22124; HI_0465.
DR   GeneID; 950636; -.
DR   KEGG; hin:HI0465; -.
DR   PATRIC; fig|71421.8.peg.485; -.
DR   eggNOG; ENOG4108JQ1; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   KO; K00058; -.
DR   OMA; YHAIGIR; -.
DR   PhylomeDB; P43885; -.
DR   BioCyc; HINF71421:G1GJ1-481-MONOMER; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009070; P:serine family amino acid biosynthetic process; IBA:GO_Central.
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; IPR010771; IgaA.
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   ProDom; PD147088; IgaA; 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   CHAIN         1    410       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076002.
FT   DOMAIN      341    410       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     162    163       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     239    241       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     293    296       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    241    241       {ECO:0000250}.
FT   ACT_SITE    270    270       {ECO:0000250}.
FT   ACT_SITE    293    293       Proton donor. {ECO:0000250}.
FT   BINDING     182    182       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     265    265       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
SQ   SEQUENCE   410 AA;  44665 MW;  C5A75E6D685B7C80 CRC64;
     MTNKVSLDKS KIKFVLFEGV HQSALDTLHA AGYTNIDYYK KALDGDELKE AIKDVHFIGL
     RSRTHLTAEM IEAAPKLIAV GCFCIGTNQV DLNAAKARGI PVFNAPFSNT RSVAELVLGE
     ILLLMRNVPQ ANAEVHRGVW NKSATGSHEV RGKKLGIIGY GHIGSQLSII AESLGMDVYF
     YDIENKLPLG NAKQVRSLEE LLSSCDVVSL HVPELPSTKN LMNVARIAQL KQGAILINAA
     RGTVVDIDAL AQALKDGKLQ GAAIDVFPVE PASINEEFIS PLREFDNVIL TPHIGGSTAE
     AQENIGFEVA GKFVKYSDNG STLSSVNFPE VSLPEHEGTK RLLHIHENRP GILNKLNQIF
     VEANLNIAAQ YLQTDPKIGY VVVDVETNDA SPLLTKLKEI DGTIRARVLY
//
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