SERA_HAEIN
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 03-AUG-2022, entry version 147.
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., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., 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-glycerate
CC to 3-phosphonooxypyruvate, the first step of the phosphorylated L-
CC serine biosynthesis pathway. Also catalyzes the reversible oxidation of
CC 2-hydroxyglutarate to 2-oxoglutarate. {ECO:0000250|UniProtKB:P0A9T0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, 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, ChEBI:CHEBI:15801,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.399; Evidence={ECO:0000250|UniProtKB:P0A9T0};
CC -!- ACTIVITY REGULATION: In bacteria displays feedback inhibition by L-
CC serine. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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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 AlphaFoldDB; P43885; -.
DR SMR; P43885; -.
DR STRING; 71421.HI_0465; -.
DR PRIDE; P43885; -.
DR EnsemblBacteria; AAC22124; AAC22124; HI_0465.
DR KEGG; hin:HI_0465; -.
DR PATRIC; fig|71421.8.peg.485; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_9_2_6; -.
DR OMA; YGNIGTQ; -.
DR PhylomeDB; P43885; -.
DR BioCyc; HINF71421:G1GJ1-481-MON; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
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; IPR045865; ACT-like_dom_sf.
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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF55021; SSF55021; 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; NAD; Oxidoreductase; Reference proteome;
KW Serine biosynthesis.
FT CHAIN 1..410
FT /note="D-3-phosphoglycerate dehydrogenase"
FT /id="PRO_0000076002"
FT DOMAIN 341..410
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT ACT_SITE 241
FT /evidence="ECO:0000250"
FT ACT_SITE 270
FT /evidence="ECO:0000250"
FT ACT_SITE 293
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 162..163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 239..241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 293..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="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
