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 02-SEP-2026, entry version 163. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; 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 + NADH CC + H(+); 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 + NADH + CC H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22124.1; -; Genomic_DNA. DR PIR; C64070; C64070. DR AlphaFoldDB; P43885; -. DR SMR; P43885; -. DR STRING; 71421.HI_0465; -. 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 OrthoDB; 9805416at2; -. DR PhylomeDB; P43885; -. DR BioCyc; HINF71421:G1GJ1-481-MONOMER; -. DR UniPathway; UPA00135; UER00196. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0120568; F:(R)-2-hydroxyglutarate (NAD+) dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd04901; ACT_3PGDH; 1. DR CDD; cd12176; PGDH_3; 1. DR FunFam; 3.30.70.260:FF:000007; D-3-phosphoglycerate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000041; D-3-phosphoglycerate dehydrogenase; 1. DR Gene3D; 3.30.70.260; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR InterPro; IPR045865; ACT-like_dom_sf. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR054480; AHAS_small-like_ACT. DR InterPro; IPR050418; D-iso_2-hydroxyacid_DH_PdxB. 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 NCBIfam; NF008759; PRK11790.1; 1. DR PANTHER; PTHR43761:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE CATALYTIC DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR Pfam; PF22629; ACT_AHAS_ss; 1. DR SUPFAM; SSF55021; ACT-like; 1. DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 //