ID F0RHP6_CELLC Unreviewed; 630 AA. AC F0RHP6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582}; DE EC=1.1.1.399 {ECO:0000256|ARBA:ARBA00013001}; DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143}; DE AltName: Full=2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00030455}; GN OrderedLocusNames=Celly_0320 {ECO:0000313|EMBL:ADY28155.1}; OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / OS NCIMB 1423 / VKM B-1433 / Cy l20). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY28155.1, ECO:0000313|Proteomes:UP000007487}; RN [1] {ECO:0000313|EMBL:ADY28155.1, ECO:0000313|Proteomes:UP000007487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 / RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487}; RX PubMed=21677859; DOI=10.4056/sigs.1774329; RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C., RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Ivanova N.; RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21)."; RL Stand. Genomic Sci. 4:221-232(2011). 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:0000256|ARBA:ARBA00003800}. 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:0000256|ARBA:ARBA00001878}; 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:0000256|ARBA:ARBA00000646}; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216}. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}. 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; CP002534; ADY28155.1; -; Genomic_DNA. DR RefSeq; WP_013619903.1; NC_015167.1. DR AlphaFoldDB; F0RHP6; -. DR STRING; 867900.Celly_0320; -. DR KEGG; cly:Celly_0320; -. DR eggNOG; COG0111; Bacteria. DR eggNOG; COG0560; Bacteria. DR HOGENOM; CLU_029190_0_0_10; -. DR OrthoDB; 9777288at2; -. DR UniPathway; UPA00135; UER00196. DR Proteomes; UP000007487; Chromosome. 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 CDD; cd04901; ACT_3PGDH; 1. DR CDD; cd12176; PGDH_3; 1. DR Gene3D; 3.30.70.260; -; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; 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; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01488; HAD-SF-IB; 1. DR PANTHER; PTHR43761:SF1; 2-HACID_DH 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; PF12710; HAD; 1. DR SUPFAM; SSF55021; ACT-like; 1. DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1. DR SUPFAM; SSF56784; HAD-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; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000007487}. FT DOMAIN 561..630 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" SQ SEQUENCE 630 AA; 70491 MW; 1BB0D7EAFEDE8046 CRC64; MVDQGRKYVF DFDSTLTRVE ALDVLAEITL QGNANKDEII KEIQEITNLG IDGDISFTES LEKRIKLLNA HKSHLTQLVA ELRDKISKSI ETNKEFFHNY SDDIYVISCG FKEFIDPIVE EYNIPSSKVY ANTFKFDEDG NIIGFDEANV LASHNGKIEC LKNLDLDGEV QVIGDGYSDY VMREAGIADK FFAYTENVSR DKATTNADHV TPNMDEFLFV NDLPRKISYP KNRIKILLLE NVHPAAFHNL SEDGFSVELV KHSLPEEELI EKLKGVHVLG IRSKTQVTKK VLEAADKLLV VGAFCIGTTQ IDLESAKKRG VVVFNAPYSN TRSVVELAIG EIITLMRNVF PRSQEIHSGQ WNKTAVNSRE VRGKNLGIVG YGNIGKQLSV LAEAIGMRVY YYDVNDQLAL GNATKCSTLE NLLNVSDVVT LHIDDNKANK NFIGEREIKQ MKNGAMLINL SRGFVVDIQA LVAALKSGKI GGAAVDVYPE EPRSNGEFFT ELQGLENVIL TPHVGGSTEE AQRDIADFVP NKIMEYINSG NTVDAVNFPS IRLPRQTNAH RFLHIHKNVP GIMAKINKVL AEYEMNINGQ YLSTDSEVGY VITDLDKKYN KEVIKALKKV ENTIKFRVLY //