ID DHGY_HYPME Reviewed; 322 AA. AC P36234; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 116. DE RecName: Full=Glycerate dehydrogenase; DE Short=GDH; DE EC=1.1.1.29; DE AltName: Full=Glyoxylate reductase; DE AltName: Full=Hydroxypyruvate dehydrogenase; DE AltName: Full=NADH-dependent hydroxypyruvate reductase; DE Short=HPR; OS Hyphomicrobium methylovorum. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=84; RN [1] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=8120891; DOI=10.1016/0022-2836(94)90016-7; RA Goldberg J.D., Yoshida T., Brick P.; RT "Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4-A RT resolution."; RL J. Mol. Biol. 236:1123-1140(1994). RN [2] RP CHARACTERIZATION. RC STRAIN=KM146 / GM2; RX PubMed=2114287; DOI=10.1111/j.1432-1033.1990.tb15573.x; RA Izumi Y., Yoshida T., Kanzaki H., Toki S., Miyazaki S.S., Yamada H.; RT "Purification and characterization of hydroxypyruvate reductase from a RT serine-producing methylotroph, Hyphomicrobium methylovorum GM2."; RL Eur. J. Biochem. 190:279-284(1990). CC -!- FUNCTION: Active on hydroxypyruvate and glyoxylate. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH; CC Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659, CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.29; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.8.; CC Temperature dependence: CC Optimum temperature is 45 degrees Celsius.; CC -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine CC pathway. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: By methanol. 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 PDB; 1GDH; X-ray; 2.40 A; A/B=3-322. DR PDBsum; 1GDH; -. DR AlphaFoldDB; P36234; -. DR SMR; P36234; -. DR BioCyc; MetaCyc:MONOMER-4245; -. DR UniPathway; UPA00927; -. DR EvolutionaryTrace; P36234; -. DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR CDD; cd05301; GDH; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. 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 PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1. DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 1: Evidence at protein level; KW 3D-structure; NAD; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..322 FT /note="Glycerate dehydrogenase" FT /id="PRO_0000075942" FT ACT_SITE 241 FT ACT_SITE 270 FT ACT_SITE 288 FT /note="Proton donor" FT BINDING 158..159 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 178 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 239..241 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 265 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 288..291 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 14..21 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 37..44 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 60..65 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 72..78 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 85..90 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 103..118 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 121..129 FT /evidence="ECO:0007829|PDB:1GDH" FT TURN 138..141 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 158..168 FT /evidence="ECO:0007829|PDB:1GDH" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 184..189 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 198..204 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 206..210 FT /evidence="ECO:0007829|PDB:1GDH" FT TURN 216..220 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 247..255 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 258..265 FT /evidence="ECO:0007829|PDB:1GDH" FT TURN 268..271 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:1GDH" FT HELIX 294..312 FT /evidence="ECO:0007829|PDB:1GDH" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:1GDH" SQ SEQUENCE 322 AA; 35115 MW; CA5E39C1617AF2FE CRC64; MSKKKILITW PLPEAAMARA RESYDVIAHG DDPKITIDEM IETAKSVDAL LITLNEKCRK EVIDRIPENI KCISTYSIGF DHIDLDACKA RGIKVGNAPH GVTVATAEIA MLLLLGSARR AGEGEKMIRT RSWPGWEPLE LVGEKLDNKT LGIYGFGSIG QALAKRAQGF DMDIDYFDTH RASSSDEASY QATFHDSLDS LLSVSQFFSL NAPSTPETRY FFNKATIKSL PQGAIVVNTA RGDLVDNELV VAALEAGRLA YAGFDVFAGE PNINEGYYDL PNTFLFPHIG SAATQAREDM AHQANDLIDA LFGGADMSYA LA //