DHGY_HYPME
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 03-AUG-2022, entry version 111.
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; Proteobacteria; 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}.
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DR PDB; 1GDH; X-ray; 2.40 A; A/B=3-322.
DR PDBsum; 1GDH; -.
DR AlphaFoldDB; P36234; -.
DR SMR; P36234; -.
DR BioCyc; MetaCyc:MON-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 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 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
