ID   DHGY_CUCSA              Reviewed;         382 AA.
AC   P13443;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Glycerate dehydrogenase;
DE            Short=GDH;
DE            EC=1.1.1.29;
DE   AltName: Full=NADH-dependent hydroxypyruvate reductase;
DE            Short=HPR;
GN   Name=HPR-A;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Improved long green; TISSUE=Cotyledon;
RX   PubMed=2519111; DOI=10.1007/bf00016133;
RA   Greenler J.M., Sloan J.S., Schwartz B.W., Becker W.M.;
RT   "Isolation, characterization and sequence analysis of a full-length cDNA
RT   clone encoding NADH-dependent hydroxypyruvate reductase from cucumber.";
RL   Plant Mol. Biol. 13:139-150(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Wisconsin 2238G;
RX   PubMed=1912510; DOI=10.1007/bf00037078;
RA   Schwartz B.W., Sloan J.S., Becker W.M.;
RT   "Characterization of genes encoding hydroxypyruvate reductase in
RT   cucumber.";
RL   Plant Mol. Biol. 17:941-947(1991).
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   -!- PATHWAY: Photosynthesis; photorespiration; 3-phospho-D-glycerate from
CC       glycine: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- INDUCTION: The appearance of HPR in the cotyledons of cucumber
CC       seedlings is both developmentally and light-regulated possibly at the
CC       level of transcription.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; X14609; CAA32764.1; -; mRNA.
DR   EMBL; X58542; CAA41434.1; -; Genomic_DNA.
DR   PIR; S17733; DEKVG.
DR   RefSeq; NP_001267567.1; NM_001280638.1.
DR   AlphaFoldDB; P13443; -.
DR   SMR; P13443; -.
DR   STRING; 3659.XP_004144850.1; -.
DR   PRIDE; P13443; -.
DR   EnsemblPlants; KGN43256; KGN43256; Csa_7G012940.
DR   GeneID; 101209132; -.
DR   Gramene; KGN43256; KGN43256; Csa_7G012940.
DR   KEGG; csv:101209132; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   OMA; RMMVEGH; -.
DR   UniPathway; UPA00951; UER00916.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-UniPathway.
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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   2: Evidence at transcript level;
KW   Glycolate pathway; NAD; Oxidoreductase; Peroxisome; Photorespiration.
FT   CHAIN           1..382
FT                   /note="Glycerate dehydrogenase"
FT                   /id="PRO_0000075941"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        320
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..176
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         320..323
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  41706 MW;  4E326485ACD0E080 CRC64;
     MAKPVQIEVW NPNGKYRVVS TKPMPGTRWI NLLIEQDCRV EICTEKKTIL SVEDILALIG
     DKCDGVIGQL TEDWGEVLFS ALSRAGGKAF SNMAVGYNNV DVNAANKYGV AVGNTPGVLT
     ETTAELAASL SLAAARRIVE ADEFMRAGRY DGWLPNLFVG NLLKGQTVGV IGAGRIGSAY
     ARMMVEGFKM NLIYFDLYQS TRLEKFVTAY GEFLKANGEA PVTWRRASSM DEVLREADVI
     SLHPVLDKTT FHLVNKESLK AMKKDAILIN CSRGPVIDEA ALVDHLRDNP MFRVGLDVFE
     DEPYMKPGLA DMKNAIIVPH IASASKWTRE GMATLAALNV LGKIKGYPVW SDPNRVEPFL
     DENVSPPAAS PSIVNAKALG NA