ID   GRDH_DAUCA              Reviewed;         291 AA.
AC   Q5KTS5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Glucose and ribitol dehydrogenase;
DE            EC=1.1.1.-;
DE   AltName: Full=Carrot ABA-induced in somatic embryos 5 protein;
GN   Name=CAISE5;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=cv. US-Harumakigosun; TISSUE=Somatic embryo;
RA   Shiota H., Yang G., Shen S., Eun C.-H., Watabe K., Tanaka I., Kamada H.;
RT   "Isolation and characterization of six abscisic acid-inducible genes from
RT   carrot somatic embryos.";
RL   Plant Biotechnol. 21:309-314(2004).
CC   -!- FUNCTION: May act as a short alcohol-polyol-sugar dehydrogenase
CC       possibly related to carbohydrate metabolism and the acquisition of
CC       desiccation tolerance. May also be involved in signal transduction.
CC   -!- TISSUE SPECIFICITY: Expressed in embryogenic cells, somatic embryos and
CC       seeds in the later stages of development, but not in non-embryogenic
CC       cells and mature leaves. {ECO:0000269|Ref.1}.
CC   -!- DEVELOPMENTAL STAGE: Increased expression during seed maturation (after
CC       29 days after fertilization). {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: By abscisic acid. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB105043; BAD86648.1; -; mRNA.
DR   AlphaFoldDB; Q5KTS5; -.
DR   SMR; Q5KTS5; -.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   CDD; cd05355; SDR_c1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR48107:SF16; NADPH-DEPENDENT ALDEHYDE REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48107; NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase.
FT   CHAIN           1..291
FT                   /note="Glucose and ribitol dehydrogenase"
FT                   /id="PRO_0000239259"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         45..69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  31501 MW;  68F776A30091CC71 CRC64;
     MASGGQFPPQ KQESQPGKEH LMDPSPQHAS PHYKPANKLQ GKVALVTGGD SGIGRSVCYH
     FALEGATVAF TFVKGHEDKD ANETLELLRK AKSSDAKDPI AIAADLGFDD NCKKVVDQVV
     NAFGSIDVLV NNAAEQYKAS TVEDIDEERL ERVFRTNIFA YFFMARHALK HMREGSTIIN
     TTSINAYKGN AKLLDYTATK GAIVAFTRGL SLQLISKGIR VNGVAPGPVW TPLIPSSFDE
     EEVKQFGSEV PMKRAGQPYE IATAYVFLAS CDSSYYSGQV LHPNGGAIVN G
//