GRDH_DAUCA
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 03-AUG-2022, entry version 49.
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 PRIDE; Q5KTS5; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 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