ID   ANR_GINBI               Reviewed;         342 AA.
AC   Q5XLY0;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Putative anthocyanidin reductase {ECO:0000303|PubMed:16399014};
DE            Short=GbANR {ECO:0000303|PubMed:16399014};
DE            EC=1.3.1.- {ECO:0000250|UniProtKB:Q5FB34};
OS   Ginkgo biloba (Ginkgo) (Maidenhair tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Ginkgoidae; Ginkgoales; Ginkgoaceae; Ginkgo.
OX   NCBI_TaxID=3311 {ECO:0000312|EMBL:AAU95082.1};
RN   [1] {ECO:0000312|EMBL:AAU95082.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16399014; DOI=10.1016/j.jplph.2005.06.012;
RA   Shen G.A., Pang Y., Wu W., Liu X., Zhao L., Sun X., Tang K.;
RT   "Isolation and characterization of a putative anthocyanidin reductase gene
RT   from Ginkgo biloba.";
RL   J. Plant Physiol. 163:224-227(2006).
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC       {ECO:0000250|UniProtKB:Q5FB34}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in leaves and weakly in stems. Not
CC       expressed in roots. {ECO:0000269|PubMed:16399014}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR   EMBL; AY750963; AAU95082.1; -; mRNA.
DR   AlphaFoldDB; Q5XLY0; -.
DR   SMR; Q5XLY0; -.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Flavonoid biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..342
FT                   /note="Putative anthocyanidin reductase"
FT                   /id="PRO_0000439090"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12068"
FT   BINDING         44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P51110"
FT   BINDING         51
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P51110"
FT   BINDING         71..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P51110"
FT   BINDING         91..93
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P51110"
FT   BINDING         172
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   BINDING         176
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P51110"
FT   BINDING         199..202
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P51110"
FT   BINDING         214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P51110"
SQ   SEQUENCE   342 AA;  37130 MW;  1BA18FA2D4EB10F8 CRC64;
     MAPQAYPTAG QTTTVCVTGA AGFMASWLVK RLLEKGYIVH ATVRDPENKA KVSHLLNLPG
     ATDRLKLFRA ELCEDGSFDA AVAGCNGVFH VATPTEFMPK DPENDLIKPA IEGTLNVLKS
     CTKVDSIKRV VVTSSAATVS INNSSEQNQY IDESCWTDVN FLTSQKPPGW AYPVSKTLAE
     QAALKYAEEH SLDVVTVIPV LVVGPAVTPT VPSSVELALS LITGDEFKMG ALKGMQFVSG
     SISLVHIDDV CSAQIFLMEK PSAQGRYICF PVNTGIPQLA EFLSKRYPQY KVPTKFDDVP
     ATPKLTISSQ KLLDCGFSFK YGIEDIYDQA IEYMKTKGLL TC