ID   GALUR_FRAAN             Reviewed;         319 AA.
AC   O49133;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=D-galacturonate reductase;
DE            Short=FaGalUR;
DE            EC=1.1.1.365;
DE   AltName: Full=Aldo-keto reductase 2;
GN   Name=GALUR; Synonyms=AKR2;
OS   Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC   Fragaria.
OX   NCBI_TaxID=3747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Chandler;
RX   PubMed=12524550; DOI=10.1038/nbt777;
RA   Agius F., Gonzalez-Lamothe R., Caballero J.L., Munoz-Blanco J.,
RA   Botella M.A., Valpuesta V.;
RT   "Engineering increased vitamin C levels in plants by overexpression of a D-
RT   galacturonic acid reductase.";
RL   Nat. Biotechnol. 21:177-181(2003).
RN   [2]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=21561953; DOI=10.1093/jxb/err122;
RA   Cruz-Rus E., Amaya I., Sanchez-Sevilla J.F., Botella M.A., Valpuesta V.;
RT   "Regulation of L-ascorbic acid content in strawberry fruits.";
RL   J. Exp. Bot. 62:4191-4201(2011).
CC   -!- FUNCTION: Involved in ascorbic acid (vitamin C) biosynthesis.
CC       {ECO:0000269|PubMed:12524550, ECO:0000269|PubMed:21561953}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-galactonate + NADP(+) = aldehydo-D-galacturonate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:26345, ChEBI:CHEBI:12952, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:53071, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.365; Evidence={ECO:0000269|PubMed:12524550};
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in the receptacle tissue of
CC       the fruit. {ECO:0000269|PubMed:12524550}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during ripening, with a highest
CC       expression in fully mature red fruit. {ECO:0000269|PubMed:12524550,
CC       ECO:0000269|PubMed:21561953}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AF039182; AAB97005.1; -; mRNA.
DR   AlphaFoldDB; O49133; -.
DR   SMR; O49133; -.
DR   KEGG; ag:AAB97005; -.
DR   BioCyc; MetaCyc:MON-21181; -.
DR   BRENDA; 1.1.1.365; 2320.
DR   UniPathway; UPA00132; -.
DR   GO; GO:0102098; F:D-galacturonate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd19124; AKR_AKR4A_4B; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044497; AKR4A/B.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   1: Evidence at protein level;
KW   Ascorbate biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..319
FT                   /note="D-galacturonate reductase"
FT                   /id="PRO_0000425862"
FT   ACT_SITE        58
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..275
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   319 AA;  35669 MW;  ABE8523B6E383349 CRC64;
     MAKVPSVTLS SCGDDIQTMP VIGMGTSSYP RADPETAKAA ILEAIRAGYR HFDTAAAYGS
     EKDLGEAIAE ALRLQLIKSR DELFITTKLW ASFAEKDLVL PSIKASLSNL QVEYIDMYII
     HWPFKLGKEV RTMPVERDLV QPLDIKSVWE AMEECKKLGL ARGIGVSNFT SSMLEELLSF
     AEIPPAVNQL EMNPAWQLKK LRDFCKAKGI HVTAYSPLGA ARTKWGDDRV LGSDIIEEIA
     QAKGKSTAQI SLRWVYEQGV SIVTKSYNKE RMRQNLDIFD FCLTEEELEK MSHLPQRKGV
     TFASILGPHD IVLEVDEEL