ID   LDOX_MALDO              Reviewed;         357 AA.
AC   P51091;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Leucoanthocyanidin dioxygenase;
DE            Short=LDOX;
DE            Short=Leucocyanidin oxygenase;
DE            EC=1.14.20.4 {ECO:0000250|UniProtKB:Q96323};
DE   AltName: Full=Anthocyanidin synthase;
DE   AltName: Full=Leucoanthocyanidin hydroxylase;
GN   Name=ANS;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8022923; DOI=10.1104/pp.103.3.1015;
RA   Davies K.M.;
RT   "A Malus cDNA with homology to the Antirrhinum Candica and Zea A2 genes.";
RL   Plant Physiol. 103:1015-1015(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Fuji; TISSUE=Peelings;
RA   Lee J.-R., Hong S.-T., Yoo Y.G., Kim S.-R.;
RT   "Molecular cloning and expression of anthocyanin biosynthesis genes from
RT   'Fuji apple'.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Oxidation of leucoanthocyanidins into anthocyanidins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + a (2R,3S,4S)-leucoanthocyanidin + O2 = a 4-H-
CC         anthocyanidin with a 3-hydroxy group + CO2 + 2 H2O + succinate;
CC         Xref=Rhea:RHEA:54432, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:138176, ChEBI:CHEBI:138177; EC=1.14.20.4;
CC         Evidence={ECO:0000250|UniProtKB:Q96323};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC       Note=Binds 1 ascorbate molecule per subunit. {ECO:0000250};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; X71360; CAA50498.1; -; mRNA.
DR   EMBL; AF117269; AAD26205.1; -; mRNA.
DR   PIR; S33144; S33144.
DR   AlphaFoldDB; P51091; -.
DR   SMR; P51091; -.
DR   STRING; 3750.XP_008356542.1; -.
DR   EnsemblPlants; mRNA:MD06G0056100; mRNA:MD06G0056100; MD06G0056100.
DR   Gramene; mRNA:MD06G0056100; mRNA:MD06G0056100; MD06G0056100.
DR   BRENDA; 1.14.20.4; 3164.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0050589; F:leucocyanidin oxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW   Vitamin C.
FT   CHAIN           1..357
FT                   /note="Leucoanthocyanidin dioxygenase"
FT                   /id="PRO_0000067301"
FT   DOMAIN          212..311
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         236
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         292
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   357 AA;  40332 MW;  FA5D97C25267B3E6 CRC64;
     MVSSDSVNSR VETLAGSGIS TIPKEYIRPK DELVNIGDIF EQEKNNEGPQ VPTIDLKEIE
     SDNEKVRAKC REKLKKAAVD WGVMHLVNHG ISDELMDKVR KAGKAFFDLP IEQKEKYAND
     QASGKIQGYG SKLANNASGQ LEWEDYFFHC VYPEDKRDLS IWPQTPADYI EATAEYAKQL
     RELATKVLKV LSLGLGLDEG RLEKEVGGLE ELLLQMKINY YPKCPQPELA LGVEAHTDVS
     ALTFILHNMV PGLQLFYEGK WVTAKCVPNS IVMHIGDTLE ILSNGKYKSI LHRGMVNKEK
     VRISWAVFCE PPKEKIILKP LPETVSEDEP AMFPPRTFAE HIQHKLFRKS QEALLPK