ID   LDOX_VITVI              Reviewed;         362 AA.
AC   P51093;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Leucoanthocyanidin hydroxylase;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Lambrusco Foglia Frastagliata;
RX   PubMed=8193299; DOI=10.1007/bf00029856;
RA   Sparvoli F., Martin C., Scienza A., Gavazzi G., Tonelli C.;
RT   "Cloning and molecular analysis of structural genes involved in flavonoid
RT   and stilbene biosynthesis in grape (Vitis vinifera L.).";
RL   Plant Mol. Biol. 24:743-755(1994).
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   -!- INDUCTION: By light.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; X75966; CAA53580.1; -; mRNA.
DR   AlphaFoldDB; P51093; -.
DR   SMR; P51093; -.
DR   STRING; 29760.VIT_02s0025g04720.t01; -.
DR   PRIDE; P51093; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   UniPathway; UPA00009; -.
DR   ExpressionAtlas; P51093; baseline and differential.
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..362
FT                   /note="Leucoanthocyanidin dioxygenase"
FT                   /id="PRO_0000067304"
FT   DOMAIN          211..313
FT                   /note="Fe2OG dioxygenase"
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         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         294
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   362 AA;  41036 MW;  D3D0686C386A9315 CRC64;
     MVTSVAPRVE SLSSSGIQSI PKEYIRPQEE LTSIGNVFEE EKKDEGPQVP TIDLKDIESE
     DEVVRREIRE RCREELKKAA MEWGVMHLVN HGISDDLINR VKVAGETFFN LPMEEKEKYA
     NDQASGKIAG YGSKLANNAS GQLEWEDYFF HLIFPEDKRD MTIWPKTPSD YVPATCEYSV
     KLRSLATKIL SVLSLGLGLE EGRLEKEVGG MEELLLQKKI NYYPKCPQPE LALGVEAHTD
     VSALTFILHN MVPGLQLFYE GKWVTAKCVP NSIIMHIGDT IEILSNGKYK SILHRGLVNK
     EKVRISWAVF CEPPKEKIIL KAHCQRRCLR LSHHSSHLAP FPNIFSTSSS GRPRRLYSPN
     EL