ID   LDOX_PERFR              Reviewed;         362 AA.
AC   O04274;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Leucoanthocyanidin dioxygenase;
DE            Short=LDOX;
DE            Short=Leucocyanidin oxygenase;
DE            EC=1.14.20.4 {ECO:0000269|PubMed:10074715};
DE   AltName: Full=Leucoanthocyanidin hydroxylase;
GN   Name=ANS;
OS   Perilla frutescens (Beefsteak mint) (Perilla ocymoides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX   NCBI_TaxID=48386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC   TISSUE=Leaf;
RX   PubMed=10074715; DOI=10.1046/j.1365-313x.1999.00365.x;
RA   Saito K., Kobayashi M., Gong Z., Tanaka Y., Yamazaki M.;
RT   "Direct evidence for anthocyanidin synthase as a 2-oxoglutarate-dependent
RT   oxygenase: molecular cloning and functional expression of cDNA from a red
RT   forma of Perilla frutescens.";
RL   Plant J. 17:181-189(1999).
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:0000269|PubMed:10074715};
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   -!- TISSUE SPECIFICITY: Expressed in red but not in green forma of
CC       P.frutescens. In red forma, it is predominantly expressed in stems and
CC       leaves, but not in roots. {ECO:0000269|PubMed:10074715}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB003779; BAA20143.1; -; mRNA.
DR   AlphaFoldDB; O04274; -.
DR   SMR; O04274; -.
DR   KEGG; ag:BAA20143; -.
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   GO; GO:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEA:UniProt.
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_0000067302"
FT   DOMAIN          214..313
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000255"
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;  40826 MW;  7A03B4E86F91E1EA CRC64;
     MVTSAMGPSP RVEELARSGL DTIPKDYVRP EEELKSIIGN ILAEEKSSEG PQLPTIDLEE
     MDSRDEEGRK KCHEELKKAA TDWGVMHLIN HGIPEELIDR VKAAGKEFFE LPVEEKEAYA
     NDQAAGNVQG YGSKLANNAS GQLEWEDYFF HCVYPEHKTD LSIWPTKPPD YIPATSEYAK
     QLRALATKIL SVLSIGLGLE KGRLEKEVGG AEDLIVQMKI NFYPKCPQPE LALGWEAHTD
     VSALTFILHN MVPGLQLFYE DKWVTAKCVP NSIIMHIGDT LEILSNGKYK SILHRGLVNK
     EKVRISWAVF CEPPKEKIVL QPLPETVSEV EPPRFPPRTF AQHLKHKLFR KTDGDLDEKP
     TY