LDOX_PETHY
ID LDOX_PETHY Reviewed; 430 AA.
AC P51092;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
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;
GN Name=ANT17;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Violet 26; TISSUE=Corolla;
RX PubMed=8358035; DOI=10.1007/bf00027374;
RA Weiss D., van der Luit A.H., Kroon J.T.M., Mol J.N.M., Kooter J.M.;
RT "The petunia homologue of the Antirrhinum majus candi and Zea mays A2
RT flavonoid genes; homology to flavanone 3-hydroxylase and ethylene-forming
RT enzyme.";
RL Plant Mol. Biol. 22:893-897(1993).
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 -!- TISSUE SPECIFICITY: Predominantly expressed in corollas and at lower
CC levels in anthers.
CC -!- INDUCTION: By gibberellic acid (GA).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; X70786; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S36233; S36233.
DR AlphaFoldDB; P51092; -.
DR SMR; P51092; -.
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..430
FT /note="Leucoanthocyanidin dioxygenase"
FT /id="PRO_0000067303"
FT DOMAIN 212..311
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 376..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 430 AA; 48433 MW; 72AB3DA2ACA7D22C CRC64;
MVNAVVTTPS RVESLAKSGI QAIPKEYVRP QEELNGIGNI FEEEKKDEGP QVPTIDLKEI
DSEDKEIREK CHQLKKAAME WGVMHLVNHG ISDELINRVK VAGETFFDQP VEEKEKYAND
QANGNVQGYG SKLANSACGQ LEWEDYFFHC AFPEDKRDLS IWPKNPTDYT PATSEYAKQI
RALATKILTV LSIGLGLEEG RLEKEVGGME DLLLQMKINY YPKCPQPELA LGVEAHTDVS
ALTFILHNMV PGLQLFYEGQ WVTAKCVPNS IIMHIGDTIE ILSNGKYKSI LHRGVVNKEK
VRFSWAIFCE PPKEKIILKP LPETVTEAEP PRFPPRTFAQ HMAHKLFRKD DKDAAVEHKV
FNEDELDTAA EHKVLKKDNQ DAVAENKDIK EDEQCGPAEH KDIKEDGQGA AAENKVFKEN
NQDVAAEESK
