LDOX_MAIZE
ID LDOX_MAIZE Reviewed; 395 AA.
AC P41213;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=A2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2170105; DOI=10.1002/j.1460-2075.1990.tb07501.x;
RA Menssen A., Hoehmann S., Martin W., Schnable P.S., Peterson P.S.,
RA Saedler H., Gierl A.;
RT "The En/Spm transposable element of Zea mays contains splice sites at the
RT termini generating a novel intron from a dSpm element in the A2 gene.";
RL EMBO J. 9:3051-3057(1990).
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; X55314; CAA39022.1; -; mRNA.
DR PIR; S12043; S12043.
DR RefSeq; NP_001106074.1; NM_001112604.1.
DR AlphaFoldDB; P41213; -.
DR SMR; P41213; -.
DR STRING; 4577.GRMZM2G345717_P01; -.
DR PaxDb; P41213; -.
DR PRIDE; P41213; -.
DR GeneID; 100127010; -.
DR KEGG; zma:100127010; -.
DR MaizeGDB; 99960; -.
DR eggNOG; KOG0143; Eukaryota.
DR OMA; REDRISM; -.
DR OrthoDB; 830141at2759; -.
DR UniPathway; UPA00009; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; P41213; baseline and differential.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
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:0010023; P:proanthocyanidin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0009753; P:response to jasmonic acid; IEA:EnsemblPlants.
DR GO; GO:0009611; P:response to wounding; IEA:EnsemblPlants.
DR GO; GO:0007033; P:vacuole organization; IEA:EnsemblPlants.
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 Reference proteome; Vitamin C.
FT CHAIN 1..395
FT /note="Leucoanthocyanidin dioxygenase"
FT /id="PRO_0000067300"
FT DOMAIN 230..329
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 360..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 310
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 395 AA; 43356 MW; C43B91DDC6FC7F1A CRC64;
MESSPLLQLP AARVEALSLS GLSAIPPEYV RPADERAGLG DAFDLARTHA NDHTAPRIPV
VDISPFLDSS SQQQQRDECV EAVRAAAADW GVMHIAGHGI PAELMDRLRA AGTAFFALPV
QDKEAYANDP AAGRLQGYGS RLATNTCGQR EWEDYLFHLV HPDGLADHAL WPAYPPDYIA
ATRDFGRRTR DLASTLLAIL SMGLLGTDRG DALEKALTTT TTRTAADDDL LLQLKINYYP
RCPQPELAVG VEAHTDVSAL SFILHNGVPG LQVLHGARWV TARHEPGTII VHVGDALEIL
SNGRYTSVLH RGLVNREAVR ISWVVFCEPP PDSVLLHPLP ELVTEGHPAR FTPRTFKQHL
DRKLFKKKQQ HKAKAEEEDG GNGDHHRHEP PPQTN
