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 05-MAY-2009, entry version 46. DE RecName: Full=Leucoanthocyanidin dioxygenase; DE Short=LDOX; DE Short=Leucocyanidin oxygenase; DE EC=1.14.11.19; DE AltName: Full=Leucoanthocyanidin hydroxylase; DE AltName: Full=Anthocyanidin synthase; GN Name=ANS; OS Malus domestica (Apple) (Malus sylvestris). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Rosales; Rosaceae; Maloideae; Malus. OX NCBI_TaxID=3750; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX MEDLINE=94294547; 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 RT 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 RT from 'Fuji apple'."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Oxidation of leucoanthocyanidins into anthocyanidins. CC -!- CATALYTIC ACTIVITY: Leucocyanidin + 2-oxoglutarate + O(2) = cis- CC and trans-dihydroquercetins + succinate + CO(2) + H(2)O. CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity). CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X71360; CAA50498.1; -; mRNA. DR EMBL; AF117269; AAD26205.1; -; mRNA. DR PIR; S33144; S33144. DR HSSP; Q96323; 1GP6. DR SMR; P51091; 10-354. DR BRENDA; 1.14.11.19; 66979. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0050589; F:leucocyanidin oxygenase activity; IEA:EC. DR GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW. DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. PE 2: Evidence at transcript level; KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; KW Oxidoreductase; Vitamin C. FT CHAIN 1 357 Leucoanthocyanidin dioxygenase. FT /FTId=PRO_0000067301. FT METAL 236 236 Iron (By similarity). FT METAL 238 238 Iron (By similarity). FT METAL 292 292 Iron (By similarity). 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 //