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 04-NOV-2008, entry version 47. DE RecName: Full=Leucoanthocyanidin dioxygenase; DE Short=LDOX; DE Short=Leucocyanidin oxygenase; DE EC=1.14.11.19; DE AltName: Full=Leucoanthocyanidin hydroxylase; GN Name=ANT17; OS Petunia hybrida (Petunia). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 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 MEDLINE=93363921; 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- RT forming enzyme."; RL Plant Mol. Biol. 22:893-897(1993). 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 -!- TISSUE SPECIFICITY: Predominantly expressed in corollas and at CC lower levels in anthers. CC -!- INDUCTION: By gibberellic acid (GA). 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; X70786; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; S36233; S36233. DR HSSP; Q96323; 1GP5. DR SMR; P51092; 11-353. 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; 2OG-FeII_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 1 430 Leucoanthocyanidin dioxygenase. FT /FTId=PRO_0000067303. FT METAL 236 236 Iron (By similarity). FT METAL 238 238 Iron (By similarity). FT METAL 292 292 Iron (By similarity). 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 //