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 05-MAY-2009, entry version 43. 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=ANS; OS Perilla frutescens (Beefsteak plant) (Chinese basil). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; OC Perilla. OX NCBI_TaxID=48386; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY. RC TISSUE=Leaf; RX MEDLINE=99174284; PubMed=10074715; RX 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- RT dependent oxygenase: molecular cloning and functional expression of RT cDNA from a red forma of Perilla frutescens."; RL Plant J. 17:181-189(1999). 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: Expressed in red but not in green forma of CC P.frutescens. In red forma, it is predominantly expressed in stems CC and leaves, but not in roots. 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; AB003779; BAA20143.1; -; mRNA. DR HSSP; Q96323; 1GP5. DR SMR; O04274; 11-356. DR BRENDA; 1.14.11.19; 142935. 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 1 362 Leucoanthocyanidin dioxygenase. FT /FTId=PRO_0000067302. FT ACT_SITE 304 304 Potential. FT METAL 238 238 Iron (By similarity). FT METAL 240 240 Iron (By similarity). FT METAL 294 294 Iron (By similarity). 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 //