C75A4_GENTR
ID C75A4_GENTR Reviewed; 516 AA.
AC Q96581;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Flavonoid 3',5'-hydroxylase;
DE Short=F3'5'H;
DE EC=1.14.14.81 {ECO:0000250|UniProtKB:P48418};
DE AltName: Full=Cytochrome P450 75A4;
GN Name=CYP75A4;
OS Gentiana triflora (Clustered gentian).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Gentianaceae; Gentianeae; Gentianinae;
OC Gentiana.
OX NCBI_TaxID=55190;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Petal;
RX PubMed=8819318; DOI=10.1093/oxfordjournals.pcp.a029004;
RA Tanaka Y., Yonekura K., Fukuchi-Mizutani M., Fukui Y., Fujiwara H.,
RA Ashikari T., Kusumi T.;
RT "Molecular and biochemical characterization of three anthocyanin synthetic
RT enzymes from Gentiana triflora.";
RL Plant Cell Physiol. 37:711-716(1996).
CC -!- FUNCTION: Catalyzes the 3'5'-hydroxylation of naringenin and
CC eriodictyol to form 5,7,3,'4',5'-pentahydroxyflavanone and 3',5'-
CC hydroxylation of dihydrokaempferol and dihydroquercetin to form
CC dihydromyricetin. {ECO:0000250|UniProtKB:P48418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3',5'-unsubstituted flavanone + 2 O2 + 2 reduced [NADPH--
CC hemoprotein reductase] = a 3',5'-dihydroxyflavanone + 2 H(+) + 2 H2O
CC + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55448,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:48025,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138897;
CC EC=1.14.14.81; Evidence={ECO:0000250|UniProtKB:P48418};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D85184; BAA12735.1; -; mRNA.
DR AlphaFoldDB; Q96581; -.
DR SMR; Q96581; -.
DR BRENDA; 1.14.14.81; 2412.
DR UniPathway; UPA00009; -.
DR GO; GO:0033772; F:flavonoid 3',5'-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..516
FT /note="Flavonoid 3',5'-hydroxylase"
FT /id="PRO_0000052132"
FT BINDING 453
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 58088 MW; 148259BB35743731 CRC64;
MSPIYTTLTL HLATALFLFF HVQKLVHYLH GKATGHRCRR LPPGPTGWPI LGALPLLGNM
PHVTFANMAK KYGSVMYLKV GSHGLAIAST PDAAKAFLKT LDLNFSNRPP NAGATHLAYN
AQDMVFAHYG PKWKLLRKLS NLHMLGGKAL ENWADVRKTE LGYMLKAMFE SSQNNEPVMI
SEMLTYAMAN MLSQVILSRR VFNKKGAKSN EFKDMVVELM TSAGYFNIGD FIPSIGWMDL
QGIEGGMKRL HKKFDVLLTR LLDDHKRTSQ ERKQKPDFLD FVIANGDNSD GERLNTDNIK
ALLLNLFTAG TDTSSSIIEW ALAELLKNRT LLTRAQDEMD RVIGRDRRLL ESDIPNLPYL
QAICKETFRK HPSTPLNLPR NCIRGHVDVN GYYIPKGTRL NVNIWAIGRD PSVWGDNPNE
FDPERFLYGR NAKIDPRGNH FELIPFGAGR RICAGTRMGI LLVEYILGTL VHSFDWKLGF
SEDELNMDET FGLALQKAVP LAAMVIPRLP LHVYAP
