ID   C75A7_EUSER             Reviewed;         510 AA.
AC   O04790;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Flavonoid 3',5'-hydroxylase;
DE            Short=F3'5'H;
DE            EC=1.14.14.81 {ECO:0000269|PubMed:10567704};
DE   AltName: Full=Cytochrome P450 75A7;
GN   Name=CYP75A7;
OS   Eustoma exaltatum subsp. russellianum (Bluebells) (Eustoma grandiflorum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Gentianaceae; Chironieae; Chironiinae;
OC   Eustoma.
OX   NCBI_TaxID=52518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10567704; DOI=10.1016/s0014-5793(99)01425-8;
RA   Shimada Y., Nakano-Shimada R., Ohbayashi M., Okinaka Y., Kiyokawa S.,
RA   Kikuchi Y.;
RT   "Expression of chimeric P450 genes encoding flavonoid-3', 5'-hydroxylase in
RT   transgenic tobacco and petunia plants.";
RL   FEBS Lett. 461:241-245(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Petal;
RA   Noda N., Kanno Y., Kato N., Kazuma K., Suzuki M.;
RT   "Regulation of gene expression involved in flavonol and anthocyanin
RT   biosynthesis during petal development in lisianthus (Eustoma
RT   grandiflorum).";
RL   Physiol. Plantarum 122:305-313(2004).
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:0000269|PubMed:10567704}.
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:0000269|PubMed:10567704};
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; D14589; BAA03439.1; -; mRNA.
DR   EMBL; AB078957; BAD34460.1; -; mRNA.
DR   AlphaFoldDB; O04790; -.
DR   SMR; O04790; -.
DR   KEGG; ag:BAA03439; -.
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   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..510
FT                   /note="Flavonoid 3',5'-hydroxylase"
FT                   /id="PRO_0000052134"
FT   BINDING         447
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   510 AA;  56732 MW;  B0A84B8F2DB2771D CRC64;
     MAVGNGVLLH IAASLMLFFH VQKLVQYLWM NSRRHRLPPG PIGWPVLGAL RLLGTMPHVA
     LANMAKKYGP VMYLKVGSCG LAVASTPEAA KAFLKTLDMN FSNRPPNAGA THLAYNAQDM
     VFADYGPRWK LLRKLSNIHI LGGKALQGWE EVRKKELGYM LYAMAESGRH GQPVVVSEML
     TYAMANMLGQ VMLSKRVFGS QGSESNEFKD MVVELMTVAG YFNIGDFIPS IAWMDLQGIQ
     GGMKRLHKKF DALLTRLLEE HTASAHERKG SPDFLDFVVA NGDNSEGERL QTVNIKALLL
     NMFTAGTDTS SSVIEWALAE LLKNPIILRR AQEEMDGVIG RDRRFLEADI SKLPYLQAIC
     KEAFRKHPST PLNLPRIASQ ACEVNGHYIP KGTRLSVNIW AIGRDPSVWE NPNEFNPDRF
     LERKNAKIDP RGNDFELIPF GAGRRICAGT RLGILLVEYI LGTLVHSFVW ELPSSVIELN
     MDESFGLALQ KAVPLAAMVT PRLPLHIYSP