ID   C75A3_PETHY             Reviewed;         508 AA.
AC   P48419;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Flavonoid 3',5'-hydroxylase 2;
DE            Short=F3'5'H;
DE            EC=1.14.14.81 {ECO:0000250|UniProtKB:P48418};
DE   AltName: Full=CYPLXXVA3;
DE   AltName: Full=Cytochrome P450 75A3;
GN   Name=CYP75A3; Synonyms=HF2;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Old Glory Blue; TISSUE=Petal;
RX   PubMed=8232589; DOI=10.1038/366276a0;
RA   Holton T.A., Brugliera F., Lester D.R., Tanaka Y., Hyland C.D.,
RA   Menting J.G.T., Lu C.-Y., Farcy E., Stevenson T.W., Cornish E.C.;
RT   "Cloning and expression of cytochrome P450 genes controlling flower
RT   colour.";
RL   Nature 366:276-279(1993).
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   -!- SUBCELLULAR LOCATION: Microsome {ECO:0000305}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Flowers.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; Z22544; CAA80265.1; -; mRNA.
DR   PIR; S38984; S38984.
DR   AlphaFoldDB; P48419; -.
DR   SMR; P48419; -.
DR   BioCyc; MetaCyc:MON-12019; -.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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   Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome; Monooxygenase;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..508
FT                   /note="Flavonoid 3',5'-hydroxylase 2"
FT                   /id="PRO_0000052130"
FT   BINDING         443
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   508 AA;  56721 MW;  70989FF2B3AD4FD8 CRC64;
     MVLLSELAAA TLIFLTTHIF ISTLLSITNG RRLPPGPRGW PVIGALPLLG AMPHVSLAKM
     AKKYGAIMYL KVGTCGMVVA STPDAAKAFL KTLDLNFSNR PPNAGATHLA YGAQDMVFAH
     YGPRWKLLRK LSNLHMLGGK ALENWANVRA NELGHMLKSM FDMSREGERV VVAEMLTFAM
     ANMIGQVILS KRVFVNKGVE VNEFKDMVVE LMTTAGYFNI GDFIPCLAWM DLQGIEKGMK
     RLHKKFDALL TKMFDEHKAT SYERKGKPDF LDCVMENRDN SEGERLSTTN IKALLLNLFT
     AGTDTSSSAI EWALAEMMKN PAILKKAQGE MDQVIGNNRR LLESDIPNLP YLRAICKETF
     RKHPSTPLNL PRISNEPCIV DGYYIPKNTR LSVNIWAIGR DPEVWENPLE FYPERFLSGR
     NSKIDPRGND FELIPFGAGR RICAGTRMGI VMVEYILGTL VHSFDWKLPS EVIELNMEEA
     FGLALQKAVP LEAMVTPRLP IDVYAPLA