ID   F3PH_PETHY              Reviewed;         512 AA.
AC   Q9SBQ9;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Flavonoid 3'-monooxygenase;
DE            EC=1.14.14.82;
DE   AltName: Full=Cytochrome P450 75B2;
DE   AltName: Full=Flavonoid 3'-hydroxylase;
GN   Name=CYP75B2; Synonyms=HT1;
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 Red; TISSUE=Corolla;
RX   PubMed=10504566; DOI=10.1046/j.1365-313x.1999.00539.x;
RA   Brugliera F., Barri-Rewell G., Holton T.A., Mason J.G.;
RT   "Isolation and characterization of a flavonoid 3'-hydroxylase cDNA clone
RT   corresponding to the Ht1 locus of Petunia hybrida.";
RL   Plant J. 19:441-451(1999).
CC   -!- FUNCTION: Catalyzes the 3'-hydroxylation of the flavonoid B-ring to the
CC       3',4'-hydroxylated state. Convert naringenin to eriodictyol and
CC       dihydrokaempferol to dihydroquercetin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-unsubstituted flavone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = a 3'-hydroxyflavone + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:16337, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:27741, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:138726; EC=1.14.14.82;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type III membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: High expression in petals and ovaries and to a
CC       lower extent in sepals, pedicels, anthers and stems. Not detected in
CC       leaves, style or roots.
CC   -!- DEVELOPMENTAL STAGE: High expression early in flower development and
CC       then declines as the corolla becomes fully pigmented and opened.
CC   -!- MISCELLANEOUS: May act as a membrane anchor for localization of other,
CC       soluble, flavonoid enzymes to the endoplasmic reticulum.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF155332; AAD56282.1; -; mRNA.
DR   AlphaFoldDB; Q9SBQ9; -.
DR   SMR; Q9SBQ9; -.
DR   KEGG; ag:AAD56282; -.
DR   BRENDA; 1.14.14.82; 4700.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016711; F:flavonoid 3'-monooxygenase 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:0009813; P:flavonoid 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; Flavonoid biosynthesis; Heme; Iron; Membrane;
KW   Metal-binding; Monooxygenase; NADP; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..512
FT                   /note="Flavonoid 3'-monooxygenase"
FT                   /id="PRO_0000052137"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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   512 AA;  56936 MW;  1843AC1BEB32BAE2 CRC64;
     MEILSLILYT VIFSFLLQFI LRSFFRKRYP LPLPPGPKPW PIIGNLVHLG PKPHQSTAAM
     AQTYGPLMYL KMGFVDVVVA ASASVAAQFL KTHDANFSSR PPNSGAEHMA YNYQDLVFAP
     YGPRWRMLRK ICSVHLFSTK ALDDFRHVRQ DEVKTLTRAL ASAGQKPVKL GQLLNVCTTN
     ALARVMLGKR VFADGSGDVD PQAAEFKSMV VEMMVVAGVF NIGDFIPQLN WLDIQGVAAK
     MKKLHARFDA FLTDILEEHK GKIFGEMKDL LSTLISLKND DADNDGGKLT DTEIKALLLN
     LFVAGTDTSS STVEWAIAEL IRNPKILAQA QQEIDKVVGR DRLVGELDLA QLTYLEAIVK
     ETFRLHPSTP LSLPRIASES CEINGYFIPK GSTLLLNVWA IARDPNAWAD PLEFRPERFL
     PGGEKPKVDV RGNDFEVIPF GAGRRICAGM NLGIRMVQLM IATLIHAFNW DLVSGQLPEM
     LNMEEAYGLT LQRADPLVVH PRPRLEAQAY IG