ID   C93B2_GERHY             Reviewed;         511 AA.
AC   Q9XGT9;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Cytochrome P450 93B2 {ECO:0000303|PubMed:10652133};
DE            EC=1.14.19.76 {ECO:0000269|PubMed:10652133};
DE   AltName: Full=Flavone synthase II {ECO:0000303|PubMed:10652133};
DE            Short=FNSII {ECO:0000303|PubMed:10652133};
GN   Name=CYP93B2 {ECO:0000303|PubMed:10652133};
OS   Gerbera hybrida (Daisy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Mutisioideae; Mutisieae;
OC   Gerbera.
OX   NCBI_TaxID=18101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10652133; DOI=10.1046/j.1365-313x.1999.00636.x;
RA   Martens S., Forkmann G.;
RT   "Cloning and expression of flavone synthase II from Gerbera hybrids.";
RL   Plant J. 20:611-618(1999).
CC   -!- FUNCTION: Functions as flavone synthase II (FNSII) that catalyzes the
CC       direct conversion of flavanones to flavones (PubMed:10652133). In
CC       vitro, can convert liquiritigenin, naringenin and eriodictyol to 7,4'-
CC       dihydroxyflavone, apigenin and luteolin, respectively
CC       (PubMed:10652133). {ECO:0000269|PubMed:10652133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a flavanone + O2 + reduced [NADPH--hemoprotein reductase] = a
CC         flavone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:57680, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:24043, ChEBI:CHEBI:28863, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.19.76;
CC         Evidence={ECO:0000269|PubMed:10652133};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57681;
CC         Evidence={ECO:0000269|PubMed:10652133};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF156976; AAD39549.1; -; mRNA.
DR   AlphaFoldDB; Q9XGT9; -.
DR   SMR; Q9XGT9; -.
DR   KEGG; ag:AAD39549; -.
DR   BRENDA; 1.14.19.76; 2420.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IDA:UniProtKB.
DR   GO; GO:0051553; P:flavone biosynthetic process; IDA:UniProtKB.
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   Flavonoid biosynthesis; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..511
FT                   /note="Cytochrome P450 93B2"
FT                   /id="PRO_0000452209"
FT   TRANSMEM        4..24
FT                   /note="Helical"
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|UniProtKB:Q94IP1"
SQ   SEQUENCE   511 AA;  58217 MW;  955AA1EDADF65CF2 CRC64;
     MNTLQLIFLL FFFPTLLFLY CLPYKRNQNH RRLPPSPPSF PIIGHLHHLG PLIHQSFHAL
     STRYGSLIHL RLGSVPCVVV STPDLAKDFL KTNELAFSSR KHSLAIDHIT YGVAFAFAPY
     GTYWKFIKKL FTVELLGTQN LSHFLPIRTH EIRELLRTLM VKSRAKERVN LTEELLKLTN
     NVISQMMMSI RCSGTNSEAD EAKNLVREVT KIFGQFNVSD FIWFCKNIDL QGFKKRYEGT
     HRRYDALLER IIMGREENRR RGKIKDGEGK DFLDMLLDVL EDGKAEIKIT RDHIKALILD
     FLTAGTDTTA IAIEWALVEL INNPNALEKA RQEIDQVIGD ERLVQESDTP NLPYIQAIIK
     EALRLHPPIP MLIRKSTENV IVQGYDIPAG TLLFVNIWSI GRNPQCWETP LEFKPHRFLD
     GGDLKSSLDI KGHNFQLLPF GTGRRGCPGV NLAMRELSVV IANLIQCFDW DVVGERLLNT
     DERAGLTAPR AVDFVCVPLE RGNTLKILGS N