C75A6_CAMME
ID C75A6_CAMME Reviewed; 523 AA.
AC O04773;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 75A6;
GN Name=CYP75A6;
OS Campanula medium (Canterbury bells).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Campanulaceae; Campanula.
OX NCBI_TaxID=56154;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Petal;
RA Ohbayashi M.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
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; D14590; BAA03440.1; -; mRNA.
DR AlphaFoldDB; O04773; -.
DR SMR; O04773; -.
DR PRIDE; O04773; -.
DR BRENDA; 1.14.14.81; 14359.
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..523
FT /note="Flavonoid 3',5'-hydroxylase"
FT /id="PRO_0000052135"
FT BINDING 460
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 523 AA; 58726 MW; 70E39C6B76F387D9 CRC64;
MSIDISTLFY ELVAAISLYL ATYSFIRFLF KPSHHHHLPP GPTGWPIIGA LPLLGTMPHV
SLADMAVKYG PIMYLKLGSK GTVVASNPKA ARAFLKTHDA NFSNRPIDGG PTYLAYNAQD
MVFAEYGPKW KLLRKLCSLH MLGPKALEDW AHVKVSEVGH MLKEMYEQSS KSVPVPVVVP
EMLTYAMANM IGRIILSRRP FVITSKLDSS ASASASVSEF QYMVMELMRM AGLFNIGDFI
PYIAWMDLQG IQRDMKVIQK KFDVLLNKMI KEHTESAHDR KDNPDFLDIL MAATQENTEG
IQLNLVNVKA LLLDLFTAGT DTSSSVIEWA LAEMLNHRQI LNRAHEEMDQ VIGRNRRLEQ
SDIPNLPYFQ AICKETFRKH PSTPLNLPRI STEACEVDGF HIPKNTRLIV NIWAIGRDPK
VWENPLDFTP ERFLSEKHAK IDPRGNHFEL IPFGAGRRIC AGARMGAASV EYILGTLVHS
FDWKLPDGVV EVNMEESFGI ALQKKVPLSA IVTPRLPPSS YTV
