C75A5_EUSER
ID C75A5_EUSER Reviewed; 510 AA.
AC Q96418;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 75A5;
GN Name=CYP75A5;
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].
RC TISSUE=Petal;
RA Nielsen K.M., Podivinsky E.;
RT "cDNA Cloning and Expression of a flavonoid 3'5'-hydroxylase from petals of
RT lisianthus (Eustoma grandiflorum Grise).";
RL Submitted (SEP-1996) 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; U72654; AAB17562.1; -; mRNA.
DR AlphaFoldDB; Q96418; -.
DR SMR; Q96418; -.
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..510
FT /note="Flavonoid 3',5'-hydroxylase"
FT /id="PRO_0000052133"
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; 56894 MW; 8E6A802DD9A5BAB9 CRC64;
MAVGNGVLLH IARSLMLFFH VQKLVQYLWM NSRRHRLPPG PIGWPVLGAL PLLGTMPHVA
LANMAKKYGP VMYLKVGSCG LAVASTPEAA KAFLKTLDMN FSNRPPNAGA THLAYNAQDM
VFADYGPRWK LLRKLSNIHI LGGKALQGWE EVRKKELGYM LYAMAESGRH GQPVVVSEML
TYAMANMLGQ VMLSKRVFGS QGSESNEFKD MVVELMTVAG YFNIGDFIPS IAWMDLQGIQ
GGMKRLHKKF DALLTRLLEE HTASAHERKG SPDFLDFVVA NRDNSEGERL HTVNIKALLL
NMFTAGTDTS SSVIEWALAE LLKNPIILKR AQEEMDGVIG RDRRFLEADI SKLPYLQAIC
KEAFRKHPST PLNLPRIASQ ACEVNGHYIP KGTRLSVNIW AIGRDPSLWE NPNEFNPDRF
LERKNAKIDP RGNDFELIPF GAGRRICAGT RLGILLVEYI LGTLVHSFDW ELPSSVIELN
MDEPFGLALQ KAVPLAAMVT PRLPLHIYCP
