C75A1_PETHY
ID C75A1_PETHY Reviewed; 506 AA.
AC P48418;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Flavonoid 3',5'-hydroxylase 1;
DE Short=F3'5'H;
DE EC=1.14.14.81 {ECO:0000269|PubMed:10567704};
DE AltName: Full=CYPLXXVA1;
DE AltName: Full=Cytochrome P450 75A1;
GN Name=CYP75A1; Synonyms=HF1;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Falcon Blue; TISSUE=Petal;
RA Ohbayashi M., Shimada Y., Nakano R., Kiyokawa S., Kikuchi Y.;
RT "Molecular cloning of cDNA encoding flavonoid-3',5'-hydroxylase from
RT Petunia hybrida.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Hwang T.S., Chen Y.C., Wu R.Y.;
RT "Cloning and sequencing of the genomic flavonoid 3',5'-hydroxylase
RT (F3',5'Hase) gene from Petunia hybrida.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Carnival violet; TISSUE=Petal;
RA Baek S.H.;
RT "Isolation and characterization of cytochrome P450 genes.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1-425.
RC STRAIN=cv. Blue-star; TISSUE=Flower;
RA Toguri T., Azuma M., Ohtani T.;
RT "The cloning and characterization of a cDNA encoding a cytochrome P450 from
RT the flowers of Petunia hybrida.";
RL Plant Sci. 94:119-126(1993).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10567704; DOI=10.1016/s0014-5793(99)01425-8;
RA Shimada Y., Nakano-Shimada R., Ohbayashi M., Okinaka Y., Kiyokawa S.,
RA Kikuchi Y.;
RT "Expression of chimeric P450 genes encoding flavonoid-3', 5'-hydroxylase in
RT transgenic tobacco and petunia plants.";
RL FEBS Lett. 461:241-245(1999).
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:0000269|PubMed:10567704}.
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:0000269|PubMed:10567704};
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; Z22545; CAA80266.1; -; mRNA.
DR EMBL; D14588; BAA03438.1; -; mRNA.
DR EMBL; AF081575; AAC32274.1; -; Genomic_DNA.
DR EMBL; AY245545; AAO91941.1; -; mRNA.
DR EMBL; X71130; CAA50442.1; -; mRNA.
DR PIR; S32110; S32110.
DR PIR; S38985; S38985.
DR AlphaFoldDB; P48418; -.
DR SMR; P48418; -.
DR BioCyc; MetaCyc:MON-12020; -.
DR BRENDA; 1.14.14.81; 4700.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome; Monooxygenase;
KW NADP; Oxidoreductase.
FT CHAIN 1..506
FT /note="Flavonoid 3',5'-hydroxylase 1"
FT /id="PRO_0000052129"
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 506 AA; 56548 MW; FCF3F9623BD82B3E CRC64;
MMLLTELGAA TSIFLIAHII ISTLISKTTG RHLPPGPRGW PVIGALPLLG AMPHVSLAKM
AKKYGAIMYL KVGTCGMAVA STPDAAKAFL KTLDINFSNR PPNAGATHLA YNAQDMVFAH
YGPRWKLLRK LSNLHMLGGK ALENWANVRA NELGHMLKSM SDMSREGQRV VVAEMLTFAM
ANMIGQVMLS KRVFVDKGVE VNEFKDMVVE LMTIAGYFNI GDFIPCLAWM DLQGIEKRMK
RLHKKFDALL TKMFDEHKAT TYERKGKPDF LDVVMENGDN SEGERLSTTN IKALLLNLFT
AGTDTSSSAI EWALAEMMKN PAILKKAQAE MDQVIGRNRR LLESDIPNLP YLRAICKETF
RKHPSTPLNL PRISNEPCIV DGYYIPKNTR LSVNIWAIGR DPQVWENPLE FNPERFLSGR
NSKIDPRGND FELIPFGAGR RICAGTRMGI VMVEYILGTL VHSFDWKLPS EVIELNMEEA
FGLALQKAVP LEAMVTPRLQ LDVYVP
