ID   F3PH_ARATH              Reviewed;         513 AA.
AC   Q9SD85;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 169.
DE   RecName: Full=Flavonoid 3'-monooxygenase;
DE            EC=1.14.14.82;
DE   AltName: Full=Cytochrome P450 75B1;
DE   AltName: Full=Flavonoid 3'-hydroxylase;
DE            Short=AtF3'H;
DE   AltName: Full=Protein TRANSPARENT TESTA 7;
GN   Name=CYP75B1; Synonyms=F3'H, TT7; OrderedLocusNames=At5g07990;
GN   ORFNames=F13G24.190;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=11030432; DOI=10.1515/bc.2000.095;
RA   Schoenbohm C., Martens S., Eder C., Forkmann G., Weisshaar B.;
RT   "Identification of the Arabidopsis thaliana flavonoid 3'-hydroxylase gene
RT   and functional expression of the encoded P450 enzyme.";
RL   Biol. Chem. 381:749-753(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RA   Cordiner T.D., Barri-Rewell G., Brugliera F., Cobbett C., Holton T.A.;
RT   "Isolation of a flavonoid 3'-hydroxylase gene corresponding to the Tt7
RT   locus of Arabidopsis thaliana.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RA   Saslowsky D., Winkel-Shirley B.;
RT   "Sequence of flavonoid 3'hydroxylase (F3'H).";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=11489181; DOI=10.1046/j.1365-313x.2001.01073.x;
RA   Saslowsky D., Winkel-Shirley B.;
RT   "Localization of flavonoid enzymes in Arabidopsis roots.";
RL   Plant J. 27:37-48(2001).
RN   [8]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA   Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA   Tohge T., Fernie A.R.;
RT   "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT   diversity.";
RL   Plant Physiol. Biochem. 72:21-34(2013).
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 + reduced [NADPH--hemoprotein
CC         reductase] + O2 = a 3'-hydroxyflavone + oxidized [NADPH--hemoprotein
CC         reductase] + H2O + H(+); 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 siliques and to a lower extent
CC       in stems, flowers and senescing leaves.
CC   -!- INDUCTION: By UV light treatment.
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; AF271651; AAG16746.1; -; mRNA.
DR   EMBL; AF271650; AAG16745.1; -; mRNA.
DR   EMBL; AF155171; AAF73253.1; -; Genomic_DNA.
DR   EMBL; AH009204; AAF60189.1; -; Genomic_DNA.
DR   EMBL; AL133421; CAB62611.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91232.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7051483.1; -; Genomic_DNA.
DR   PIR; T45624; T45624.
DR   RefSeq; NP_196416.1; NM_120881.3.
DR   AlphaFoldDB; Q9SD85; -.
DR   SMR; Q9SD85; -.
DR   BioGRID; 15971; 1.
DR   FunCoup; Q9SD85; 549.
DR   STRING; 3702.Q9SD85; -.
DR   PaxDb; 3702-Q9SD85; -.
DR   ProteomicsDB; 222359; -.
DR   GeneID; 830693; -.
DR   KEGG; ath:AT5G07990; -.
DR   Araport; AT5G07990; -.
DR   TAIR; AT5G07990; TT7.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; Q9SD85; -.
DR   OMA; QIRLGNC; -.
DR   PhylomeDB; Q9SD85; -.
DR   BioCyc; MetaCyc:AT5G07990-MONOMER; -.
DR   BRENDA; 1.14.14.82; 399.
DR   UniPathway; UPA00154; -.
DR   PRO; PR:Q9SD85; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9SD85; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; ISM:TAIR.
DR   GO; GO:0016711; F:flavonoid 3'-monooxygenase activity; IDA:TIGR.
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; TAS:TIGR.
DR   GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR   GO; GO:0009411; P:response to UV; IEP:TIGR.
DR   CDD; cd20657; CYP75; 1.
DR   FunFam; 1.10.630.10:FF:000056; Red aleurone1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR47944; CYTOCHROME P450 98A9; 1.
DR   PANTHER; PTHR47944:SF18; FLAVONOID 3'-MONOOXYGENASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Flavonoid biosynthesis; Heme; Iron; Membrane;
KW   Metal-binding; Monooxygenase; NADP; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..513
FT                   /note="Flavonoid 3'-monooxygenase"
FT                   /id="PRO_0000052136"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..513
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         445
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   513 AA;  56787 MW;  C0C740FBE4559C40 CRC64;
     MATLFLTILL ATVLFLILRI FSHRRNRSHN NRLPPGPNPW PIIGNLPHMG TKPHRTLSAM
     VTTYGPILHL RLGFVDVVVA ASKSVAEQFL KIHDANFASR PPNSGAKHMA YNYQDLVFAP
     YGHRWRLLRK ISSVHLFSAK ALEDFKHVRQ EEVGTLTREL VRVGTKPVNL GQLVNMCVVN
     ALGREMIGRR LFGADADHKA DEFRSMVTEM MALAGVFNIG DFVPSLDWLD LQGVAGKMKR
     LHKRFDAFLS SILKEHEMNG QDQKHTDMLS TLISLKGTDL DGDGGSLTDT EIKALLLNMF
     TAGTDTSAST VDWAIAELIR HPDIMVKAQE ELDIVVGRDR PVNESDIAQL PYLQAVIKEN
     FRLHPPTPLS LPHIASESCE INGYHIPKGS TLLTNIWAIA RDPDQWSDPL AFKPERFLPG
     GEKSGVDVKG SDFELIPFGA GRRICAGLSL GLRTIQFLTA TLVQGFDWEL AGGVTPEKLN
     MEESYGLTLQ RAVPLVVHPK PRLAPNVYGL GSG
//