F3PH_ARATH
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 03-AUG-2022, entry version 152.
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 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 [7]
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 + O2 + reduced [NADPH--hemoprotein
CC reductase] = a 3'-hydroxyflavone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; 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 PIR; T45624; T45624.
DR RefSeq; NP_196416.1; NM_120881.3.
DR AlphaFoldDB; Q9SD85; -.
DR SMR; Q9SD85; -.
DR BioGRID; 15971; 1.
DR STRING; 3702.AT5G07990.1; -.
DR PaxDb; Q9SD85; -.
DR PRIDE; Q9SD85; -.
DR ProteomicsDB; 222359; -.
DR EnsemblPlants; AT5G07990.1; AT5G07990.1; AT5G07990.
DR GeneID; 830693; -.
DR Gramene; AT5G07990.1; AT5G07990.1; AT5G07990.
DR KEGG; ath:AT5G07990; -.
DR Araport; AT5G07990; -.
DR TAIR; locus:2142878; AT5G07990.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR OMA; VPRCTAV; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9SD85; -.
DR BioCyc; MetaCyc:AT5G07990-MON; -.
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 Genevisible; Q9SD85; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016711; F:flavonoid 3'-monooxygenase 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:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
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; 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
