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UniProtKB/Swiss-Prot entry Q9SD85


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name F3PH_ARATH
Primary accession number Q9SD85
Secondary accession numbers None
Integrated into Swiss-Prot on December 13, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 60)
Name and origin of the protein
Protein name Flavonoid 3'-monooxygenase
Synonyms EC 1.14.13.21
Flavonoid 3'-hydroxylase
AtF3'H
Cytochrome P450 75B1
Protein TRANSPARENT TESTA 7
Gene name
Name: CYP75B1
Synonyms: F3'H, TT7
OrderedLocusNames: At5g07990
ORFNames: F13G24.190
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia, and cv. Landsberg erecta;
DOI=10.1515/BC.2000.095; PubMed=11030432 [NCBI, ExPASy, EBI, Israel, Japan]
Schoenbohm C., Martens S., Eder C., Forkmann G., Weisshaar B.;
"Identification of the Arabidopsis thaliana flavonoid 3'-hydroxylase gene and functional expression of the encoded P450 enzyme.";
Biol. Chem. 381:749-753(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Cordiner T.D., Barri-Rewell G., Brugliera F., Cobbett C., Holton T.A.;
"Isolation of a flavonoid 3'-hydroxylase gene corresponding to the Tt7 locus of Arabidopsis thaliana.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Saslowsky D., Winkel-Shirley B.;
"Sequence of flavonoid 3'hydroxylase (F3'H).";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[5]
CHARACTERIZATION.
PubMed=11489181 [NCBI, ExPASy, EBI, Israel, Japan]
Saslowsky D., Winkel-Shirley B.;
"Localization of flavonoid enzymes in Arabidopsis roots.";
Plant J. 27:37-48(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF271651; AAG16746.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF271650; AAG16745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF155171; AAF73253.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF241646; AAF60189.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF241643; AAF60189.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF241644; AAF60189.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF241645; AAF60189.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133421; CAB62611.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T45624; T45624.
RefSeq NP_196416.1; -.
UniGene At.12059
3D structure databases
ModBase Q9SD85.
Organism-specific databases
GeneFarm 1262; 94.
TAIR At5g07990; -.
Gene expression databases
ArrayExpress Q9SD85; -.
GermOnline AT5G07990; Arabidopsis thaliana.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.
Gene3D G3DSA:1.10.630.10; Cyt_P450; 1.
PANTHER PTHR19383; Cyt_P450; 1.
Pfam PF00067; p450; 1.
Pfam graphical view of domain structure.
PRINTS PR00463; EP450I.
PR00385; P450.
PROSITE PS00086; CYTOCHROME_P450; 1.
BLOCKS Q9SD85.
Genome annotation databases
GeneID 830693; -.
GenomeReviews BA000015_GR; AT5G07990.
KEGG ath:AT5G07990; -.
NMPDR fig|3702.1.peg.22940; -.
Other
ProtoNet Q9SD85.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Flavonoid biosynthesis; Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   513  513     Flavonoid 3'-monooxygenase. PRO_0000052136
TRANSMEM   1    21  21     Potential. 
TOPO_DOM   22   513  492     Cytoplasmic (Potential). 
METAL   445   445        Iron (heme axial ligand) (By similarity). 
Sequence information
Length: 513 AA [This is the length of the unprocessed precursor] Molecular weight: 56787 Da [This is the MW of the unprocessed precursor] CRC64: C0C740FBE4559C40 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATLFLTILL ATVLFLILRI FSHRRNRSHN NRLPPGPNPW PIIGNLPHMG TKPHRTLSAM 

        70         80         90        100        110        120 
VTTYGPILHL RLGFVDVVVA ASKSVAEQFL KIHDANFASR PPNSGAKHMA YNYQDLVFAP 

       130        140        150        160        170        180 
YGHRWRLLRK ISSVHLFSAK ALEDFKHVRQ EEVGTLTREL VRVGTKPVNL GQLVNMCVVN 

       190        200        210        220        230        240 
ALGREMIGRR LFGADADHKA DEFRSMVTEM MALAGVFNIG DFVPSLDWLD LQGVAGKMKR 

       250        260        270        280        290        300 
LHKRFDAFLS SILKEHEMNG QDQKHTDMLS TLISLKGTDL DGDGGSLTDT EIKALLLNMF 

       310        320        330        340        350        360 
TAGTDTSAST VDWAIAELIR HPDIMVKAQE ELDIVVGRDR PVNESDIAQL PYLQAVIKEN 

       370        380        390        400        410        420 
FRLHPPTPLS LPHIASESCE INGYHIPKGS TLLTNIWAIA RDPDQWSDPL AFKPERFLPG 

       430        440        450        460        470        480 
GEKSGVDVKG SDFELIPFGA GRRICAGLSL GLRTIQFLTA TLVQGFDWEL AGGVTPEKLN 

       490        500        510 
MEESYGLTLQ RAVPLVVHPK PRLAPNVYGL GSG 

Q9SD85 in FASTA format

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