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Protein

Cytochrome P450 81F1

Gene

CYP81F1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in indole glucosinolate biosynthesis. Catalyzes hydroxylation reactions of the glucosinolate indole ring. Converts indol-3-yl-methylglucosinolate (I3M) to 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and/or 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) intermediates. These hydroxy intermediates are converted to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate (1MO-I3M) by indole glucosinolate methyltransferase 1 and 2 (IGMT1 and IGMT2).1 Publication

Cofactori

hemeBy similarity

Pathwayi: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.Curated
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi438 – 4381Iron (heme axial ligand)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G37430-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 81F1Curated (EC:1.14.-.-Curated)
Gene namesi
Name:CYP81F11 Publication
Synonyms:CYP91A2
Ordered Locus Names:At4g37430
ORF Names:F6G17.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G37430.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500Cytochrome P450 81F1PRO_0000052161Add
BLAST

Proteomic databases

PaxDbiO65790.
PRIDEiO65790.

PTM databases

iPTMnetiO65790.

Expressioni

Gene expression databases

GenevisibleiO65790. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G37430.1.

Structurei

3D structure databases

ProteinModelPortaliO65790.
SMRiO65790. Positions 47-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0156. Eukaryota.
COG2124. LUCA.
HOGENOMiHOG000218627.
InParanoidiO65790.
KOiK00517.
OMAiVAYNHTT.
PhylomeDBiO65790.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O65790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYFILLPLL FLVISYKFLY SKTQRFNLPP GPPSRPFVGH LHLMKPPIHR
60 70 80 90 100
LLQRYSNQYG PIFSLRFGSR RVVVITSPSL AQESFTGQND IVLSSRPLQL
110 120 130 140 150
TAKYVAYNHT TVGTAPYGDH WRNLRRICSQ EILSSHRLIN FQHIRKDEIL
160 170 180 190 200
RMLTRLSRYT QTSNESNDFT HIELEPLLSD LTFNNIVRMV TGKRYYGDDV
210 220 230 240 250
NNKEEAELFK KLVYDIAMYS GANHSADYLP ILKLFGNKFE KEVKAIGKSM
260 270 280 290 300
DDILQRLLDE CRRDKEGNTM VNHLISLQQQ QPEYYTDVII KGLMMSMMLA
310 320 330 340 350
GTETSAVTLE WAMANLLRNP EVLEKARSEI DEKIGKDRLI DESDIAVLPY
360 370 380 390 400
LQNVVSETFR LFPVAPFLIP RSPTDDMKIG GYDVPRDTIV MVNAWAIHRD
410 420 430 440 450
PEIWEEPEKF NPDRYNDGCG SDYYVYKLMP FGNGRRTCPG AGLGQRIVTL
460 470 480 490 500
ALGSLIQCFE WENVKGEEMD MSESTGLGMR KMDPLRAMCR PRPIMSKLLL
Length:500
Mass (Da):57,555
Last modified:December 1, 2000 - v2
Checksum:i0FB453D2070EA2EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021A → S in AAM67324 (Ref. 5) Curated
Sequence conflicti106 – 1061A → V in BAA28539 (PubMed:9620263).Curated
Sequence conflicti127 – 1271I → M in BAA28539 (PubMed:9620263).Curated
Sequence conflicti140 – 1401N → I in BAA28539 (PubMed:9620263).Curated
Sequence conflicti454 – 4541S → T in BAA28539 (PubMed:9620263).Curated
Sequence conflicti495 – 4951M → I in AAM67324 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78607 mRNA. Translation: BAA28539.1.
AL035601 Genomic DNA. Translation: CAB38210.1.
AL161591 Genomic DNA. Translation: CAB80408.1.
CP002687 Genomic DNA. Translation: AEE86792.1.
AY039844 mRNA. Translation: AAK63948.1.
AY087256 mRNA. Translation: AAM67324.1.
PIRiT04737.
T52175.
RefSeqiNP_195459.1. NM_119906.3.
UniGeneiAt.20210.

Genome annotation databases

EnsemblPlantsiAT4G37430.1; AT4G37430.1; AT4G37430.
GeneIDi829897.
GrameneiAT4G37430.1; AT4G37430.1; AT4G37430.
KEGGiath:AT4G37430.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78607 mRNA. Translation: BAA28539.1.
AL035601 Genomic DNA. Translation: CAB38210.1.
AL161591 Genomic DNA. Translation: CAB80408.1.
CP002687 Genomic DNA. Translation: AEE86792.1.
AY039844 mRNA. Translation: AAK63948.1.
AY087256 mRNA. Translation: AAM67324.1.
PIRiT04737.
T52175.
RefSeqiNP_195459.1. NM_119906.3.
UniGeneiAt.20210.

3D structure databases

ProteinModelPortaliO65790.
SMRiO65790. Positions 47-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G37430.1.

PTM databases

iPTMnetiO65790.

Proteomic databases

PaxDbiO65790.
PRIDEiO65790.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G37430.1; AT4G37430.1; AT4G37430.
GeneIDi829897.
GrameneiAT4G37430.1; AT4G37430.1; AT4G37430.
KEGGiath:AT4G37430.

Organism-specific databases

TAIRiAT4G37430.

Phylogenomic databases

eggNOGiKOG0156. Eukaryota.
COG2124. LUCA.
HOGENOMiHOG000218627.
InParanoidiO65790.
KOiK00517.
OMAiVAYNHTT.
PhylomeDBiO65790.

Enzyme and pathway databases

BioCyciARA:AT4G37430-MONOMER.

Miscellaneous databases

PROiO65790.

Gene expression databases

GenevisibleiO65790. AT.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cytochrome P450 superfamily in Arabidopsis thaliana: isolation of cDNAs, differential expression, and RFLP mapping of multiple cytochromes P450."
    Mizutani M., Ward E., Ohta D.
    Plant Mol. Biol. 37:39-52(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Seedling.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Metabolic engineering in Nicotiana benthamiana reveals key enzyme functions in Arabidopsis indole glucosinolate modification."
    Pfalz M., Mikkelsen M.D., Bednarek P., Olsen C.E., Halkier B.A., Kroymann J.
    Plant Cell 23:716-729(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiC81F1_ARATH
AccessioniPrimary (citable) accession number: O65790
Secondary accession number(s): Q7FBW2, Q8LBE7, Q9SZU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.