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O49342 (C71AD_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Indoleacetaldoxime dehydratase

EC=4.99.1.6
Alternative name(s):
Cytochrome P450 71A13
Gene names
Name:CYP71A13
Ordered Locus Names:At2g30770
ORF Names:T11J7.16
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of the indole-derived phytoalexin camalexin. Catalyzes the conversion of indole-3-acetaldoxime to indole-3-acetonitrile. Required for resistance to A.brassicicola and B.cinerea. Ref.4 Ref.7

Catalytic activity

(Indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O. Ref.4

Subcellular location

Membrane; Single-pass membrane protein Potential.

Induction

By Pseudomonas syringae pv. tomato DC3000, Botrytis cinerea, flagellin, BTH and UV-C. Repressed by the transcription factors WRKY18 and WRKY40 upon infection with Golovinomyces orontii. Ref.5 Ref.6 Ref.7 Ref.8

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence caution

The sequence AEC08439.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Indoleacetaldoxime dehydratase
PRO_0000052064

Regions

Transmembrane2 – 2019Helical; Potential
Compositional bias164 – 1696Poly-Ser

Sequences

Sequence LengthMass (Da)Tools
O49342 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 3C8CE0773624B59B

FASTA49756,086
        10         20         30         40         50         60 
MEMILSISLC LTTLITLLLL RRFLKRTATK VNLPPSPWRL PVIGNLHQLS LHPHRSLRSL 

        70         80         90        100        110        120 
SLRYGPLMLL HFGRVPILVV SSGEAAQEVL KTHDHKFANR PRSKAVHGLM NGGRDVVFAP 

       130        140        150        160        170        180 
YGEYWRQMKS VCILNLLTNK MVESFEKVRE DEVNAMIEKL EKASSSSSSE NLSELFITLP 

       190        200        210        220        230        240 
SDVTSRVALG RKHSEDETAR DLKKRVRQIM ELLGEFPIGE YVPILAWIDG IRGFNNKIKE 

       250        260        270        280        290        300 
VSRGFSDLMD KVVQEHLEAS NDKADFVDIL LSIEKDKNSG FQVQRNDIKF MILDMFIGGT 

       310        320        330        340        350        360 
STTSTLLEWT MTELIRSPKS MKKLQDEIRS TIRPHGSYIK EKEVENMKYL KAVIKEVLRL 

       370        380        390        400        410        420 
HPSLPMILPR LLSEDVKVKG YNIAAGTEVI INAWAIQRDT AIWGPDAEEF KPERHLDSGL 

       430        440        450        460        470        480 
DYHGKNLNYI PFGSGRRICP GINLALGLAE VTVANLVGRF DWRVEAGPNG DQPDLTEAIG 

       490 
IDVCRKFPLI AFPSSVV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Arabidopsis cytochrome P450 monooxygenase 71A13 catalyzes the conversion of indole-3-acetaldoxime in camalexin synthesis."
Nafisi M., Goregaoker S., Botanga C.J., Glawischnig E., Olsen C.E., Halkier B.A., Glazebrook J.
Plant Cell 19:2039-2052(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[5]"Arabidopsis MAP kinase 4 regulates gene expression through transcription factor release in the nucleus."
Qiu J.L., Fiil B.K., Petersen K., Nielsen H.B., Botanga C.J., Thorgrimsen S., Palma K., Suarez-Rodriguez M.C., Sandbech-Clausen S., Lichota J., Brodersen P., Grasser K.D., Mattsson O., Glazebrook J., Mundy J., Petersen M.
EMBO J. 27:2214-2221(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"Glycerol-3-phosphate levels are associated with basal resistance to the hemibiotrophic fungus Colletotrichum higginsianum in Arabidopsis."
Chanda B., Venugopal S.C., Kulshrestha S., Navarre D.A., Downie B., Vaillancourt L., Kachroo A., Kachroo P.
Plant Physiol. 147:2017-2029(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"The ABC transporter BcatrB from Botrytis cinerea exports camalexin and is a virulence factor on Arabidopsis thaliana."
Stefanato F.L., Abou-Mansour E., Buchala A., Kretschmer M., Mosbach A., Hahn M., Bochet C.G., Metraux J.P., Schoonbeek H.J.
Plant J. 58:499-510(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[8]"Transcriptional reprogramming regulated by WRKY18 and WRKY40 facilitates powdery mildew infection of Arabidopsis."
Pandey S.P., Roccaro M., Schoen M., Logemann E., Somssich I.E.
Plant J. 64:912-923(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC002340 Genomic DNA. Translation: AAC02748.1.
CP002685 Genomic DNA. Translation: AEC08439.1. Different initiation.
BX820453 mRNA. No translation available.
IPIIPI00527969.
PIRE84712.
RefSeqNP_180635.2. NM_128630.2.
UniGeneAt.20309.
At.68697.

3D structure databases

ProteinModelPortalO49342.
SMRO49342. Positions 33-495.
ModBaseSearch...

Protein-protein interaction databases

IntActO49342. 1 interaction.
STRING3702.AT2G30770.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID817628.
KEGGath:AT2G30770.

Organism-specific databases

GeneFarm1175. 94.
TAIRAt2g30770.

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000218629.
InParanoidO49342.
KOK11868.
PhylomeDBO49342.

Enzyme and pathway databases

BioCycARA:AT2G30770-MONOMER.
MetaCyc:AT2G30770-MONOMER.

Gene expression databases

GenevestigatorO49342.
GermOnlineAT2G30770. Arabidopsis thaliana.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC71AD_ARATH
AccessionPrimary (citable) accession number: O49342
Secondary accession number(s): F4INY1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families