ID   C71AD_ARATH             Reviewed;         497 AA.
AC   O49342; F4INY1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Indoleacetaldoxime dehydratase;
DE            EC=4.99.1.6;
DE   AltName: Full=Cytochrome P450 71A13;
GN   Name=CYP71A13; OrderedLocusNames=At2g30770; ORFNames=T11J7.16;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17573535; DOI=10.1105/tpc.107.051383;
RA   Nafisi M., Goregaoker S., Botanga C.J., Glawischnig E., Olsen C.E.,
RA   Halkier B.A., Glazebrook J.;
RT   "Arabidopsis cytochrome P450 monooxygenase 71A13 catalyzes the conversion
RT   of indole-3-acetaldoxime in camalexin synthesis.";
RL   Plant Cell 19:2039-2052(2007).
RN   [5]
RP   INDUCTION.
RX   PubMed=18650934; DOI=10.1038/emboj.2008.147;
RA   Qiu J.L., Fiil B.K., Petersen K., Nielsen H.B., Botanga C.J.,
RA   Thorgrimsen S., Palma K., Suarez-Rodriguez M.C., Sandbech-Clausen S.,
RA   Lichota J., Brodersen P., Grasser K.D., Mattsson O., Glazebrook J.,
RA   Mundy J., Petersen M.;
RT   "Arabidopsis MAP kinase 4 regulates gene expression through transcription
RT   factor release in the nucleus.";
RL   EMBO J. 27:2214-2221(2008).
RN   [6]
RP   INDUCTION.
RX   PubMed=18567828; DOI=10.1104/pp.108.121335;
RA   Chanda B., Venugopal S.C., Kulshrestha S., Navarre D.A., Downie B.,
RA   Vaillancourt L., Kachroo A., Kachroo P.;
RT   "Glycerol-3-phosphate levels are associated with basal resistance to the
RT   hemibiotrophic fungus Colletotrichum higginsianum in Arabidopsis.";
RL   Plant Physiol. 147:2017-2029(2008).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=19154205; DOI=10.1111/j.1365-313x.2009.03794.x;
RA   Stefanato F.L., Abou-Mansour E., Buchala A., Kretschmer M., Mosbach A.,
RA   Hahn M., Bochet C.G., Metraux J.P., Schoonbeek H.J.;
RT   "The ABC transporter BcatrB from Botrytis cinerea exports camalexin and is
RT   a virulence factor on Arabidopsis thaliana.";
RL   Plant J. 58:499-510(2009).
RN   [8]
RP   INDUCTION.
RX   PubMed=21143673; DOI=10.1111/j.1365-313x.2010.04387.x;
RA   Pandey S.P., Roccaro M., Schoen M., Logemann E., Somssich I.E.;
RT   "Transcriptional reprogramming regulated by WRKY18 and WRKY40 facilitates
RT   powdery mildew infection of Arabidopsis.";
RL   Plant J. 64:912-923(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of the indole-derived
CC       phytoalexin camalexin. Catalyzes the conversion of indole-3-
CC       acetaldoxime to indole-3-acetonitrile. Required for resistance to
CC       A.brassicicola and B.cinerea. {ECO:0000269|PubMed:17573535,
CC       ECO:0000269|PubMed:19154205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-(indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile
CC         + H2O; Xref=Rhea:RHEA:23156, ChEBI:CHEBI:15377, ChEBI:CHEBI:17545,
CC         ChEBI:CHEBI:17566; EC=4.99.1.6;
CC         Evidence={ECO:0000269|PubMed:17573535};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: By Pseudomonas syringae pv. tomato DC3000, Botrytis cinerea,
CC       flagellin, BTH and UV-C. Repressed by the transcription factors WRKY18
CC       and WRKY40 upon infection with Golovinomyces orontii.
CC       {ECO:0000269|PubMed:18567828, ECO:0000269|PubMed:18650934,
CC       ECO:0000269|PubMed:19154205, ECO:0000269|PubMed:21143673}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AC002340; AAC02748.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08439.2; -; Genomic_DNA.
DR   EMBL; BX820453; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; E84712; E84712.
DR   RefSeq; NP_180635.3; NM_128630.3.
DR   AlphaFoldDB; O49342; -.
DR   SMR; O49342; -.
DR   BioGRID; 2977; 1.
DR   IntAct; O49342; 1.
DR   STRING; 3702.AT2G30770.1; -.
DR   PaxDb; O49342; -.
DR   PRIDE; O49342; -.
DR   ProteomicsDB; 239080; -.
DR   EnsemblPlants; AT2G30770.1; AT2G30770.1; AT2G30770.
DR   GeneID; 817628; -.
DR   Gramene; AT2G30770.1; AT2G30770.1; AT2G30770.
DR   KEGG; ath:AT2G30770; -.
DR   Araport; AT2G30770; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; O49342; -.
DR   OMA; MEMILMI; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; O49342; -.
DR   BioCyc; ARA:AT2G30770-MON; -.
DR   BioCyc; MetaCyc:AT2G30770-MON; -.
DR   PRO; PR:O49342; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O49342; baseline and differential.
DR   Genevisible; O49342; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0047720; F:indoleacetaldoxime dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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   Iron; Lyase; Membrane; Metal-binding; Plant defense; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..497
FT                   /note="Indoleacetaldoxime dehydratase"
FT                   /id="PRO_0000052064"
FT   TRANSMEM        2..20
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         439
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|UniProtKB:Q96242"
SQ   SEQUENCE   497 AA;  56086 MW;  3C8CE0773624B59B CRC64;
     MEMILSISLC LTTLITLLLL RRFLKRTATK VNLPPSPWRL PVIGNLHQLS LHPHRSLRSL
     SLRYGPLMLL HFGRVPILVV SSGEAAQEVL KTHDHKFANR PRSKAVHGLM NGGRDVVFAP
     YGEYWRQMKS VCILNLLTNK MVESFEKVRE DEVNAMIEKL EKASSSSSSE NLSELFITLP
     SDVTSRVALG RKHSEDETAR DLKKRVRQIM ELLGEFPIGE YVPILAWIDG IRGFNNKIKE
     VSRGFSDLMD KVVQEHLEAS NDKADFVDIL LSIEKDKNSG FQVQRNDIKF MILDMFIGGT
     STTSTLLEWT MTELIRSPKS MKKLQDEIRS TIRPHGSYIK EKEVENMKYL KAVIKEVLRL
     HPSLPMILPR LLSEDVKVKG YNIAAGTEVI INAWAIQRDT AIWGPDAEEF KPERHLDSGL
     DYHGKNLNYI PFGSGRRICP GINLALGLAE VTVANLVGRF DWRVEAGPNG DQPDLTEAIG
     IDVCRKFPLI AFPSSVV