ID C71BF_ARATH Reviewed; 490 AA. AC Q9LW27; Q541X4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 13-SEP-2023, entry version 144. DE RecName: Full=Bifunctional dihydrocamalexate synthase/camalexin synthase; DE EC=1.14.19.52 {ECO:0000269|PubMed:16766671, ECO:0000269|PubMed:19567706}; DE AltName: Full=Cytochrome P450 71B15; DE AltName: Full=Dihydrocamalexate:NADP(+) oxidoreductase (decarboxylating); DE AltName: Full=Protein PHYTOALEXIN DEFICIENT 3; GN Name=CYP71B15; Synonyms=PAD3; OrderedLocusNames=At3g26830; GN ORFNames=MDJ14.15; 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=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). 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=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., RA Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=8090752; DOI=10.1073/pnas.91.19.8955; RA Glazebrook J., Ausubel F.M.; RT "Isolation of phytoalexin-deficient mutants of Arabidopsis thaliana and RT characterization of their interactions with bacterial pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 91:8955-8959(1994). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=10476063; DOI=10.1046/j.1365-313x.1999.00513.x; RA Thomma B.P., Nelissen I., Eggermont K., Broekaert W.F.; RT "Deficiency in phytoalexin production causes enhanced susceptibility of RT Arabidopsis thaliana to the fungus Alternaria brassicicola."; RL Plant J. 19:163-171(1999). RN [6] RP FUNCTION, INDUCTION, AND MUTAGENESIS OF GLY-176. RX PubMed=10590168; DOI=10.1105/tpc.11.12.2419; RA Zhou N., Tootle T.L., Glazebrook J.; RT "Arabidopsis PAD3, a gene required for camalexin biosynthesis, encodes a RT putative cytochrome P450 monooxygenase."; RL Plant Cell 11:2419-2428(1999). RN [7] RP FUNCTION. RX PubMed=11722772; DOI=10.1046/j.1365-313x.2001.01148.x; RA Roetschi A., Si-Ammour A., Belbahri L., Mauch F., Mauch-Mani B.; RT "Characterization of an Arabidopsis-Phytophthora pathosystem: resistance RT requires a functional PAD2 gene and is independent of salicylic acid, RT ethylene and jasmonic acid signalling."; RL Plant J. 28:293-305(2001). RN [8] RP FUNCTION. RX PubMed=11884688; DOI=10.1105/tpc.010481; RA Kus J.V., Zaton K., Sarkar R., Cameron R.K.; RT "Age-related resistance in Arabidopsis is a developmentally regulated RT defense response to Pseudomonas syringae."; RL Plant Cell 14:479-490(2002). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12848825; DOI=10.1046/j.1365-313x.2003.01794.x; RA Ferrari S., Plotnikova J.M., De Lorenzo G., Ausubel F.M.; RT "Arabidopsis local resistance to Botrytis cinerea involves salicylic acid RT and camalexin and requires EDS4 and PAD2, but not SID2, EDS5 or PAD4."; RL Plant J. 35:193-205(2003). RN [10] RP FUNCTION. RX PubMed=14675428; DOI=10.1046/j.1365-313x.2003.01927.x; RA Bohman S., Staal J., Thomma B.P., Wang M., Dixelius C.; RT "Characterisation of an Arabidopsis-Leptosphaeria maculans pathosystem: RT resistance partially requires camalexin biosynthesis and is independent of RT salicylic acid, ethylene and jasmonic acid signalling."; RL Plant J. 37:9-20(2004). RN [11] RP INDUCTION. RX PubMed=16769150; DOI=10.1016/j.jplph.2006.04.012; RA Schuhegger R., Rauhut T., Glawischnig E.; RT "Regulatory variability of camalexin biosynthesis."; RL J. Plant Physiol. 164:636-644(2007). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION. RX PubMed=16766671; DOI=10.1104/pp.106.082024; RA Schuhegger R., Nafisi M., Mansourova M., Petersen B.L., Olsen C.E., RA Svatos A., Halkier B.A., Glawischnig E.; RT "CYP71B15 (PAD3) catalyzes the final step in camalexin biosynthesis."; RL Plant Physiol. 141:1248-1254(2006). RN [13] RP FUNCTION. RX PubMed=20507477; DOI=10.1111/j.1364-3703.2006.00367.x; RA van Baarlen P., Woltering E.J., Staats M., van Kan J.A.; RT "Histochemical and genetic analysis of host and non-host interactions of RT Arabidopsis with three Botrytis species: an important role for cell death RT control."; RL Mol. Plant Pathol. 8:41-54(2007). RN [14] RP FUNCTION, AND INDUCTION. 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 [15] RP FUNCTION, AND INDUCTION. RX PubMed=17384165; DOI=10.1104/pp.107.095596; RA Ferrari S., Galletti R., Denoux C., De Lorenzo G., Ausubel F.M., RA Dewdney J.; RT "Resistance to Botrytis cinerea induced in Arabidopsis by elicitors is RT independent of salicylic acid, ethylene, or jasmonate signaling but RT requires PHYTOALEXIN DEFICIENT3."; RL Plant Physiol. 144:367-379(2007). RN [16] 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 [17] RP INDUCTION BY OLIGOGALACTURONIDES. RX PubMed=18790995; DOI=10.1104/pp.108.127845; RA Galletti R., Denoux C., Gambetta S., Dewdney J., Ausubel F.M., RA De Lorenzo G., Ferrari S.; RT "The AtrbohD-mediated oxidative burst elicited by oligogalacturonides in RT Arabidopsis is dispensable for the activation of defense responses RT effective against Botrytis cinerea."; RL Plant Physiol. 148:1695-1706(2008). RN [18] RP FUNCTION. 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 [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19567706; DOI=10.1105/tpc.109.066670; RA Boettcher C., Westphal L., Schmotz C., Prade E., Scheel D., Glawischnig E.; RT "The multifunctional enzyme CYP71B15 (PHYTOALEXIN DEFICIENT3) converts RT cysteine-indole-3-acetonitrile to camalexin in the indole-3-acetonitrile RT metabolic network of Arabidopsis thaliana."; RL Plant Cell 21:1830-1845(2009). RN [20] 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). CC -!- FUNCTION: Multifunctional enzyme involved in the biosynthesis of the CC indole-derived phytoalexin camalexin. Catalyzes two reactions, the CC formation of dihydrocamalexate from indole-3-acetonitrile-cysteine CC conjugate and the oxidative decarboxylation of dihydrocamalexate which CC is the final step in camalexin biosynthesis. Required for the CC resistance to the fungal pathogens A.brassicicola, B.cinerea, CC B.elliptica, B.tulipae, L.maculans and Colletotrichum higginsianum. CC Seems not to be required for resistance to P.syringae, P.porri, and not CC involved in age-related resistance. {ECO:0000269|PubMed:10476063, CC ECO:0000269|PubMed:10590168, ECO:0000269|PubMed:11722772, CC ECO:0000269|PubMed:11884688, ECO:0000269|PubMed:12848825, CC ECO:0000269|PubMed:14675428, ECO:0000269|PubMed:16766671, CC ECO:0000269|PubMed:17384165, ECO:0000269|PubMed:17573535, CC ECO:0000269|PubMed:18567828, ECO:0000269|PubMed:19154205, CC ECO:0000269|PubMed:19567706, ECO:0000269|PubMed:20507477, CC ECO:0000269|PubMed:8090752}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(L-cystein-S-yl)-2-(1H-indol-3-yl)-acetonitrile + 2 O2 + 2 CC reduced [NADPH--hemoprotein reductase] = camalexin + CO2 + 2 H(+) + 4 CC H2O + hydrogen cyanide + 2 oxidized [NADPH--hemoprotein reductase]; CC Xref=Rhea:RHEA:52776, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18407, ChEBI:CHEBI:22990, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:79191; CC EC=1.14.19.52; Evidence={ECO:0000269|PubMed:16766671, CC ECO:0000269|PubMed:19567706}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52777; CC Evidence={ECO:0000305|PubMed:16766671, ECO:0000305|PubMed:19567706}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(L-cystein-S-yl)-2-(1H-indol-3-yl)-acetonitrile + O2 + CC reduced [NADPH--hemoprotein reductase] = (R)-dihydrocamalexate + 2 CC H(+) + 2 H2O + hydrogen cyanide + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:10452, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18407, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:79191, ChEBI:CHEBI:79200; CC Evidence={ECO:0000269|PubMed:16766671, ECO:0000269|PubMed:19567706}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10453; CC Evidence={ECO:0000305|PubMed:16766671, ECO:0000305|PubMed:19567706}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-dihydrocamalexate + O2 + reduced [NADPH--hemoprotein CC reductase] = camalexin + CO2 + 2 H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:34807, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:22990, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:79200; Evidence={ECO:0000269|PubMed:16766671, CC ECO:0000269|PubMed:19567706}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34808; CC Evidence={ECO:0000305|PubMed:16766671, ECO:0000305|PubMed:19567706}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- INDUCTION: By salicylic acid, flagellin, oligogalacturonides, silver CC nitrate, UV-C and infection with A.alternata and various strains of CC P.syringae. Activated by the transcription factor WRKY33 upon infection CC with P.syringae. {ECO:0000269|PubMed:10590168, CC ECO:0000269|PubMed:16766671, ECO:0000269|PubMed:16769150, CC ECO:0000269|PubMed:17384165, ECO:0000269|PubMed:17573535, CC ECO:0000269|PubMed:18650934, ECO:0000269|PubMed:18790995, CC ECO:0000269|PubMed:19154205}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth CC conditions, but deficient in the phytoalexin camalexin accumulation CC upon bacterial infection and markedly increased susceptibility to CC infection by the necrotrophic fungus Alternaria brassicicola. CC {ECO:0000269|PubMed:10476063, ECO:0000269|PubMed:12848825, CC ECO:0000269|PubMed:8090752}. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB016889; BAB01230.1; -; Genomic_DNA. DR EMBL; CP002686; AEE77220.1; -; Genomic_DNA. DR EMBL; AK117967; BAC42604.1; -; mRNA. DR RefSeq; NP_189318.1; NM_113595.4. DR AlphaFoldDB; Q9LW27; -. DR SMR; Q9LW27; -. DR BioGRID; 7628; 3. DR ComplexPortal; CPX-2833; Camalexin biosynthetic metabolon complex. DR IntAct; Q9LW27; 3. DR STRING; 3702.AT3G26830.1; -. DR PaxDb; Q9LW27; -. DR ProteomicsDB; 240527; -. DR EnsemblPlants; AT3G26830.1; AT3G26830.1; AT3G26830. DR GeneID; 822298; -. DR Gramene; AT3G26830.1; AT3G26830.1; AT3G26830. DR KEGG; ath:AT3G26830; -. DR Araport; AT3G26830; -. DR TAIR; AT3G26830; PAD3. DR eggNOG; KOG0156; Eukaryota. DR HOGENOM; CLU_001570_4_1_1; -. DR InParanoid; Q9LW27; -. DR OMA; INDLECC; -. DR OrthoDB; 2900138at2759; -. DR PhylomeDB; Q9LW27; -. DR BioCyc; ARA:AT3G26830-MONOMER; -. DR BioCyc; MetaCyc:AT3G26830-MONOMER; -. DR BRENDA; 1.14.19.52; 399. DR PRO; PR:Q9LW27; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9LW27; baseline and differential. DR Genevisible; Q9LW27; AT. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010298; F:dihydrocamalexic acid decarboxylase activity; IDA:TAIR. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; ISS:TAIR. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR GO; GO:0010120; P:camalexin biosynthetic process; IDA:TAIR. DR GO; GO:0006952; P:defense response; IMP:TAIR. DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR. DR GO; GO:0009700; P:indole phytoalexin biosynthetic process; IMP:TAIR. DR GO; GO:0010112; P:regulation of systemic acquired resistance; IEP:TAIR. DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR. DR GO; GO:0009617; P:response to bacterium; IMP:TAIR. DR GO; GO:0009625; P:response to insect; IEP:TAIR. DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR. DR CDD; cd11072; CYP71-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR47956:SF50; BIFUNCTIONAL DIHYDROCAMALEXATE SYNTHASE/CAMALEXIN SYNTHASE-RELATED; 1. DR PANTHER; PTHR47956; CYTOCHROME P450 71B11-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Membrane; NADP; Oxidoreductase; Plant defense; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..490 FT /note="Bifunctional dihydrocamalexate synthase/camalexin FT synthase" FT /id="PRO_0000052093" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255" FT MUTAGEN 176 FT /note="G->E: In pad3-2." FT /evidence="ECO:0000269|PubMed:10590168" SQ SEQUENCE 490 AA; 56061 MW; B8F84D85F252668D CRC64; MSVFLCFLVL LPLILIFLNV LKPSKYKLPP GPKKLPIIGN LHQRRTLHPR NRRNLAEMYG PVALLQYGFV PVVAISSKEA AEEVLKINDL ECCSRPEAAG MRATFYNFKD IGMAPFGDEW SLMRKLSVVE LFSVKKLQSF KYIIEEENNL CVKKLSEFAT RQSPVNLERA IFTLVGNIVC RIGYGINLYE CDFFEADRVV DLVLKAEAVI RETVFSDFFP GRIGRFIDCI SGQNRRLKNN FSVVDTFFQN VLNEHLKPGR ESSTIVDLMI DMKKKQENDG DALKFTTDHL KGMISDIFVA GIGGVAGITL WGMTELIRNP RVMKKVQDEI RTTLGDKKER IKEEDLNQLH YFKLVVKETL RLHPTTPLLL PRQTMSHIKI QGYDVPAKTQ ILVNVYAMGR DPKLWENADE FNPDRFLDSS VDFKGKNYEF IPFGSGRRIC PGMTMGTILV EMALLNLLYF FDWGLAKQEE AKEIINGEEN FLAFFQVLHH //