C79B2_ARATH
ID C79B2_ARATH Reviewed; 541 AA.
AC O81346; Q9SMR0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Tryptophan N-monooxygenase 1;
DE EC=1.14.14.156 {ECO:0000269|PubMed:10681464};
DE AltName: Full=Cytochrome P450 79B2;
DE AltName: Full=Tryptophan N-hydroxylase 1;
GN Name=CYP79B2; OrderedLocusNames=At4g39950; ORFNames=T5J17.120;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 160-541.
RX PubMed=9862490; DOI=10.1023/a:1006064202774;
RA Bak S., Nielsen H.L., Halkier B.A.;
RT "The presence of CYP79 homologues in glucosinolate-producing plants shows
RT evolutionary conservation of the enzymes in the conversion of amino acid to
RT aldoxime in the biosynthesis of cyanogenic glucosides and glucosinolates.";
RL Plant Mol. Biol. 38:725-734(1998).
RN [5]
RP FUNCTION, CHARACTERIZATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10922360; DOI=10.1074/jbc.m001667200;
RA Mikkelsen M.D., Hansen C.H., Wittstock U., Halkier B.A.;
RT "Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of
RT tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates
RT and indole-3-acetic acid.";
RL J. Biol. Chem. 275:33712-33717(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-477.
RX PubMed=10681464; DOI=10.1073/pnas.040569997;
RA Hull A.K., Vij R., Celenza J.L.;
RT "Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-
RT dependent indole-3-acetic acid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2379-2384(2000).
RN [7]
RP FUNCTION.
RX PubMed=26352477; DOI=10.1038/nature14907;
RA Rajniak J., Barco B., Clay N.K., Sattely E.S.;
RT "A new cyanogenic metabolite in Arabidopsis required for inducible pathogen
RT defence.";
RL Nature 525:376-379(2015).
CC -!- FUNCTION: Converts tryptophan to indole-3-acetaldoxime, a precursor for
CC tryptophan-derived glucosinolates and indole-3-acetic acid (IAA)
CC (PubMed:10681464, PubMed:10922360). Involved in the biosynthetic
CC pathway to 4-hydroxyindole-3-carbonyl nitrile (4-OH-ICN), a cyanogenic
CC metabolite required for inducible pathogen defense (PubMed:26352477).
CC {ECO:0000269|PubMed:10681464, ECO:0000269|PubMed:10922360,
CC ECO:0000269|PubMed:26352477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + 2 O2 + 2 reduced [NADPH--hemoprotein reductase]
CC = (E)-(indol-3-yl)acetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:33279,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17545, ChEBI:CHEBI:57618, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58210; EC=1.14.14.156;
CC Evidence={ECO:0000269|PubMed:10681464};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for tryptophan {ECO:0000269|PubMed:10922360};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Found in all tissues tested. Highest expression in
CC roots, and low expression in stem. {ECO:0000269|PubMed:10922360}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AL035708; CAB38908.1; -; Genomic_DNA.
DR EMBL; AL161596; CAB80658.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87143.1; -; Genomic_DNA.
DR EMBL; AF069495; AAD03416.1; -; mRNA.
DR EMBL; AY046017; AAK76691.1; -; mRNA.
DR EMBL; AY091437; AAM14376.1; -; mRNA.
DR PIR; T06101; T06101.
DR PIR; T51718; T51718.
DR RefSeq; NP_195705.1; NM_120158.2.
DR AlphaFoldDB; O81346; -.
DR SMR; O81346; -.
DR BioGRID; 15434; 2.
DR IntAct; O81346; 2.
DR STRING; 3702.AT4G39950.1; -.
DR iPTMnet; O81346; -.
DR PaxDb; O81346; -.
DR PRIDE; O81346; -.
DR ProteomicsDB; 239140; -.
DR EnsemblPlants; AT4G39950.1; AT4G39950.1; AT4G39950.
DR GeneID; 830154; -.
DR Gramene; AT4G39950.1; AT4G39950.1; AT4G39950.
DR KEGG; ath:AT4G39950; -.
DR Araport; AT4G39950; -.
DR TAIR; locus:2140020; AT4G39950.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; O81346; -.
DR OMA; PANDPWI; -.
DR PhylomeDB; O81346; -.
DR BioCyc; ARA:AT4G39950-MON; -.
DR BioCyc; MetaCyc:AT4G39950-MON; -.
DR BRENDA; 1.14.14.156; 399.
DR SABIO-RK; O81346; -.
DR PRO; PR:O81346; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81346; baseline and differential.
DR Genevisible; O81346; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0010120; P:camalexin biosynthetic process; TAS:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0002229; P:defense response to oomycetes; IGI:TAIR.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP: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 GO; GO:0006569; P:tryptophan catabolic process; IDA:TAIR.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..541
FT /note="Tryptophan N-monooxygenase 1"
FT /id="PRO_0000052154"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 477
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"
FT MUTAGEN 477
FT /note="C->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10681464"
SQ SEQUENCE 541 AA; 61348 MW; 190C26D2FC2E5C08 CRC64;
MNTFTSNSSD LTTTATETSS FSTLYLLSTL QAFVAITLVM LLKKLMTDPN KKKPYLPPGP
TGWPIIGMIP TMLKSRPVFR WLHSIMKQLN TEIACVKLGN THVITVTCPK IAREILKQQD
ALFASRPLTY AQKILSNGYK TCVITPFGDQ FKKMRKVVMT ELVCPARHRW LHQKRSEEND
HLTAWVYNMV KNSGSVDFRF MTRHYCGNAI KKLMFGTRTF SKNTAPDGGP TVEDVEHMEA
MFEALGFTFA FCISDYLPML TGLDLNGHEK IMRESSAIMD KYHDPIIDER IKMWREGKRT
QIEDFLDIFI SIKDEQGNPL LTADEIKPTI KELVMAAPDN PSNAVEWAMA EMVNKPEILR
KAMEEIDRVV GKERLVQESD IPKLNYVKAI LREAFRLHPV AAFNLPHVAL SDTTVAGYHI
PKGSQVLLSR YGLGRNPKVW ADPLCFKPER HLNECSEVTL TENDLRFISF STGKRGCAAP
ALGTALTTMM LARLLQGFTW KLPENETRVE LMESSHDMFL AKPLVMVGDL RLPEHLYPTV
K
