O81346 (C79B2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan N-monooxygenase 1
EC=1.14.13.125

Alternative name(s):
Cytochrome P450 79B2
Tryptophan N-hydroxylase 1

Gene names

Name:	CYP79B2
Ordered Locus Names:	At4g39950
ORF Names:	T5J17.120

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts tryptophan to indole-3-acetaldoxime, a precursor for tryptophan derived glucosinolates and indole-3-acetic acid (IAA). Ref.5 Ref.6
Catalytic activity	L-tryptophan + 2 NADPH + 2 O2 = indole-3-acetaldoxime + 2 NADP+ + 3 H2O + CO2. Ref.6
Cofactor	Heme group By similarity.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Tissue specificity	Found in all tissues tested. Highest expression in roots, and low expression in stem. Ref.5
Sequence similarities	Belongs to the cytochrome P450 family.
Biophysicochemical properties	Kinetic parameters: KM=21 µM for tryptophan Ref.5

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	camalexin biosynthetic process Traceable author statement PubMed 16167893. Source: TAIR defense response by callose deposition in cell wall Inferred from mutant phenotype PubMed 19095898. Source: TAIR defense response to oomycetes Inferred from genetic interaction PubMed 20230487. Source: TAIR indoleacetic acid biosynthetic process Inferred from mutant phenotype PubMed 15772288. Source: TAIR induced systemic resistance Inferred from mutant phenotype PubMed 23073694. Source: TAIR response to insect Inferred from expression pattern PubMed 23144921. Source: TAIR response to water deprivation Inferred from expression pattern PubMed 23144921. Source: TAIR tryptophan catabolic process Inferred from direct assay Ref.6. Source: TAIR
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 541	541	Tryptophan N-monooxygenase 1		PRO_0000052154
Regions
	Transmembrane	21 – 41	21	Helical; Potential
Sites
	Metal binding	477	1	Iron (heme axial ligand) By similarity
Experimental info
	Mutagenesis	477	1	C → A: Complete loss of activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O81346 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 190C26D2FC2E5C08	FASTA	541	61,348
	10 20 30 40 50 60 MNTFTSNSSD LTTTATETSS FSTLYLLSTL QAFVAITLVM LLKKLMTDPN KKKPYLPPGP 70 80 90 100 110 120 TGWPIIGMIP TMLKSRPVFR WLHSIMKQLN TEIACVKLGN THVITVTCPK IAREILKQQD 130 140 150 160 170 180 ALFASRPLTY AQKILSNGYK TCVITPFGDQ FKKMRKVVMT ELVCPARHRW LHQKRSEEND 190 200 210 220 230 240 HLTAWVYNMV KNSGSVDFRF MTRHYCGNAI KKLMFGTRTF SKNTAPDGGP TVEDVEHMEA 250 260 270 280 290 300 MFEALGFTFA FCISDYLPML TGLDLNGHEK IMRESSAIMD KYHDPIIDER IKMWREGKRT 310 320 330 340 350 360 QIEDFLDIFI SIKDEQGNPL LTADEIKPTI KELVMAAPDN PSNAVEWAMA EMVNKPEILR 370 380 390 400 410 420 KAMEEIDRVV GKERLVQESD IPKLNYVKAI LREAFRLHPV AAFNLPHVAL SDTTVAGYHI 430 440 450 460 470 480 PKGSQVLLSR YGLGRNPKVW ADPLCFKPER HLNECSEVTL TENDLRFISF STGKRGCAAP 490 500 510 520 530 540 ALGTALTTMM LARLLQGFTW KLPENETRVE LMESSHDMFL AKPLVMVGDL RLPEHLYPTV K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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.
[4]	"The presence of CYP79 homologues in glucosinolate-producing plants shows evolutionary conservation of the enzymes in the conversion of amino acid to aldoxime in the biosynthesis of cyanogenic glucosides and glucosinolates." Bak S., Nielsen H.L., Halkier B.A. Plant Mol. Biol. 38:725-734(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 160-541.
[5]	"Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid." Mikkelsen M.D., Hansen C.H., Wittstock U., Halkier B.A. J. Biol. Chem. 275:33712-33717(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis." Hull A.K., Vij R., Celenza J.L. Proc. Natl. Acad. Sci. U.S.A. 97:2379-2384(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-477.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL035708 Genomic DNA. Translation: CAB38908.1. AL161596 Genomic DNA. Translation: CAB80658.1. CP002687 Genomic DNA. Translation: AEE87143.1. AF069495 mRNA. Translation: AAD03416.1. AY046017 mRNA. Translation: AAK76691.1. AY091437 mRNA. Translation: AAM14376.1.
IPI	IPI00548595.
PIR	T06101. T51718.
RefSeq	NP_195705.1. NM_120158.2.
UniGene	At.20632.
3D structure databases
ProteinModelPortal	O81346.
SMR	O81346. Positions 57-526.
ModBase	Search...
Protein-protein interaction databases
IntAct	O81346. 1 interaction.
STRING	3702.AT4G39950.1-P.
Proteomic databases
PaxDb	O81346.
PRIDE	O81346.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G39950.1; AT4G39950.1; AT4G39950.
GeneID	830154.
KEGG	ath:AT4G39950.
Organism-specific databases
GeneFarm	1316. 94.
TAIR	At4g39950.
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000218628.
InParanoid	O81346.
KO	K11812.
OMA	KLPENET.
PhylomeDB	O81346.
ProtClustDB	PLN02971.
Enzyme and pathway databases
BioCyc	MetaCyc:AT4G39950-MONOMER.
Gene expression databases
Genevestigator	O81346.
GermOnline	AT4G39950. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C79B2_ARATH

Accession

Primary (citable) accession number: O81346
Secondary accession number(s): Q9SMR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program