ID G0CEL0_XANCA Unreviewed; 535 AA.
AC G0CEL0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Tryptophan 2-monooxygenase {ECO:0000256|ARBA:ARBA00017871};
DE EC=1.13.12.3 {ECO:0000256|ARBA:ARBA00012535};
GN ORFNames=XCR_3620 {ECO:0000313|EMBL:AEL08481.1};
OS Xanthomonas campestris pv. raphani 756C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL08481.1, ECO:0000313|Proteomes:UP000001633};
RN [1] {ECO:0000313|EMBL:AEL08481.1, ECO:0000313|Proteomes:UP000001633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=756C {ECO:0000313|EMBL:AEL08481.1,
RC ECO:0000313|Proteomes:UP000001633};
RX PubMed=21784931; DOI=10.1128/JB.05262-11;
RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA Leach J.E., White F.F., Salzberg S.L.;
RT "Two new complete genome sequences offer insight into host and tissue
RT specificity of plant pathogenic Xanthomonas spp.";
RL J. Bacteriol. 193:5450-5464(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = CO2 + H2O + indole-3-acetamide;
CC Xref=Rhea:RHEA:16165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16031, ChEBI:CHEBI:16526, ChEBI:CHEBI:57912;
CC EC=1.13.12.3; Evidence={ECO:0000256|ARBA:ARBA00000112};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004814}.
CC -!- SIMILARITY: Belongs to the tryptophan 2-monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00005833}.
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DR EMBL; CP002789; AEL08481.1; -; Genomic_DNA.
DR RefSeq; WP_014508856.1; NC_017271.1.
DR AlphaFoldDB; G0CEL0; -.
DR KEGG; xcp:XCR_3620; -.
DR PATRIC; fig|990315.4.peg.3412; -.
DR HOGENOM; CLU_004498_8_3_6; -.
DR Proteomes; UP000001633; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1440.240; -; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Auxin biosynthesis {ECO:0000256|ARBA:ARBA00023070};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033}.
FT DOMAIN 64..522
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 535 AA; 58622 MW; 97CBCBA0EC1DFC30 CRC64;
MQGKHTGAMT RRQLLARIGM TAGGAMMYQA MSSLGMAAES TFTGPLQLDG DAKGASVLIL
GAGLAGMTAA FELRKAGYRV QVMEYNDRPG GRNWTLRGGD RYTELGGAAQ HCQFDEGHYL
NPGPWRIPHH HRAVLSYCKQ FGVALEAFNQ VNYNALLHSQ HGFDGKPQRF RAIDADYKGH
VSELLAKCTQ QHALDSLVSS EDQQILLESL RTWGALDKRF GYVKGKDSSE RRGFARYPGG
GLSGKPEFSD PFSVQDVLRS RLWTTLAAGN NYEMQTTMFQ PVGGMDQIGK AFARQLGNAI
TYNAKVTKID QDGSGVRVSW QDAARGGAEQ VASADWCICT IPLSVLSRIP VTASDAMTTA
IGKVPYAASV KVGLQFKRRF WEEDEAIYGG ISYTDLPITL ISYPSTGYHS PGKGVLLGAY
VWGLDAYQFT SMSPEQRVRK AVEYGTQLHP QYPREFETGI AVGWHRVPFT HGCFGMWSEA
ARAEHYAPLC QIDGRLALAG EHVSYIPAWQ EGAILSAHDV VGRLHRKVLA QGARA
//
