ID   A0A158K593_9BURK        Unreviewed;       522 AA.
AC   A0A158K593;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Tryptophan 2-monooxygenase {ECO:0000256|ARBA:ARBA00017871};
DE            EC=1.13.12.3 {ECO:0000256|ARBA:ARBA00012535};
GN   Name=rebO {ECO:0000313|EMBL:SAL75889.1};
GN   ORFNames=AWB68_04867 {ECO:0000313|EMBL:SAL75889.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL75889.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; FCON02000062; SAL75889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158K593; -.
DR   Proteomes; UP000054770; Unassembled WGS sequence.
DR   GO; GO:0050361; F:tryptophan 2-monooxygenase activity; IEA:RHEA.
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   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.
PE   3: Inferred from homology;
KW   Auxin biosynthesis {ECO:0000256|ARBA:ARBA00023070};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000313|EMBL:SAL75889.1}.
FT   DOMAIN          56..511
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   522 AA;  57046 MW;  394BF8649E825E93 CRC64;
     MSRRHLLTLI GKNLGAAAMM QGMGTLGFAA ASTYAGPIRL DGAPKGTRIL VLGAGMAGLV
     AAFELRNAGY HVQVLEYNDR AGGRAWTVRG GDRYTELGGA TQYCDFADGL YLNPGPWRIP
     YHHQGVLDYA KRLKVPLEPF IQVNYNAYLH STEAFGGKPQ RFRAVQTDYQ GYIAELLSKA
     IRKDALDDAL SVEDAHLLLE SLRQWGALDR DGRYQAGRRS SERRGFATAH GGGLMPKAVP
     STLLPRDPLL ASSLWQWLSS GNEQDFQSTI FQPVGGMDRI AHALHSQVAN AVVFNARVTA
     ILQDERGVTV RYTDTTTRTE RNAHADWLVC TIPLSILSQI DMAVGPAMRA AIDAVPYETS
     VKVGLQFGRR FWEEDEQIYG GITHTDLPIS AIGYPATGYG STGPAVLLGA YMWGPASYEM
     GALPPAERIA VALSQGSQIH PQYAREYQNG FAMSWSRSPF TNGCFAAWTE ALRKAHYANL
     CQIDGRIILA GEHASHIPAW QEGAVLSSLD AITRLHRRIV NG
//