ID   TR2M_PANAY              Reviewed;         562 AA.
AC   Q47861;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Tryptophan 2-monooxygenase;
DE            EC=1.13.12.3;
GN   Name=iaaM;
OS   Pantoea agglomerans pv. gypsophilae (Erwinia herbicola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=48984;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PD713;
RA   Gafni Y., Manulis S., Kunik T., Lichter A.L., Barash I.B., Ophir Y.;
RT   "Characterization of the auxin synthesis genes of Erwinia herbicola pv.
RT   gypsophilae.";
RL   Isr. J. Plant Sci. 45:279-284(1997).
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;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250};
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC   -!- SIMILARITY: Belongs to the tryptophan 2-monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; L33867; AAC17187.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47861; -.
DR   SMR; Q47861; -.
DR   PRIDE; Q47861; -.
DR   UniPathway; UPA00151; -.
DR   GO; GO:0050361; F:tryptophan 2-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Auxin biosynthesis; Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..562
FT                   /note="Tryptophan 2-monooxygenase"
FT                   /id="PRO_0000065589"
FT   BINDING         54
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   562 AA;  62513 MW;  621E7AA389DDF886 CRC64;
     MKPHSVFADS LWPSIDLLYD YAPFLQQSMV DGHIGFFPTG ITPPRVAIIG AGISGLIAAT
     ELLRAGVRDI TLFEARDRLG GRAWSQLFDP HYYPRLIAEM GAMRFPPSAT GLFHYLNRFS
     IQTSASFPDP GIVDTELHYR GVRHLWPAGE QPPALFTRVH NGWRALLYEG CLLDGVSLVG
     PLQITAMLKS ERFDEAAEAW QIWLNVFRDC SFYSAMVTIF TGTNPPGGIA WERRDDFELF
     GALGIGSGGF LPVYQAGFTE ILRMVINGYE DDQRLIIGGI STLAEQLARQ EIRGTTPGRH
     VRFSKVNRIS KDNGKISLAT DVKPVDAFDR VIVTSNNRAM QMVHGLSADE TFLNQDVCRA
     VRETHLTGSS KLFMLTRDKF WLKNKLPLTI QSDGLVRGVY VLDYESDNPE GRGVVLLSYT
     WEDDAHKLLA ITDKKQRGQH LVDELSAIHP EFARYLVPAG ADYERYVLHH DWLTDPCSAG
     AFKLNYPGED VYSQRLFFQF KTANHPEQDS GLLLAGCGCS FTGGWVEGAV QTAVNSACAV
     IRSTGGTLYG NPLDSVHSIY DY