ID   MTOX_ECOSE              Reviewed;         372 AA.
AC   B6I9D6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=N-methyl-L-tryptophan oxidase {ECO:0000255|HAMAP-Rule:MF_00515};
DE            Short=MTOX {ECO:0000255|HAMAP-Rule:MF_00515};
DE            EC=1.5.3.- {ECO:0000255|HAMAP-Rule:MF_00515};
GN   Name=solA {ECO:0000255|HAMAP-Rule:MF_00515}; OrderedLocusNames=ECSE_1122;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
CC   -!- FUNCTION: Catalyzes the oxidative demethylation of N-methyl-L-
CC       tryptophan. {ECO:0000255|HAMAP-Rule:MF_00515}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(alpha)-methyl-L-tryptophan + O2 = formaldehyde + H2O2
CC         + L-tryptophan; Xref=Rhea:RHEA:28006, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:57283, ChEBI:CHEBI:57912; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00515};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00515};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00515};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00515}.
CC   -!- SIMILARITY: Belongs to the MSOX/MTOX family. MTOX subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00515}.
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DR   EMBL; AP009240; BAG76646.1; -; Genomic_DNA.
DR   RefSeq; WP_000872815.1; NC_011415.1.
DR   AlphaFoldDB; B6I9D6; -.
DR   SMR; B6I9D6; -.
DR   EnsemblBacteria; BAG76646; BAG76646; ECSE_1122.
DR   KEGG; ecy:ECSE_1122; -.
DR   HOGENOM; CLU_007884_2_1_6; -.
DR   OMA; EMYSDPV; -.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050131; F:N-methyl-L-amino-acid oxidase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_00515; MTOX; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023493; Me_Trp_Oxase_MTOX.
DR   InterPro; IPR045170; MTOX.
DR   PANTHER; PTHR10961; PTHR10961; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..372
FT                   /note="N-methyl-L-tryptophan oxidase"
FT                   /id="PRO_1000127440"
FT   BINDING         4..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00515"
FT   MOD_RES         308
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00515"
SQ   SEQUENCE   372 AA;  40914 MW;  41B0CDB0D562BE67 CRC64;
     MKYDLIIIGS GSVGAAAGYY ATRAGLNVLM TDAHMPPHQH GSHHGDTRLI RHAYGEGEKY
     VPLVLRAQTL WDELSRHNED DPIFVRSGVI NLGPADSAFL ANVAHSAEQW QLNVEKLDAQ
     GIMARWPEIR VPDNYIGLFE TDSGFLRSEL AIKTWIQLAK EAGCAQLFNC PVTAIRHDDD
     GVTIETVDGE YQAKKAIVCA GTWVKDLLPE LPVQPVRKVF AWYQADGRYS VKNKFPAFTG
     ELPNGDQYYG FPAENDALKI GKHNGGQVIH SADERVPFAE VVSDGSEAFP FLRNVLPGIG
     CCLYGAACTY DNSPDEDFII DTLPGHDNTL LITGLSGHGF KFASVLGEIA ADFAQDKKSD
     FDLTPFRLSR FQ