ID   MTOX_ECOBW              Reviewed;         372 AA.
AC   C4ZRZ9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=BWG_0907;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001396; ACR63915.1; -; Genomic_DNA.
DR   RefSeq; WP_000872833.1; NC_012759.1.
DR   AlphaFoldDB; C4ZRZ9; -.
DR   SMR; C4ZRZ9; -.
DR   KEGG; ebw:BWG_0907; -.
DR   HOGENOM; CLU_007884_2_1_6; -.
DR   OMA; EMYSDPV; -.
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_1000206630"
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;  40902 MW;  DF5F4411D71610FD CRC64;
     MKYDLIIIGS GSVGAAAGYY ATRAGLNVLM TDAHMPPHQH GSHHGDTRLI RHAYGEGEKY
     VPLVLRAQTL WDELSRHNEE DPIFVRSGVI NLGPADSTFL ANVAHSAEQW QLNVEKLDAQ
     GIMARWPEIR VPDNYIGLFE TDSGFLRSEL AIKTWIQLAK EAGCAQLFNC PVTAIRHDDD
     GVTIETADGE YQAKKAIVCA GTWVKDLLPE LPVQPVRKVF AWYQADGRYS VKNKFPAFTG
     ELPNGDQYYG FPAENDALKI GKHNGGQVIH SADERVPFAE VASDGSEAFP FLRNVLPGIG
     CCLYGAACTY DNSPDEDFII DTLPGHDNTL LITGLSGHGF KFASVLGEIA ADFAQDKKSD
     FDLTPFRLSR FQ