ID   MTOX_ECO45              Reviewed;         372 AA.
AC   B7MIK0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=ECS88_1073;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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}.
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DR   EMBL; CU928161; CAR02400.1; -; Genomic_DNA.
DR   RefSeq; WP_000872794.1; NC_011742.1.
DR   AlphaFoldDB; B7MIK0; -.
DR   SMR; B7MIK0; -.
DR   EnsemblBacteria; CAR02400; CAR02400; ECS88_1073.
DR   KEGG; ecz:ECS88_1073; -.
DR   HOGENOM; CLU_007884_2_1_6; -.
DR   OMA; EMYSDPV; -.
DR   Proteomes; UP000000747; 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_1000127434"
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;  40916 MW;  F42E15656ECC6889 CRC64;
     MKYDLIIIGS GSVGAAAGYY ATRAGLNVLM TDAHMPPHQH GSHHGDTRLI RHAYGEGEKY
     VPLVLRAQML WDELSRHNED DPIFVRSGVI NLGPADSAFL ANVAHSAEQW QLNVEKLDAQ
     GIMARWPEIR VPDNYIGLFE TDSGFLRSEL AIKTWIQLAK EAGCAQLFNC PVTAIRHDDD
     GVTIETADGE YQAKKAIVCA GTWVKDLLPE LPVQPVRKVF AWYQADGRYS VKNKFPAFTG
     ELPNGDQYYG FPAENDALKI GKHNGGQVIH SADERVPFAE VVSDGSEAFP FLRNVLPGIG
     CCLYGAACTY DNSPDEDFII DTLPGHDNTL LITGLSGHGF KFASVLGEIA ADFAQDKKSD
     FDLTPFRLSR FQ