ID   MTOX_ECOLC              Reviewed;         372 AA.
AC   B1IV43;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=EcolC_2541;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA78172.1; -; Genomic_DNA.
DR   RefSeq; WP_000872811.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IV43; -.
DR   SMR; B1IV43; -.
DR   KEGG; ecl:EcolC_2541; -.
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_1000081636"
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;  40886 MW;  5EA8CAB8DA7AB967 CRC64;
     MKYDLIIIGS GSVGAAAGYY ATRAGLNVLM TDAHMPPHQH GSHHGDTRLI RHAYGEGEKY
     VPLVLRAQTL 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