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MTOX_SALTY
ID   MTOX_SALTY              Reviewed;         372 AA.
AC   P58525;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=STM1160;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL20090.1; -; Genomic_DNA.
DR   RefSeq; NP_460131.1; NC_003197.2.
DR   RefSeq; WP_000872773.1; NC_003197.2.
DR   AlphaFoldDB; P58525; -.
DR   SMR; P58525; -.
DR   STRING; 99287.STM1160; -.
DR   PaxDb; P58525; -.
DR   EnsemblBacteria; AAL20090; AAL20090; STM1160.
DR   GeneID; 1252678; -.
DR   KEGG; stm:STM1160; -.
DR   PATRIC; fig|99287.12.peg.1228; -.
DR   HOGENOM; CLU_007884_2_1_6; -.
DR   OMA; EMYSDPV; -.
DR   PhylomeDB; P58525; -.
DR   BioCyc; SENT99287:STM1160-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   GO; GO:0008115; F:sarcosine oxidase activity; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..372
FT                   /note="N-methyl-L-tryptophan oxidase"
FT                   /id="PRO_0000213769"
FT   BINDING         4..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00515"
FT   MOD_RES         307
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00515"
SQ   SEQUENCE   372 AA;  40664 MW;  D5153BE90D6E6C00 CRC64;
     MKYDLIIIGS GSVGAAAGYY ATRAGLKVLM TDAHMPPHQQ GSHHGDTRLI RHAYGEGEKY
     VPLVLRAQTL WDELSTHNEE PIFVRSGVVN LGPADSAFLA NVARSAQQWQ LNVERLDATA
     LMTRWPEIRV PDNYIGLFEA DSGFLRSELA ITTWLRLARE AGCAQLFNSP VSHIHHDDNG
     VTIETSEGCY HASKALISAG TWVKALVPEL PVQPVRKVFA WFKADGRYST KNRFPAFTGE
     MPNGDQYYGF PAENDELKIG KHNGGQLIQA PEERKPFAAV ASDGAEAFPF LRNVLPGIGG
     CLHGAACTYD NSPDEDFIID TLPGHENTLV ITGLSGHGFK FAPVLGEIAA DFALGKTPSF
     DLTPFRLSRF SQ
 
 
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