MTOX_SHIBS
ID MTOX_SHIBS Reviewed; 372 AA.
AC Q31ZB5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SBO_2005;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000036; ABB66593.1; -; Genomic_DNA.
DR RefSeq; WP_000872815.1; NC_007613.1.
DR AlphaFoldDB; Q31ZB5; -.
DR SMR; Q31ZB5; -.
DR EnsemblBacteria; ABB66593; ABB66593; SBO_2005.
DR KEGG; sbo:SBO_2005; -.
DR HOGENOM; CLU_007884_2_1_6; -.
DR OMA; EMYSDPV; -.
DR Proteomes; UP000007067; 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_0000259023"
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
