MTOX_SHIF8
ID MTOX_SHIF8 Reviewed; 372 AA.
AC Q0T5X2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=SFV_1082;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF03293.1; -; Genomic_DNA.
DR RefSeq; WP_000872813.1; NC_008258.1.
DR AlphaFoldDB; Q0T5X2; -.
DR SMR; Q0T5X2; -.
DR EnsemblBacteria; ABF03293; ABF03293; SFV_1082.
DR GeneID; 58391670; -.
DR KEGG; sfv:SFV_1082; -.
DR HOGENOM; CLU_007884_2_1_6; -.
DR OMA; QEQPAHF; -.
DR BioCyc; SFLE373384:SFV_RS05995-MON; -.
DR Proteomes; UP000000659; 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_1000050794"
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; 85C0DBD7C313D96D 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 VASDGSEAFP FLRNVLPGIG
CCLYGAACTY DNSPDEDFII DTLPGHDNTL LITGLSGHGF KFASVLGEIA ADFAQDQKSD
FDLTPFRLSR FQ
