MTOX_YERPY
ID MTOX_YERPY Reviewed; 371 AA.
AC B1JHH1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=YPK_1672;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
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; CP000950; ACA67965.1; -; Genomic_DNA.
DR RefSeq; WP_002211850.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JHH1; -.
DR SMR; B1JHH1; -.
DR EnsemblBacteria; ACA67965; ACA67965; YPK_1672.
DR GeneID; 66845091; -.
DR KEGG; ypy:YPK_1672; -.
DR PATRIC; fig|502800.11.peg.2332; -.
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..371
FT /note="N-methyl-L-tryptophan oxidase"
FT /id="PRO_1000127453"
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 371 AA; 40467 MW; 4376B8954E78DC6E CRC64;
MDYDLIVIGS GSVGSAAGYY ASQAGLNVLM IDSAMPPHQA GSHHGETRIM RHAYGEGEKY
VPLVLRAQAL WDQLAAQTGE KLFQACGVIN LGPDNSTFLQ NVQRSAQQYD LPVETLNSTQ
IREKWPVFTV PDNYIAVFEP QSGYLRSELA VKTLIKAVTE AGCGILFNCP VTAIESHQAG
VDVVTIDGTY SATKVVVTAG TWVKELLPTL PVTPVRKVFS WHQADGRYSE ANHFPAFTVE
MPDNILYYGF PAQNDALKLG KHHGGQLIES AAQRKPFGRY AEDGTEVFSF LRHFLPGVGV
CLRGEACSYD MSPDEDFIID TLPEDERVMV VSGLSGHGFK FATALGEVAA LFAQDKPSPI
DISAFSLARF R