MTOX_YERPE
ID MTOX_YERPE Reviewed; 371 AA.
AC P58526; Q0WE76;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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};
GN OrderedLocusNames=YPO2448, y1742, YP_2268;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL21076.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85310.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62474.1; -; Genomic_DNA.
DR PIR; AI0298; AI0298.
DR RefSeq; WP_002211850.1; NZ_VWRZ01000013.1.
DR RefSeq; YP_002347412.1; NC_003143.1.
DR AlphaFoldDB; P58526; -.
DR SMR; P58526; -.
DR IntAct; P58526; 6.
DR STRING; 214092.YPO2448; -.
DR PaxDb; P58526; -.
DR DNASU; 1146689; -.
DR EnsemblBacteria; AAM85310; AAM85310; y1742.
DR EnsemblBacteria; AAS62474; AAS62474; YP_2268.
DR GeneID; 66845091; -.
DR KEGG; ype:YPO2448; -.
DR KEGG; ypk:y1742; -.
DR KEGG; ypm:YP_2268; -.
DR PATRIC; fig|214092.21.peg.2860; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_2_1_6; -.
DR OMA; EMYSDPV; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..371
FT /note="N-methyl-L-tryptophan oxidase"
FT /id="PRO_0000213771"
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"
FT CONFLICT 349
FT /note="A -> T (in Ref. 2; AAM85310)"
FT /evidence="ECO:0000305"
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
