ID F4TCW8_ECOLX Unreviewed; 372 AA.
AC F4TCW8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=N-methyl-L-tryptophan oxidase {ECO:0000256|HAMAP-Rule:MF_00515};
DE Short=MTOX {ECO:0000256|HAMAP-Rule:MF_00515};
DE EC=1.5.3.- {ECO:0000256|HAMAP-Rule:MF_00515};
GN Name=solA {ECO:0000256|HAMAP-Rule:MF_00515};
GN ORFNames=ECJG_00543 {ECO:0000313|EMBL:EGI22448.1};
OS Escherichia coli M718.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656419 {ECO:0000313|EMBL:EGI22448.1, ECO:0000313|Proteomes:UP000002790};
RN [1] {ECO:0000313|EMBL:EGI22448.1, ECO:0000313|Proteomes:UP000002790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M718 {ECO:0000313|EMBL:EGI22448.1,
RC ECO:0000313|Proteomes:UP000002790};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli M718.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidative demethylation of N-methyl-L-
CC tryptophan. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00515};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00515};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_00515};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00515}.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MTOX subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00515}.
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DR EMBL; GL884111; EGI22448.1; -; Genomic_DNA.
DR RefSeq; WP_000872806.1; NZ_GL884111.1.
DR AlphaFoldDB; F4TCW8; -.
DR HOGENOM; CLU_007884_2_1_6; -.
DR Proteomes; UP000002790; Unassembled WGS sequence.
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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR PANTHER; PTHR10961:SF7; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_00515};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00515};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00515}.
FT DOMAIN 4..352
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 4..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00515"
FT MOD_RES 308
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00515"
SQ SEQUENCE 372 AA; 40872 MW; 198956F76E81EFE2 CRC64;
MKYDLIIIGS GSVGAAAGYY ATRAGLNVLM TDAHMPPHQH GSHHGDTRLI RHAYGEGEKY
VPLVLRAQTL WDELSRHNED DPIFVRSGVI NLGPADSAFL ANVAHSAEQW QLNVEKLDAQ
GIMARWPEIR VPDNYIGLFE TDSGFLRSEL AIKTWIQLAK EAGCAQLFNC PVTAIRHDDD
GVTIETADGE YQAKKAIVCA GTWVKDLLPE LPVQPVRKVF AWYQADGRYS VKNKFPAFTG
ELPNGDQYYG FPAENDALKI GKHNGGQIIH SADERVPFAE VASDGSEAFP FLRNVLPGIG
CCLYGAACTY DNSPDEDFII DTLPGHDNTL LITGLSGHGF KFASVLGEIA ADFAQDKKSD
FDLTPFRLSR FQ
//
