MTOX_ECOLI
ID MTOX_ECOLI Reviewed; 372 AA.
AC P40874; Q47144;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=N-methyl-L-tryptophan oxidase;
DE Short=MTOX;
DE EC=1.5.3.-;
GN Name=solA; OrderedLocusNames=b1059, JW1046;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8973328; DOI=10.1016/s0378-1119(96)00500-8;
RA Koyama Y., Ohmori H.;
RT "Nucleotide sequence of the Escherichia coli solA gene encoding a sarcosine
RT oxidase-like protein and characterization of its product.";
RL Gene 181:179-183(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=K12 / DH1 / ATCC 33849 / DSM 4235 / NCIB 12045;
RX PubMed=10220347; DOI=10.1021/bi982955o;
RA Wagner M.A., Khanna P., Jorns M.S.;
RT "Structure of the flavocoenzyme of two homologous amine oxidases: monomeric
RT sarcosine oxidase and N-methyltryptophan oxidase.";
RL Biochemistry 38:5588-5595(1999).
RN [6]
RP CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11170472; DOI=10.1021/bi0024411;
RA Khanna P., Jorns M.S.;
RT "Characterization of the FAD-containing N-methyltryptophan oxidase from
RT Escherichia coli.";
RL Biochemistry 40:1441-1450(2001).
RN [7]
RP CHARACTERIZATION.
RX PubMed=11170473; DOI=10.1021/bi002442t;
RA Khanna P., Jorns M.S.;
RT "N-methyltryptophan oxidase from Escherichia coli: reaction kinetics with
RT N-methyl amino acid and carbinolamine substrates.";
RL Biochemistry 40:1451-1459(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-372 IN COMPLEX WITH FAD.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18186483; DOI=10.1002/prot.21898;
RA Ilari A., Bonamore A., Franceschini S., Fiorillo A., Boffi A., Colotti G.;
RT "The X-ray structure of N-methyltryptophan oxidase reveals the structural
RT determinants of substrate specificity.";
RL Proteins 71:2065-2075(2008).
CC -!- FUNCTION: Catalyzes the oxidative demethylation of N-methyl-L-
CC tryptophan. Can also use other N-methyl amino acids, including
CC sarcosine, which, however, is a poor substrate.
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;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- ACTIVITY REGULATION: Aromatic carboxylates are competitive inhibitors.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0.;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=41684; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10220347};
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MTOX subfamily.
CC {ECO:0000305}.
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DR EMBL; D31709; BAA06516.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74143.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35856.1; -; Genomic_DNA.
DR PIR; JC5371; JC5371.
DR RefSeq; NP_415577.1; NC_000913.3.
DR RefSeq; WP_000872833.1; NZ_LN832404.1.
DR PDB; 2UZZ; X-ray; 3.20 A; A/B/C/D=1-372.
DR PDBsum; 2UZZ; -.
DR AlphaFoldDB; P40874; -.
DR SMR; P40874; -.
DR BioGRID; 4261754; 81.
DR IntAct; P40874; 9.
DR STRING; 511145.b1059; -.
DR jPOST; P40874; -.
DR PaxDb; P40874; -.
DR PRIDE; P40874; -.
DR EnsemblBacteria; AAC74143; AAC74143; b1059.
DR EnsemblBacteria; BAA35856; BAA35856; BAA35856.
DR GeneID; 944983; -.
DR KEGG; ecj:JW1046; -.
DR KEGG; eco:b1059; -.
DR PATRIC; fig|1411691.4.peg.1209; -.
DR EchoBASE; EB2535; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_2_1_6; -.
DR InParanoid; P40874; -.
DR OMA; EMYSDPV; -.
DR PhylomeDB; P40874; -.
DR BioCyc; EcoCyc:SARCOX-MON; -.
DR BioCyc; MetaCyc:SARCOX-MON; -.
DR SABIO-RK; P40874; -.
DR EvolutionaryTrace; P40874; -.
DR PRO; PR:P40874; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0050131; F:N-methyl-L-amino-acid oxidase activity; IDA:EcoCyc.
DR GO; GO:0008115; F:sarcosine oxidase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..372
FT /note="N-methyl-L-tryptophan oxidase"
FT /id="PRO_0000213765"
FT BINDING 4..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MOD_RES 308
FT /note="S-8alpha-FAD cysteine"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2UZZ"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2UZZ"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 343..354
FT /evidence="ECO:0007829|PDB:2UZZ"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:2UZZ"
SQ SEQUENCE 372 AA; 40902 MW; DF5F4411D71610FD CRC64;
MKYDLIIIGS GSVGAAAGYY ATRAGLNVLM TDAHMPPHQH GSHHGDTRLI RHAYGEGEKY
VPLVLRAQTL WDELSRHNEE DPIFVRSGVI NLGPADSTFL ANVAHSAEQW QLNVEKLDAQ
GIMARWPEIR VPDNYIGLFE TDSGFLRSEL AIKTWIQLAK EAGCAQLFNC PVTAIRHDDD
GVTIETADGE YQAKKAIVCA GTWVKDLLPE LPVQPVRKVF AWYQADGRYS VKNKFPAFTG
ELPNGDQYYG FPAENDALKI GKHNGGQVIH SADERVPFAE VASDGSEAFP FLRNVLPGIG
CCLYGAACTY DNSPDEDFII DTLPGHDNTL LITGLSGHGF KFASVLGEIA ADFAQDKKSD
FDLTPFRLSR FQ
