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Protein

N-methyl-L-tryptophan oxidase

Gene

solA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative demethylation of N-methyl-L-tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate.

Catalytic activityi

N-methyl-L-tryptophan + H2O + O2 = L-tryptophan + formaldehyde + H2O2.

Cofactori

FADNote: Binds 1 FAD per subunit.

Enzyme regulationi

Aromatic carboxylates are competitive inhibitors.

pH dependencei

Optimum pH is 8.0.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 3431FADSequence analysisAdd
BLAST

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoCyc
  • N-methyl-L-amino-acid oxidase activity Source: EcoCyc

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:SARCOX-MONOMER.
ECOL316407:JW1046-MONOMER.
MetaCyc:SARCOX-MONOMER.
SABIO-RKP40874.

Names & Taxonomyi

Protein namesi
Recommended name:
N-methyl-L-tryptophan oxidase (EC:1.5.3.-)
Short name:
MTOX
Gene namesi
Name:solA
Ordered Locus Names:b1059, JW1046
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12669. solA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372N-methyl-L-tryptophan oxidasePRO_0000213765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei308 – 3081S-8alpha-FAD cysteine

Proteomic databases

EPDiP40874.
PaxDbiP40874.
PRIDEiP40874.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi4261754. 77 interactions.
IntActiP40874. 9 interactions.
STRINGi511145.b1059.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi12 – 2312Combined sources
Beta strandi28 – 314Combined sources
Beta strandi36 – 427Combined sources
Beta strandi45 – 506Combined sources
Helixi58 – 603Combined sources
Helixi61 – 7616Combined sources
Beta strandi79 – 813Combined sources
Beta strandi83 – 853Combined sources
Beta strandi89 – 946Combined sources
Helixi98 – 10912Combined sources
Beta strandi114 – 1185Combined sources
Helixi119 – 1257Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi144 – 1474Combined sources
Helixi148 – 16114Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi179 – 18810Combined sources
Beta strandi190 – 1989Combined sources
Helixi201 – 2066Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi220 – 2234Combined sources
Helixi227 – 2293Combined sources
Turni231 – 2344Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi258 – 2647Combined sources
Helixi272 – 2743Combined sources
Helixi284 – 2863Combined sources
Helixi289 – 2957Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi320 – 3234Combined sources
Beta strandi326 – 3327Combined sources
Helixi340 – 3423Combined sources
Helixi343 – 35412Combined sources
Helixi364 – 3663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UZZX-ray3.20A/B/C/D1-372[»]
ProteinModelPortaliP40874.
SMRiP40874. Positions 1-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40874.

Family & Domainsi

Sequence similaritiesi

Belongs to the MSOX/MTOX family. MTOX subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105F76. Bacteria.
COG0665. LUCA.
HOGENOMiHOG000236098.
InParanoidiP40874.
KOiK02846.
OMAiDGDYQAK.
OrthoDBiEOG6DNT6G.
PhylomeDBiP40874.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
HAMAPiMF_00515. MTOX.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR023493. Me_Trp_Oxase_MTOX.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P40874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYDLIIIGS GSVGAAAGYY ATRAGLNVLM TDAHMPPHQH GSHHGDTRLI
60 70 80 90 100
RHAYGEGEKY VPLVLRAQTL WDELSRHNEE DPIFVRSGVI NLGPADSTFL
110 120 130 140 150
ANVAHSAEQW QLNVEKLDAQ GIMARWPEIR VPDNYIGLFE TDSGFLRSEL
160 170 180 190 200
AIKTWIQLAK EAGCAQLFNC PVTAIRHDDD GVTIETADGE YQAKKAIVCA
210 220 230 240 250
GTWVKDLLPE LPVQPVRKVF AWYQADGRYS VKNKFPAFTG ELPNGDQYYG
260 270 280 290 300
FPAENDALKI GKHNGGQVIH SADERVPFAE VASDGSEAFP FLRNVLPGIG
310 320 330 340 350
CCLYGAACTY DNSPDEDFII DTLPGHDNTL LITGLSGHGF KFASVLGEIA
360 370
ADFAQDKKSD FDLTPFRLSR FQ
Length:372
Mass (Da):40,902
Last modified:November 1, 1997 - v1
Checksum:iDF5F4411D71610FD
GO

Mass spectrometryi

Molecular mass is 41684 Da from positions 1 - 372. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31709 Genomic DNA. Translation: BAA06516.1.
U00096 Genomic DNA. Translation: AAC74143.1.
AP009048 Genomic DNA. Translation: BAA35856.1.
PIRiJC5371.
RefSeqiNP_415577.1. NC_000913.3.
WP_000872833.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74143; AAC74143; b1059.
BAA35856; BAA35856; BAA35856.
GeneIDi944983.
KEGGiecj:JW1046.
eco:b1059.
PATRICi32117357. VBIEscCol129921_1101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31709 Genomic DNA. Translation: BAA06516.1.
U00096 Genomic DNA. Translation: AAC74143.1.
AP009048 Genomic DNA. Translation: BAA35856.1.
PIRiJC5371.
RefSeqiNP_415577.1. NC_000913.3.
WP_000872833.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UZZX-ray3.20A/B/C/D1-372[»]
ProteinModelPortaliP40874.
SMRiP40874. Positions 1-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261754. 77 interactions.
IntActiP40874. 9 interactions.
STRINGi511145.b1059.

Proteomic databases

EPDiP40874.
PaxDbiP40874.
PRIDEiP40874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74143; AAC74143; b1059.
BAA35856; BAA35856; BAA35856.
GeneIDi944983.
KEGGiecj:JW1046.
eco:b1059.
PATRICi32117357. VBIEscCol129921_1101.

Organism-specific databases

EchoBASEiEB2535.
EcoGeneiEG12669. solA.

Phylogenomic databases

eggNOGiENOG4105F76. Bacteria.
COG0665. LUCA.
HOGENOMiHOG000236098.
InParanoidiP40874.
KOiK02846.
OMAiDGDYQAK.
OrthoDBiEOG6DNT6G.
PhylomeDBiP40874.

Enzyme and pathway databases

BioCyciEcoCyc:SARCOX-MONOMER.
ECOL316407:JW1046-MONOMER.
MetaCyc:SARCOX-MONOMER.
SABIO-RKP40874.

Miscellaneous databases

EvolutionaryTraceiP40874.
PROiP40874.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
HAMAPiMF_00515. MTOX.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR023493. Me_Trp_Oxase_MTOX.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Escherichia coli solA gene encoding a sarcosine oxidase-like protein and characterization of its product."
    Koyama Y., Ohmori H.
    Gene 181:179-183(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Structure of the flavocoenzyme of two homologous amine oxidases: monomeric sarcosine oxidase and N-methyltryptophan oxidase."
    Wagner M.A., Khanna P., Jorns M.S.
    Biochemistry 38:5588-5595(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
    Strain: K12 / DH1 / ATCC 33849 / DSM 4235 / NCIB 12045.
  6. "Characterization of the FAD-containing N-methyltryptophan oxidase from Escherichia coli."
    Khanna P., Jorns M.S.
    Biochemistry 40:1441-1450(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "N-methyltryptophan oxidase from Escherichia coli: reaction kinetics with N-methyl amino acid and carbinolamine substrates."
    Khanna P., Jorns M.S.
    Biochemistry 40:1451-1459(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity."
    Ilari A., Bonamore A., Franceschini S., Fiorillo A., Boffi A., Colotti G.
    Proteins 71:2065-2075(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-372 IN COMPLEX WITH FAD.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiMTOX_ECOLI
AccessioniPrimary (citable) accession number: P40874
Secondary accession number(s): Q47144
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 13, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.