ID   MTO_HYPSQ               Reviewed;         435 AA.
AC   A0A291P0C1;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Methanethiol oxidase {ECO:0000303|PubMed:29064480};
DE            Short=MTO {ECO:0000303|PubMed:29064480};
DE            EC=1.8.3.4 {ECO:0000269|PubMed:29064480};
DE   Flags: Precursor;
GN   Name=mtoX {ECO:0000303|PubMed:29064480};
OS   Hyphomicrobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium; unclassified Hyphomicrobium.
OX   NCBI_TaxID=82;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VS;
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-39, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=VS;
RX   PubMed=29064480; DOI=10.1038/ismej.2017.148;
RA   Eyice O., Myronova N., Pol A., Carrion O., Todd J.D., Smith T.J.,
RA   Gurman S.J., Cuthbertson A., Mazard S., Mennink-Kersten M.A., Bugg T.D.,
RA   Andersson K.K., Johnston A.W., Op den Camp H.J., Schaefer H.;
RT   "Bacterial SBP56 identified as a Cu-dependent methanethiol oxidase widely
RT   distributed in the biosphere.";
RL   ISME J. 12:145-160(2018).
CC   -!- FUNCTION: Catalyzes the oxidation of methanethiol. Can also degrade
CC       ethanethiol, but not methanol, methylamine or dimethylsulfide.
CC       {ECO:0000269|PubMed:29064480}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + methanethiol + O2 = formaldehyde + H(+) + H2O2 +
CC         hydrogen sulfide; Xref=Rhea:RHEA:11812, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16007,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:29919; EC=1.8.3.4;
CC         Evidence={ECO:0000269|PubMed:29064480};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000269|PubMed:29064480};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA but not by EGTA.
CC       {ECO:0000269|PubMed:29064480}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 uM for methanethiol {ECO:0000269|PubMed:29064480};
CC         Vmax=16 umol/min/mg enzyme {ECO:0000269|PubMed:29064480};
CC   -!- PATHWAY: Organosulfur degradation. {ECO:0000269|PubMed:29064480}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29064480}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:29064480}.
CC   -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; KY242492; ATJ26742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291P0C1; -.
DR   SMR; A0A291P0C1; -.
DR   BioCyc; MetaCyc:MON-21332; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0018549; F:methanethiol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008430; F:selenium binding; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR008826; Se-bd.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR23300; PTHR23300; 1.
DR   Pfam; PF05694; SBP56; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:29064480"
FT   CHAIN           25..435
FT                   /note="Methanethiol oxidase"
FT                   /id="PRO_5012855470"
SQ   SEQUENCE   435 AA;  48307 MW;  B95E8111006BD8E8 CRC64;
     MKKHLLAGAC ALAMGFAVIP GTFADETCNS PFTTALITGQ EQYLHVWTLG MPGVGDESDK
     LVTISVDPKS DKYGKVINTL SVGGRGEAHH TGFTDDRRYL WAGRLDDNKI FIFDLIDPAN
     PKLIKTITDF ADRTGYVGPH TFYALPGRML IQALSNTKTH DGQTGLAVYS NAGELVSLHP
     MPVTDGGDGY GYDIGINPAK NVLLTSSFTG WNNYMMDLGK MVKDPEAMKR FGNTMAIWDL
     KSMKAEKILN VPGAPLEIRW SLKPEHNWAY TATALTSKLW LIKQDDKGEW IAKETGTIGD
     PSKIPLPVDI SITADAKGLW VNTFLDGTTR FYDISEPEHP KEVFSKKMGN QVNMVSQSYD
     GKRVYFTTSL IANWDKKGAE NDQWLKAYDW DGKELVEKFT VDFNELKLGR AHHMKFSSKT
     NAAELGTNQS FPTRQ