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MTO_RUEPO
ID   MTO_RUEPO               Reviewed;         436 AA.
AC   Q5LKW0;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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};
GN   OrderedLocusNames=SPOA0269 {ECO:0000312|EMBL:AAV97403.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OG   Plasmid megaplasmid Spo.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
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.
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   -!- PATHWAY: Organosulfur degradation. {ECO:0000269|PubMed:29064480}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- INDUCTION: Induced by methanethiol, dimethylsulfoniopropionate (DMSP)
CC       and methylmercaptopropionic acid (MMPA). {ECO:0000269|PubMed:29064480}.
CC   -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; CP000032; AAV97403.1; -; Genomic_DNA.
DR   RefSeq; WP_011242048.1; NC_006569.1.
DR   AlphaFoldDB; Q5LKW0; -.
DR   SMR; Q5LKW0; -.
DR   STRING; 246200.SPOA0269; -.
DR   EnsemblBacteria; AAV97403; AAV97403; SPOA0269.
DR   KEGG; sil:SPOA0269; -.
DR   eggNOG; COG3391; Bacteria.
DR   HOGENOM; CLU_628344_0_0_5; -.
DR   OMA; DETCQSP; -.
DR   OrthoDB; 469959at2; -.
DR   Proteomes; UP000001023; Plasmid megaplasmid Spo.
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   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR008826; Se-bd.
DR   PANTHER; PTHR23300; PTHR23300; 1.
DR   Pfam; PF05694; SBP56; 1.
DR   SUPFAM; SSF50969; SSF50969; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase; Periplasm; Plasmid; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..436
FT                   /note="Methanethiol oxidase"
FT                   /id="PRO_5004259185"
SQ   SEQUENCE   436 AA;  48555 MW;  C03F79CADEDA62DE CRC64;
     MKRREFGALA AGALAMGLPF RAFADETCQS PYMPKITGQE EFVYVWTLGV EGMGDEQDKL
     VTIDLRPGSA TRGQVINSVS VGGRNEAHHG GFSADRRFFW TGGLDTNRIF IFDVHSDPSN
     PKLHKTIDTF VKDSGGVVGP HTFFALPGSM MITGLSNDDD HGGRTALVEY NDDGEYVATY
     WMPTADDMQG AVAVGDAVAD GYGYDIRALI RKNVMLTSSF TGWSNYMMDF GQMLQDAEAM
     KRFGNTIVQW DLHTRQPKKV FNVPGAPLEI RFPWGSNANY AFSTTALTSQ LWLIYEDDAG
     EWQAKAVADI GNPADIPLPV DISIAADDQT LWINSFMDGK TRLFDISDPH KPFQIYEKVI
     DRQVNMVSQS WDGKRVYFSS SLLANWDKKG KDDAQYLKAY NWDGKELVED FAVDFYELGL
     GRAHIMRFGS SALYSS
 
 
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