ID   MDDA_MYCTU              Reviewed;         244 AA.
AC   O05883; F2GKB4; I6Y304; Q7D5V3;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Methanethiol S-methyltransferase {ECO:0000303|PubMed:25807229};
DE            EC=2.1.1.334 {ECO:0000269|PubMed:25807229};
GN   Name=mddA {ECO:0000303|PubMed:25807229};
GN   OrderedLocusNames=Rv3238c {ECO:0000312|EMBL:CCP46057.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv {ECO:0000312|Proteomes:UP000001584};
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=H37Rv;
RX   PubMed=25807229; DOI=10.1038/ncomms7579;
RA   Carrion O., Curson A.R., Kumaresan D., Fu Y., Lang A.S., Mercade E.,
RA   Todd J.D.;
RT   "A novel pathway producing dimethylsulphide in bacteria is widespread in
RT   soil environments.";
RL   Nat. Commun. 6:6579-6579(2015).
CC   -!- FUNCTION: Catalyzes the methylation of methanethiol (MeSH) to yield
CC       dimethylsulphide (DMS). {ECO:0000269|PubMed:25807229}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=methanethiol + S-adenosyl-L-methionine = dimethyl sulfide +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50428,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16007, ChEBI:CHEBI:17437,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.334;
CC         Evidence={ECO:0000269|PubMed:25807229};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the nurim family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46057.1; -; Genomic_DNA.
DR   RefSeq; NP_217755.1; NC_000962.3.
DR   RefSeq; WP_003416945.1; NZ_NVQJ01000003.1.
DR   AlphaFoldDB; O05883; -.
DR   SMR; O05883; -.
DR   STRING; 83332.Rv3238c; -.
DR   PaxDb; O05883; -.
DR   DNASU; 888858; -.
DR   GeneID; 888858; -.
DR   KEGG; mtu:Rv3238c; -.
DR   PATRIC; fig|83332.111.peg.3616; -.
DR   TubercuList; Rv3238c; -.
DR   eggNOG; COG2020; Bacteria.
DR   OMA; WSIWFPL; -.
DR   PhylomeDB; O05883; -.
DR   BRENDA; 2.1.1.334; 3445.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR033580; Nurim-like.
DR   PANTHER; PTHR31040; PTHR31040; 1.
PE   1: Evidence at protein level;
KW   Membrane; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..244
FT                   /note="Methanethiol S-methyltransferase"
FT                   /id="PRO_0000444498"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   244 AA;  28031 MW;  4653BEF3A8FD540B CRC64;
     MKRYLTIIYG AASYLVFLVA FGYAIGFVGD VVVPRTVDHA IAAPIGQAVV VNLVLLGVFA
     VQHSVMARQG FKRWWTRFVP PSIERSTYVL LASVALLLLY WQWRTMPAVI WDVRQPAGRV
     ALWALFWLGW ATVLTSTFMI NHFELFGLRQ VYLAWRGKPY TEIGFQAHLL YRWVRHPIML
     GFVVAFWATP MMTAGHLLFA IGATGYILVA LQFEERDLLA ALGDQYRDYR REVSMLLPWP
     HRHT