ID   MDDA1_BRADU             Reviewed;         285 AA.
AC   Q89V40;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Methanethiol S-methyltransferase 1 {ECO:0000303|PubMed:25807229};
DE            EC=2.1.1.334 {ECO:0000269|PubMed:25807229};
GN   Name=mddA1 {ECO:0000303|PubMed:25807229};
GN   OrderedLocusNames=blr1218 {ECO:0000312|EMBL:BAC46483.1};
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC   {ECO:0000312|Proteomes:UP000002526};
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
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; BA000040; BAC46483.1; -; Genomic_DNA.
DR   RefSeq; NP_767858.1; NC_004463.1.
DR   AlphaFoldDB; Q89V40; -.
DR   STRING; 224911.27349469; -.
DR   EnsemblBacteria; BAC46483; BAC46483; BAC46483.
DR   KEGG; bja:blr1218; -.
DR   PATRIC; fig|224911.5.peg.1263; -.
DR   eggNOG; COG2020; Bacteria.
DR   HOGENOM; CLU_084189_0_0_5; -.
DR   InParanoid; Q89V40; -.
DR   OMA; HTINDGP; -.
DR   PhylomeDB; Q89V40; -.
DR   BRENDA; 2.1.1.334; 14426.
DR   Proteomes; UP000002526; 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; IPR009915; NnrU_dom.
DR   InterPro; IPR033580; Nurim-like.
DR   PANTHER; PTHR31040; PTHR31040; 1.
DR   Pfam; PF07298; NnrU; 1.
PE   1: Evidence at protein level;
KW   Membrane; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..285
FT                   /note="Methanethiol S-methyltransferase 1"
FT                   /id="PRO_0000444500"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   285 AA;  32581 MW;  220704B18D21286F CRC64;
     MERPIRHGAK TKQCRCLGTT ELSMSQIDHQ VHSIGPEVTG SRIFKFIAFL YGIAAYLVFF
     VTILYAIGFV MGLVVPKTID TGTDTSTAEA VIINLLLMAL FAVQHSVMAR QRFKTWWTQF
     VSKPIERSTY VLFASLSLLL LFWQWRPLPT VIWEVEDPDL AVTLVTVSFA GWVLVFTSTF
     IINHFELFGL HQVTNHLVGK EATPPRFKTP LLYKFVRHPI YLGFIVAFWA APVMTAGHLL
     FAAVTTIYIF VGIALEERDL IDLFGDEYRQ YKQRVSMLIP WRRSV