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MDDA2_BRADU
ID   MDDA2_BRADU             Reviewed;         259 AA.
AC   Q89I98;
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 2 {ECO:0000303|PubMed:25807229};
DE            EC=2.1.1.334 {ECO:0000269|PubMed:25807229};
GN   Name=mddA2 {ECO:0000303|PubMed:25807229};
GN   OrderedLocusNames=blr5741 {ECO:0000312|EMBL:BAC51006.1};
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; BAC51006.1; -; Genomic_DNA.
DR   RefSeq; NP_772381.1; NC_004463.1.
DR   RefSeq; WP_011088485.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89I98; -.
DR   STRING; 224911.27354018; -.
DR   EnsemblBacteria; BAC51006; BAC51006; BAC51006.
DR   GeneID; 64025510; -.
DR   KEGG; bja:blr5741; -.
DR   PATRIC; fig|224911.44.peg.5673; -.
DR   eggNOG; COG2020; Bacteria.
DR   HOGENOM; CLU_084189_0_0_5; -.
DR   InParanoid; Q89I98; -.
DR   OMA; WSIWFPL; -.
DR   PhylomeDB; Q89I98; -.
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..259
FT                   /note="Methanethiol S-methyltransferase 2"
FT                   /id="PRO_0000444501"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   259 AA;  29478 MW;  A38696BAA1C3D0F7 CRC64;
     MFARLAILLY AIVSYAAFTV SFLYALGFVG NYVVPKSIDV GSPTNLGEAI LVNLLLMSLF
     AIQHSVMARP AFKRWWAKFL PLACQRSTYV LLSSLILLLL FWQWRPIPTP VWQTSGIAAW
     LLIGVHWLGW LIAFASTHMI DHFDLFGLRQ AFVAFRGTEI SGQSFRTPLL YKIVRHPLML
     GFLLAFWATP AMTAGHLLFA LANTAYILVA LQFEERDLIA EFGATYQDYR RRVPMLVPRL
     FARRRTDDRK SPRPVGAPR
 
 
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