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