ID   MDDA_PSESZ              Reviewed;         260 AA.
AC   W6VBF4;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 29.
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   ORFNames=PMI27_002062 {ECO:0000312|EMBL:EUB75886.1};
OS   Pseudomonas sp. (strain GM41(2012)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1144708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM41(2012) {ECO:0000312|Proteomes:UP000007282};
RX   PubMed=23045501; DOI=10.1128/jb.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=GM41(2012);
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; AKJN02000006; EUB75886.1; -; Genomic_DNA.
DR   RefSeq; WP_008148420.1; NZ_AKJN02000006.1.
DR   AlphaFoldDB; W6VBF4; -.
DR   BRENDA; 2.1.1.334; 17210.
DR   Proteomes; UP000007282; Unassembled WGS sequence.
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; S-adenosyl-L-methionine; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..260
FT                   /note="Methanethiol S-methyltransferase"
FT                   /id="PRO_0000444497"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   260 AA;  29447 MW;  CFAD38EBA6D30514 CRC64;
     MNPPNRTGHR FFVFSGKLAG LLYSLCCYLF FLLTALYLIG FLAGIGVPKD INSGPGITWP
     LAVLVDAILI TLFAAQHSGM ARKNFKRWWM RFIPATLERA TYVLSSCLVL ALLFVLWQPI
     ATPVWNVESP WGKGLLIALF WLGWGIVLLA TFLISHFELF GVKQTLDAWR KRIPEKPAFK
     SPWLYKLVRH PLYVGFLIAF WATPDMTAGH LLFAILSTSY ILIGAHLEEK DLVDSLGEVY
     QSYQQEVGML VPKRNQTKGR