ID   MDDA_PSEDM              Reviewed;         262 AA.
AC   A0A0F6P9C0;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   03-AUG-2022, entry version 23.
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=SAMN04489800_4417 {ECO:0000312|EMBL:SEF08080.1};
OS   Pseudomonas deceptionensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=882211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=M1T {ECO:0000312|EMBL:AJE75769.1};
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25555 {ECO:0000312|EMBL:SEF08080.1,
RC   ECO:0000312|Proteomes:UP000183613};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:25807229}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:25807229}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC       dimethylsulphide (DMS). {ECO:0000269|PubMed:25807229}.
CC   -!- SIMILARITY: Belongs to the nurim family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KM030271; AJE75769.1; -; Genomic_DNA.
DR   EMBL; FNUD01000002; SEF08080.1; -; Genomic_DNA.
DR   RefSeq; WP_048359798.1; NZ_JYKX01000002.1.
DR   AlphaFoldDB; A0A0F6P9C0; -.
DR   SMR; A0A0F6P9C0; -.
DR   EnsemblBacteria; SEF08080; SEF08080; SAMN04489800_4417.
DR   KEGG; ag:AJE75769; -.
DR   PATRIC; fig|882211.3.peg.2020; -.
DR   BioCyc; MetaCyc:MON-19896; -.
DR   BRENDA; 2.1.1.334; 15037.
DR   Proteomes; UP000183613; 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   InterPro; IPR007318; Phopholipid_MeTrfase.
DR   PANTHER; PTHR31040; PTHR31040; 1.
DR   Pfam; PF04191; PEMT; 1.
PE   1: Evidence at protein level;
KW   Membrane; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..262
FT                   /note="Methanethiol S-methyltransferase"
FT                   /id="PRO_0000444496"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   262 AA;  29637 MW;  8C961A3AD2F8FFAD CRC64;
     MHTRTAPRVR PPSRAAKLAG LLYSLLSYLF FLMTLLYLIG FVGNVGVPKT IDSGPGASWP
     LALLVDVLLI TLFAVQHSVM ARKSFKQWWR PVVPAPIERA TYVLASSVVL VVMFWLWQPI
     DLRVWQVESR LGSAVLTTLF WLGWGLILVA TFLISHFELF GVKQALDALR PAKPVDGSFR
     TPLLYKIVRH PMYMGFLMAF WATPEMTVGH LVFALTSTIY ILIGTQLEEK DLVEIFGEKY
     RNYQKNVGML LPSLRRNPGS QD