ID   A0A1Z4VS77_9GAMM        Unreviewed;       132 AA.
AC   A0A1Z4VS77;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=methanethiol S-methyltransferase {ECO:0000256|ARBA:ARBA00012149};
DE            EC=2.1.1.334 {ECO:0000256|ARBA:ARBA00012149};
GN   ORFNames=FOKN1_1887 {ECO:0000313|EMBL:BAZ94272.1};
OS   Thiohalobacter thiocyanaticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalobacterales;
OC   Thiohalobacteraceae; Thiohalobacter.
OX   NCBI_TaxID=585455 {ECO:0000313|EMBL:BAZ94272.1, ECO:0000313|Proteomes:UP000218765};
RN   [1] {ECO:0000313|EMBL:BAZ94272.1, ECO:0000313|Proteomes:UP000218765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOKN1 {ECO:0000313|EMBL:BAZ94272.1,
RC   ECO:0000313|Proteomes:UP000218765};
RA   Oshiki M., Fukushima T., Kawano S., Nakagawa J.;
RT   "Thiocyanate degradation by Thiohalobacter thiocyanaticus FOKN1.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of methanethiol (MeSH) to yield
CC       dimethylsulphide (DMS). {ECO:0000256|ARBA:ARBA00002096}.
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:0000256|ARBA:ARBA00000602};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the nurim family.
CC       {ECO:0000256|ARBA:ARBA00010631}.
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DR   EMBL; AP018052; BAZ94272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4VS77; -.
DR   KEGG; ttc:FOKN1_1887; -.
DR   Proteomes; UP000218765; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR033580; Nurim-like.
DR   PANTHER; PTHR31040; NURIM; 1.
DR   PANTHER; PTHR31040:SF1; NURIM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218765};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   132 AA;  15341 MW;  A25CDF7456FD21D2 CRC64;
     MIWTVADPLA RAAMWGLFAF GWLYLVAATY VTDHYDLFGL RQAWLHLRGR QYRPVPFVRK
     WMYRYSRHPM MLGILIGIWA TPEMSAGHLA LALGLTGYIA LGVMLEEREL AGHFGEPYRR
     YRREVGALLP WV
//