ID A0A1F2RH23_9BACT Unreviewed; 220 AA.
AC A0A1F2RH23;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=methanethiol S-methyltransferase {ECO:0000256|ARBA:ARBA00012149};
DE EC=2.1.1.334 {ECO:0000256|ARBA:ARBA00012149};
GN ORFNames=A3H95_11490 {ECO:0000313|EMBL:OFV93032.1};
OS Acidobacteria bacterium RIFCSPLOWO2_02_FULL_64_15.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1797181 {ECO:0000313|EMBL:OFV93032.1, ECO:0000313|Proteomes:UP000179236};
RN [1] {ECO:0000313|EMBL:OFV93032.1, ECO:0000313|Proteomes:UP000179236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFV93032.1}.
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DR EMBL; MEKS01000018; OFV93032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2RH23; -.
DR STRING; 1797181.A3H95_11490; -.
DR Proteomes; UP000179236; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IEA:InterPro.
DR Gene3D; 1.20.120.1630; -; 1.
DR InterPro; IPR007269; ICMT_MeTrfase.
DR InterPro; IPR033580; Nurim-like.
DR PANTHER; PTHR31040; NURIM; 1.
DR PANTHER; PTHR31040:SF1; NURIM; 1.
DR Pfam; PF04140; ICMT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 220 AA; 24351 MW; B86C15AFED4EA6E2 CRC64;
MWTGGGLFAV SLLVCAYSYL VTWGMPDRVG GGMLAGAGNV ALFAVFALHH SLFARPWMKA
HVARVIPDRL LRSVYVWTAS VLLLIVLALW QPVGSEVYHV TGWRAVAHAG VQLAGLWLIA
RSVARIDALE LAGITPQIPG RALHVDGPYR WVRHPLYLGW VLAVVGAAHM TADRLIFAAI
SSTYVLVAVP LEERSLVNAF GEHYIRYARQ VRWRLVPYIY
//
