ID K6Z5S1_9ALTE Unreviewed; 197 AA.
AC K6Z5S1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=methanethiol S-methyltransferase {ECO:0000256|ARBA:ARBA00012149};
DE EC=2.1.1.334 {ECO:0000256|ARBA:ARBA00012149};
GN ORFNames=C427_2071 {ECO:0000313|EMBL:AGH44180.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH44180.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH44180.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH44180.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
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 ---------------------------------------------------------------------------
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; CP003837; AGH44180.1; -; Genomic_DNA.
DR RefSeq; WP_007643463.1; NZ_BAES01000098.1.
DR AlphaFoldDB; K6Z5S1; -.
DR STRING; 1129794.C427_2071; -.
DR KEGG; gps:C427_2071; -.
DR PATRIC; fig|1129794.4.peg.2050; -.
DR eggNOG; COG2020; Bacteria.
DR HOGENOM; CLU_084189_0_0_6; -.
DR OrthoDB; 9789029at2; -.
DR Proteomes; UP000011864; 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:UP000011864};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 197 AA; 22324 MW; 14E627F6528A063D CRC64;
MPHTVNSIVP SDSLVTVIVI NTFALLLFGL QHSVMARPSF KRWFTRFIDP SNERSTYVLA
TAVAIGGMCY LWIPFCTVIW QVESEMWGYV IRGIAVFGWL FLFIATFMIN HFELFGLRQT
FNPLQGKSAP TATFKMSGFY KIVRHPIQTG VLIGIWAVPV SASSHLVFAT GISVYIFIGL
YFEEKDLVQE FGETYLD
//