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Database: UniProt
Entry: A0A0M6YG63_9RHOB
LinkDB: A0A0M6YG63_9RHOB
Original site: A0A0M6YG63_9RHOB 
ID   A0A0M6YG63_9RHOB        Unreviewed;       256 AA.
AC   A0A0M6YG63;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=methanethiol S-methyltransferase {ECO:0000256|ARBA:ARBA00012149};
DE            EC=2.1.1.334 {ECO:0000256|ARBA:ARBA00012149};
GN   ORFNames=JDO7802_00948 {ECO:0000313|EMBL:CTQ48940.1};
OS   Jannaschia donghaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=420998 {ECO:0000313|EMBL:CTQ48940.1, ECO:0000313|Proteomes:UP000049222};
RN   [1] {ECO:0000313|EMBL:CTQ48940.1, ECO:0000313|Proteomes:UP000049222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7802 {ECO:0000313|EMBL:CTQ48940.1,
RC   ECO:0000313|Proteomes:UP000049222};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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; CXSU01000011; CTQ48940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M6YG63; -.
DR   STRING; 420998.JDO7802_00948; -.
DR   OrthoDB; 7066299at2; -.
DR   Proteomes; UP000049222; Unassembled WGS sequence.
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:UP000049222};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        50..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   256 AA;  28538 MW;  E373B1C3A3207CA1 CRC64;
     MLGFMTDRRR ILLALVWGAL CHGAFAVGAG LMVCHLFFGL TRSWGAVPYP FAIAANLALL
     AQFPLLHSLL LTGKGRKILA LIGPDARLAT TNYALIASVQ LALLFAFWSP SGVILWQATG
     AMFWVMCAAY AASWGYLMLA IWQGGPQLQS GMLGWFAMLR GRKPEFPDMP TGGLYRVTRQ
     PIYLGFALTL WTMPTWTPDQ LALATLWTAY CVLAPIHKER RFTAIYGDRF RAYRTRVPYW
     LPLPRKAPDD ARPPAQ
//
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