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Database: UniProt
Entry: A0A1A1YNV3_9MYCO
LinkDB: A0A1A1YNV3_9MYCO
Original site: A0A1A1YNV3_9MYCO 
ID   A0A1A1YNV3_9MYCO        Unreviewed;       249 AA.
AC   A0A1A1YNV3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, 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=A5724_20420 {ECO:0000313|EMBL:OBF32995.1};
OS   Mycobacterium sp. ACS1612.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF32995.1, ECO:0000313|Proteomes:UP000092025};
RN   [1] {ECO:0000313|Proteomes:UP000092025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA   Musoke P., Ssengooba W., Joloba M.;
RL   Submitted (JUN-2016) 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}.
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:OBF32995.1}.
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DR   EMBL; LZHZ01000037; OBF32995.1; -; Genomic_DNA.
DR   RefSeq; WP_067804429.1; NZ_LZHZ01000037.1.
DR   AlphaFoldDB; A0A1A1YNV3; -.
DR   STRING; 1834117.A5724_20420; -.
DR   OrthoDB; 9789029at2; -.
DR   Proteomes; UP000092025; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR009915; NnrU_dom.
DR   InterPro; IPR033580; Nurim-like.
DR   PANTHER; PTHR31040; NURIM; 1.
DR   PANTHER; PTHR31040:SF1; NURIM; 1.
DR   Pfam; PF07298; NnrU; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092025};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..209
FT                   /note="NnrU"
FT                   /evidence="ECO:0000259|Pfam:PF07298"
SQ   SEQUENCE   249 AA;  28372 MW;  D8DA75F017145D4C CRC64;
     MNRYFAMAYG VISYALFLVV FVYAIGFVGG LTPRNVDNAI AAPTIPALAV DAALLALFAA
     QHSVMARPAF KRWWTRYVPR PVERSTYVLL ASMVLALLLW QWRDIPAVVW QVNFQPARLA
     IWALFWLGWA IVLASTFMIN HFELFGLRQV FAVWRARPLA QTGFRTTLFY RVVRHPLNLG
     FIVAFWAAPT MTAGHLLFAA MTTAWILVAM QFEEHDLLAE LGERYAAYRK RVPMLVPGLR
     KRCTDMMVG
//
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