ID A0A4R2DGV5_9NOCA Unreviewed; 259 AA.
AC A0A4R2DGV5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=methanethiol S-methyltransferase {ECO:0000256|ARBA:ARBA00012149};
DE EC=2.1.1.334 {ECO:0000256|ARBA:ARBA00012149};
GN ORFNames=EV641_10770 {ECO:0000313|EMBL:TCN52712.1};
OS Rhodococcus sp. SMB37.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2512213 {ECO:0000313|EMBL:TCN52712.1, ECO:0000313|Proteomes:UP000295305};
RN [1] {ECO:0000313|EMBL:TCN52712.1, ECO:0000313|Proteomes:UP000295305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMB37 {ECO:0000313|EMBL:TCN52712.1,
RC ECO:0000313|Proteomes:UP000295305};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:TCN52712.1}.
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DR EMBL; SLVY01000007; TCN52712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2DGV5; -.
DR OrthoDB; 9789029at2; -.
DR Proteomes; UP000295305; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Methyltransferase {ECO:0000313|EMBL:TCN52712.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295305};
KW Transferase {ECO:0000313|EMBL:TCN52712.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..223
FT /note="NnrU"
FT /evidence="ECO:0000259|Pfam:PF07298"
SQ SEQUENCE 259 AA; 29411 MW; 34A1A0F0D5E0CC43 CRC64;
MTTTTDTGPR TRTAASRLLV TGYGVCAYLI FLAVFLYAIG WVERLVVPRN IDQGPRAPAG
IAIVIDLALL SLFAVQHSVM ARPWFKRRWI RIVPEPAERS TYVLLASAAL ALVMWQWRPL
PHPIWDIDSS PLRILLYALS LAGFGLVLVS TFAINHFDLF GLRQVIRNQR GQPPAANAFR
IPLLYRSVRH PLYLGFLVAF WVAPTMSVGH LLFAAVTTAY VLVAIRFEEH DLVATFGERY
RAYRTRVPMI VPWKWLSRR
//
