ID A0A1H0BY20_9BRAD Unreviewed; 258 AA.
AC A0A1H0BY20;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=SAMN05444050_1727 {ECO:0000313|EMBL:SDN50502.1};
OS Afipia sp. GAS231.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1882747 {ECO:0000313|EMBL:SDN50502.1, ECO:0000313|Proteomes:UP000198617};
RN [1] {ECO:0000313|EMBL:SDN50502.1, ECO:0000313|Proteomes:UP000198617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS231 {ECO:0000313|EMBL:SDN50502.1,
RC ECO:0000313|Proteomes:UP000198617};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; LT629703; SDN50502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0BY20; -.
DR STRING; 1882747.SAMN05444050_1727; -.
DR OrthoDB; 9789029at2; -.
DR Proteomes; UP000198617; Chromosome i.
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:SDN50502.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198617};
KW Transferase {ECO:0000313|EMBL:SDN50502.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..228
FT /note="NnrU"
FT /evidence="ECO:0000259|Pfam:PF07298"
SQ SEQUENCE 258 AA; 29431 MW; 336FD96454F43F6D CRC64;
MTQIHALGPE APGNRMLKLT AFLFGAVAYL TFLFTILYAI GFVEGLVVPK DIDTGAKSPV
FGALAINLAL MSLFAIQHSV MARNSFKQWW TRFIPKSVER STYVLLASLV LLLLFWQWRP
MPAVIWHIEE PEIAAVITGV SFVGWVMVFT STFLINHFEL FGLHQVANHL VGREMSPPIF
RTPLLYKFVR HPIYLGFIIA FWAAPTMTAG HLLFAAVTTA YIFVGILLEE RDLTAMFGDD
YRRYRERVSM LLPWRKQM
//
