ID A0A2Z4LUG4_9FLAO Unreviewed; 267 AA.
AC A0A2Z4LUG4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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=HME9304_02016 {ECO:0000313|EMBL:AWX45008.1};
OS Allomuricauda aurantiaca.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1383885 {ECO:0000313|EMBL:AWX45008.1, ECO:0000313|Proteomes:UP000248536};
RN [1] {ECO:0000313|EMBL:AWX45008.1, ECO:0000313|Proteomes:UP000248536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HME9304 {ECO:0000313|EMBL:AWX45008.1,
RC ECO:0000313|Proteomes:UP000248536};
RA Kang H., Kim H., Joh K.;
RT "Spongiibacterium sp. HME9304 Genome sequencing and assembly.";
RL Submitted (JUN-2018) 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; CP030104; AWX45008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4LUG4; -.
DR KEGG; spon:HME9304_02016; -.
DR Proteomes; UP000248536; Chromosome.
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:UP000248536};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..189
FT /note="NnrU"
FT /evidence="ECO:0000259|Pfam:PF07298"
SQ SEQUENCE 267 AA; 30998 MW; 6130FAF2BBA928A4 CRC64;
MKRFIYSFYG IFSYCLFLVV FSYFVFWENN ILVPTGVDKG DAPNLFKALI INILLIALFF
VPHSVMARKS FKAWWITVIP KALERSTYVL VSSSLMAVWI YFWQPIPLII YDLTDSWLGT
FLMILSFFGF GLAVFCTFLI NHFDLFGLKQ IYYAINNKKE SPYKFVTPLL YRLVRHPLYF
SFMIAFWCNP LLTVGHLLLA LMATVYTMVG IGYEEKDLSE LFGETYDLYA EKTPKLLPFV
LKSKPFLFMA GLTLLSLFLA YLIGPVQ
//
