ID H0TV34_9BRAD Unreviewed; 258 AA.
AC H0TV34;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=methanethiol S-methyltransferase {ECO:0000256|ARBA:ARBA00012149};
DE EC=2.1.1.334 {ECO:0000256|ARBA:ARBA00012149};
GN ORFNames=BRAS3843_470018 {ECO:0000313|EMBL:CCE10322.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE10322.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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:CCE10322.1}.
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DR EMBL; CAFK01000293; CCE10322.1; -; Genomic_DNA.
DR RefSeq; WP_008972832.1; NZ_CAFK01000293.1.
DR AlphaFoldDB; H0TV34; -.
DR Proteomes; UP000002686; 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:UP000002686};
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..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..226
FT /note="NnrU"
FT /evidence="ECO:0000259|Pfam:PF07298"
SQ SEQUENCE 258 AA; 29309 MW; 42149146477F90A6 CRC64;
MSQFQSTNPG IPGFRIVKLI AFLYGIAAYI AFSFTIIYAI GFVMGVFVPK TIDTGAESPD
VEALVVNLLL LSLFAVQHSV MARRQFKAWW TKFVPRPIER STYVLFASLL LLLLFWQWRP
MPAVVWQIDN PDIAAIVAVI ALLGWGFAFT STFLINHFEL FGLQQVANSL ADRAASAPRF
RTPLYYRFVR HPIYLGFIIA FWAAPSMTAG HLLFAAVSTA YILLGIVLEE RDLVEQFGEE
YRDYRQRVAM LIPWRKSA
//
