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Database: UniProt
Entry: W8ESQ2_9BACT
LinkDB: W8ESQ2_9BACT
Original site: W8ESQ2_9BACT 
ID   W8ESQ2_9BACT            Unreviewed;       177 AA.
AC   W8ESQ2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Arsenite methyltransferase {ECO:0000256|ARBA:ARBA00034545};
DE            EC=2.1.1.137 {ECO:0000256|ARBA:ARBA00034521};
GN   ORFNames=Hsw_0589 {ECO:0000313|EMBL:AHJ96184.1};
OS   Hymenobacter swuensis DY53.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ96184.1, ECO:0000313|Proteomes:UP000019423};
RN   [1] {ECO:0000313|EMBL:AHJ96184.1, ECO:0000313|Proteomes:UP000019423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY53 {ECO:0000313|EMBL:AHJ96184.1,
RC   ECO:0000313|Proteomes:UP000019423};
RA   Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT   "Complete genome sequence of ionizing-radiation resistance bacterium
RT   Hymenobacter swuensis DY53.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 [thioredoxin]-dithiol + arsenic triglutathione + H2O + 2 S-
CC         adenosyl-L-methionine = 2 [thioredoxin]-disulfide + dimethylarsinous
CC         acid + 3 glutathione + 2 H(+) + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:69464, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23808,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:59789, ChEBI:CHEBI:183640;
CC         EC=2.1.1.137; Evidence={ECO:0000256|ARBA:ARBA00034402};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 [thioredoxin]-dithiol + arsenic triglutathione + 3 S-
CC         adenosyl-L-methionine = 3 [thioredoxin]-disulfide + 3 glutathione + 3
CC         H(+) + 3 S-adenosyl-L-homocysteine + trimethylarsine;
CC         Xref=Rhea:RHEA:69432, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:27130, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57856, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:183640; EC=2.1.1.137;
CC         Evidence={ECO:0000256|ARBA:ARBA00034419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + arsenic triglutathione + 2 H2O + S-
CC         adenosyl-L-methionine = [thioredoxin]-disulfide + 3 glutathione +
CC         H(+) + methylarsonous acid + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:69460, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:59789, ChEBI:CHEBI:183640;
CC         EC=2.1.1.137; Evidence={ECO:0000256|ARBA:ARBA00034416};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC       methyltransferase family. {ECO:0000256|ARBA:ARBA00034487}.
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DR   EMBL; CP007145; AHJ96184.1; -; Genomic_DNA.
DR   RefSeq; WP_052346105.1; NZ_CP007145.1.
DR   AlphaFoldDB; W8ESQ2; -.
DR   STRING; 1227739.Hsw_0589; -.
DR   KEGG; hsw:Hsw_0589; -.
DR   PATRIC; fig|1227739.3.peg.847; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_052868_0_0_10; -.
DR   Proteomes; UP000019423; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR026669; Arsenite_MeTrfase-like.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43675; ARSENITE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43675:SF8; ARSENITE METHYLTRANSFERASE; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:AHJ96184.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019423};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHJ96184.1}.
FT   DOMAIN          2..127
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
SQ   SEQUENCE   177 AA;  20044 MW;  96677D7F8E0A25D0 CRC64;
     MDVIGVDMTE EQLDVARGHI GAHITRFGYA APNVEFRHGY IEDMATAGLP DNSVDVVVSN
     CVLNLSTDEE ATYREIFRVL RLRGELHIAD VFADQRVPVA RHQDPVLYGE CLNGALYTED
     FRRLLHRIGV RDYRLTSSRR LTIDNPGIEV KVGNIGFYSL TVRAFKLDLE DRCEDFG
//
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