ARSM_RHOPA
ID ARSM_RHOPA Reviewed; 283 AA.
AC Q6N3Y0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Arsenite methyltransferase {ECO:0000305};
DE EC=2.1.1.137 {ECO:0000269|PubMed:16452170};
DE AltName: Full=As(III) AdoMet methyltransferase {ECO:0000303|PubMed:16452170};
GN Name=arsM {ECO:0000305};
GN OrderedLocusNames=RPA3562 {ECO:0000312|EMBL:CAE29003.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=16452170; DOI=10.1073/pnas.0506836103;
RA Qin J., Rosen B.P., Zhang Y., Wang G., Franke S., Rensing C.;
RT "Arsenic detoxification and evolution of trimethylarsine gas by a microbial
RT arsenite S-adenosylmethionine methyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2075-2080(2006).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to
CC arsenite, producing methylated arsenicals. Involved in the conversion
CC of As(III) to a number of di- and trimethylated species, with
CC trimethylarsine as the end product. Reduces the arsenic toxicity in the
CC cell and may contribute to the global arsenic cycling.
CC {ECO:0000269|PubMed:16452170}.
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:0000269|PubMed:16452170};
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:0000269|PubMed:16452170};
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:0000269|PubMed:16452170};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; BX572604; CAE29003.1; -; Genomic_DNA.
DR RefSeq; WP_011159102.1; NC_005296.1.
DR AlphaFoldDB; Q6N3Y0; -.
DR SMR; Q6N3Y0; -.
DR STRING; 258594.RPA3562; -.
DR PRIDE; Q6N3Y0; -.
DR EnsemblBacteria; CAE29003; CAE29003; RPA3562.
DR GeneID; 66894664; -.
DR KEGG; rpa:RPA3562; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_052868_1_2_5; -.
DR OMA; RGSYVGC; -.
DR PhylomeDB; Q6N3Y0; -.
DR BioCyc; MetaCyc:MON-21674; -.
DR BioCyc; RPAL258594:TX73_RS18190-MON; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0030791; F:arsenite methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026669; Arsenite_MeTrfase-like.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43675; PTHR43675; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Arsenical resistance; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..283
FT /note="Arsenite methyltransferase"
FT /id="PRO_0000439595"
SQ SEQUENCE 283 AA; 29656 MW; AB2660F7FE6EB3F5 CRC64;
MPTDMQDVKD IVREKYASAA LKVATGGASC CGSSALPGAS PITSNLYDAA QEQGLPAEAM
LASLGCGNPT ALAQLSPGET VLDLGSGGGI DVLLSARRVG PTGKAYGLDM TDEMLALARD
NQRKAGLDNV EFLKGEIEAI PLPDHSVDVI ISNCVINLSG DKDRVLREAF RVLKPGGRFA
VSDVVTRGEI PEALRRDVLL WVGCLAGALD EADYVAKLAA AGFAQISIEP TRVYDIEDAR
EFLTGKGIDV DALAPQMQDK FFSGFVRATK PGADGEVPAR CCG
