ARSM_METAC
ID ARSM_METAC Reviewed; 249 AA.
AC Q8TJK1;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Arsenite methyltransferase {ECO:0000303|PubMed:25295694};
DE EC=2.1.1.137 {ECO:0000269|PubMed:25295694};
DE AltName: Full=As(III) methyltransferase {ECO:0000303|PubMed:25295694};
GN Name=arsM {ECO:0000303|PubMed:25295694};
GN OrderedLocusNames=MA_3783 {ECO:0000312|EMBL:AAM07134.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP CYS-30; CYS-31; CYS-62; CYS-150; CYS-194 AND CYS-200.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=25295694; DOI=10.1021/es503869k;
RA Wang P.P., Sun G.X., Zhu Y.G.;
RT "Identification and characterization of arsenite methyltransferase from an
RT archaeon, Methanosarcina acetivorans C2A.";
RL Environ. Sci. Technol. 48:12706-12713(2014).
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 methylated products. Reduces the arsenic
CC toxicity in the cell and may contribute to the global arsenic cycling.
CC {ECO:0000269|PubMed:25295694}.
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:25295694};
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:25295694};
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:25295694};
CC -!- ACTIVITY REGULATION: Highly dependent on the characteristics of the
CC thiol cofactors used, with some of them (coenzyme M, homocysteine, and
CC dithiothreitol) more efficient than GSH. {ECO:0000269|PubMed:25295694}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AE010299; AAM07134.1; -; Genomic_DNA.
DR RefSeq; WP_011023683.1; NC_003552.1.
DR AlphaFoldDB; Q8TJK1; -.
DR SMR; Q8TJK1; -.
DR EnsemblBacteria; AAM07134; AAM07134; MA_3783.
DR GeneID; 1475676; -.
DR KEGG; mac:MA_3783; -.
DR HOGENOM; CLU_052868_1_1_2; -.
DR InParanoid; Q8TJK1; -.
DR OMA; RGSYVGC; -.
DR OrthoDB; 64826at2157; -.
DR PhylomeDB; Q8TJK1; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0030791; F:arsenite methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
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..249
FT /note="Arsenite methyltransferase"
FT /id="PRO_0000439596"
FT MUTAGEN 30
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:25295694"
FT MUTAGEN 31
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:25295694"
FT MUTAGEN 62
FT /note="C->S: Strong decrease in activity. Can still
FT methylate monomethylarsenic."
FT /evidence="ECO:0000269|PubMed:25295694"
FT MUTAGEN 150
FT /note="C->S: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25295694"
FT MUTAGEN 194
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:25295694"
FT MUTAGEN 200
FT /note="C->S: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25295694"
SQ SEQUENCE 249 AA; 26671 MW; 032FAF1A05B085BE CRC64;
MDAAEKKEVI KKKYQEIATL GGSCCSGGGC CGDLSAADLS RSLGYSEADV QAVPDANLGL
GCGNPTAFAE LKPGDIVLDL GSGAGFDSFL AAQRVGSLGK VIGVDMTQEM VKKAQDNARK
YGYSNVEFRQ GDIEALPLDD RSVDVIISNC VINLAPDKEK VFREAFRVLK PGGRMYVSDM
VLLEDLPEDL KNDCDLLAGC VAGALLKEEY LGLLKKAGFS FKILAEDSDV SKRQYEGLPV
ESLKLKAWV
