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Arsenite methyltransferase (EC 2.1.1.137) (As(III) methyltransferase)

 ARSM_METAC              Reviewed;         249 AA.
Q8TJK1;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
12-SEP-2018, entry version 91.
RecName: Full=Arsenite methyltransferase {ECO:0000303|PubMed:25295694};
EC=2.1.1.137 {ECO:0000269|PubMed:25295694};
AltName: Full=As(III) methyltransferase {ECO:0000303|PubMed:25295694};
Name=arsM {ECO:0000303|PubMed:25295694};
OrderedLocusNames=MA_3783 {ECO:0000312|EMBL:AAM07134.1};
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
C2A).
Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
Methanosarcinaceae; Methanosarcina.
NCBI_TaxID=188937;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
PubMed=11932238; DOI=10.1101/gr.223902;
Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
Metcalf W.W., Birren B.;
"The genome of Methanosarcina acetivorans reveals extensive metabolic
and physiological diversity.";
Genome Res. 12:532-542(2002).
[2]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
CYS-30; CYS-31; CYS-62; CYS-150; CYS-194 AND CYS-200.
STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
PubMed=25295694; DOI=10.1021/es503869k;
Wang P.P., Sun G.X., Zhu Y.G.;
"Identification and characterization of arsenite methyltransferase
from an archaeon, Methanosarcina acetivorans C2A.";
Environ. Sci. Technol. 48:12706-12713(2014).
-!- FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to
arsenite, producing methylated arsenicals. Involved in the
conversion of As(III) to a number of methylated products. Reduces
the arsenic toxicity in the cell and may contribute to the global
arsenic cycling. {ECO:0000269|PubMed:25295694}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + arsenite = S-
adenosyl-L-homocysteine + methylarsonate.
{ECO:0000269|PubMed:25295694}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + methylarsonite = S-
adenosyl-L-homocysteine + dimethylarsinate.
{ECO:0000269|PubMed:25295694}.
-!- ACTIVITY REGULATION: Highly dependent on the characteristics of
the thiol cofactors used, with some of them (coenzyme M,
homocysteine, and dithiothreitol) more efficient than GSH.
{ECO:0000269|PubMed:25295694}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
methyltransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE010299; AAM07134.1; -; Genomic_DNA.
RefSeq; WP_011023683.1; NC_003552.1.
ProteinModelPortal; Q8TJK1; -.
SMR; Q8TJK1; -.
STRING; 188937.MA3783; -.
EnsemblBacteria; AAM07134; AAM07134; MA_3783.
GeneID; 1475676; -.
KEGG; mac:MA_3783; -.
eggNOG; arCOG01792; Archaea.
eggNOG; ENOG410XSKB; LUCA.
InParanoid; Q8TJK1; -.
KO; K07755; -.
OMA; YAGCVSG; -.
OrthoDB; POG093Z0A8C; -.
PhylomeDB; Q8TJK1; -.
BioCyc; MACE188937:G1FZT-4023-MONOMER; -.
Proteomes; UP000002487; Chromosome.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0030791; F:arsenite methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
GO; GO:0032259; P:methylation; IBA:GO_Central.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
InterPro; IPR025714; Methyltranfer_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF13847; Methyltransf_31; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Arsenical resistance; Complete proteome; Methyltransferase;
Reference proteome; S-adenosyl-L-methionine; Transferase.
CHAIN 1 249 Arsenite methyltransferase.
/FTId=PRO_0000439596.
MUTAGEN 30 30 C->S: No change in activity.
{ECO:0000269|PubMed:25295694}.
MUTAGEN 31 31 C->S: No change in activity.
{ECO:0000269|PubMed:25295694}.
MUTAGEN 62 62 C->S: Strong decrease in activity. Can
still methylate monomethylarsenic.
{ECO:0000269|PubMed:25295694}.
MUTAGEN 150 150 C->S: Lack of activity.
{ECO:0000269|PubMed:25295694}.
MUTAGEN 194 194 C->S: No change in activity.
{ECO:0000269|PubMed:25295694}.
MUTAGEN 200 200 C->S: Lack of activity.
{ECO:0000269|PubMed:25295694}.
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


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