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Arsenite methyltransferase (EC 2.1.1.137)

 ARSM_CLOSP              Reviewed;         270 AA.
A0A0D3MJQ5;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
27-MAY-2015, sequence version 1.
05-DEC-2018, entry version 13.
RecName: Full=Arsenite methyltransferase {ECO:0000303|PubMed:25790486};
EC=2.1.1.137 {ECO:0000269|PubMed:25790486};
Name=arsM {ECO:0000303|PubMed:25790486};
Clostridium sp.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1506;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF CYS-65; CYS-153 AND CYS-203.
STRAIN=BXM;
PubMed=25790486; DOI=10.1093/femsle/fnu003;
Wang P.P., Bao P., Sun G.X.;
"Identification and catalytic residues of the arsenite
methyltransferase from a sulfate-reducing bacterium, Clostridium sp.
BXM.";
FEMS Microbiol. Lett. 362:1-8(2015).
-!- FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to
arsenite, producing methylated arsenicals. Involved in the
conversion of As(III) to monomethylarsenic and the conversion of
monomethylarsenic to dimethylarsenic. Reduces the arsenic toxicity
in the cell and may contribute to the global arsenic cycling.
{ECO:0000269|PubMed:25790486}.
-!- CATALYTIC ACTIVITY:
Reaction=arsenite + S-adenosyl-L-methionine = H(+) +
methylarsonate + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:15293, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242,
ChEBI:CHEBI:33409, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
EC=2.1.1.137; Evidence={ECO:0000269|PubMed:25790486};
-!- CATALYTIC ACTIVITY:
Reaction=methylarsonous acid + S-adenosyl-L-methionine =
dimethylarsinate + 2 H(+) + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:11684, ChEBI:CHEBI:15378, ChEBI:CHEBI:16223,
ChEBI:CHEBI:17826, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
EC=2.1.1.137; Evidence={ECO:0000269|PubMed:25790486};
-!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
methyltransferase family. {ECO:0000305}.
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EMBL; KJ801487; AIM18906.1; -; Genomic_DNA.
ProteinModelPortal; A0A0D3MJQ5; -.
SMR; A0A0D3MJQ5; -.
GO; GO:0030791; F:arsenite methyltransferase activity; IEA:UniProtKB-EC.
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; Methyltransferase; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 270 Arsenite methyltransferase.
/FTId=PRO_0000439593.
MUTAGEN 65 65 C->S: Cannot methylate arsenite, but can
still methylate monomethylarsenic.
{ECO:0000269|PubMed:25790486}.
MUTAGEN 153 153 C->S: Lack of activity.
{ECO:0000269|PubMed:25790486}.
MUTAGEN 203 203 C->S: Lack of activity.
{ECO:0000269|PubMed:25790486}.
SEQUENCE 270 AA; 29061 MW; 0EBD5A2F604B8404 CRC64;
MDNIREGVRQ KYAFAIANRG QGCCGSPGCC SDGLSDAADP ITGNLYDESD LQGLDPELIA
NSFGCGNPTA LMNLNLGEVV LDLGSGSGLD VLLSAKRVGP TGKAYGLDMT DEMLAVAKEN
QRKSGIENAE FLKGHIEEIP LAAKSIDVII SNCVINLSGD KDKVLKEAYR VLKPQGRFAV
SDIVIKRPLP EKIRDNILAW AGCIAGAMTE EEYRGKLSRA GFENISLQVT REYNLEDPSL
RGMLEDLTDG EIKEFQGAMV SCFIRAAKPA


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