AS3MT_RAT
ID AS3MT_RAT Reviewed; 369 AA.
AC Q8VHT6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Arsenite methyltransferase;
DE EC=2.1.1.137 {ECO:0000269|PubMed:11790780};
DE AltName: Full=Methylarsonite methyltransferase;
DE AltName: Full=S-adenosyl-L-methionine:arsenic(III) methyltransferase;
GN Name=As3mt; Synonyms=Cyt19;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Fischer 344; TISSUE=Liver;
RX PubMed=11790780; DOI=10.1074/jbc.m110246200;
RA Lin S., Shi Q., Nix F.B., Styblo M., Beck M.A., Herbin-Davis K.M.,
RA Hall L.L., Simeonsson J.B., Thomas D.J.;
RT "A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat
RT liver cytosol.";
RL J. Biol. Chem. 277:10795-10803(2002).
RN [2]
RP MUTAGENESIS OF CYS-156.
RX PubMed=15808521; DOI=10.1016/j.taap.2004.12.002;
RA Li J., Waters S.B., Drobna Z., Devesa V., Styblo M., Thomas D.J.;
RT "Arsenic (+3 oxidation state) methyltransferase and the inorganic arsenic
RT methylation phenotype.";
RL Toxicol. Appl. Pharmacol. 204:164-169(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to
CC trivalent arsenicals producing methylated and dimethylated arsenicals.
CC It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is
CC reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2.
CC Methylarsonite is also a substrate and it is converted into the much
CC less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH.
CC {ECO:0000269|PubMed:11790780}.
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:11790780};
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:11790780};
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:11790780};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11790780}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AF393243; AAL61609.1; -; mRNA.
DR RefSeq; NP_543166.1; NM_080890.1.
DR AlphaFoldDB; Q8VHT6; -.
DR SMR; Q8VHT6; -.
DR BioGRID; 250859; 1.
DR STRING; 10116.ENSRNOP00000027223; -.
DR iPTMnet; Q8VHT6; -.
DR PhosphoSitePlus; Q8VHT6; -.
DR PaxDb; Q8VHT6; -.
DR PRIDE; Q8VHT6; -.
DR GeneID; 140925; -.
DR KEGG; rno:140925; -.
DR CTD; 57412; -.
DR RGD; 621325; As3mt.
DR eggNOG; ENOG502QQD6; Eukaryota.
DR InParanoid; Q8VHT6; -.
DR OrthoDB; 1025394at2759; -.
DR PhylomeDB; Q8VHT6; -.
DR BRENDA; 2.1.1.137; 5301.
DR Reactome; R-RNO-156581; Methylation.
DR PRO; PR:Q8VHT6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030791; F:arsenite methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030792; F:methylarsonite methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008276; F:protein methyltransferase activity; TAS:RGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:RGD.
DR GO; GO:0018872; P:arsonoacetate metabolic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; ISO:RGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IDA:MGI.
DR GO; GO:0009404; P:toxin metabolic process; IDA:UniProtKB.
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 Cytoplasm; Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..369
FT /note="Arsenite methyltransferase"
FT /id="PRO_0000204449"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 156
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:15808521"
SQ SEQUENCE 369 AA; 41056 MW; BD092F7317B138E6 CRC64;
MAAPRDAEIH KDVQNYYGNV LKTSADLQTN ACVTPAKGVP EYIRKSLQNV HEEVISRYYG
CGLVVPEHLE NCRILDLGSG SGRDCYVLSQ LVGQKGHITG IDMTKVQVEV AKAYLEYHTE
KFGFQTPNVT FLHGQIEMLA EAGIQKESYD IVISNCVINL VPDKQKVLRE VYQVLKYGGE
LYFSDVYASL EVSEDIKSHK VLWGECLGGA LYWKDLAVIA KKIGFCPPRL VTANIITVGN
KELERVLGDC RFVSATFRLF KLPKTEPAGR CQVVYNGGIM GHEKELIFDA NFTFKEGEAV
EVDEETAAIL RNSRFAHDFL FTPVEASLLA PQTKVIIRDP FKLAEESDKM KPRCAPEGTG
GCCGKRKSC
