ARSM_PSEA4
ID ARSM_PSEA4 Reviewed; 346 AA.
AC U2ZU49;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Arsenite methyltransferase {ECO:0000305};
DE EC=2.1.1.137 {ECO:0000269|PubMed:25681184};
GN Name=arsM {ECO:0000303|PubMed:25681184};
GN ORFNames=PA6_058_00040 {ECO:0000312|EMBL:GAD64975.1};
OS Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / NBRC
OS 14159 / NCIMB 9945 / NCTC 10367 / 1577).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1215092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 / NCTC
RC 10367 / 1577;
RA Yoshida I., Hosoyama A., Tsuchikane K., Noguchi M., Hirakata S., Ando Y.,
RA Ohji S., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Pseudomonas alcaligenes NBRC 14159.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 / NCTC
RC 10367 / 1577;
RX PubMed=25681184; DOI=10.1128/aem.03804-14;
RA Zhang J., Cao T., Tang Z., Shen Q., Rosen B.P., Zhao F.J.;
RT "Arsenic methylation and volatilization by arsenite S-adenosylmethionine
RT methyltransferase in Pseudomonas alcaligenes NBRC14159.";
RL Appl. Environ. Microbiol. 81:2852-2860(2015).
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 dimethylarsenate as the main product in the medium and
CC also produces dimethylarsine and trimethylarsine gases. Reduces the
CC arsenic toxicity in the cell and may contribute to the global arsenic
CC cycling. {ECO:0000269|PubMed:25681184}.
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:25681184};
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:25681184};
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:25681184};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:25681184};
CC -!- INDUCTION: Up-regulated by As(III). {ECO:0000269|PubMed:25681184}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant cannot methylate arsenic and
CC becomes more sensitive to As(III). {ECO:0000269|PubMed:25681184}.
CC -!- BIOTECHNOLOGY: Could be exploited in bioremediation of arsenic-
CC contaminated environments. {ECO:0000305|PubMed:25681184}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; BATI01000058; GAD64975.1; -; Genomic_DNA.
DR RefSeq; WP_021703038.1; NZ_BATI01000058.1.
DR AlphaFoldDB; U2ZU49; -.
DR SMR; U2ZU49; -.
DR STRING; 1215092.PA6_058_00040; -.
DR EnsemblBacteria; GAD64975; GAD64975; PA6_058_00040.
DR eggNOG; COG2226; Bacteria.
DR BRENDA; 2.1.1.137; 5088.
DR Proteomes; UP000016560; Unassembled WGS sequence.
DR GO; GO:0030791; F:arsenite methyltransferase activity; IEA:UniProtKB-EC.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..346
FT /note="Arsenite methyltransferase"
FT /id="PRO_0000439594"
SQ SEQUENCE 346 AA; 38023 MW; 032E1CE70A82E28C CRC64;
MHESVQNYYG KVLQNSSDLK TSACCDASSM PAWLKPLLSQ VHPEVSARYY GCGLVAPALL
DGCQVLDLGS GSGRDCYVLA QLVGASGSVL GVDMTAEQLA VANAHLDYHA ERFGFANVSF
RHGYIEDLAS LELADGSFDV IVSNCVINLS PDKDSVLREA YRLLKPGGEL YFSDVYADRR
LADELRQDEV LYGECLGGAL YWNDFEHLAR RHGFTDPRLV EDQPISITDS ALAEKLGDAR
FYSATYRLFK LDGLEPACED YGQAVIYRGS IPGAAHAFVL DKHHRIETGR VFPVCGNTWR
MLQDTRFAPH FQFIGDFSRH FGLFEGCGGG LPYDRQAAVT AATSCC
