ARSM_HALSA
ID ARSM_HALSA Reviewed; 391 AA.
AC O52025;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Arsenite methyltransferase {ECO:0000250|UniProtKB:Q8TJK1};
DE EC=2.1.1.137 {ECO:0000250|UniProtKB:Q8TJK1};
GN Name=arsM {ECO:0000303|PubMed:15126481}; OrderedLocusNames=VNG_5177C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OG Plasmid pNRC100.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=9847077; DOI=10.1101/gr.8.11.1131;
RA Ng W.V., Ciufo S.A., Smith T.M., Bumgarner R.E., Baskin D., Faust J.,
RA Hall B., Loretz C., Seto J., Slagel J., Hood L., DasSarma S.;
RT "Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid
RT or minichromosome?";
RL Genome Res. 8:1131-1141(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=15126481; DOI=10.1128/jb.186.10.3187-3194.2004;
RA Wang G., Kennedy S.P., Fasiludeen S., Rensing C., DasSarma S.;
RT "Arsenic resistance in Halobacterium sp. strain NRC-1 examined by using an
RT improved gene knockout system.";
RL J. Bacteriol. 186:3187-3194(2004).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to
CC arsenite, producing methylated arsenicals.
CC {ECO:0000250|UniProtKB:Q8TJK1}.
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:0000250|UniProtKB:Q8TJK1};
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:0000250|UniProtKB:Q8TJK1};
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:0000250|UniProtKB:Q8TJK1};
CC -!- INDUCTION: By arsenite and antimonite. {ECO:0000269|PubMed:15126481}.
CC -!- DISRUPTION PHENOTYPE: Deletion causes increased sensitivity to
CC arsenite. {ECO:0000269|PubMed:15126481}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AF016485; AAC82905.1; -; Genomic_DNA.
DR PIR; T08338; T08338.
DR AlphaFoldDB; O52025; -.
DR SMR; O52025; -.
DR EnsemblBacteria; AAC82905; AAC82905; AAC82905.
DR KEGG; hal:AAC82905.1; -.
DR HOGENOM; CLU_052868_1_1_2; -.
DR OMA; RGSYVGC; -.
DR Proteomes; UP000000554; Plasmid pNRC100.
DR GO; GO:0030791; F:arsenite methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Arsenical resistance; Plasmid; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..391
FT /note="Arsenite methyltransferase"
FT /id="PRO_0000429117"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 41696 MW; 722E02BB5FDADB60 CRC64;
MELWTHPTPA APRLATSTRT RWRRTSRCSQ PWATTPGTNS SDASRTPTTA SASATSKPQS
ASARARSVRR SPDCTPRAWS RGARKDRGAT TNRPRRPKFC SKRSTTCEAT MSNDNETMVA
DRDPEETREM VRERYAGIAT SGQDCCGDVG LDVSGDGGCC SDETEASGSE RLGYDADDVA
SVADGADLGL GCGNPKAFAA MAPGETVLDL GSGAGFDCFL AAQEVGPDGH VIGVDMTPEM
ISKARENVAK NDAENVEFRL GEIGHLPVAD ESVNVVISNC VVNLAPEKQR VFDDTYRVLR
PGGRVAISDV VQTAPFPDDV QMDPDSLTGC VAGASTVDDL KAMLDEAGFE AVEIAPKDES
TEFISDWDAD RDLGEYLVSA TIEARKPARD D
