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Database: UniProt
Entry: A0A0Q9KEP4_9MICO
LinkDB: A0A0Q9KEP4_9MICO
Original site: A0A0Q9KEP4_9MICO 
ID   A0A0Q9KEP4_9MICO        Unreviewed;       273 AA.
AC   A0A0Q9KEP4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Arsenite methyltransferase {ECO:0000256|ARBA:ARBA00034545};
DE            EC=2.1.1.137 {ECO:0000256|ARBA:ARBA00034521};
GN   ORFNames=ASG73_03665 {ECO:0000313|EMBL:KRE39430.1};
OS   Janibacter sp. Soil728.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE39430.1, ECO:0000313|Proteomes:UP000051572};
RN   [1] {ECO:0000313|EMBL:KRE39430.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39430.1,
RC   ECO:0000313|Proteomes:UP000051572};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE39430.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39430.1,
RC   ECO:0000313|Proteomes:UP000051572};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034402};
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:0000256|ARBA:ARBA00034419};
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:0000256|ARBA:ARBA00034416};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC       methyltransferase family. {ECO:0000256|ARBA:ARBA00034487}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRE39430.1}.
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DR   EMBL; LMRZ01000001; KRE39430.1; -; Genomic_DNA.
DR   RefSeq; WP_055990850.1; NZ_LMRZ01000001.1.
DR   AlphaFoldDB; A0A0Q9KEP4; -.
DR   STRING; 1736393.ASG73_03665; -.
DR   OrthoDB; 9805171at2; -.
DR   Proteomes; UP000051572; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR026669; Arsenite_MeTrfase-like.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43675; ARSENITE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43675:SF8; ARSENITE METHYLTRANSFERASE; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:KRE39430.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRE39430.1}.
FT   DOMAIN          71..203
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
SQ   SEQUENCE   273 AA;  28548 MW;  05C954A06A013311 CRC64;
     MAQQDTHAAV RDRYATAARA ALDPDTASAC CGDTATDPIT IGLYEGTDSP SDSALAASLG
     CGNPTALADL SPGEDVLDLG SGGGLDVLLS ARRVAPGGTA YGLDMTDEML ELARRNQAEA
     GIDNASFLRG MIEEIPMEDA SVDVVISNCV INLSPDKDAV IREAHRVLRP SGRFAVSDVV
     LLREIPDALR GIVGLWTGCV SGSLLDTDYV TKLTAAGFAD ASVEVTRRFE RTDLEDMSGL
     IGDELPQGWT LEGVLDALDG SFASAFVRAR KAA
//
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