ARSC_ECOLI
ID ARSC_ECOLI Reviewed; 141 AA.
AC P0AB96; P37311; Q2M7G5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Arsenate reductase;
DE EC=1.20.4.1 {ECO:0000250|UniProtKB:P08692};
DE AltName: Full=Arsenical pump modifier;
GN Name=arsC {ECO:0000303|PubMed:7721697}; Synonyms=arsG;
GN OrderedLocusNames=b3503, JW3470;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7721697; DOI=10.1128/jb.177.8.2050-2056.1995;
RA Diorio C., Cai J., Marmor J., Shinder R., Dubow M.S.;
RT "An Escherichia coli chromosomal ars operon homolog is functional in
RT arsenic detoxification and is conserved in Gram-negative bacteria.";
RL J. Bacteriol. 177:2050-2056(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Involved in resistance to arsenate. Catalyzes the reduction
CC of arsenate [As(V)] to arsenite [As(III)].
CC {ECO:0000250|UniProtKB:P08692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + arsenate + glutathione + H(+) =
CC arsenite + glutathionyl-S-S-[glutaredoxin] + H2O;
CC Xref=Rhea:RHEA:22016, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:17668,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:48597, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:146199; EC=1.20.4.1;
CC Evidence={ECO:0000250|UniProtKB:P08692};
CC -!- INDUCTION: Induced by sodium arsenite. {ECO:0000269|PubMed:7721697}.
CC -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}.
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DR EMBL; X80057; CAA56363.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18479.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76528.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77791.1; -; Genomic_DNA.
DR PIR; C56269; C56269.
DR RefSeq; NP_417960.1; NC_000913.3.
DR RefSeq; WP_000065769.1; NZ_SSZK01000042.1.
DR AlphaFoldDB; P0AB96; -.
DR SMR; P0AB96; -.
DR BioGRID; 4261140; 7.
DR IntAct; P0AB96; 2.
DR STRING; 511145.b3503; -.
DR jPOST; P0AB96; -.
DR PaxDb; P0AB96; -.
DR PRIDE; P0AB96; -.
DR EnsemblBacteria; AAC76528; AAC76528; b3503.
DR EnsemblBacteria; BAE77791; BAE77791; BAE77791.
DR GeneID; 58391093; -.
DR GeneID; 948018; -.
DR KEGG; ecj:JW3470; -.
DR KEGG; eco:b3503; -.
DR PATRIC; fig|1411691.4.peg.3217; -.
DR EchoBASE; EB2149; -.
DR eggNOG; COG1393; Bacteria.
DR HOGENOM; CLU_116644_0_0_6; -.
DR InParanoid; P0AB96; -.
DR OMA; HYLENPP; -.
DR PhylomeDB; P0AB96; -.
DR BioCyc; EcoCyc:EG12237-MON; -.
DR PRO; PR:P0AB96; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:EcoCyc.
DR CDD; cd03034; ArsC_ArsC; 1.
DR InterPro; IPR006659; Arsenate_reductase.
DR InterPro; IPR006660; Arsenate_reductase-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR30041; PTHR30041; 1.
DR Pfam; PF03960; ArsC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00014; arsC; 1.
DR PROSITE; PS51353; ARSC; 1.
PE 2: Evidence at transcript level;
KW Arsenical resistance; Oxidoreductase; Reference proteome.
FT CHAIN 1..141
FT /note="Arsenate reductase"
FT /id="PRO_0000162536"
FT ACT_SITE 12
FT /note="Nucleophile; cysteine thioarsenate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08692,
FT ECO:0000255|PROSITE-ProRule:PRU01282"
FT SITE 8
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P08692"
FT SITE 60
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P08692"
FT SITE 94
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P08692"
FT SITE 107
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P08692"
SQ SEQUENCE 141 AA; 15853 MW; 5490FBBD14B24D3C CRC64;
MSNITIYHNP ACGTSRNTLE MIRNSGTEPT IIHYLETPPT RDELVKLIAD MGISVRALLR
KNVEPYEELG LAEDKFTDDR LIDFMLQHPI LINRPIVVTP LGTRLCRPSE VVLEILPDAQ
KGAFSKEDGE KVVDEAGKRL K
