ID   ARSC_SHIFL              Reviewed;         141 AA.
AC   P0AB97; P37311;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Arsenate reductase;
DE            EC=1.20.4.1 {ECO:0000250|UniProtKB:P08692};
DE   AltName: Full=Arsenical pump modifier;
GN   Name=arsC; OrderedLocusNames=SF3536, S4234;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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   -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN44992.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19196.1; -; Genomic_DNA.
DR   RefSeq; NP_709285.1; NC_004337.2.
DR   RefSeq; WP_000065769.1; NZ_WPGW01000284.1.
DR   AlphaFoldDB; P0AB97; -.
DR   SMR; P0AB97; -.
DR   STRING; 198214.SF3536; -.
DR   EnsemblBacteria; AAN44992; AAN44992; SF3536.
DR   EnsemblBacteria; AAP19196; AAP19196; S4234.
DR   GeneID; 1025373; -.
DR   GeneID; 58391093; -.
DR   KEGG; sfl:SF3536; -.
DR   KEGG; sfx:S4234; -.
DR   PATRIC; fig|198214.7.peg.4164; -.
DR   HOGENOM; CLU_116644_0_0_6; -.
DR   OMA; HYLENPP; -.
DR   OrthoDB; 1650947at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Arsenical resistance; Oxidoreductase; Reference proteome.
FT   CHAIN           1..141
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162543"
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