ID   ARSC_YEREN              Reviewed;         141 AA.
AC   P74984;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Arsenate reductase;
DE            EC=1.20.4.1 {ECO:0000250|UniProtKB:P08692};
DE   AltName: Full=Arsenical pump modifier;
GN   Name=arsC;
OS   Yersinia enterocolitica.
OG   Plasmid pYV, and Plasmid pYVe227.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=439-80 / Serotype O:9; PLASMID=pYV; TRANSPOSON=Tn2502;
RX   PubMed=9006011; DOI=10.1128/jb.179.3.612-619.1997;
RA   Neyt C., Iriarte M., Thi V.H., Cornelis G.R.;
RT   "Virulence and arsenic resistance in Yersiniae.";
RL   J. Bacteriol. 179:612-619(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W22703 / Serotype O:9 / Biotype 2; PLASMID=pYVe227;
RA   Iriarte M., Lambermont I., Kerbourch C., Cornelis G.R.;
RT   "Detailed genetic map of the pYVe227 plasmid of Yersinia enterocolitica
RT   serotype O:9.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
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; U58366; AAB42203.1; -; Genomic_DNA.
DR   EMBL; AF102990; AAD16858.1; -; Genomic_DNA.
DR   RefSeq; NP_052438.1; NC_002120.1.
DR   RefSeq; WP_010891244.1; NZ_SJZK01000009.1.
DR   AlphaFoldDB; P74984; -.
DR   SMR; P74984; -.
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; Plasmid; Transposable element.
FT   CHAIN           1..141
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162544"
FT   REGION          122..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  15805 MW;  EE6481F5E8897CC7 CRC64;
     MSNITIYHNP TCGTSRNTLE MIRNSGNEPT VIYYLETPPT HDELVKLIAD MGITVRALLR
     KNVEPYEELG LAEGTFSDEQ LIGFMLEHPI LINRPIVVTP LGTRLCRPSE VVLDILPEPQ
     QGAFTKEDGE KITDESGKRL K