ID   ARSC_STAAR              Reviewed;         131 AA.
AC   Q6GIZ3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Arsenate reductase {ECO:0000255|HAMAP-Rule:MF_01624};
DE            EC=1.20.4.4 {ECO:0000255|HAMAP-Rule:MF_01624};
GN   Name=arsC {ECO:0000255|HAMAP-Rule:MF_01624}; OrderedLocusNames=SAR0692;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite
CC       [As(III)]. {ECO:0000255|HAMAP-Rule:MF_01624}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-
CC         disulfide + arsenite + H2O; Xref=Rhea:RHEA:43848, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:48597, ChEBI:CHEBI:50058; EC=1.20.4.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01624};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01624}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. Thioredoxin-coupled ArsC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01624}.
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DR   EMBL; BX571856; CAG39708.1; -; Genomic_DNA.
DR   RefSeq; WP_000358995.1; NC_002952.2.
DR   AlphaFoldDB; Q6GIZ3; -.
DR   BMRB; Q6GIZ3; -.
DR   SMR; Q6GIZ3; -.
DR   KEGG; sar:SAR0692; -.
DR   HOGENOM; CLU_071415_3_2_9; -.
DR   OMA; DNAKERC; -.
DR   OrthoDB; 1800563at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR   HAMAP; MF_01624; Arsenate_reduct; 1.
DR   InterPro; IPR014064; Arsenate_reductase_ArsC.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   Pfam; PF01451; LMWPc; 1.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; SSF52788; 1.
DR   TIGRFAMs; TIGR02691; arsC_pI258_fam; 1.
PE   3: Inferred from homology;
KW   Arsenical resistance; Cytoplasm; Disulfide bond; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..131
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162525"
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   ACT_SITE        89
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   DISULFID        10..82
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   DISULFID        82..89
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
SQ   SEQUENCE   131 AA;  14813 MW;  03871148DC433A18 CRC64;
     MDKKTIYFIC TGNSCRSQMA EGWGKEILGE GWNVYSAGIE THGVNPKAIE AMKEVDIDIS
     NHTSDLIDND ILKQSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKE WSEFQRVRDE
     IKLAIEKFKL R