ID   ARSC_STAA8              Reviewed;         131 AA.
AC   Q2FXF5;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
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};
GN   OrderedLocusNames=SAOUHSC_01894;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cramton S.E., Richard C., Oberfeld B., Pfitzner U., Gotz F.;
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tibor L., Cramton S.E., Goetz F., Hunt T.K.;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; AF422190; AAN32731.1; -; Genomic_DNA.
DR   EMBL; AY194063; AAP32342.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30957.1; -; Genomic_DNA.
DR   RefSeq; WP_000163235.1; NZ_LS483365.1.
DR   RefSeq; YP_500395.1; NC_007795.1.
DR   AlphaFoldDB; Q2FXF5; -.
DR   SMR; Q2FXF5; -.
DR   STRING; 93061.SAOUHSC_01894; -.
DR   PaxDb; 1280-SAXN108_1804; -.
DR   GeneID; 3920841; -.
DR   KEGG; sao:SAOUHSC_01894; -.
DR   PATRIC; fig|93061.5.peg.1723; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_3_2_9; -.
DR   OrthoDB; 9784339at2; -.
DR   PRO; PR:Q2FXF5; -.
DR   Proteomes; UP000008816; 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   CDD; cd16345; LMWP_ArsC; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
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   NCBIfam; TIGR02691; arsC_pI258_fam; 1.
DR   PANTHER; PTHR43428; ARSENATE REDUCTASE; 1.
DR   PANTHER; PTHR43428:SF1; ARSENATE REDUCTASE; 1.
DR   Pfam; PF01451; LMWPc; 1.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; Phosphotyrosine protein phosphatases I; 1.
PE   3: Inferred from homology;
KW   Arsenical resistance; Cytoplasm; Disulfide bond; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..131
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000290356"
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;  14687 MW;  9B6AA5A854D66C89 CRC64;
     MTKKTIYFIC TGNSCRSQMA EGWAKQILAD DWNVYSAGIE THGVNPKAIE AMKEVGIDIS
     NHTSDLIDNN IIKNSNLVVT LCSDADVNCP SLPTNVKKEH WGFDDPAGKP WSEFQRVRDE
     IKIAIENFKS R
//