ID ARSC1_STAEQ Reviewed; 132 AA. AC Q5HRI4; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Arsenate reductase 1 {ECO:0000255|HAMAP-Rule:MF_01624}; DE EC=1.20.4.4 {ECO:0000255|HAMAP-Rule:MF_01624}; GN Name=arsC1 {ECO:0000255|HAMAP-Rule:MF_01624}; GN OrderedLocusNames=SERP0209; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35984 / RP62A; RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L., RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., RA Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete genome RT analysis of an early methicillin-resistant Staphylococcus aureus strain and RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis RT strain."; RL J. Bacteriol. 187:2426-2438(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000029; AAW53573.1; -; Genomic_DNA. DR RefSeq; WP_002445750.1; NC_002976.3. DR AlphaFoldDB; Q5HRI4; -. DR SMR; Q5HRI4; -. DR STRING; 176279.SERP0209; -. DR KEGG; ser:SERP0209; -. DR eggNOG; COG0394; Bacteria. DR HOGENOM; CLU_071415_3_2_9; -. DR Proteomes; UP000000531; 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..132 FT /note="Arsenate reductase 1" FT /id="PRO_0000162528" 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 132 AA; 14658 MW; 89634C648FBC115F CRC64; MQKKTIYFIC TGNSCRSQMA EGFGKLILGD KWNVYSAGIE THGVNPHAIK AMKEVGIDIS HHTSDLINND ILIASDIVVT LCSDADANCP VLPKNVTKEH WGFDDPAGKD WSEFQRVRDE IKAAIETFAH RV //