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ARSC1_STAEQ
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   25-MAY-2022, entry version 107.
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}; OrderedLocusNames=SERP0209;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; 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}.
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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   EnsemblBacteria; AAW53573; AAW53573; SERP0209.
DR   KEGG; ser:SERP0209; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_3_2_9; -.
DR   OMA; KPITAHW; -.
DR   OrthoDB; 1800563at2; -.
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   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; 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
 
 
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