ID   ARSC_BACHK              Reviewed;         134 AA.
AC   Q6HGP0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=BT9727_2963;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(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; AE017355; AAT60271.1; -; Genomic_DNA.
DR   RefSeq; WP_000428351.1; NC_005957.1.
DR   RefSeq; YP_037286.1; NC_005957.1.
DR   AlphaFoldDB; Q6HGP0; -.
DR   SMR; Q6HGP0; -.
DR   KEGG; btk:BT9727_2963; -.
DR   PATRIC; fig|281309.8.peg.3154; -.
DR   HOGENOM; CLU_071415_3_2_9; -.
DR   Proteomes; UP000001301; 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.
FT   CHAIN           1..134
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162521"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   ACT_SITE        83
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   DISULFID        11..83
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
FT   DISULFID        83..90
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01624"
SQ   SEQUENCE   134 AA;  15019 MW;  D3ADE8FC18C608A8 CRC64;
     MENKKTIYFL CTGNSCRSQM AEAWGKQYLG DKWNVYSAGI EAHGVNPNAI KAMNEVNIDI
     TNQTSDIIDA NILNRADLVV TLCSHADSVC PSTPPHVNRV HWGFDDPAGK EWSEFQRVRD
     EIGERIKCFS ETGE
//