ARSC_BACAN
ID ARSC_BACAN Reviewed; 134 AA.
AC Q81NJ6; Q6HWR0; Q6KQV2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 127.
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=BA_3196, GBAA_3196, BAS2971;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP26992.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT32312.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT55279.1; -; Genomic_DNA.
DR RefSeq; NP_845506.1; NC_003997.3.
DR RefSeq; WP_000428348.1; NZ_WXXJ01000029.1.
DR RefSeq; YP_029228.1; NC_005945.1.
DR AlphaFoldDB; Q81NJ6; -.
DR SMR; Q81NJ6; -.
DR IntAct; Q81NJ6; 3.
DR STRING; 260799.BAS2971; -.
DR DNASU; 1086394; -.
DR EnsemblBacteria; AAP26992; AAP26992; BA_3196.
DR EnsemblBacteria; AAT32312; AAT32312; GBAA_3196.
DR GeneID; 45022981; -.
DR KEGG; ban:BA_3196; -.
DR KEGG; bar:GBAA_3196; -.
DR KEGG; bat:BAS2971; -.
DR PATRIC; fig|198094.11.peg.3181; -.
DR eggNOG; COG0394; Bacteria.
DR HOGENOM; CLU_071415_3_2_9; -.
DR OMA; DNAKERC; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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..134
FT /note="Arsenate reductase"
FT /id="PRO_0000162511"
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; 15066 MW; 73B208FC18C4683E CRC64;
MENKKTIYFL CTGNSCRSQM AEAWGKQYLG DKWNVYSAGI EAHGVNPNAI KAMNEVNIDI
TNQTSDIIDA NILNRADLVV TLCSHADAVC PSTPPHVNRV HWGFDDPAGK EWPEFQRVRD
EIGERIKRFS ETGE
