ARSC1_BACC1
ID ARSC1_BACC1 Reviewed; 134 AA.
AC Q74NT6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=BCE_A0158;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OG Plasmid pBc10987.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017195; AAS45008.1; -; Genomic_DNA.
DR RefSeq; WP_000428327.1; NC_005707.1.
DR AlphaFoldDB; Q74NT6; -.
DR SMR; Q74NT6; -.
DR EnsemblBacteria; AAS45008; AAS45008; BCE_A0158.
DR KEGG; bca:BCE_A0158; -.
DR HOGENOM; CLU_071415_3_2_9; -.
DR OMA; SCRSIMA; -.
DR Proteomes; UP000002527; Plasmid pBc10987.
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; Plasmid;
KW Redox-active center.
FT CHAIN 1..134
FT /note="Arsenate reductase 1"
FT /id="PRO_0000162512"
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; 15006 MW; 63A6D7AE747B42D7 CRC64;
MENKKTIYFL CTGNSCRSQM AEAWGKKYLG DKWNVLSAGI EAHGVNPNAI KAMKEVDIDI
TDQTSDIIDR DILDKADLVV TLCGHANDVC PTTPPHVKRV HWGFDDPAGQ EWSVFQRVRD
EIGARIKKYA ETGE