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Arsenate reductase (EC 1.20.4.4)

 ARSC_STAAR              Reviewed;         131 AA.
Q6GIZ3;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
05-DEC-2018, entry version 91.
RecName: Full=Arsenate reductase {ECO:0000255|HAMAP-Rule:MF_01624};
EC=1.20.4.4 {ECO:0000255|HAMAP-Rule:MF_01624};
Name=arsC {ECO:0000255|HAMAP-Rule:MF_01624};
OrderedLocusNames=SAR0692;
Staphylococcus aureus (strain MRSA252).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=282458;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MRSA252;
PubMed=15213324; DOI=10.1073/pnas.0402521101;
Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
Spratt B.G., Parkhill J.;
"Complete genomes of two clinical Staphylococcus aureus strains:
evidence for the rapid evolution of virulence and drug resistance.";
Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
-!- FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite
[As(III)]. {ECO:0000255|HAMAP-Rule:MF_01624}.
-!- CATALYTIC ACTIVITY:
Reaction=[thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-
disulfide + arsenite + H2O; Xref=Rhea:RHEA:43848, Rhea:RHEA-
COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:29950,
ChEBI:CHEBI:48597, ChEBI:CHEBI:50058; EC=1.20.4.4;
Evidence={ECO:0000255|HAMAP-Rule:MF_01624};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01624}.
-!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
{ECO:0000255|HAMAP-Rule:MF_01624}.
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EMBL; BX571856; CAG39708.1; -; Genomic_DNA.
RefSeq; WP_000358995.1; NC_002952.2.
ProteinModelPortal; Q6GIZ3; -.
SMR; Q6GIZ3; -.
EnsemblBacteria; CAG39708; CAG39708; SAR0692.
KEGG; sar:SAR0692; -.
HOGENOM; HOG000273093; -.
KO; K03741; -.
OMA; CSHADSV; -.
BioCyc; SAUR282458:G1G3O-742-MONOMER; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
HAMAP; MF_01624; Arsenate_reduct; 1.
InterPro; IPR014064; Arsenate_reductase_ArsC.
InterPro; IPR023485; Ptyr_pPase.
InterPro; IPR036196; Ptyr_pPase_sf.
Pfam; PF01451; LMWPc; 1.
SMART; SM00226; LMWPc; 1.
SUPFAM; SSF52788; SSF52788; 1.
TIGRFAMs; TIGR02691; arsC_pI258_fam; 1.
3: Inferred from homology;
Arsenical resistance; Cytoplasm; Disulfide bond; Oxidoreductase;
Redox-active center.
CHAIN 1 131 Arsenate reductase.
/FTId=PRO_0000162525.
ACT_SITE 10 10 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01624}.
ACT_SITE 82 82 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01624}.
ACT_SITE 89 89 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01624}.
DISULFID 10 82 Redox-active; alternate.
{ECO:0000255|HAMAP-Rule:MF_01624}.
DISULFID 82 89 Redox-active; alternate.
{ECO:0000255|HAMAP-Rule:MF_01624}.
SEQUENCE 131 AA; 14813 MW; 03871148DC433A18 CRC64;
MDKKTIYFIC TGNSCRSQMA EGWGKEILGE GWNVYSAGIE THGVNPKAIE AMKEVDIDIS
NHTSDLIDND ILKQSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKE WSEFQRVRDE
IKLAIEKFKL R


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