ARSC_MACCJ
ID ARSC_MACCJ Reviewed; 131 AA.
AC B9E7M5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
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}; OrderedLocusNames=MCCL_1486;
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402;
RX PubMed=19074389; DOI=10.1128/jb.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH18193.1; -; Genomic_DNA.
DR RefSeq; WP_012657391.1; NC_011999.1.
DR AlphaFoldDB; B9E7M5; -.
DR SMR; B9E7M5; -.
DR STRING; 458233.MCCL_1486; -.
DR EnsemblBacteria; BAH18193; BAH18193; MCCL_1486.
DR KEGG; mcl:MCCL_1486; -.
DR eggNOG; COG0394; Bacteria.
DR HOGENOM; CLU_071415_3_2_9; -.
DR OMA; DNAKERC; -.
DR OrthoDB; 1800563at2; -.
DR Proteomes; UP000001383; 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..131
FT /note="Arsenate reductase"
FT /id="PRO_1000186120"
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 131 AA; 14739 MW; 36E609D9B95FA1E5 CRC64;
MEKKTLYFIC TGNSCRSQMA EGWGKHILGD TWNVYSAGIE THGVNPKAIE AMREVGIDIS
HHTSDLIDQD ILNNSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKA WSEFQRVRDE
IGHAIEQFKL R
