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ARSC_ALKHC
ID   ARSC_ALKHC              Reviewed;         139 AA.
AC   Q9K8K8;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=BH2998;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06717.1; -; Genomic_DNA.
DR   PIR; F84024; F84024.
DR   RefSeq; WP_010899142.1; NC_002570.2.
DR   AlphaFoldDB; Q9K8K8; -.
DR   SMR; Q9K8K8; -.
DR   STRING; 272558.10175620; -.
DR   EnsemblBacteria; BAB06717; BAB06717; BAB06717.
DR   KEGG; bha:BH2998; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_3_2_9; -.
DR   OMA; DNAKERC; -.
DR   OrthoDB; 1800563at2; -.
DR   Proteomes; UP000001258; 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..139
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162517"
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   139 AA;  15464 MW;  947770F370847DEB CRC64;
     MNKKVIYFLC TGNSCRSQMA EGWGKKYLGD EWDVYSAGIE AHGVNPNAVK AMKEIGIDIS
     EQTSDTIDQE LLQKADLVVT LCGHAADVCP ATPSNKERVH WGFDDPAKAE GTDEEKWAVF
     RRVRDEIGKR IKTFAETGK
 
 
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