ARSC_PRIM3
ID ARSC_PRIM3 Reviewed; 140 AA.
AC Q8GJ74; D5DDN1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=BMD_1727;
OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=592022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15758224; DOI=10.1099/mic.0.27626-0;
RA Nahrstedt H., Schroder C., Meinhardt F.;
RT "Evidence for two recA genes mediating DNA repair in Bacillus megaterium.";
RL Microbiology 151:775-787(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 319 / IMG 1521;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
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; AJ515540; CAD56680.1; -; Genomic_DNA.
DR EMBL; CP001982; ADF38582.1; -; Genomic_DNA.
DR RefSeq; WP_013082636.1; NC_014103.1.
DR AlphaFoldDB; Q8GJ74; -.
DR SMR; Q8GJ74; -.
DR EnsemblBacteria; ADF38582; ADF38582; BMD_1727.
DR KEGG; bmd:BMD_1727; -.
DR HOGENOM; CLU_071415_3_2_9; -.
DR OMA; DNAKERC; -.
DR Proteomes; UP000002365; 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.
FT CHAIN 1..140
FT /note="Arsenate reductase"
FT /id="PRO_0000162519"
FT ACT_SITE 10
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 10..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 140 AA; 15688 MW; 046DD5DB132DDCA9 CRC64;
MSKKTLYFLC TGNSCRSQMA EGWAKKYLNN NEWDVRSAGL EAHGLNPNAV KAMKEAGVDI
SNQTSDVIDP EILNNADLVV TLCGHAADHC PVTPPHVKRE HWGFDDPAKA EGTDEEKWAF
FQRVRDEIAE RIQRFAETGK