ID ARSC_BACME Reviewed; 140 AA. AC Q8GJ74; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 30. DE RecName: Full=Protein arsC; DE AltName: Full=Arsenate reductase; DE EC=1.20.4.-; DE AltName: Full=Arsenical pump modifier; DE AltName: Full=Low molecular weight protein-tyrosine-phosphatase; DE EC=3.1.3.48; GN Name=arsC; OS Bacillus megaterium. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1404; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 319; 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 RT megaterium."; RL Microbiology 151:775-787(2005). CC -!- FUNCTION: Reduces arsenate [As(V)] to arsenite [As(III)] and CC dephosphorylates tyrosine phosphorylated proteins, low-MW aryl CC phosphates and natural and synthetic acyl phosphates. Could switch CC between different functions in different circumstances (By CC similarity). CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- CATALYTIC ACTIVITY: Arsenate + thioredoxin = arsenite + CC thioredoxin disulfide + H(2)O. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine CC protein phosphatase superfamily. ArsC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ515540; CAD56680.1; -; Genomic_DNA. DR HSSP; P45947; 1JL3. DR SMR; Q8GJ74; 4-140. DR BRENDA; 3.1.3.48; 325. DR GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:HAMAP. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro. DR GO; GO:0046685; P:response to arsenic; IEA:UniProtKB-KW. DR HAMAP; MF_01624; -; 1. DR InterPro; IPR014064; Arsenate_reductase_StaphA. DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt. DR PANTHER; PTHR11717; Low_mwt_PTPase; 1. DR Pfam; PF01451; LMWPc; 1. DR SMART; SM00226; LMWPc; 1. DR TIGRFAMs; TIGR02691; arsC_pI258_fam; 1. PE 3: Inferred from homology; KW Arsenical resistance; Disulfide bond; Hydrolase; Oxidoreductase; KW Redox-active center. FT CHAIN 1 140 Protein arsC. FT /FTId=PRO_0000162519. FT ACT_SITE 10 10 Nucleophile; for reductase activity and FT phosphatase activity (By similarity). FT ACT_SITE 83 83 Nucleophile; for reductase activity (By FT similarity). FT ACT_SITE 90 90 Nucleophile; for reductase activity (By FT similarity). FT DISULFID 10 83 Redox-active; alternate (By similarity). FT DISULFID 83 90 Redox-active; alternate (By similarity). SQ SEQUENCE 140 AA; 15688 MW; 046DD5DB132DDCA9 CRC64; MSKKTLYFLC TGNSCRSQMA EGWAKKYLNN NEWDVRSAGL EAHGLNPNAV KAMKEAGVDI SNQTSDVIDP EILNNADLVV TLCGHAADHC PVTPPHVKRE HWGFDDPAKA EGTDEEKWAF FQRVRDEIAE RIQRFAETGK //