ID   ARSC_OCEIH              Reviewed;         139 AA.
AC   Q8ENQ5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 36.
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; OrderedLocusNames=OB2423;
OS   Oceanobacillus iheyensis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=182710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
RX   MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya
RT   Ridge and its unexpected adaptive capabilities to extreme
RT   environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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.
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DR   EMBL; BA000028; BAC14379.1; -; Genomic_DNA.
DR   RefSeq; NP_693344.1; -.
DR   HSSP; P45947; 1JL3.
DR   SMR; Q8ENQ5; 4-139.
DR   GeneID; 1017228; -.
DR   GenomeReviews; BA000028_GR; OB2423.
DR   KEGG; oih:OB2423; -.
DR   NMPDR; fig|221109.1.peg.2420; -.
DR   HOGENOM; Q8ENQ5; -.
DR   OMA; Q8ENQ5; EMRIVIT.
DR   BioCyc; OIHE221109:OB2423-MON; -.
DR   BRENDA; 3.1.3.48; 278212.
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; Complete proteome; Disulfide bond; Hydrolase;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN         1    139       Protein arsC.
FT                                /FTId=PRO_0000162522.
FT   ACT_SITE     10     10       Nucleophile; for reductase activity and
FT                                phosphatase activity (By similarity).
FT   ACT_SITE     82     82       Nucleophile; for reductase activity (By
FT                                similarity).
FT   ACT_SITE     89     89       Nucleophile; for reductase activity (By
FT                                similarity).
FT   DISULFID     10     82       Redox-active; alternate (By similarity).
FT   DISULFID     82     89       Redox-active; alternate (By similarity).
SQ   SEQUENCE   139 AA;  15676 MW;  09F5110ED5E43249 CRC64;
     MSKKIIYFLC TGNSCRSQMA EGWGKKILGE EWDVYSAGIE AHGLNPNAIK AMREVDIDIT
     NQTSDQIDKD ILNKADFVVT LCGDAKDKCP MTPPHVKRDH WGFEDPAKAQ GTEEEKWTVF
     QQVRDKIGDR IKVFAKTGE
//