(data stored in ACNUC7421 zone)

HOGENOM: STAHJ_1_PE101

ID   STAHJ_1_PE101                        STANDARD;      PRT;   133 AA.
AC   STAHJ_1_PE101; Q4LAB5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Protein ArsC 1;AltName: Full=Arsenate reductase 1;
DE   EC=1.20.4.-;AltName: Full=Arsenical pump modifier 1;AltName: Full=Low
DE   molecular weight protein-tyrosine-phosphatase 1; EC=3.1.3 48;
DE   (STAHJ_1.PE101).
GN   Name=arsC1; OrderedLocusNames=SH0101;
OS   STAPHYLOCOCCUS HAEMOLYTICUS JCSC1435.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAHJ_1.PE101.
CC       Staphylococcus haemolyticus JCSC1435, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ARSC1_STAHJ
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   -!- GENE_FAMILY: HOG000273093 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q4LAB5; -.
DR   EMBL; AP006716; BAE03410.1; -; Genomic_DNA.
DR   RefSeq; YP_252016.1; NC_007168.1.
DR   ProteinModelPortal; Q4LAB5; -.
DR   SMR; Q4LAB5; 2-129.
DR   STRING; Q4LAB5; -.
DR   EnsemblBacteria; EBSTAT00000044114; EBSTAP00000042565; EBSTAG00000044112.
DR   GeneID; 3482395; -.
DR   GenomeReviews; AP006716_GR; SH0101.
DR   KEGG; sha:SH0101; -.
DR   NMPDR; fig|279808.3.peg.113; -.
DR   eggNOG; COG0394; -.
DR   GeneTree; EBGT00050000024620; -.
DR   OMA; WHKSKAT; -.
DR   ProtClustDB; PRK13530; -.
DR   BioCyc; SHAE279808:SH0101-MON; -.
DR   GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
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_SF.
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   SUPFAM; SSF52788; Tyr_Pase_low_mol_wt; 1.
DR   TIGRFAMs; TIGR02691; ArsC_pI258_fam; 1.
DR   HOGENOMDNA; STAHJ_1.PE101; -.
KW   arsenate reductase;
KW   Arsenical resistance; Complete proteome; Disulfide bond; Hydrolase;
KW   Oxidoreductase; Redox-active center.
SQ   SEQUENCE   133 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDKKTIYFIC SGNSCRSQMA EGWGKEILGE DWNVYSAGIE THGVNPKAIE AMKEVDIDIS
     NHTSDLIDSD ILEQSDLVVT LCSDADDNCP ILPPNVKKEH WGFDDPAGKE WPEFQRVRDE
     IGKRIQEFKE TLV
//

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