(data stored in ACNUC7421 zone)

SWISSPROT: D6XY51_BACIE

ID   D6XY51_BACIE            Unreviewed;       139 AA.
AC   D6XY51;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Arsenate reductase {ECO:0000256|HAMAP-Rule:MF_01624};
DE            EC=1.20.4.4 {ECO:0000256|HAMAP-Rule:MF_01624};
GN   Name=arsC {ECO:0000256|HAMAP-Rule:MF_01624};
GN   OrderedLocusNames=Bsel_0588 {ECO:0000313|EMBL:ADH98124.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98124.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98124.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite
CC       [As(III)]. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01624};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01624}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
CC       protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01624}.
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DR   EMBL; CP001791; ADH98124.1; -; Genomic_DNA.
DR   RefSeq; WP_013171553.1; NC_014219.1.
DR   STRING; 439292.Bsel_0588; -.
DR   EnsemblBacteria; ADH98124; ADH98124; Bsel_0588.
DR   KEGG; bse:Bsel_0588; -.
DR   eggNOG; ENOG4107VD5; Bacteria.
DR   eggNOG; COG0394; LUCA.
DR   HOGENOM; HOG000273093; -.
DR   KO; K03741; -.
DR   OMA; CSHADSV; -.
DR   OrthoDB; 1800563at2; -.
DR   BioCyc; BSEL439292:G1GLR-631-MONOMER; -.
DR   Proteomes; UP000000271; 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;
DR   PRODOM; D6XY51.
DR   SWISS-2DPAGE; D6XY51.
KW   Arsenical resistance {ECO:0000256|HAMAP-Rule:MF_01624};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01624};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01624};
KW   Hydrolase {ECO:0000313|EMBL:ADH98124.1};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01624};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_01624};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN        4    137       LMWPc. {ECO:0000259|SMART:SM00226}.
FT   ACT_SITE     10     10       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01624}.
FT   ACT_SITE     82     82       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01624}.
FT   ACT_SITE     89     89       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01624}.
FT   DISULFID     10     82       Redox-active; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01624}.
FT   DISULFID     82     89       Redox-active; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01624}.
SQ   SEQUENCE   139 AA;  15374 MW;  15B7D12513E9F01B CRC64;
     MTKPILYFLC TGNSCRSQMA EGWGKEILGE EWDVYSAGIE AHGVNPNAVK AMNEVAIDIS
     GQTSDTIDQD LLNKADFVVT LCGHANDVCP ATPPNKERAH WGFDDPAKAE GTDTEKWAVF
     QRVRDEIGER IRTFKETGK
//

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