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InterPro: IPR014064 Arsenate reductase StaphA (thioredoxin)

Protein matchesHelp
UniProtKB
Matches:
192 proteins
AccessionHelp IPR014064 Arsenate_reductase_StaphA
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Process GO:0046685 response to arsenic
GO:0055114 oxidation reduction
Function GO:0004725 protein tyrosine phosphatase activity
GO:0030612 arsenate reductase (thioredoxin) activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulphide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. This group of arsenate reductases belongs to the low-molecular weight protein-tyrosine phosphatase family (IPR000106), as does a group of glutathione/glutaredoxin type arsenate reductases (IPR014062). At least two other, non-homologous groups of arsenate reductases involved in arsenical resistance are also known. This enzyme reduces arsenate to arsenite, which may be more toxic but which is more easily exported.

Structural linksHelp
SCOP: c.44.1.1
CATH: 3.40.50.270
Database linksHelp

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR014064 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P0A006 Protein arsC

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR014064 Arsenate reductase StaphA (thioredoxin)
IPR017867 Protein-tyrosine phosphatase, low molecular weight
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Messens J, Martins JC, Van Belle K, Brosens E, Desmyter A, De Gieter M, Wieruszeski JM, Willem R, Wyns L, Zegers I.
All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
Proc. Natl. Acad. Sci. U.S.A. 99 2002 8506-11 [PubMed: 12072565]
http://dx.doi.org/10.1073/pnas.132142799
Messens J, Van Molle I, Vanhaesebrouck P, Van Belle K, Wahni K, Martins JC, Wyns L, Loris R.
The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 1180-4 [PubMed: 15159594]
http://dx.doi.org/10.1107/S0907444904007334
Roos G, Buts L, Van Belle K, Brosens E, Geerlings P, Loris R, Wyns L, Messens J.
Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family.
J. Mol. Biol. 360 2006 826-38 [PubMed: 16797027]
http://dx.doi.org/10.1016/j.jmb.2006.05.054
Guo X, Li Y, Peng K, Hu Y, Li C, Xia B, Jin C.
Solution structures and backbone dynamics of arsenate reductase from Bacillus subtilis: reversible conformational switch associated with arsenate reduction.
J. Biol. Chem. 280 2005 39601-8 [PubMed: 16192272]
http://dx.doi.org/10.1074/jbc.M508132200
Li Y, Hu Y, Zhang X, Xu H, Lescop E, Xia B, Jin C.
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis.
J. Biol. Chem. 282 2007 11078-83 [PubMed: 17303556]
http://dx.doi.org/10.1074/jbc.M700970200
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InterPro 23.1