EC 7.3.2.7 - Arsenite-transporting ATPase

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IntEnz Enzyme Nomenclature
EC 7.3.2.7

Names

Accepted name:
arsenite-transporting ATPase
Other names:
arsenite-translocating ATPase
arsenical resistance ATPase
arsenical pump-driving ATPase
Systematic name:
ATP phosphohydrolase (arsenite-exporting)

Reaction

Comments:

This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family. The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions. Formerly EC 3.6.3.16.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0015446
UniProtKB/Swiss-Prot: (11) [show] [UniProt]

References

  1. Silver, S., Misra, T.K. and Laddaga, R.A.
    DNA sequence analysis of bacterial toxic heavy metal resistance.
    Biol. Trace Elem. Res. 21: 145-163 (1989). [PMID: 2484581]
  2. Rosen, B.P., Weigel, U., Monticello, R.A. and Edwards, B.P.
    Molecular analysis of an anion pump: purification of the ArsC protein. Arch. Biochem.
    Biophys. 284: 381-385 (1991). [PMID: 1703401]
  3. Bruhn, D.F., Li, J., Silver, S., Roberto, F. and Rosen, B.P.
    The arsenical resistance operon of IncN plasmid R46. FEMS Microbiol.
    Lett. 139: 149-153 (1996). [PMID: 8674982]
  4. Zhou, T., Rosen, B.P. and Gatti, D.L.
    Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773.
    Acta Crystallogr. D Biol. Crystallogr. 55: 921-924 (1999). [PMID: 10089335]

[EC 7.3.2.7 created 2000 as EC 3.6.3.16, transferred 2019 to EC 7.3.2.7]