The Enzyme Database

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EC 7.3.2.7     
Accepted name: arsenite-transporting ATPase
Reaction: ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]
Other name(s): arsAB (gene names)
Systematic name: ATP phosphohydrolase (arsenite-exporting)
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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 (1989) 145–163. [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 (1991) 381–385. [DOI] [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 (1996) 149–153. [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 (1999) 921–924. [PMID: 10089335]
[EC 7.3.2.7 created 2000 as EC 3.6.3.16, transferred 2019 to EC 7.3.2.7]
 
 


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