Protein Variants | Comment | Organism |
---|---|---|
C108A | alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain | Alkaliphilus metalliredigens |
C120A | alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain | Alkaliphilus metalliredigens |
additional information | heterologous expression of one of the Alkaliphilus metalliredigens ars operons (ars1) confers arsenite but not antimonite resistance to DELTAars Escherichia coli strain AW3110. Only the co-expressed AmArsA1 and AmArsA2 display arsenite or antimonite stimulate ATPase activity, phenotype, overview | Alkaliphilus metalliredigens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
As3+ | As(III)-stimulated ATPase activity | Alkaliphilus metalliredigens | |
Sb3+ | Sb(III)-stimulated ATPase activity 4-8fold | Alkaliphilus metalliredigens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + antimonite/in | Alkaliphilus metalliredigens | - |
ADP + phosphate + antimonite/out | - |
? | |
ATP + H2O + arsenite/in | Alkaliphilus metalliredigens | - |
ADP + phosphate + arsenite/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alkaliphilus metalliredigens | - |
two ars operons, ars1 and ars2, the arsA gene is split in halves, amarsA1 and amarsA2, and, acr3 but not an arsB gene coexists with arsA | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + antimonite/in | - |
Alkaliphilus metalliredigens | ADP + phosphate + antimonite/out | - |
? | |
ATP + H2O + arsenite/in | - |
Alkaliphilus metalliredigens | ADP + phosphate + arsenite/out | - |
? | |
additional information | the AmArsA1-AmArsA2 complex has metalloid-stimulated ATPase activity. ArsB transports antimonite, while Acr3 does not appear to do so | Alkaliphilus metalliredigens | ? | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | 7.8 | - |
Alkaliphilus metalliredigens |
General Information | Comment | Organism |
---|---|---|
additional information | the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain | Alkaliphilus metalliredigens |
physiological function | AmArsA1-AmArsA2 interaction is needed to form the functional ArsA ATPase. This novel AmArsA1-AmArsA2 complex may provide insight in how it participates with Acr3 in arsenite detoxification. ArsB transports antimonite, while Acr3 does not appear to do so | Alkaliphilus metalliredigens |