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Literature summary extracted from
- Magnesium transporters: properties, regulation and structure (2006), Front. Biosci., 11, 3149-3163.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.2.2.14 | gene corA, DNA and amino acid asequence determination | Escherichia coli |
| 7.2.2.14 | gene corA, DNA and amino acid asequence determination | Arabidopsis thaliana |
| 7.2.2.14 | gene corA, DNA and amino acid asequence determination | Thermotoga maritima |
| 7.2.2.14 | gene corA, DNA and amino acid sequence determination | Methanocaldococcus jannaschii |
| 7.2.2.14 | gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium | Cytobacillus firmus |
| 7.2.2.14 | gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium | Providencia stuartii |
| 7.2.2.14 | genes mgtA and mgtB, from complementation of the Mg2+ growth phenotype mutants MM7 and MM281, gene corA, DNA and amino acid sequence determination, the corA promoter does not respond to extracellular Mg2+ concentration, transcription factor PhoP is important in corA transcription regulation, overview | Salmonella enterica subsp. enterica serovar Typhimurium |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 7.2.2.14 | crystal structure analysis from PDB ID BBJ2 at 3.9 A resolution for the whole enzyme, and at 1.8 A resolution for the soluble domain, overview | Thermotoga maritima |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.2.2.14 | additional information | mutant atmrs2-2 lacks any domain sufficiently hydrophobic to insert in a membrane and does not complement the yeast mutant, as does sibling atmrs2-1 | Arabidopsis thaliana |
| 7.2.2.14 | additional information | mutations of mgtA, mgtB, and corA result in protein incapable of Mg2+ ransport, the Mg2+ transport mutant MM281 can be rescued by complementation with corA from Bacillus firmus strain OB4 or Providencia stuartii, mutation of corA leads to attenuation of virulence and to other defects, but not to growth defects, the CorA-mediated Ni2+ uptake is 2fold increased in a phoP strain compared to wild-type without any increase in the amount of CorA protein | Salmonella enterica subsp. enterica serovar Typhimurium |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.14 | Ca2+ | inhibition of MgtE | Cytobacillus firmus |  |
| 7.2.2.14 | Ca2+ | weak inhibition of CorA, MgtA, and MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | Co2+ | inhibition of MgtA and MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | Mn2+ | inhibition of MgtE | Cytobacillus firmus | |
| 7.2.2.14 | Mn2+ | weak, noncompetitive inhibition | Escherichia coli | |
| 7.2.2.14 | Mn2+ | inhibition of CorA, MgtA, and MgtB, inhibition of CorA is noncompetitive, maximal 35% inhibition of MgtA at over 1 mM | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | additional information | no inhibition of MgtE by Ba2+ | Cytobacillus firmus | |
| 7.2.2.14 | additional information | no inhibition of CorA by Fe2+ and Fe3+ | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | Ni2+ | slight inhibition of MgtE | Cytobacillus firmus | |
| 7.2.2.14 | Sr2+ | inhibition of MgtE | Cytobacillus firmus | |
| 7.2.2.14 | Zn2+ | inhibition of MgtE | Cytobacillus firmus | |
| 7.2.2.14 | Zn2+ | inhibition of MgtA | Salmonella enterica subsp. enterica serovar Typhimurium | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.14 | additional information | - |
additional information | Mg2+ uptake kinetics for CorA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.002 | - |
Ni2+ | pH 7.4, 37°C, MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.005 | - |
Ni2+ | pH 7.4, 37°C, MgtA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.006 | - |
Mg2+ | pH 7.4, 37°C, MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.01 | 0.015 | Mg2+ | pH 7.4, 37°C, CorA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.02 | 0.03 | Co2+ | pH 7.4, 37°C, CorA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.03 | - |
Mg2+ | pH 7.4, 37°C, MgtA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.04 | - |
Co2+ | pH 7.4, 37°C, CorA | Escherichia coli | |
| 7.2.2.14 | 0.05 | - |
Mg2+ | pH 7.4, 37°C, MgtE | Cytobacillus firmus | |
| 7.2.2.14 | 0.08 | - |
Co2+ | pH 7.4, 37°C, MgtE | Cytobacillus firmus | |
| 7.2.2.14 | 0.2 | - |
Ni2+ | pH 7.4, 37°C, CorA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.4 | - |
Ni2+ | pH 7.4, 37°C, CorA | Escherichia coli | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.2.2.14 | membrane | - |
Salmonella enterica subsp. enterica serovar Typhimurium | 16020 | - |
| 7.2.2.14 | membrane | - |
Escherichia coli | 16020 | - |
| 7.2.2.14 | membrane | - |
Arabidopsis thaliana | 16020 | - |
| 7.2.2.14 | membrane | - |
Mycobacterium tuberculosis | 16020 | - |
| 7.2.2.14 | membrane | - |
Aeromonas hydrophila | 16020 | - |
| 7.2.2.14 | membrane | - |
Cytobacillus firmus | 16020 | - |
| 7.2.2.14 | membrane | - |
Providencia stuartii | 16020 | - |
| 7.2.2.14 | membrane | - |
Methanosarcina sp. | 16020 | - |
| 7.2.2.14 | membrane | - |
Thermotoga maritima | 16020 | - |
| 7.2.2.14 | membrane | - |
Methanothermobacter sp. | 16020 | - |
| 7.2.2.14 | membrane | - |
Methanocaldococcus jannaschii | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.14 | additional information | no or poor inhibition of CorA by Ca2+, Sr2+, Ba2+, Zn2+, Fe2+, and Fe3+ | Escherichia coli |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.14 | 42000 | - |
5 * 42000, about, SDS-PAGE | Escherichia coli |
| 7.2.2.14 | 42000 | - |
5 * 42000, about, SDS-PAGE | Arabidopsis thaliana |
| 7.2.2.14 | 42000 | - |
5 * 42000, about, SDS-PAGE | Methanocaldococcus jannaschii |
| 7.2.2.14 | 42000 | - |
5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview | Thermotoga maritima |
| 7.2.2.14 | 42000 | - |
5 * 42000, about, SDS-PAGE, CorA is a homopentamer with two transmembrane domains per monomer, the first of which forms the ion conduction pathway, CorA structure analysis, overview | Salmonella enterica subsp. enterica serovar Typhimurium |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.14 | ATP + H2O + Mg2+/out | Escherichia coli | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Arabidopsis thaliana | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Mycobacterium tuberculosis | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Aeromonas hydrophila | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Cytobacillus firmus | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Providencia stuartii | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Methanosarcina sp. | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Thermotoga maritima | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Methanothermobacter sp. | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Methanocaldococcus jannaschii | - |
ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Salmonella enterica subsp. enterica serovar Typhimurium | CorA and MgtE are not transcriptionally regulated | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | Cytobacillus firmus OF4 | - |
ADP + phosphate + Mg2+/in | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.2.2.14 | Aeromonas hydrophila | - |
gene mgtE | - |
| 7.2.2.14 | Arabidopsis thaliana | - |
gene corA | - |
| 7.2.2.14 | Cytobacillus firmus | - |
- |
- |
| 7.2.2.14 | Cytobacillus firmus OF4 | - |
- |
- |
| 7.2.2.14 | Escherichia coli | - |
gene corA | - |
| 7.2.2.14 | Methanocaldococcus jannaschii | Q58439 | gene corA | - |
| 7.2.2.14 | Methanosarcina sp. | - |
gene mgtC | - |
| 7.2.2.14 | Methanothermobacter sp. | - |
gene mgtC | - |
| 7.2.2.14 | Mycobacterium tuberculosis | - |
gene mgtC | - |
| 7.2.2.14 | Providencia stuartii | - |
gene mgtE | - |
| 7.2.2.14 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
genes corA, mgtA/B, mgtE | - |
| 7.2.2.14 | Thermotoga maritima | Q9WZ31 | gene corA | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Escherichia coli | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Arabidopsis thaliana | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Mycobacterium tuberculosis | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Aeromonas hydrophila | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Cytobacillus firmus | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Providencia stuartii | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Methanosarcina sp. | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Thermotoga maritima | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Methanothermobacter sp. | |
| 7.2.2.14 | ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] | Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview | Methanocaldococcus jannaschii |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 7.2.2.14 | additional information | constitutive expression of corA | Salmonella enterica subsp. enterica serovar Typhimurium | - |
| 7.2.2.14 | additional information | constitutive expression of MgtE | Aeromonas hydrophila | - |
| 7.2.2.14 | additional information | constitutive expression of MgtE | Cytobacillus firmus | - |
| 7.2.2.14 | additional information | constitutive expression of MgtE | Providencia stuartii | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.14 | ATP + H2O + Co2+/out | - |
Escherichia coli | ADP + phosphate + Co2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Co2+/out | - |
Cytobacillus firmus | ADP + phosphate + Co2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Co2+/out | - |
Methanocaldococcus jannaschii | ADP + phosphate + Co2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Co2+/out | transported by CorA | Salmonella enterica subsp. enterica serovar Typhimurium | ADP + phosphate + Co2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Co2+/out | - |
Cytobacillus firmus OF4 | ADP + phosphate + Co2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Escherichia coli | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Arabidopsis thaliana | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Mycobacterium tuberculosis | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Aeromonas hydrophila | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Cytobacillus firmus | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Providencia stuartii | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Methanosarcina sp. | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Thermotoga maritima | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Methanothermobacter sp. | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Methanocaldococcus jannaschii | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | CorA and MgtE are not transcriptionally regulated | Salmonella enterica subsp. enterica serovar Typhimurium | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | transported by CorA, MgtA, and MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Cytobacillus firmus OF4 | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Ni2+/out | - |
Escherichia coli | ADP + phosphate + Ni2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Ni2+/out | - |
Methanocaldococcus jannaschii | ADP + phosphate + Ni2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Ni2+/out | transported by CorA, MgtA, and MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | ADP + phosphate + Ni2+/in | - |
? | |
| 7.2.2.14 | additional information | CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential | Escherichia coli | ? | - |
? | |
| 7.2.2.14 | additional information | CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential | Thermotoga maritima | ? | - |
? | |
| 7.2.2.14 | additional information | CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential | Methanocaldococcus jannaschii | ? | - |
? | |
| 7.2.2.14 | additional information | CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential, the different cation influx activities do not influence each other activity, MgtA and MgtB are P-type ATPases | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| 7.2.2.14 | additional information | the Arabidopsis thaliana CorA homologues of the Mrs2p family have putative transmembrane segments and catalyzes Mg2+ transport, CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential | Arabidopsis thaliana | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.2.2.14 | More | secondary structure determination | Thermotoga maritima |
| 7.2.2.14 | pentamer | 5 * 42000, about, SDS-PAGE | Escherichia coli |
| 7.2.2.14 | pentamer | 5 * 42000, about, SDS-PAGE | Arabidopsis thaliana |
| 7.2.2.14 | pentamer | 5 * 42000, about, SDS-PAGE | Methanocaldococcus jannaschii |
| 7.2.2.14 | pentamer | 5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview | Thermotoga maritima |
| 7.2.2.14 | pentamer | 5 * 42000, about, SDS-PAGE, CorA is a homopentamer with two transmembrane domains per monomer, the first of which forms the ion conduction pathway, CorA structure analysis, overview | Salmonella enterica subsp. enterica serovar Typhimurium |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.2.2.14 | CorA | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | CorA | - |
Escherichia coli |
| 7.2.2.14 | CorA | - |
Thermotoga maritima |
| 7.2.2.14 | CorA | - |
Methanocaldococcus jannaschii |
| 7.2.2.14 | CorA/Mrs2p | - |
Arabidopsis thaliana |
| 7.2.2.14 | magnesium transporter | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | Mg2+ transporter | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | MgtA | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | MgtB | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | MgtC | - |
Mycobacterium tuberculosis |
| 7.2.2.14 | MgtC | - |
Methanosarcina sp. |
| 7.2.2.14 | MgtC | - |
Methanothermobacter sp. |
| 7.2.2.14 | MgtE | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | MgtE | - |
Aeromonas hydrophila |
| 7.2.2.14 | MgtE | - |
Cytobacillus firmus |
| 7.2.2.14 | MgtE | - |
Providencia stuartii |
| 7.2.2.14 | More | MgtA/B transporters belong to the P-type ATPase superfamily | Salmonella enterica subsp. enterica serovar Typhimurium |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.14 | 37 | - |
assay at | Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | 37 | - |
assay at | Escherichia coli |
| 7.2.2.14 | 37 | - |
assay at | Cytobacillus firmus |
| 7.2.2.14 | 37 | - |
assay at | Methanocaldococcus jannaschii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.14 | 7.4 | - |
assay at | Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.2.2.14 | 7.4 | - |
assay at | Cytobacillus firmus |
| 7.2.2.14 | 7.4 | - |
assay at | Methanocaldococcus jannaschii |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.14 | 0.007 | - |
Zn2+ | pH 7.4, 37°C, MgtA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.008 | - |
Co2+ | pH 7.4, 37°C, MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.02 | - |
Zn2+ | pH 7.4, 37°C, MgtE | Cytobacillus firmus | |
| 7.2.2.14 | 0.03 | - |
Mn2+ | pH 7.4, 37°C, CorA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.04 | - |
Co2+ | pH 7.4, 37°C, MgtA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.04 | - |
Mn2+ | pH 7.4, 37°C, MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 0.05 | - |
Ca2+ | pH 7.4, 37°C, MgtE | Cytobacillus firmus | |
| 7.2.2.14 | 0.07 | - |
Mn2+ | pH 7.4, 37°C, MgtE | Cytobacillus firmus | |
| 7.2.2.14 | 0.08 | - |
Sr2+ | pH 7.4, 37°C, MgtE | Cytobacillus firmus | |
| 7.2.2.14 | 0.2 | - |
Ni2+ | pH 7.4, 37°C, MgtE, above | Cytobacillus firmus | |
| 7.2.2.14 | 0.3 | - |
Ca2+ | pH 7.4, 37°C, MgtA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 5 | - |
Ca2+ | pH 7.4, 37°C, CorA | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 7.2.2.14 | 30 | - |
Ca2+ | pH 7.4, 37°C, MgtB | Salmonella enterica subsp. enterica serovar Typhimurium | |
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Release 2023.1 (January 2023)
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