EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.2.17 | - |
Mycobacterium tuberculosis |
2.4.2.17 | - |
Campylobacter jejuni |
2.4.2.17 | - |
Lactococcus lactis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.4.2.17 | hanging drop vapor diffusion method | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.4.2.17 | AMP | - |
Campylobacter jejuni | |
2.4.2.17 | AMP | - |
Lactococcus lactis | |
2.4.2.17 | AMP | - |
Mycobacterium tuberculosis | |
2.4.2.17 | L-histidine | - |
Campylobacter jejuni | |
2.4.2.17 | L-histidine | - |
Lactococcus lactis | |
2.4.2.17 | L-histidine | - |
Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.4.2.17 | Mg2+ | required for activity | Mycobacterium tuberculosis | |
2.4.2.17 | Mg2+ | required for activity | Campylobacter jejuni | |
2.4.2.17 | Mg2+ | required for activity | Lactococcus lactis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Mycobacterium tuberculosis | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Campylobacter jejuni | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Lactococcus lactis | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Mycobacterium tuberculosis H37Rv | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Campylobacter jejuni RM1221 | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.2.17 | Campylobacter jejuni | Q5HSJ4 | - |
- |
2.4.2.17 | Campylobacter jejuni RM1221 | Q5HSJ4 | - |
- |
2.4.2.17 | Lactococcus lactis | Q02129 | - |
- |
2.4.2.17 | Mycobacterium tuberculosis | P9WMN1 | - |
- |
2.4.2.17 | Mycobacterium tuberculosis H37Rv | P9WMN1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.4.2.17 | metal affinity column chromatography | Campylobacter jejuni |
2.4.2.17 | metal affinity column chromatography | Lactococcus lactis |
2.4.2.17 | metal affinity column chromatography and Sephacryl S-200 gel filtration | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Mycobacterium tuberculosis | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Campylobacter jejuni | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Lactococcus lactis | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Mycobacterium tuberculosis H37Rv | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
2.4.2.17 | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Campylobacter jejuni RM1221 | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.4.2.17 | homohexamer or heterooctamer | the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine | Mycobacterium tuberculosis |
2.4.2.17 | homohexamer or heterooctamer | the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine | Campylobacter jejuni |
2.4.2.17 | homohexamer or heterooctamer | the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine | Lactococcus lactis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.2.17 | adenosine triphosphate phosphoribosyltransferase | - |
Mycobacterium tuberculosis |
2.4.2.17 | adenosine triphosphate phosphoribosyltransferase | - |
Campylobacter jejuni |
2.4.2.17 | adenosine triphosphate phosphoribosyltransferase | - |
Lactococcus lactis |
2.4.2.17 | ATP-PRT | - |
Mycobacterium tuberculosis |
2.4.2.17 | ATP-PRT | - |
Campylobacter jejuni |
2.4.2.17 | ATP-PRT | - |
Lactococcus lactis |