EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.7.1.169 | purified recombinant enzyme in apoform or in complex with ATP and a magnesium ion, mixing of 5-10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, with 18%-20% PEG 8000 solutions containing 200 mM calcium acetate and 100 mM MES, pH 6.0, as a precipitant, 1-2 weeks, 20°C, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution, single isomorphous replacement (SIR) method using derivative data of K2Pt (NO2)4 collected at 3.0 A resolution, modeling. In TkPoK/ATP, the adenine ring of the ATP is not included in the crystal structure, because its electron density is very poor | Thermococcus kodakarensis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.169 | Mg2+ | required | Thermococcus kodakarensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.169 | ATP + (R)-pantoate | Thermococcus kodakarensis | - |
ADP + (R)-4-phosphopantoate | - |
? | |
2.7.1.169 | ATP + (R)-pantoate | Thermococcus kodakarensis JCM 12380 | - |
ADP + (R)-4-phosphopantoate | - |
? | |
2.7.1.169 | ATP + (R)-pantoate | Thermococcus kodakarensis ATCC BAA-918 | - |
ADP + (R)-4-phosphopantoate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.169 | Thermococcus kodakarensis | Q5JHF1 | Pyrococcus kodakaraensis strain KOD1 | - |
2.7.1.169 | Thermococcus kodakarensis ATCC BAA-918 | Q5JHF1 | Pyrococcus kodakaraensis strain KOD1 | - |
2.7.1.169 | Thermococcus kodakarensis JCM 12380 | Q5JHF1 | Pyrococcus kodakaraensis strain KOD1 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.169 | ATP + (R)-pantoate | - |
Thermococcus kodakarensis | ADP + (R)-4-phosphopantoate | - |
? | |
2.7.1.169 | ATP + (R)-pantoate | - |
Thermococcus kodakarensis JCM 12380 | ADP + (R)-4-phosphopantoate | - |
? | |
2.7.1.169 | ATP + (R)-pantoate | - |
Thermococcus kodakarensis ATCC BAA-918 | ADP + (R)-4-phosphopantoate | - |
? | |
2.7.1.169 | additional information | the enzyme shows broad nucleotide specificity | Thermococcus kodakarensis | ? | - |
- |
|
2.7.1.169 | additional information | the enzyme shows broad nucleotide specificity | Thermococcus kodakarensis JCM 12380 | ? | - |
- |
|
2.7.1.169 | additional information | the enzyme shows broad nucleotide specificity | Thermococcus kodakarensis ATCC BAA-918 | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.1.169 | dimer | 2 * 33000, about, sequence calculation and crystal structure analysis | Thermococcus kodakarensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.1.169 | PoK | - |
Thermococcus kodakarensis |
2.7.1.169 | TK2141 | - |
Thermococcus kodakarensis |
2.7.1.169 | TkPoK | - |
Thermococcus kodakarensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.169 | ATP | the electron density for the adenosine moiety of ATP is very weak, which most likely relates to its broad nucleotide specificity. The triphosphate moiety of ATP is surrounded by the lycine-rich loop of motif II (P96NGYGFGNSAG106). The magnesium ion can interact with oxygen atoms of beta- and gamma-phosphates, and with the O5' atom of ATP which bridges the adenosine and the triphosphate groups | Thermococcus kodakarensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.1.169 | metabolism | the CoA biosynthesis pathway involves reactions that convert pantoate to 4'-phosphopantothenate. For this conversion, bacteria/eukaryotes commonly use two enzymes, pantothenate synthetase (PS) and pantothenate kinase (PanK). In the PS/PanK pathway, pantoate and beta-alanine are first condensed to form pantothenate by the reaction of PS, and then pantothenate is phosphorylated to generate 40-phosphopantothenate by the reaction of PanK | Thermococcus kodakarensis |