CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.1190 | UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase | |
3.40.1190.20 | Ribokinase |
Domain Context
CATH Clusters
Superfamily | 3.40.1190.20 |
Functional Family |
Enzyme Information
2.7.1.146 |
ADP-specific phosphofructokinase.
based on mapping to UniProt Q58999
ADP + D-fructose 6-phosphate = AMP + D-fructose 1,6-bisphosphate.
-!- ADP can be replaced by GDP, ATP and GTP, to a limited extent.
|
2.7.1.147 |
ADP-specific glucokinase.
based on mapping to UniProt Q58999
ADP + D-glucose = AMP + D-glucose 6-phosphate.
-!- The enzyme from Pyrococcus furiosus is highly specific for D-glucose; there is some activity with 2-deoxy-D-glucose, but no activity with D-fructose, D-mannose or D-galactose as the substrate. -!- No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate.
|
UniProtKB Entries (1)
Q58999 |
K6PF_METJA
Methanocaldococcus jannaschii DSM 2661
Bifunctional ADP-specific glucokinase/phosphofructokinase
|
PDB Structure
PDB | 5OD2 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal structure of ADP-dependent glucokinase from Methanocaldococcus jannaschii in complex with 5-iodotubercidin reveals phosphoryl transfer mechanism.
Protein Sci.
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