4IQE
Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis str. Ames Ancestor
Replaces: 3KZ2Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016833 | molecular_function | oxo-acid-lyase activity |
A | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
A | 0046421 | molecular_function | methylisocitrate lyase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016833 | molecular_function | oxo-acid-lyase activity |
B | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
B | 0046421 | molecular_function | methylisocitrate lyase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00161 |
Number of Residues | 6 |
Details | ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHL |
Chain | Residue | Details |
A | LYS127-LEU132 |