ENZYME entry: EC 2.7.3.13
Accepted Name | ||
---|---|---|
glutamine kinase | ||
Reaction catalysed | ||
ATP + H2O + L-glutamine = AMP + 2 H(+) + N(5)-phospho-L-glutamine + phosphate | ||
Comment(s) | ||
The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides. | ||
Cross-references | ||
BRENDA | 2.7.3.13 | |
EC2PDB | 2.7.3.13 | |
ExplorEnz | 2.7.3.13 | |
PRIAM enzyme-specific profiles | 2.7.3.13 | |
KEGG Ligand Database for Enzyme Nomenclature | 2.7.3.13 | |
IUBMB Enzyme Nomenclature | 2.7.3.13 | |
IntEnz | 2.7.3.13 | |
MEDLINE | Find literature relating to 2.7.3.13 | |
MetaCyc | 2.7.3.13 | |
Rhea expert-curated reactions | 2.7.3.13 | |
UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot
entries referenced
in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.3.-All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-