Accepted Name |
bacterial tyrosine kinase
|
Alternative Name(s) |
bacterial protein tyrosine kinase |
BY-kinase |
Reaction catalysed |
ATP + L-tyrosyl-[protein] <=> ADP + H(+) + O-phospho-L-tyrosyl-[protein] |
Comment(s) |
- This family of enzymes includes most of the bacterial tyrosine
kinases.
- These enzymes do not share sequence or structural homology with
eukaryotic tyrosine kinases, and exploit ATP/GTP-binding Walker
motifs to catalyze autophosphorylation and substrate phosphorylation
on tyrosine.
- Two subfamilies have been defined: P-type enzymes contain an
N-terminal transmembrane portion and an extracellular hairpin loop
domain. The intracellular portion comprises the catalytic domain and
a tyrosine-rich C-terminal domain that contains the site for
autophosphorylation.
- In F-type enzymes the extracellular transmembrane domain and the
intracellular catalytic domain are two independent proteins encoded
by two separate genes.
- The majority of characterized bacterial tyrosine kinases regulate the
production and export of capsular and extracellular polysaccharides,
but other members are involved in many other functions.
|
Cross-references |
BRENDA | 2.7.10.3 |
EC2PDB | 2.7.10.3 |
ExplorEnz | 2.7.10.3 |
PRIAM enzyme-specific profiles | 2.7.10.3 |
KEGG Ligand Database for Enzyme Nomenclature | 2.7.10.3 |
IUBMB Enzyme Nomenclature | 2.7.10.3 |
IntEnz | 2.7.10.3 |
MEDLINE | Find literature relating to 2.7.10.3 |
MetaCyc | 2.7.10.3 |
Rhea expert-curated reactions | 2.7.10.3 |
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