|
|
||
|
|
|
|
|
UniProt functional annotation for P0AB89 | ||
|
|
|
|
|
|
||
| UniProt code: P0AB89. |
|
||
| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
|
||
| Catalytic activity: | |
Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate; Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567, ChEBI:CHEBI:456215; EC=4.3.2.2; Evidence={ECO:0000269|PubMed:17531264}; |
| Catalytic activity: | |
Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamido]succinate = 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920, ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2; Evidence={ECO:0000269|PubMed:17531264}; |
| Pathway: | |
Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. |
| Pathway: | |
Purine metabolism; IMP biosynthesis via de novo pathway; 5- amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5- phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. |
| Subunit: | |
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site. {ECO:0000269|PubMed:17531264}. |
| Similarity: | |
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.