|
|
||
|
|
|
|
|
UniProt functional annotation for P0A790 | ||
|
|
|
|
|
|
||
| UniProt code: P0A790. |
|
||
| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
|
||
|
||
| Function: | |
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000269|PubMed:6767707}. |
|
||
| Catalytic activity: | |
Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000269|PubMed:6767707}; |
| Cofactor: | |
Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.; |
| Activity regulation: | |
Inhibited by hydroxylamine, sodium borohydride, D- cycloserine, hydrazine, semicarbazine and succinic dehydrazine (PubMed:6767707). D-serine is a competitive inhibitor (PubMed:6767707). Cleavage and catalytic activity are regulated by PanZ in a coenzyme A (CoA)-dependent fashion (PubMed:23170229, PubMed:25910242). {ECO:0000269|PubMed:23170229, ECO:0000269|PubMed:25910242, ECO:0000269|PubMed:6767707}. |
| Pathway: | |
Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta- alanine from L-aspartate: step 1/1. |
| Subunit: | |
Heterooctamer of four alpha and four beta subunits (PubMed:9546220). Interacts with PanZ (PubMed:23170229, PubMed:25910242). {ECO:0000269|PubMed:23170229, ECO:0000269|PubMed:25910242, ECO:0000269|PubMed:9546220}. |
| Subcellular location: | |
Cytoplasm {ECO:0000269|PubMed:6767707}. |
| Ptm: | |
Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta- subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. |
| Similarity: | |
Belongs to the PanD family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.