3 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004418 | IPR022419 |
| GO:0018160 | IPR022419 |
| GO:0033014 | IPR022419 |
| Type: | Binding_site | Name: | Porphobilinogen deaminase, dipyrromethane cofactor binding site |
| Description: | This entry represents the region around a cysteine residues that is conserved in porphobilinogen deaminases from various prokaryotic and eukaryotic sources. The sulphur atom of this cysteine residue has been shown in the Escherichia colienzyme (gene hemC) to be bound to the dipyrromethane cofactor []. Porphobilinogen deaminase covalently binds a dipyrromethane cofactor to which the PBG subunits are added in a stepwise fashion. Porphobilinogen deaminase has a three-domain structure. Domains 1 (N-terminal) and 2 are duplications with the same structure, resembling the transferrins and periplasmic binding proteins. The dipyrromethane cofactor is covalently linked to domain 3 (C-terminal), but is bound by extensive salt-bridges and hydrogen-bonds within the cleft between domains 1 and 2, at a position corresponding to the binding sites for small-molecule ligands in the analogous proteins []. The enzyme has a single catalytic site, and the flexibility between domains is thought to aid elongation of the polypyrrole product in the active-site cleft of the enzyme. | Short Name: | Porphobilin_deaminase_cofac_BS |
| GO Term | Gene Name |
|---|---|
| GO:0004418 | IPR022419 |
| GO:0018160 | IPR022419 |
| GO:0033014 | IPR022419 |
