v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | This entry represents the CpcT/CpeT biliprotein lyase, which has been shown to covalently attach chromophores to cystiene residue(s) of phycobiliproteins [ , ]. These proteins contain a conserved motif PYR in the amino terminal half of the protein that may be functionally important. In the chromatically adapting cyanobacterium Fremyella diplosiphon, the proteins have been shown to be induced by green light, as part of the cpeCDESTR operon [].Structurally, CpcT forms a dimer and adopts a calyx-shaped β-barrel fold. Each CpcT subunit adopts a conical, goblet-shaped β-barrel with 10 anti-parallel β-strands; this fold is characteristic for the FABP subfamily of the calycin superfamily. |
| Short Name | CpcT/CpeT_sf |