LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Bacterial microcompartments (BCMs) function as organelles by sequestering particular metabolic processes within the cell. The shells of varied microcompartments are built primarily from small proteins belonging to the BMC domain family.This family represents Bacterial microcompartment shell protein EutS, PduU and CutR, all of them components of the BMC.PduU is minor shell protein of the BMC dedicated to the coenzyme B12-dependent degradation of 1,2-propanediol (1,2-PD) [ , ]. This protein exists as a hexamer which might further assemble into the flat facets of the polyhedral outer shell of the pdu microcompartments []. The core of PduU is related to the typical bacterial BMC domain and its natural oligomeric state is a cyclic hexamer. Unlike other typical BMC domain proteins, the 3D topology of PduU reveals a circular permuted variation on the typical BMC fold which leads to several unique features. The exact functions related to those unique features are still not clear. Another difference is the presence of a deep cavity on one side of the hexamer as well as an intermolecular six-stranded beta barrel that seems to block the central pore that is present in other BMC domain proteins.EutS proteins included in this family are sequence homologues of PduU. They are encoded within eut operon and may be required for the formation of the outer shell of bacterial eut polyhedral organelles which are involved in the cobalamin-dependent degradation of ethanolamine [ , ].CutR is a minor shell protein of the choline degradation-specific BMC. It may play a key role in conferring heterogeneity and flexibility in this BMC [ ]. |
| Short Name | EutS/PduU/CutR |
