1,2-propanediol utilization protein U (PduU)/ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain; PduU encapsulates several related enzymes within a shell composed of a few thousand protein subunits. PduU exists as a hexamer which might further assemble into the flat facets of the polyhedral outer shell of the pdu organelle. This proteinaceous noncarboxysome microcompartment is involved in coenzyme B12-dependent degradation of 1,2-propanediol. The core of PduU is related to the typical 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 CD are sequence homologs 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. Although it has been suggested that EutS might also form hexamers and play similar functional roles in the construction of the eut organelle outer shell at present no experimental evidence directly supports this view.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496551236   8 IRIVQETVAGKEITFAHVIGGPAPIIYQKLGLNPAIDygaAAIGIMNMTPPESAVIAADIAVKSGDVYLGFADRFTGTVI 87
Cdd:cd07046    1 QRIIQEYVPGKQITLAHLIANPDPEIYQKLGLNPGVD---EAIGILTITPSEAAIIAADIATKAADVEIGFLDRFSGALV 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 496551236  88 ITGELADVTSALTEIVNYFRDELGYVVCRITKR 120
Cdd:cd07046   78 ITGDVSEVESALEAVVDYLRETLGFTVCPITKT 110

BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein subunits. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. These proteins for hexameric structure.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496551236   49 AIGIMNMTPPESAVIAADIAVKSGDVYLGFADRFTG---TVIITGELADVTSALTEIVNYFRDELGYV 113
Cdd:pfam00936   1 ALGLIETRGLAAGIEAADAMLKAANVELVGYELIGGgkvTVIITGDVAAVKAAVEAGVEAAERIGELV 68

1,2-propanediol utilization protein U (PduU)/ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain; PduU encapsulates several related enzymes within a shell composed of a few thousand protein subunits. PduU exists as a hexamer which might further assemble into the flat facets of the polyhedral outer shell of the pdu organelle. This proteinaceous noncarboxysome microcompartment is involved in coenzyme B12-dependent degradation of 1,2-propanediol. The core of PduU is related to the typical 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 CD are sequence homologs 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. Although it has been suggested that EutS might also form hexamers and play similar functional roles in the construction of the eut organelle outer shell at present no experimental evidence directly supports this view.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496551236   8 IRIVQETVAGKEITFAHVIGGPAPIIYQKLGLNPAIDygaAAIGIMNMTPPESAVIAADIAVKSGDVYLGFADRFTGTVI 87
Cdd:cd07046    1 QRIIQEYVPGKQITLAHLIANPDPEIYQKLGLNPGVD---EAIGILTITPSEAAIIAADIATKAADVEIGFLDRFSGALV 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 496551236  88 ITGELADVTSALTEIVNYFRDELGYVVCRITKR 120
Cdd:cd07046   78 ITGDVSEVESALEAVVDYLRETLGFTVCPITKT 110

BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein subunits. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. These proteins for hexameric structure.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496551236   49 AIGIMNMTPPESAVIAADIAVKSGDVYLGFADRFTG---TVIITGELADVTSALTEIVNYFRDELGYV 113
Cdd:pfam00936   1 ALGLIETRGLAAGIEAADAMLKAANVELVGYELIGGgkvTVIITGDVAAVKAAVEAGVEAAERIGELV 68

Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shell at present no experimental evidence directly supports this view.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496551236  49 AIGIMNMTPPESAVIAADIAVKSGDVYLGFADRF----TGTVIITGELADVTSALTEI 102
Cdd:cd06169    1 ALGLLEVRGLAAAIVAADAAVKAADVELVGIERAggggLVTLIIRGDVSAVKAAVEAA 58

1,2-propanediol utilization protein K (PduK), Bacterial Micro-Compartment (BMC) domain repeat 1l; PduK proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduK might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles at present no experimental evidence directly supports this view.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496551236  49 AIGIMNMTPPESAVIAADIAVKSGDVYLGFADRFTG----TVIITGELADVTSALTEIVNYFRDELGYVVCRITKR 120
Cdd:cd07056    1 SLGLLEVSGLSGAIVVADRMAKTANVRLLGLENTKGsgwmTVKISGDVAAVNAAIEAGKQTAGASDGYVASTVIAR 76