| IED ID | IndEnz0018000609 |
| Enzyme Type ID | peroxidase000609 |
| Protein Name |
Bacterial microcompartment shell protein PduA Bacterial microcompartment protein homohexamer BMC-H Propanediol utilization protein PduA |
| Gene Name | pduA STM2038 |
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Enzyme Sequence | MQQEALGMVETKGLTAAIEAADAMVKSANVMLVGYEKIGSGLVTVIVRGDVGAVKAATDAGAAAARNVGEVKAVHVIPRPHTDVEKILPKGISQ |
| Enzyme Length | 94 |
| Uniprot Accession Number | P0A1C7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation (PubMed:11844753, PubMed:21239588) (Probable). At least one of PduA or PduJ is required for BMC assembly; it must be encoded as the first gene in the pdu operon (PubMed:33227310, PubMed:27561553). Not required for structural integrity of BMCs, it is required to mitigate propionaldehyde toxicity (PubMed:21239588). Controls diffusion of 1,2-PD into and propionaldehyde out of the BMC shell; residue 40 is particularly important for pore permeability (PubMed:28585808, PubMed:25713376, PubMed:27561553) (Probable). Overexpression of this protein leads to aberrant filaments that extend the length of the cell, cross the cleavage furrow and impair division. The filaments form nanotubes with a hollow center (PubMed:11844753, PubMed:33227310). The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). Edge residues (particularly Lys-26) are important for function and assembly of the BMC, and influence array formation by hexamers (PubMed:24747050). Interaction with PduA allows encapsulation of at least PduP in BMCs (PubMed:22927404). Probably also targets PduD to the BMC (Probable). PduA is probably the hub for binding multiple enzymes to the interior of the BMC; modeling suggests PduC, PduD, PduE, PduG, PduL and PduP are targeted to PduA (Probable). {ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21239588, ECO:0000269|PubMed:22927404, ECO:0000269|PubMed:24747050, ECO:0000269|PubMed:25713376, ECO:0000269|PubMed:27561553, ECO:0000269|PubMed:28585808, ECO:0000269|PubMed:33227310, ECO:0000305|PubMed:20870711, ECO:0000305|PubMed:24747050, ECO:0000305|PubMed:25646976, ECO:0000305|PubMed:26283792, ECO:0000305|PubMed:28829618}.; FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. {ECO:0000269|PubMed:18296526, ECO:0000269|PubMed:25713376, ECO:0000305|PubMed:28475631}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000305|PubMed:10498708}. |
| nucleotide Binding | |
| Features | Beta strand (4); Chain (1); Domain (1); Helix (2); Mutagenesis (18); Turn (1) |
| Keywords | 3D-structure;Bacterial microcompartment;Direct protein sequencing;Reference proteome;Transport |
| Interact With | |
| Induction | INDUCTION: The first gene in the pdu operon. BMC production is induced by growth on 1,2-PD vitamin B12 medium (PubMed:10498708, PubMed:26283792). No change when grown in the presence of 1,2-PD, ethanolamine and vitamin B12, suggesting it is possible for both the eut and pdu operons to be expressed at the same time (PubMed:26283792). {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:26283792}. |
| Subcellular Location | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:24747050, ECO:0000269|PubMed:25713376, ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:28585808}. Note=The C-terminus probably faces the interior of the BMC (Probable). Modeling suggests the concave face (with both termini) is in the interior of the BMC (Probable). {ECO:0000305|PubMed:22927404, ECO:0000305|PubMed:25646976}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 3NGK; 4PPD; 4QIE; 4QIF; 4QIG; 4RBT; 4RBU; 4RBV; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 9,592 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |