| IED ID | IndEnz0002008585 |
| Enzyme Type ID | protease008585 |
| Protein Name |
Proteasome subunit alpha 1 20S proteasome alpha subunit 1 Proteasome core protein PrcA 1 |
| Gene Name | prcA1 |
| Organism | Rhodococcus erythropolis (Arthrobacter picolinophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Nocardiaceae Rhodococcus Rhodococcus erythropolis group Rhodococcus erythropolis (Arthrobacter picolinophilus) |
| Enzyme Sequence | MTMPYYASAEQIMRDRSELARKGIARGRSVVVLTFRDGVLFVAENPSTALHKVSELYDRLGFAAVGKYNEFENLRRAGIVHADMRGYSYDRRDVTGRSLANAYAQTLGTIFTEQPKPYEVEICVAEVGRVGSPKAPQLYRITYDGSIVDEQHFVVMGGTTEPIATAMRESYRADLDLEAAVGIAVNALRQGGAGEGEKRNVDVASLEVAVLDQSRPRRAFRRIAGTALEQLVPAEPAAASESAPEPKPDTETKPADTQD |
| Enzyme Length | 259 |
| Uniprot Accession Number | Q53080 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity. {ECO:0000255|HAMAP-Rule:MF_00289}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:7583123, ECO:0000269|PubMed:9000518}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. {ECO:0000255|HAMAP-Rule:MF_00289}. |
| nucleotide Binding | |
| Features | Beta strand (13); Chain (1); Helix (7); Region (1); Turn (1) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Proteasome |
| Interact With | Q53079 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1Q5Q; 1Q5R; 2H6J; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,312 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=61.4 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha1 proteasome subtype) {ECO:0000269|PubMed:9000518}; KM=66.4 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha2 proteasome subtype) {ECO:0000269|PubMed:9000518}; KM=71.2 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha2 proteasome subtype) {ECO:0000269|PubMed:9000518}; KM=84.3 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha1 proteasome subtype) {ECO:0000269|PubMed:9000518}; Note=The Vmax observed with the beta2-alpha1 proteasome subtype is 2.2-fold, 1.2-fold and 4-fold higher than that with the beta2-alpha2, beta1-alpha2 and beta1-alpha1 subtypes, respectively.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |