| IED ID | IndEnz0002009057 | 
| Enzyme Type ID | protease009057 | 
| Protein Name | 
                        
                            
                                Proteasome subunit alpha 2  20S proteasome alpha subunit 2 Proteasome core protein PsmA 2  | 
                    
| Gene Name | psmA2 psmC HVO_2923 | 
| Organism | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) | 
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Haloferacales Haloferacaceae Haloferax Haloferax volcanii (Halobacterium volcanii) Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) | 
| Enzyme Sequence | MNRNDKQAYDRGTSLFSPDGRIYQVEYAREAVKRGAPVLGVRTADGVVLAALRSTPSELMEAESIEKLHKLDDALGAATAGHVADARKLVDFARTTAQREHLRYGEPIGVETLTKTITDNIQESTQSGGTRPYGASLLIGGVENGSGRLFATDPSGTPQEWKAVAIGGHREDVQAALEDGYAEDLSLEDGLALAVEALVAADEEIESDELNLVTVSEAGYEIVDEETIAELFADATADDESDETDEREE | 
| Enzyme Length | 249 | 
| Uniprot Accession Number | Q9V2V5 | 
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers 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 H.volcanii alpha1-beta-alpha2 proteasome is able to cleave oligopeptides after Tyr and thus displays chymotrypsin-like activity. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:10482525, ECO:0000269|PubMed:12486053}. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Modified residue (1) | 
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Proteasome;Reference proteome | 
| Interact With | |
| Induction | INDUCTION: Up-regulated at mRNA and protein levels during transition from exponential to stationary phase. {ECO:0000269|PubMed:15516591}. | 
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}. | 
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000269|PubMed:16950923 | 
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 26,727 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |