| IED ID | IndEnz0002010004 |
| Enzyme Type ID | protease010004 |
| Protein Name |
Proteasome subunit alpha 1 20S proteasome alpha subunit 1 Proteasome core protein PsmA 1 Cleaved into: Proteasome subunit alpha 1, N-terminally processed |
| Gene Name | psmA1 psmA HVO_1091 |
| 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 | MQGQAQQQAYDRGITIFSPDGRLYQVEYAREAVKRGTASIGVRTPEGVVLAADKRSRSPLMEPTSVEKIHKADDHIGIASAGHVADARQLIDFARRQSQVNRLRYGEPIGIETLTKEVTDHIQQYTQVGGARPFGVALLIGGVENGTPRLYETDPSGTPYEWKAVSIGADRGDHQEHLEENFRDDLTLDEGIELALEAIASTSDEGTAPDGVDVATVSAETERFVELSNDEIESYLEANDLLATEDDEQTEE |
| Enzyme Length | 252 |
| Uniprot Accession Number | Q9V2V6 |
| 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 (By similarity). In vitro, the chymotrypsin-like activity of the alpha1-beta proteasome is potently inhibited by carbobenzoxyl-leucinyl-leucinyl-leucinal-H (MG132) and significantly by N-acetyl-leucinyl-leucinyl-norleucinal-H (calpain inhibitor I). {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:10482525}. |
| 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 proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:10482525}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-9.3 for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Initiator methionine (1); Modified residue (1); Mutagenesis (3); Sequence conflict (1) |
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Proteasome;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PsmA 1 is expressed at a high and relatively constant level throughout growth. {ECO:0000269|PubMed:15516591}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; alternate; /evidence=ECO:0000269|PubMed:16950923 |
| Post Translational Modification | PTM: Acetylated. The acetylated form at Met-1 was shown to be in 100-fold excess of the unacetylated form with the initiator methionine removed in whole cells and purified 20S proteasomes. {ECO:0000269|PubMed:16950923, ECO:0000269|PubMed:19376868}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,613 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |