| IED ID | IndEnz0002001858 |
| Enzyme Type ID | protease001858 |
| Protein Name |
Proteasome subunit beta type-1 EC 3.4.25.1 Macropain subunit PRE3 Multicatalytic endopeptidase complex subunit PRE3 Proteasome component PRE3 Proteinase YSCE subunit PRE3 |
| Gene Name | PRE3 YJL001W J1407 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MNGIQVDINRLKKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL |
| Enzyme Length | 215 |
| Uniprot Accession Number | P38624 |
| Absorption | |
| Active Site | ACT_SITE 20; /note=Nucleophile; /evidence=ECO:0000269|PubMed:9087403 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; |
| DNA Binding | |
| EC Number | 3.4.25.1 |
| Enzyme Function | FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.; FUNCTION: This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Chain (1); Erroneous initiation (2); Helix (7); Modified residue (1); Propeptide (1); Turn (3) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0007744|PubMed:22814378 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (25); X-ray crystallography (285) |
| Cross Reference PDB | 1FNT; 1G0U; 1G65; 1JD2; 1RYP; 1Z7Q; 2F16; 2FAK; 2GPL; 2ZCY; 3BDM; 3D29; 3DY3; 3DY4; 3E47; 3GPJ; 3GPT; 3GPW; 3HYE; 3JCO; 3JCP; 3MG0; 3MG4; 3MG6; 3MG7; 3MG8; 3NZJ; 3NZW; 3NZX; 3OEU; 3OEV; 3OKJ; 3SDI; 3SDK; 3SHJ; 3TDD; 3UN4; 3UN8; 3WXR; 4CR2; 4CR3; 4CR4; 4EU2; 4FZC; 4FZG; 4G4S; 4GK7; 4HNP; 4HRC; 4HRD; 4INR; 4INT; 4INU; 4J70; 4JSQ; 4JSU; 4JT0; 4LQI; 4LTC; 4NNN; 4NNW; 4NO1; 4NO6; 4NO8; 4NO9; 4Q1S; 4QBY; 4QLQ; 4QLS; 4QLT; 4QLU; 4QLV; 4QUX; 4QUY; 4QV0; 4QV1; 4QV3; 4QV4; 4QV5; 4QV6; 4QV7; 4QV8; 4QV9; 4QVL; 4QVM; 4QVN; 4QVP; 4QVQ; 4QVV; 4QVW; 4QVY; 4QW0; 4QW1; 4QW3; 4QW4; 4QW5; 4QW6; 4QW7; 4QWF; 4QWG; 4QWI; 4QWJ; 4QWK; 4QWL; 4QWR; 4QWS; 4QWU; 4QWX; 4QXJ; 4QZ0; 4QZ1; 4QZ2; 4QZ3; 4QZ4; 4QZ5; 4QZ6; 4QZ7; 4QZW; 4QZX; 4QZZ; 4R00; 4R02; 4R17; 4R18; 4RUR; 4V7O; 4X6Z; 4Y69; 4Y6A; 4Y6V; 4Y6Z; 4Y70; 4Y74; 4Y75; 4Y77; 4Y78; 4Y7W; 4Y7X; 4Y7Y; 4Y80; 4Y81; 4Y82; 4Y84; 4Y8G; 4Y8H; 4Y8I; 4Y8J; 4Y8K; 4Y8L; 4Y8M; 4Y8N; 4Y8O; 4Y8P; 4Y8Q; 4Y8R; 4Y8S; 4Y8T; 4Y8U; 4Y9Y; 4Y9Z; 4YA0; 4YA1; 4YA2; 4YA3; 4YA4; 4YA5; 4YA7; 4YA9; 4Z1L; 5A5B; 5AHJ; 5BOU; 5BXL; 5BXN; 5CGF; 5CGG; 5CGH; 5CGI; 5CZ4; 5CZ5; 5CZ6; 5CZ7; 5CZ8; 5CZ9; 5CZA; 5D0S; 5D0T; 5D0V; 5D0W; 5D0X; 5D0Z; 5DKI; 5DKJ; 5FG7; 5FG9; 5FGA; 5FGD; 5FGE; 5FGF; 5FGG; 5FGH; 5FGI; 5FHS; 5JHR; 5JHS; 5L52; 5L54; 5L55; 5L5A; 5L5B; 5L5D; 5L5E; 5L5F; 5L5H; 5L5I; 5L5J; 5L5O; 5L5P; 5L5Q; 5L5R; 5L5S; 5L5T; 5L5U; 5L5V; 5L5W; 5L5X; 5L5Y; 5L5Z; 5L60; 5L61; 5L62; 5L63; 5L64; 5L65; 5L66; 5L67; 5L68; 5L69; 5L6A; 5L6B; 5L6C; 5LAI; 5LAJ; 5LTT; 5M2B; 5MP9; 5MPA; 5MPB; 5MPC; 5NIF; 5WVI; 5WVK; 6EF3; 6FVT; 6FVU; 6FVV; 6FVW; 6FVX; 6FVY; 6G7F; 6G8M; 6G8N; 6GOP; 6H39; 6HTB; 6HTC; 6HTD; 6HTP; 6HTR; 6HUB; 6HUC; 6HUQ; 6HUU; 6HUV; 6HV3; 6HV4; 6HV5; 6HV7; 6HVA; 6HVR; 6HVS; 6HVT; 6HVU; 6HVV; 6HVW; 6HVX; 6HVY; 6HW0; 6HW3; 6HW4; 6HW5; 6HW6; 6HW7; 6HW8; 6HW9; 6HWA; 6HWB; 6HWC; 6HWD; 6HWE; 6HWF; 6J2C; 6J2N; 6J2Q; 6J2X; 6J30; 6ZOU; 6ZP6; 6ZP8; 7LS5; |
| Mapped Pubmed ID | 10393174; 10452902; 10500111; 10688190; 10872471; 11283351; 11493007; 11545745; 11595789; 11805826; 11805837; 12940990; 14722099; 14759368; 15571806; 15905137; 15916965; 16284124; 16429126; 16507144; 16537370; 16554755; 16713559; 16861887; 16922378; 17431397; 17911112; 18401409; 18482702; 18504300; 18928262; 19029916; 19162040; 19359491; 19678642; 19679091; 20625982; 20632995; 20715286; 20875739; 21139140; 21154547; 21211719; 21543789; 21685082; 21878652; 21946808; 22105886; 22229461; 22311637; 22341445; 22350874; 22350895; 22529852; 22822185; 22870914; 22930756; 23091006; 23202731; 23320547; 23540790; 23545414; 23547757; 23593271; 24285701; 24396728; 24403024; 24586798; 24706844; 24930969; 24979800; 25006746; 25038530; 25083872; 25087721; 25244435; 25332237; 25333764; 25486049; 25549323; 25581903; 25599643; 25609009; 25812915; 25973989; 26020686; 26050527; 26130806; 26242779; 26262643; 26365526; 26471124; 26563572; 26929360; 26964885; 27438186; 27677933; 27709817; 27789522; 28098422; 28106073; 28115689; 28733623; 29654304; 30029468; 30067984; 30165344; 30309908; 30365892; 30657666; 30792173; 3294103; 33452852; 33846632; 8861011; 9087396; 9207060; 9312134; 9398670; 9491890; 9642094; 9677364; 9748229; 9770515; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,548 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.25.1; |