DB code: M00174

RLCP classification 1.13.30010.35 : Hydrolysis
CATH domain 3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
E.C. 3.4.25.1
CSA 1pma
M-CSA 1pma
MACiE

CATH domain Related DB codes (homologues)
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 T00201 M00123 D00300

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam MEROPS
P25156 Proteasome subunit alpha
EC 3.4.25.1
20S proteasome alpha subunit
Proteasome core protein PsmA
NP_394744.1 (Protein)
NC_002578.1 (DNA/RNA sequence)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P28061 Proteasome subunit beta
EC 3.4.25.1
20S proteasome beta subunit
Proteasome core protein PsmB
NP_394085.1 (Protein)
NC_002578.1 (DNA/RNA sequence)
PF00227 (Proteasome)
[Graphical View]
T01.002 (Threonine)

KEGG enzyme name
proteasome endopeptidase complex
ingensin
macropain
multicatalytic endopeptidase complex
prosome
multicatalytic proteinase (complex)
MCP
proteasome
large multicatalytic protease
multicatalytic proteinase
proteasome organelle
alkaline protease
26S protease
tricorn proteinase
tricorn protease

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P28061 PSMB_THEAC Cleavage of peptide bonds with very broad specificity. Composed of two subunits, alpha and beta. The complex is formed of four rings. The two outer rings are each composed of seven alpha subunits. The two inner rings are each composed of seven beta subunits. Cytoplasm.
P25156 PSMA_THEAC Cleavage of peptide bonds with very broad specificity. Composed of two subunits, alpha and beta. The complex is formed of four rings. The two outer rings are each composed of seven alpha subunits. The two inner rings are each composed of seven beta subunits. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00012 C00001 C00017 C00012
E.C.
Compound Protein Peptide H2O Protein Peptide
Type peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 15377
PubChem 22247451
962
1pmaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaO Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaP Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaQ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaR Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaS Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaT Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaU Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaV Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaW Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaX Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaY Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pmaZ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pma1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pma2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7L Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7M Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ya7N Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yarN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yauN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1pmaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaO Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ya7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ya7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ya7C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ya7D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ya7E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ya7F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ya7G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yarA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yarB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yarC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yarD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yarE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yarF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yarG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yauA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yauB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yauC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yauD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yauE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yauF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yauG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pmaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaP Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaQ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaR Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaS Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaT Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaU Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaV Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaW Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaX Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaY Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pmaZ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pma1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1pma2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1ya7H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1ya7I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1ya7J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1ya7K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1ya7L Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1ya7M Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1ya7N Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yarH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yarI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yarJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yarK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yarL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yarM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yarN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yauH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yauI Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yauJ Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yauK Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yauL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yauM Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47
1yauN Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 1;GLU 17;LYS 33;ASP 166 THR 1;GLY 47

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.4, p.517-519
[4]
Fig.5A, p.529-530
[11]
p.418
[13]
p.381-382
[16]
p.275-276
[18]
Fig.2, p.4-5
[19]
p.840-841
[20]
Fig.2

References
[1]
Resource
Comments
Medline ID
PubMed ID 7697124
Journal Enzyme Protein
Year 1993
Volume 47
Pages 252-73
Authors Lupas A, Koster AJ, Baumeister W
Title Structural features of 26S and 20S proteasomes.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7697123
Journal Enzyme Protein
Year 1993
Volume 47
Pages 241-51
Authors Tanahashi N, Tsurumi C, Tamura T, Tanaka K
Title Molecular structure of 20S and 26S proteasomes.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8824424
Journal Cold Spring Harb Symp Quant Biol
Year 1995
Volume 60
Pages 515-24
Authors Lupas A, Zwickl P, Wenzel T, Seemuller E, Baumeister W
Title Structure and function of the 20S proteasome and of its regulatory complexes.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8824425
Journal Cold Spring Harb Symp Quant Biol
Year 1995
Volume 60
Pages 525-32
Authors Stock D, Ditzel L, Baumeister W, Huber R, Lowe J
Title Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7867793
Journal FEBS Lett
Year 1995
Volume 359
Pages 173-8
Authors Seemuller E, Lupas A, Zuhl F, Zwickl P, Baumeister W
Title The proteasome from Thermoplasma acidophilum is neither a cysteine nor a serine protease.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 7565658
Journal Mol Biol Rep
Year 1995
Volume 21
Pages 11-20
Authors Koster AJ, Walz J, Lupas A, Baumeister W
Title Structural features of archaebacterial and eukaryotic proteasomes.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 7477383
Journal Nature
Year 1995
Volume 378
Pages 416-9
Authors Brannigan JA, Dodson G, Duggleby HJ, Moody PC, Smith JL, Tomchick DR, Murzin AG
Title A protein catalytic framework with an N-terminal nucleophile is capable of self-activation.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 7725095
Journal Science
Year 1995
Volume 268
Pages 522-3
Authors Goldberg AL
Title Functions of the proteasome: the lysis at the end of the tunnel.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7725097
Journal Science
Year 1995
Volume 268
Pages 533-9
Authors Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R
Title Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
Related PDB 1pma
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 7725107
Journal Science
Year 1995
Volume 268
Pages 579-82
Authors Seemuller E, Lupas A, Stock D, Lowe J, Huber R, Baumeister W
Title Proteasome from Thermoplasma acidophilum: a threonine protease.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 7663937
Journal Structure
Year 1995
Volume 3
Pages 417-20
Authors Wlodawer A
Title Proteasome: a complex protease with a new fold and a distinct mechanism.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8811196
Journal Annu Rev Biochem
Year 1996
Volume 65
Pages 801-47
Authors Coux O, Tanaka K, Goldberg AL
Title Structure and functions of the 20S and 26S proteasomes.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8768894
Journal Curr Opin Biotechnol
Year 1996
Volume 7
Pages 376-85
Authors Stock D, Nederlof PM, Seemuller E, Baumeister W, Huber R, Lowe J
Title Proteasome: from structure to function.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 8684489
Journal Nature
Year 1996
Volume 382
Pages 468-71
Authors Seemuller E, Lupas A, Baumeister W
Title Autocatalytic processing of the 20S proteasome.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9377486
Journal Biol Chem
Year 1997
Volume 378
Pages 893-8
Authors Escherich A, Ditzel L, Musiol HJ, Groll M, Huber R, Moroder L
Title Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9094332
Journal Curr Opin Struct Biol
Year 1997
Volume 7
Pages 273-8
Authors Baumeister W, Lupas A
Title The proteasome.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9334174
Journal J Biol Chem
Year 1997
Volume 272
Pages 26103-9
Authors Mc Cormack T, Baumeister W, Grenier L, Moomaw C, Plamondon L, Pramanik B, Slaughter C, Soucy F, Stein R, Zuhl F, Dick L
Title Active site-directed inhibitors of Rhodococcus 20 S proteasome. Kinetics and mechanism.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 11097171
Journal Arch Biochem Biophys
Year 2000
Volume 383
Pages 1-16
Authors Orlowski M, Wilk S
Title Catalytic activities of the 20 S proteasome, a multicatalytic proteinase complex.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 10966872
Journal Front Biosci
Year 2000
Volume 5
Pages D837-65
Authors Maupin-Furlow JA, Wilson HL, Kaczowka SJ, Ou MS
Title Proteasomes in the archaea: from structure to function.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 10809725
Journal J Biol Chem
Year 2000
Volume 275
Pages 14831-7
Authors Kisselev AF, Songyang Z, Goldberg AL
Title Why does threonine, and not serine, function as the active site nucleophile in proteasomes?
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 10843865
Journal J Mol Biol
Year 2000
Volume 299
Pages 1147-54
Authors Gille C, Goede A, Preissner R, Rother K, Frommel C
Title Conservation of substructures in proteins: interfaces of secondary structural elements in proteasomal subunits.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 12083009
Journal Curr Top Microbiol Immunol
Year 2002
Volume 268
Pages 73-89
Authors Hill CP, Masters EI, Whitby FG
Title The 11S regulators of 20S proteasome activity.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 12083007
Journal Curr Top Microbiol Immunol
Year 2002
Volume 268
Pages 23-41
Authors Zwickl P
Title The 20S proteasome.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 12354607
Journal FEBS Lett
Year 2002
Volume 529
Pages 22-6
Authors Dantuma NP, Masucci MG
Title Stabilization signals: a novel regulatory mechanism in the ubiquitin/proteasome system.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 12941688
Journal EMBO J
Year 2003
Volume 22
Pages 4356-64
Authors Forster A, Whitby FG, Hill CP
Title The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 12614609
Journal J Mol Biol
Year 2003
Volume 327
Pages 75-83
Authors Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R
Title Investigations on the maturation and regulation of archaebacterial proteasomes.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 15916965
Journal Mol Cell
Year 2005
Volume 18
Pages 589-99
Authors Forster A, Masters EI, Whitby FG, Robinson H, Hill CP
Title The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions.
Related PDB 1ya7 1yar 1yau
Related UniProtKB

Comments
This enzyme was transferred from E.C. 3.4.99.46 to E.C. 3.4.25.1.
The structure of this enzyme is cylindrical with four layers of seven subunits, composed of two different subunits, alpha and beta. All the alpha subunits are enzymatically inactive, whereas the beta-subunits exhibit proteolytic activity. Alpha- and beta-subunits belong to peptidase family-T1A and -T1B, respectively.
According to the literature [18], this enzyme has got a similar mechanism to that of its counterpart in yeast (M00123 in EzCatDB).
(1) Alpha-amino group of Thr1 acts as a general base to activate the nucleophile, sidechain of Thr1, through a water molecule (NUK). At the same time, Lys33, which is modulated by Glu17, might modulate or stabilize the nucleophilicity of Thr1.
(2) Thr1 makes a nucleophilic attack on the carbonyl carbon of the target peptide bond, forming a tetrahedral (hemiacetal) transition-state.
(3) The alpha-amino group of Thr1 acts as a general acid to protonate the leaving group, giving a carbonyl intermediate through a water. The intermediate might be stabilized by an oxyanion hole, composed of the sidechain of Lys33 and mainchain amide of Gly47.
(4) Alpha-amino group of Thr1 acts as a general base to activate the NUK water, through another water, which completes hydrolysis.
###
Autocatalysis, in which Thr1 acts as a nucleophile and Ser129 forms an oxyanion hole, activates the catalytic site of this enzyme (see [14]).

Created Updated
2002-07-01 2010-02-03