DB code: M00123

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
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
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
E.C. 3.4.25.1
CSA
M-CSA
MACiE M0177

CATH domain Related DB codes (homologues)
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 T00201 M00174 D00300

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq MEROPS Pfam
P40302 Proteasome component PRE5
EC 3.4.25.1
Macropain subunit PRE5
Proteinase YSCE subunit PRE5
Multicatalytic endopeptidase complex subunit PRE5
NP_014045.1 (Protein)
NM_001182825.1 (DNA/RNA sequence)
T01.976 (Threonine)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P23639 Proteasome component Y7
EC 3.4.25.1
Macropain subunit Y7
Proteinase YSCE subunit 7
Multicatalytic endopeptidase complex subunit Y7
NP_013618.1 (Protein)
NM_001182451.1 (DNA/RNA sequence)
T01.972 (Threonine)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P21242 Proteasome component C1
EC 3.4.25.1
Macropain subunit C1
Proteinase YSCE subunit 1
Multicatalytic endopeptidase complex subunit C1
NP_015007.1 (Protein)
NM_001183782.1 (DNA/RNA sequence)
T01.977 (Threonine)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P23638 Proteasome component Y13
EC 3.4.25.1
Macropain subunit Y13
Proteinase YSCE subunit 13
Multicatalytic endopeptidase complex subunit Y13
NP_011651.3 (Protein)
NM_001181264.3 (DNA/RNA sequence)
T01.973 (Threonine)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P32379 Proteasome component PUP2
EC 3.4.25.1
Macropain subunit PUP2
Proteinase YSCE subunit PUP2
Multicatalytic endopeptidase complex subunit PUP2
NP_011769.1 (Protein)
NM_001181382.1 (DNA/RNA sequence)
T01.975 (Threonine)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P21243 Proteasome component C7-alpha
EC 3.4.25.1
Macropain subunit C7-alpha
Proteinase YSCE subunit 7
Multicatalytic endopeptidase complex C7
Proteasome component Y8
SCL1 suppressor protein
NP_011504.3 (Protein)
NM_001180876.3 (DNA/RNA sequence)
T01.971 (Threonine)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P40303 Proteasome component PRE6
EC 3.4.25.1
Macropain subunit PRE6
Proteinase YSCE subunit PRE6
Multicatalytic endopeptidase complex subunit PRE6
NP_014604.1 (Protein)
NM_001183292.1 (DNA/RNA sequence)
T01.974 (Threonine)
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical View]
P23724 Proteasome component C5
EC 3.4.25.1
Multicatalytic endopeptidase complex subunit C5
NP_009512.1 (Protein)
NM_001178281.1 (DNA/RNA sequence)
T01.986 (Threonine)
PF00227 (Proteasome)
[Graphical View]
P22141 Proteasome component C11
EC 3.4.25.1
Macropain subunit C11
Proteinase YSCE subunit 11
Multicatalytic endopeptidase complex subunit C11
NP_010928.1 (Protein)
NM_001178903.1 (DNA/RNA sequence)
T01.984 (Threonine)
PF00227 (Proteasome)
[Graphical View]
P25451 Proteasome component PUP3
EC 3.4.25.1
Macropain subunit PUP3
Multicatalytic endopeptidase complex subunit PUP3
NP_011020.3 (Protein)
NM_001178985.3 (DNA/RNA sequence)
PF00227 (Proteasome)
[Graphical View]
P30657 Proteasome component PRE4
EC 3.4.25.1
Macropain subunit PRE4
Proteinase YSCE subunit PRE4
Multicatalytic endopeptidase complex subunit PRE4
NP_116708.1 (Protein)
NM_001180015.1 (DNA/RNA sequence)
T01.987 (Threonine)
PF00227 (Proteasome)
[Graphical View]
P30656 Proteasome component PRE2
EC 3.4.25.1
Macropain subunit PRE2
Proteinase YSCE subunit PRE2
Multicatalytic endopeptidase complex subunit PRE2
NP_015428.1 (Protein)
NM_001184200.1 (DNA/RNA sequence)
T01.012 (Threonine)
PF00227 (Proteasome)
[Graphical View]
P38624 Proteasome component PRE3
EC 3.4.25.1
Macropain subunit PRE3
Proteinase YSCE subunit PRE3
Multicatalytic endopeptidase complex subunit PRE3
NP_012533.1 (Protein)
NM_001181435.1 (DNA/RNA sequence)
T01.010 (Threonine)
PF00227 (Proteasome)
[Graphical View]
P25043 Proteasome component PUP1
EC 3.4.25.1
Macropain subunit PUP1
Proteinase YSCE subunit PUP1
Multicatalytic endopeptidase complex subunit PUP1
NP_014800.3 (Protein)
NM_001183576.3 (DNA/RNA sequence)
T01.011 (Threonine)
PF12465 (Pr_beta_C)
PF00227 (Proteasome)
[Graphical View]

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
P40302 PSA1_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P23639 PSA2_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P21242 PSA3_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P23638 PSA4_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P32379 PSA5_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P21243 PSA6_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1. Cytoplasm. Nucleus.
P40303 PSA7_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1. Cytoplasm. Nucleus.
P23724 PSB1_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P22141 PSB2_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P25451 PSB3_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P30657 PSB4_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1. Cytoplasm. Nucleus.
P30656 PSB5_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P38624 PSB6_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.
P25043 PSB7_YEAST Cleavage of peptide bonds with very broad specificity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Cytoplasm. Nucleus.

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
 15377
PubChem 22247451
 962
 22247451
 962
1fntA Unbound Unbound Unbound Unbound Unbound
1fntO Unbound Unbound Unbound Unbound Unbound
1g0uG Unbound Unbound Unbound Unbound Unbound
1g0uU Unbound Unbound Unbound Unbound Unbound
1g65G Unbound Unbound Unbound Unbound Unbound
1g65U Unbound Unbound Unbound Unbound Unbound
1jd22 Unbound Unbound Unbound Unbound Unbound
1jd2G Unbound Unbound Unbound Unbound Unbound
1rypA Unbound Unbound Unbound Unbound Unbound
1rypO Unbound Unbound Unbound Unbound Unbound
1fntB Unbound Unbound Unbound Unbound Unbound
1fntP Unbound Unbound Unbound Unbound Unbound
1g0uA Unbound Unbound Unbound Unbound Unbound
1g0uO Unbound Unbound Unbound Unbound Unbound
1g65A Unbound Unbound Unbound Unbound Unbound
1g65O Unbound Unbound Unbound Unbound Unbound
1jd2A Unbound Unbound Unbound Unbound Unbound
1jd2V Unbound Unbound Unbound Unbound Unbound
1rypB Unbound Unbound Unbound Unbound Unbound
1rypP Unbound Unbound Unbound Unbound Unbound
1fntC Unbound Unbound Unbound Unbound Unbound
1fntQ Unbound Unbound Unbound Unbound Unbound
1g0uB Unbound Unbound Unbound Unbound Unbound
1g0uP Unbound Unbound Unbound Unbound Unbound
1g65B Unbound Unbound Unbound Unbound Unbound
1g65P Unbound Unbound Unbound Unbound Unbound
1jd2B Unbound Unbound Unbound Unbound Unbound
1jd2W Unbound Unbound Unbound Unbound Unbound
1rypC Unbound Unbound Unbound Unbound Unbound
1rypQ Unbound Unbound Unbound Unbound Unbound
1fntD Unbound Unbound Unbound Unbound Unbound
1fntR Unbound Unbound Unbound Unbound Unbound
1g0uC Unbound Unbound Unbound Unbound Unbound
1g0uQ Unbound Unbound Unbound Unbound Unbound
1g65C Unbound Unbound Unbound Unbound Unbound
1g65Q Unbound Unbound Unbound Unbound Unbound
1jd2C Unbound Unbound Unbound Unbound Unbound
1jd2X Unbound Unbound Unbound Unbound Unbound
1rypD Unbound Unbound Unbound Unbound Unbound
1rypR Unbound Unbound Unbound Unbound Unbound
1fntE Unbound Unbound Unbound Unbound Unbound
1fntS Unbound Unbound Unbound Unbound Unbound
1g0uD Unbound Unbound Unbound Unbound Unbound
1g0uR Unbound Unbound Unbound Unbound Unbound
1g65D Unbound Unbound Unbound Unbound Unbound
1g65R Unbound Unbound Unbound Unbound Unbound
1jd2D Unbound Unbound Unbound Unbound Unbound
1jd2Y Unbound Unbound Unbound Unbound Unbound
1rypE Unbound Unbound Unbound Unbound Unbound
1rypS Unbound Unbound Unbound Unbound Unbound
1fntF Unbound Unbound Unbound Unbound Unbound
1fntT Unbound Unbound Unbound Unbound Unbound
1g0uE Unbound Unbound Unbound Unbound Unbound
1g0uS Unbound Unbound Unbound Unbound Unbound
1g65E Unbound Unbound Unbound Unbound Unbound
1g65S Unbound Unbound Unbound Unbound Unbound
1jd2E Unbound Unbound Unbound Unbound Unbound
1jd2Z Unbound Unbound Unbound Unbound Unbound
1rypF Unbound Unbound Unbound Unbound Unbound
1rypT Unbound Unbound Unbound Unbound Unbound
1fntG Unbound Unbound Unbound Unbound Unbound
1fntU Unbound Unbound Unbound Unbound Unbound
1g0uF Unbound Unbound Unbound Unbound Unbound
1g0uT Unbound Unbound Unbound Unbound Unbound
1g65F Unbound Unbound Unbound Unbound Unbound
1g65T Unbound Unbound Unbound Unbound Unbound
1jd21 Unbound Unbound Unbound Unbound Unbound
1jd2F Unbound Unbound Unbound Unbound Unbound
1rypG Unbound Unbound Unbound Unbound Unbound
1rypU Unbound Unbound Unbound Unbound Unbound
1fntH Unbound Unbound Unbound Unbound Unbound
1fntV Unbound Unbound Unbound Unbound Unbound
1g0u2 Unbound Unbound Unbound Unbound Unbound
1g0uN Unbound Unbound Unbound Unbound Unbound
1g652 Unbound Unbound Unbound Unbound Unbound
1g65N Unbound Unbound Unbound Unbound Unbound
1jd2N Unbound Unbound Unbound Unbound Unbound
1jd2U Unbound Unbound Unbound Unbound Unbound
1rypH Unbound Unbound Unbound Unbound Unbound
1rypV Unbound Unbound Unbound Unbound Unbound
1fntI Unbound Unbound Unbound Unbound Unbound
1fntW Unbound Unbound Unbound Unbound Unbound
1g0uH Unbound Unbound Unbound Unbound Unbound
1g0uV Unbound Unbound Unbound Unbound Unbound
1g65H Unbound Unbound Unbound Unbound Unbound
1g65V Unbound Unbound Unbound Unbound Unbound
1jd2H Unbound Analogue:95A Unbound Unbound Unbound
1jd2O Unbound Analogue:95A Unbound Unbound Unbound
1rypI Unbound Unbound Unbound Unbound Unbound
1rypW Unbound Unbound Unbound Unbound Unbound
1fntJ Unbound Unbound Unbound Unbound Unbound
1fntX Unbound Unbound Unbound Unbound Unbound
1g0uI Unbound Unbound Unbound Unbound Unbound
1g0uW Unbound Unbound Unbound Unbound Unbound
1g65I Unbound Unbound Unbound Unbound Unbound
1g65W Unbound Unbound Unbound Unbound Unbound
1jd2I Unbound Unbound Unbound Unbound Unbound
1jd2P Unbound Unbound Unbound Unbound Unbound
1rypJ Unbound Unbound Unbound Unbound Unbound
1rypX Unbound Unbound Unbound Unbound Unbound
1fntK Unbound Unbound Unbound Unbound Unbound
1fntY Unbound Unbound Unbound Unbound Unbound
1g0uJ Unbound Unbound Unbound Unbound Unbound
1g0uX Unbound Unbound Unbound Unbound Unbound
1g65J Unbound Unbound Unbound Unbound Unbound
1g65X Unbound Unbound Unbound Unbound Unbound
1jd2J Unbound Unbound Unbound Unbound Unbound
1jd2Q Unbound Unbound Unbound Unbound Unbound
1rypK Unbound Unbound Unbound Unbound Unbound
1rypY Unbound Unbound Unbound Unbound Unbound
1fntL Unbound Unbound Unbound Unbound Unbound
1fntZ Unbound Unbound Unbound Unbound Unbound
1g0uK Unbound Unbound Unbound Unbound Unbound
1g0uY Unbound Unbound Unbound Unbound Unbound
1g65K Unbound Unbound Unbound Unbound Intermediate-analogue:EPX
1g65Y Unbound Unbound Unbound Unbound Intermediate-analogue:EPX
1jd2K Unbound Unbound Unbound Unbound Unbound
1jd2R Unbound Unbound Unbound Unbound Unbound
1rypL Unbound Unbound Unbound Unbound Unbound
1rypZ Unbound Unbound Unbound Unbound Unbound
1fnta Unbound Unbound Unbound Unbound Unbound
1fntM Unbound Unbound Unbound Unbound Unbound
1g0uL Unbound Unbound Unbound Unbound Unbound
1g0uZ Unbound Unbound Unbound Unbound Unbound
1g65L Unbound Unbound Unbound Unbound Unbound
1g65Z Unbound Unbound Unbound Unbound Unbound
1jd2L Unbound Unbound Unbound Unbound Unbound
1jd2S Unbound Unbound Unbound Unbound Unbound
1ryp1 Unbound Unbound Unbound Unbound Unbound
1rypM Unbound Unbound Unbound Unbound Unbound
1fntb Unbound Unbound Unbound Unbound Unbound
1fntN Unbound Unbound Unbound Unbound Unbound
1g0u1 Unbound Unbound Unbound Unbound Unbound
1g0uM Unbound Unbound Unbound Unbound Unbound
1g651 Unbound Unbound Unbound Unbound Unbound
1g65M Unbound Unbound Unbound Unbound Unbound
1jd2M Unbound Unbound Unbound Unbound Unbound
1jd2T Unbound Unbound Unbound Unbound Unbound
1ryp2 Unbound Unbound Unbound Unbound Unbound
1rypN Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [8], [11], [16], [18], [20], [23] & [35]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1fntA
1fntO
1g0uG
1g0uU
1g65G
1g65U
1jd22
1jd2G
1rypA
1rypO
1fntB
1fntP
1g0uA
1g0uO
1g65A
1g65O
1jd2A
1jd2V
1rypB
1rypP
1fntC
1fntQ
1g0uB
1g0uP
1g65B
1g65P
1jd2B
1jd2W
1rypC
1rypQ
1fntD
1fntR
1g0uC
1g0uQ
1g65C
1g65Q
1jd2C
1jd2X
1rypD
1rypR
1fntE
1fntS
1g0uD
1g0uR
1g65D
1g65R
1jd2D
1jd2Y
1rypE
1rypS
1fntF
1fntT
1g0uE
1g0uS
1g65E
1g65S
1jd2E
1jd2Z
1rypF
1rypT
1fntG
1fntU
1g0uF
1g0uT
1g65F
1g65T
1jd21
1jd2F
1rypG
1rypU
1fntH THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1fntV THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g0u2 THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g0uN THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g652 THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g65N THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1jd2N THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1jd2U THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1rypH ;ASP 17;LYS 33;SER 129;ASP 166;SER 169 ;GLY 47 mutant T1A
1rypV ;ASP 17;LYS 33;SER 129;ASP 166;SER 169 ;GLY 47 mutant T1A
1fntI THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1fntW THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g0uH THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g0uV THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g65H THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g65V THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1jd2H THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1jd2O THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1rypI THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1rypW THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1fntJ
1fntX
1g0uI
1g0uW
1g65I
1g65W
1jd2I
1jd2P
1rypJ
1rypX
1fntK
1fntY
1g0uJ
1g0uX
1g65J
1g65X
1jd2J
1jd2Q
1rypK
1rypY
1fntL THR 1;ASP 17; ;SER 131;ASP 168;SER 171 THR 1;GLY 47 mutant K33R
1fntZ THR 1;ASP 17; ;SER 131;ASP 168;SER 171 THR 1;GLY 47 mutant K33R
1g0uK THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g0uY THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1g65K ;ASP 17;LYS 33;SER 129;ASP 166;SER 169 ;GLY 47 complex with ligand (T1)
1g65Y ;ASP 17;LYS 33;SER 129;ASP 166;SER 169 ;GLY 47 complex with ligand (T1)
1jd2K THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1jd2R THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169 THR 1;GLY 47
1rypL THR 1;ASP 17; ;SER 131;ASP 168;SER 171 THR 1;GLY 47 mutant K33R
1rypZ THR 1;ASP 17; ;SER 131;ASP 168;SER 171 THR 1;GLY 47 mutant K33R
1fnta
1fntM
1g0uL
1g0uZ
1g65L
1g65Z
1jd2L
1jd2S
1ryp1
1rypM
1fntb
1fntN
1g0u1
1g0uM
1g651
1g65M
1jd2M
1jd2T
1ryp2
1rypN

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
p.812-814
[7]
p.969
[10]
p.105-106
[11]
Fig.5, p.466-470
[14]
Figure 4, p.1190-1191
[16]
p.3582
[18]
p.10980-10981
[20]
Fig.2, p.1237-1238
[29]
p.28-29
[35]
p.34-36

References
[1]
Resource
Comments
Medline ID
PubMed ID 7781614
Journal EMBO J
Year 1995
Volume 14
Pages 2620-30
Authors Chen P, Hochstrasser M
Title Biogenesis, structure and function of the yeast 20S proteasome.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7565661
Journal Mol Biol Rep
Year 1995
Volume 21
Pages 3-10
Authors Hilt W, Wolf DH
Title Proteasomes of the yeast S. cerevisiae: genes, structure and functions.
Related PDB
Related UniProtKB
[3]
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
[4]
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
[5]
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
[6]
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
[7]
Resource
Comments
Medline ID
PubMed ID 8808631
Journal Cell
Year 1996
Volume 86
Pages 961-72
Authors Chen P, Hochstrasser M
Title Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 9003765
Journal EMBO J
Year 1996
Volume 15
Pages 6887-98
Authors Schmidtke G, Kraft R, Kostka S, Henklein P, Frommel C, Lowe J, Huber R, Kloetzel PM, Schmidt M
Title Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis.
Related PDB
Related UniProtKB
[9]
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
[10]
Resource
Comments
Medline ID
PubMed ID 9228290
Journal Mol Biol Rep
Year 1997
Volume 24
Pages 103-12
Authors Schmidt M, Schmidtke G, Kloetzel PM
Title Structure and structure formation of the 20S proteasome.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID
PubMed ID 9087403
Journal Nature
Year 1997
Volume 386
Pages 463-71
Authors Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R
Title Structure of 20S proteasome from yeast at 2.4 A resolution.
Related PDB 1ryp
Related UniProtKB P40302 P23639 P21242 P23638 P32379 P21243 P40303 P23724 P22141 P25451 P30657 P30656 P38624 P25043
[12]
Resource
Comments
Medline ID
PubMed ID 9207060
Journal Proc Natl Acad Sci U S A
Year 1997
Volume 94
Pages 7156-61
Authors Arendt CS, Hochstrasser M
Title Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9538192
Journal J Biochem (Tokyo)
Year 1998
Volume 123
Pages 195-204
Authors Tanaka K
Title Proteasomes: structure and biology.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9642094
Journal J Mol Biol
Year 1998
Volume 279
Pages 1187-91
Authors Ditzel L, Huber R, Mann K, Heinemeyer W, Wolf DH, Groll M
Title Conformational constraints for protein self-cleavage in the proteasome.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 10099130
Journal Chem Biol
Year 1999
Volume 6
Pages 197-204
Authors Loidl G, Groll M, Musiol HJ, Ditzel L, Huber R, Moroder L
Title Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 10393174
Journal EMBO J
Year 1999
Volume 18
Pages 3575-85
Authors Arendt CS, Hochstrasser M
Title Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 10452902
Journal J Mol Biol
Year 1999
Volume 291
Pages 997-1013
Authors Jager S, Groll M, Huber R, Wolf DH, Heinemeyer W
Title Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 10500111
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 10976-83
Authors Groll M, Heinemeyer W, Jager S, Ullrich T, Bochtler M, Wolf DH, Huber R
Title The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 10318898
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 5418-22
Authors Loidl G, Groll M, Musiol HJ, Huber R, Moroder L
Title Bivalency as a principle for proteasome inhibition.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 2000
Volume 122
Pages 1237-8
Authors Groll M, Kim KB, Kairies N, Crews C
Title Crystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity of alpha,beta-epoxyketone proteasome inhibitors.
Related PDB 1g65
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 10747864
Journal J Biol Chem
Year 2000
Volume 275
Pages 13171-4
Authors Osmulski PA, Gaczynska M
Title Atomic force microscopy reveals two conformations of the 20 S proteasome from fission yeast.
Related PDB
Related UniProtKB
[22]
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
[23]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11062564
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 1062-7
Authors Groll M, Bajorek M, Kohler A, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D
Title A gated channel into the proteasome core particle.
Related PDB 1g0u
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 11062549
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 999-1001
Authors Pickart CM, VanDemark AP
Title Opening doors into the proteasome.
Related PDB
Related UniProtKB
[25]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11081519
Journal Nature
Year 2000
Volume 408
Pages 115-20
Authors Whitby FG, Masters EI, Kramer L, Knowlton JR, Yao Y, Wang CC, Hill CP
Title Structural basis for the activation of 20S proteasomes by 11S regulators.
Related PDB 1fnt
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 11295493
Journal Biochimie
Year 2001
Volume 83
Pages 325-32
Authors Kohler A, Bajorek M, Groll M, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D
Title The substrate translocation channel of the proteasome.
Related PDB
Related UniProtKB
[27]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11493007
Journal J Mol Biol
Year 2001
Volume 311
Pages 543-8
Authors Groll M, Koguchi Y, Huber R, Kohno J
Title Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor.
Related PDB 1jd2
Related UniProtKB
[28]
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
[29]
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
[30]
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
[31]
Resource
Comments
Medline ID
PubMed ID 11820928
Journal J Biochem (Tokyo)
Year 2002
Volume 131
Pages 171-3
Authors Unno M, Mizushima T, Morimoto Y, Tomisugi Y, Tanaka K, Yasuoka N, Tsukihara T
Title Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 A resolution.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 11927581
Journal J Biol Chem
Year 2002
Volume 277
Pages 22260-70
Authors Kisselev AF, Kaganovich D, Goldberg AL
Title Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 12015144
Journal Structure (Camb)
Year 2002
Volume 10
Pages 609-18
Authors Unno M, Mizushima T, Morimoto Y, Tomisugi Y, Tanaka K, Yasuoka N, Tsukihara T
Title The structure of the mammalian 20S proteasome at 2.75 A resolution.
Related PDB
Related UniProtKB
[34]
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
[35]
Resource
Comments
Medline ID
PubMed ID 15571807
Journal Biochim Biophys Acta
Year 2004
Volume 1695
Pages 33-44
Authors Groll M, Huber R
Title Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 15589823
Journal FEBS Lett
Year 2004
Volume 578
Pages 217-23
Authors Ferrington DA, Kapphahn RJ
Title Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 14722099
Journal J Biol Chem
Year 2004
Volume 279
Pages 14323-30
Authors Ramos PC, Marques AJ, London MK, Dohmen RJ
Title Role of C-terminal extensions of subunits beta2 and beta7 in assembly and activity of eukaryotic proteasomes.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 15713476
Journal J Mol Biol
Year 2005
Volume 346
Pages 1221-7
Authors Ortega J, Heymann JB, Kajava AV, Ustrell V, Rechsteiner M, Steven AC
Title The axial channel of the 20S proteasome opens upon binding of the PA200 activator.
Related PDB
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 14 different subunits. All the alpha-subunits are enzymatically inactive, whereas three of seven beta-subunits (PRE3, PUP1 & PRE2) exhibit proteolytic activity.
According to the protein names in Swiss-prot, corresponding subunits of these structures seem to be as follows (see [11] & [18]):
These subunits are homologous but different.
alpha1 = PSA6_YEAST;P21243 (PRS2 PRC2 SCL1)
alpha2 = PSA2_YEAST;P23639 (PRE8 PRS4 Y7)
alpha3 = PSA4_YEAST;P23638 (PRE9 PRS5 Y13)
alpha4 = PSA7_YEAST;P40303 (PRE6)
alpha5 = PSA5_YEAST;P32379 (PUP2 DOA5)
alpha6 = PSA1_YEAST;P40302 (PRE5)
alpha7 = PSA3_YEAST;P21242 (PRE10 PRS1 PRC1)
beta1 = PSB6_YEAST;P38624 (PRE3) (Catalytic subunit)
beta2 = PSB7_YEAST;P25043 (PUP1) (Catalytic subunit)
beta3 = PSB3_YEAST;P25451 (PUP3)
beta4 = PSB2_YEAST;P22141 (PRE1 C11)
beta5 = PSB5_YEAST;P30656 (PRE2 DOA3 PRG1) (Catalytic subunit)
beta6 = PSB1_YEAST;P23724 (PRE7 PRS3 PTS1 C5)
beta7 = PSB4_YEAST;P30657 (PRE4)
Chains of PDB entries (above) were grouped in each subunit.
According to the literature [8], [11], [16], [18], [20], [29] & [35], the catalytic reaction probably proceeds as follwos:
(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 Asp17, 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. 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, which completes hydrolysis.

Created Updated
2002-07-01 2009-02-26