EzCatDB: M00123
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeM00123
RLCP classification1.13.30010.35 : Hydrolysis
CATH domainDomain 13.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 23.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 33.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 43.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 53.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 63.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 73.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 83.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 93.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 103.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 113.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 123.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 133.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 143.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 153.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1Catalytic domain
Domain 163.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1Catalytic domain
Domain 173.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1Catalytic domain
Domain 183.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1Catalytic domain
Domain 193.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 203.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 213.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 223.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 233.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1Catalytic domain
Domain 243.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1Catalytic domain
Domain 253.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 263.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 273.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Domain 283.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
E.C.3.4.25.1
MACiEM0177

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

Enzyme Name
UniProtKBKEGG

P40302P23639P21242P23638P32379P21243P40303P23724P22141P25451P30657P30656P38624P25043
Protein nameProteasome component PRE5Proteasome component Y7Proteasome component C1Proteasome component Y13Proteasome component PUP2Proteasome component C7-alphaProteasome component PRE6Proteasome component C5Proteasome component C11Proteasome component PUP3Proteasome component PRE4Proteasome component PRE2Proteasome component PRE3Proteasome component PUP1proteasome 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
SynonymsEC 3.4.25.1
Macropain subunit PRE5
Proteinase YSCE subunit PRE5
Multicatalytic endopeptidase complex subunit PRE5
EC 3.4.25.1
Macropain subunit Y7
Proteinase YSCE subunit 7
Multicatalytic endopeptidase complex subunit Y7
EC 3.4.25.1
Macropain subunit C1
Proteinase YSCE subunit 1
Multicatalytic endopeptidase complex subunit C1
EC 3.4.25.1
Macropain subunit Y13
Proteinase YSCE subunit 13
Multicatalytic endopeptidase complex subunit Y13
EC 3.4.25.1
Macropain subunit PUP2
Proteinase YSCE subunit PUP2
Multicatalytic endopeptidase complex subunit PUP2
EC 3.4.25.1
Macropain subunit C7-alpha
Proteinase YSCE subunit 7
Multicatalytic endopeptidase complex C7
Proteasome component Y8
SCL1 suppressor protein
EC 3.4.25.1
Macropain subunit PRE6
Proteinase YSCE subunit PRE6
Multicatalytic endopeptidase complex subunit PRE6
EC 3.4.25.1
Multicatalytic endopeptidase complex subunit C5
EC 3.4.25.1
Macropain subunit C11
Proteinase YSCE subunit 11
Multicatalytic endopeptidase complex subunit C11
EC 3.4.25.1
Macropain subunit PUP3
Multicatalytic endopeptidase complex subunit PUP3
EC 3.4.25.1
Macropain subunit PRE4
Proteinase YSCE subunit PRE4
Multicatalytic endopeptidase complex subunit PRE4
EC 3.4.25.1
Macropain subunit PRE2
Proteinase YSCE subunit PRE2
Multicatalytic endopeptidase complex subunit PRE2
EC 3.4.25.1
Macropain subunit PRE3
Proteinase YSCE subunit PRE3
Multicatalytic endopeptidase complex subunit PRE3
EC 3.4.25.1
Macropain subunit PUP1
Proteinase YSCE subunit PUP1
Multicatalytic endopeptidase complex subunit PUP1
RefSeqNP_014045.1 (Protein)
NM_001182825.1 (DNA/RNA sequence)
NP_013618.1 (Protein)
NM_001182451.1 (DNA/RNA sequence)
NP_015007.1 (Protein)
NM_001183782.1 (DNA/RNA sequence)
NP_011651.3 (Protein)
NM_001181264.3 (DNA/RNA sequence)
NP_011769.1 (Protein)
NM_001181382.1 (DNA/RNA sequence)
NP_011504.3 (Protein)
NM_001180876.3 (DNA/RNA sequence)
NP_014604.1 (Protein)
NM_001183292.1 (DNA/RNA sequence)
NP_009512.1 (Protein)
NM_001178281.1 (DNA/RNA sequence)
NP_010928.1 (Protein)
NM_001178903.1 (DNA/RNA sequence)
NP_011020.3 (Protein)
NM_001178985.3 (DNA/RNA sequence)
NP_116708.1 (Protein)
NM_001180015.1 (DNA/RNA sequence)
NP_015428.1 (Protein)
NM_001184200.1 (DNA/RNA sequence)
NP_012533.1 (Protein)
NM_001181435.1 (DNA/RNA sequence)
NP_014800.3 (Protein)
NM_001183576.3 (DNA/RNA sequence)
MEROPST01.976 (Threonine)
T01.972 (Threonine)
T01.977 (Threonine)
T01.973 (Threonine)
T01.975 (Threonine)
T01.971 (Threonine)
T01.974 (Threonine)
T01.986 (Threonine)
T01.984 (Threonine)

T01.987 (Threonine)
T01.012 (Threonine)
T01.010 (Threonine)
T01.011 (Threonine)
PfamPF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical view]
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical view]
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical view]
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical view]
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical view]
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical view]
PF00227 (Proteasome)
PF10584 (Proteasome_A_N)
[Graphical view]
PF00227 (Proteasome)
[Graphical view]
PF00227 (Proteasome)
[Graphical view]
PF00227 (Proteasome)
[Graphical view]
PF00227 (Proteasome)
[Graphical view]
PF00227 (Proteasome)
[Graphical view]
PF00227 (Proteasome)
[Graphical view]
PF12465 (Pr_beta_C)
PF00227 (Proteasome)
[Graphical view]


UniProtKB:Accession NumberP40302P23639P21242P23638P32379P21243P40303P23724P22141P25451P30657P30656P38624P25043
Entry namePSA1_YEASTPSA2_YEASTPSA3_YEASTPSA4_YEASTPSA5_YEASTPSA6_YEASTPSA7_YEASTPSB1_YEASTPSB2_YEASTPSB3_YEASTPSB4_YEASTPSB5_YEASTPSB6_YEASTPSB7_YEAST
ActivityCleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.Cleavage of peptide bonds with very broad specificity.
SubunitThe 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.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.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.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.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.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.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.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.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.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.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.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.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.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.
Subcellular locationCytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.Cytoplasm. Nucleus.
Cofactor














Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00017C00012
CompoundProteinPeptideH2OProteinPeptide
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI

15377



PubChem

962
22247451



              
1fntAUnboundUnbound UnboundUnboundUnbound
1fntOUnboundUnbound UnboundUnboundUnbound
1g0uGUnboundUnbound UnboundUnboundUnbound
1g0uUUnboundUnbound UnboundUnboundUnbound
1g65GUnboundUnbound UnboundUnboundUnbound
1g65UUnboundUnbound UnboundUnboundUnbound
1jd22UnboundUnbound UnboundUnboundUnbound
1jd2GUnboundUnbound UnboundUnboundUnbound
1rypAUnboundUnbound UnboundUnboundUnbound
1rypOUnboundUnbound UnboundUnboundUnbound
1fntBUnboundUnbound UnboundUnboundUnbound
1fntPUnboundUnbound UnboundUnboundUnbound
1g0uAUnboundUnbound UnboundUnboundUnbound
1g0uOUnboundUnbound UnboundUnboundUnbound
1g65AUnboundUnbound UnboundUnboundUnbound
1g65OUnboundUnbound UnboundUnboundUnbound
1jd2AUnboundUnbound UnboundUnboundUnbound
1jd2VUnboundUnbound UnboundUnboundUnbound
1rypBUnboundUnbound UnboundUnboundUnbound
1rypPUnboundUnbound UnboundUnboundUnbound
1fntCUnboundUnbound UnboundUnboundUnbound
1fntQUnboundUnbound UnboundUnboundUnbound
1g0uBUnboundUnbound UnboundUnboundUnbound
1g0uPUnboundUnbound UnboundUnboundUnbound
1g65BUnboundUnbound UnboundUnboundUnbound
1g65PUnboundUnbound UnboundUnboundUnbound
1jd2BUnboundUnbound UnboundUnboundUnbound
1jd2WUnboundUnbound UnboundUnboundUnbound
1rypCUnboundUnbound UnboundUnboundUnbound
1rypQUnboundUnbound UnboundUnboundUnbound
1fntDUnboundUnbound UnboundUnboundUnbound
1fntRUnboundUnbound UnboundUnboundUnbound
1g0uCUnboundUnbound UnboundUnboundUnbound
1g0uQUnboundUnbound UnboundUnboundUnbound
1g65CUnboundUnbound UnboundUnboundUnbound
1g65QUnboundUnbound UnboundUnboundUnbound
1jd2CUnboundUnbound UnboundUnboundUnbound
1jd2XUnboundUnbound UnboundUnboundUnbound
1rypDUnboundUnbound UnboundUnboundUnbound
1rypRUnboundUnbound UnboundUnboundUnbound
1fntEUnboundUnbound UnboundUnboundUnbound
1fntSUnboundUnbound UnboundUnboundUnbound
1g0uDUnboundUnbound UnboundUnboundUnbound
1g0uRUnboundUnbound UnboundUnboundUnbound
1g65DUnboundUnbound UnboundUnboundUnbound
1g65RUnboundUnbound UnboundUnboundUnbound
1jd2DUnboundUnbound UnboundUnboundUnbound
1jd2YUnboundUnbound UnboundUnboundUnbound
1rypEUnboundUnbound UnboundUnboundUnbound
1rypSUnboundUnbound UnboundUnboundUnbound
1fntFUnboundUnbound UnboundUnboundUnbound
1fntTUnboundUnbound UnboundUnboundUnbound
1g0uEUnboundUnbound UnboundUnboundUnbound
1g0uSUnboundUnbound UnboundUnboundUnbound
1g65EUnboundUnbound UnboundUnboundUnbound
1g65SUnboundUnbound UnboundUnboundUnbound
1jd2EUnboundUnbound UnboundUnboundUnbound
1jd2ZUnboundUnbound UnboundUnboundUnbound
1rypFUnboundUnbound UnboundUnboundUnbound
1rypTUnboundUnbound UnboundUnboundUnbound
1fntGUnboundUnbound UnboundUnboundUnbound
1fntUUnboundUnbound UnboundUnboundUnbound
1g0uFUnboundUnbound UnboundUnboundUnbound
1g0uTUnboundUnbound UnboundUnboundUnbound
1g65FUnboundUnbound UnboundUnboundUnbound
1g65TUnboundUnbound UnboundUnboundUnbound
1jd21UnboundUnbound UnboundUnboundUnbound
1jd2FUnboundUnbound UnboundUnboundUnbound
1rypGUnboundUnbound UnboundUnboundUnbound
1rypUUnboundUnbound UnboundUnboundUnbound
1fntHUnboundUnbound UnboundUnboundUnbound
1fntVUnboundUnbound UnboundUnboundUnbound
1g0u2UnboundUnbound UnboundUnboundUnbound
1g0uNUnboundUnbound UnboundUnboundUnbound
1g652UnboundUnbound UnboundUnboundUnbound
1g65NUnboundUnbound UnboundUnboundUnbound
1jd2NUnboundUnbound UnboundUnboundUnbound
1jd2UUnboundUnbound UnboundUnboundUnbound
1rypHUnboundUnbound UnboundUnboundUnbound
1rypVUnboundUnbound UnboundUnboundUnbound
1fntIUnboundUnbound UnboundUnboundUnbound
1fntWUnboundUnbound UnboundUnboundUnbound
1g0uHUnboundUnbound UnboundUnboundUnbound
1g0uVUnboundUnbound UnboundUnboundUnbound
1g65HUnboundUnbound UnboundUnboundUnbound
1g65VUnboundUnbound UnboundUnboundUnbound
1jd2HUnboundAnalogue:95A UnboundUnboundUnbound
1jd2OUnboundAnalogue:95A UnboundUnboundUnbound
1rypIUnboundUnbound UnboundUnboundUnbound
1rypWUnboundUnbound UnboundUnboundUnbound
1fntJUnboundUnbound UnboundUnboundUnbound
1fntXUnboundUnbound UnboundUnboundUnbound
1g0uIUnboundUnbound UnboundUnboundUnbound
1g0uWUnboundUnbound UnboundUnboundUnbound
1g65IUnboundUnbound UnboundUnboundUnbound
1g65WUnboundUnbound UnboundUnboundUnbound
1jd2IUnboundUnbound UnboundUnboundUnbound
1jd2PUnboundUnbound UnboundUnboundUnbound
1rypJUnboundUnbound UnboundUnboundUnbound
1rypXUnboundUnbound UnboundUnboundUnbound
1fntKUnboundUnbound UnboundUnboundUnbound
1fntYUnboundUnbound UnboundUnboundUnbound
1g0uJUnboundUnbound UnboundUnboundUnbound
1g0uXUnboundUnbound UnboundUnboundUnbound
1g65JUnboundUnbound UnboundUnboundUnbound
1g65XUnboundUnbound UnboundUnboundUnbound
1jd2JUnboundUnbound UnboundUnboundUnbound
1jd2QUnboundUnbound UnboundUnboundUnbound
1rypKUnboundUnbound UnboundUnboundUnbound
1rypYUnboundUnbound UnboundUnboundUnbound
1fntLUnboundUnbound UnboundUnboundUnbound
1fntZUnboundUnbound UnboundUnboundUnbound
1g0uKUnboundUnbound UnboundUnboundUnbound
1g0uYUnboundUnbound UnboundUnboundUnbound
1g65KUnboundUnbound UnboundUnboundIntermediate-analogue:EPX
1g65YUnboundUnbound UnboundUnboundIntermediate-analogue:EPX
1jd2KUnboundUnbound UnboundUnboundUnbound
1jd2RUnboundUnbound UnboundUnboundUnbound
1rypLUnboundUnbound UnboundUnboundUnbound
1rypZUnboundUnbound UnboundUnboundUnbound
1fntaUnboundUnbound UnboundUnboundUnbound
1fntMUnboundUnbound UnboundUnboundUnbound
1g0uLUnboundUnbound UnboundUnboundUnbound
1g0uZUnboundUnbound UnboundUnboundUnbound
1g65LUnboundUnbound UnboundUnboundUnbound
1g65ZUnboundUnbound UnboundUnboundUnbound
1jd2LUnboundUnbound UnboundUnboundUnbound
1jd2SUnboundUnbound UnboundUnboundUnbound
1ryp1UnboundUnbound UnboundUnboundUnbound
1rypMUnboundUnbound UnboundUnboundUnbound
1fntbUnboundUnbound UnboundUnboundUnbound
1fntNUnboundUnbound UnboundUnboundUnbound
1g0u1UnboundUnbound UnboundUnboundUnbound
1g0uMUnboundUnbound UnboundUnboundUnbound
1g651UnboundUnbound UnboundUnboundUnbound
1g65MUnboundUnbound UnboundUnboundUnbound
1jd2MUnboundUnbound UnboundUnboundUnbound
1jd2TUnboundUnbound UnboundUnboundUnbound
1ryp2UnboundUnbound UnboundUnboundUnbound
1rypNUnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
literature [8], [11], [16], [18], [20], [23] & [35]
pdbCatalytic residuesMain-chain involved in catalysiscomment
           
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                                            
 
 
1fntHTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1fntVTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g0u2THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g0uNTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g652THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g65NTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1jd2NTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1jd2UTHR 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
1fntITHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1fntWTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g0uHTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g0uVTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g65HTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g65VTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1jd2HTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1jd2OTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1rypITHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1rypWTHR 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                                            
 
 
1fntLTHR 1;ASP 17;      ;SER 131;ASP 168;SER 171
THR 1;GLY 47
mutant K33R
1fntZTHR 1;ASP 17;      ;SER 131;ASP 168;SER 171
THR 1;GLY 47
mutant K33R
1g0uKTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1g0uYTHR 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)
1jd2KTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1jd2RTHR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
THR 1;GLY 47
 
1rypLTHR 1;ASP 17;      ;SER 131;ASP 168;SER 171
THR 1;GLY 47
mutant K33R
1rypZTHR 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
ReferencesSectionsNo. 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]
PubMed ID7781614
JournalEMBO J
Year1995
Volume14
Pages2620-30
AuthorsChen P, Hochstrasser M
TitleBiogenesis, structure and function of the yeast 20S proteasome.
[2]
PubMed ID7565661
JournalMol Biol Rep
Year1995
Volume21
Pages3-10
AuthorsHilt W, Wolf DH
TitleProteasomes of the yeast S. cerevisiae: genes, structure and functions.
[3]
PubMed ID7565658
JournalMol Biol Rep
Year1995
Volume21
Pages11-20
AuthorsKoster AJ, Walz J, Lupas A, Baumeister W
TitleStructural features of archaebacterial and eukaryotic proteasomes.
[4]
PubMed ID7477383
JournalNature
Year1995
Volume378
Pages416-9
AuthorsBrannigan JA, Dodson G, Duggleby HJ, Moody PC, Smith JL, Tomchick DR, Murzin AG
TitleA protein catalytic framework with an N-terminal nucleophile is capable of self-activation.
[5]
PubMed ID7725095
JournalScience
Year1995
Volume268
Pages522-3
AuthorsGoldberg AL
TitleFunctions of the proteasome: the lysis at the end of the tunnel.
[6]
PubMed ID8811196
JournalAnnu Rev Biochem
Year1996
Volume65
Pages801-47
AuthorsCoux O, Tanaka K, Goldberg AL
TitleStructure and functions of the 20S and 26S proteasomes.
[7]
PubMed ID8808631
JournalCell
Year1996
Volume86
Pages961-72
AuthorsChen P, Hochstrasser M
TitleAutocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly.
[8]
PubMed ID9003765
JournalEMBO J
Year1996
Volume15
Pages6887-98
AuthorsSchmidtke G, Kraft R, Kostka S, Henklein P, Frommel C, Lowe J, Huber R, Kloetzel PM, Schmidt M
TitleAnalysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis.
[9]
PubMed ID9377486
JournalBiol Chem
Year1997
Volume378
Pages893-8
AuthorsEscherich A, Ditzel L, Musiol HJ, Groll M, Huber R, Moroder L
TitleSynthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae.
[10]
PubMed ID9228290
JournalMol Biol Rep
Year1997
Volume24
Pages103-12
AuthorsSchmidt M, Schmidtke G, Kloetzel PM
TitleStructure and structure formation of the 20S proteasome.
[11]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed ID9087403
JournalNature
Year1997
Volume386
Pages463-71
AuthorsGroll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R
TitleStructure of 20S proteasome from yeast at 2.4 A resolution.
Related PDB1ryp
Related UniProtKBP40302,P23639,P21242,P23638,P32379,P21243,P40303,P23724,P22141,P25451,P30657,P30656,P38624,P25043
[12]
PubMed ID9207060
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages7156-61
AuthorsArendt CS, Hochstrasser M
TitleIdentification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation.
[13]
PubMed ID9538192
JournalJ Biochem (Tokyo)
Year1998
Volume123
Pages195-204
AuthorsTanaka K
TitleProteasomes: structure and biology.
[14]
PubMed ID9642094
JournalJ Mol Biol
Year1998
Volume279
Pages1187-91
AuthorsDitzel L, Huber R, Mann K, Heinemeyer W, Wolf DH, Groll M
TitleConformational constraints for protein self-cleavage in the proteasome.
[15]
PubMed ID10099130
JournalChem Biol
Year1999
Volume6
Pages197-204
AuthorsLoidl G, Groll M, Musiol HJ, Ditzel L, Huber R, Moroder L
TitleBifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes.
[16]
PubMed ID10393174
JournalEMBO J
Year1999
Volume18
Pages3575-85
AuthorsArendt CS, Hochstrasser M
TitleEukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly.
[17]
PubMed ID10452902
JournalJ Mol Biol
Year1999
Volume291
Pages997-1013
AuthorsJager S, Groll M, Huber R, Wolf DH, Heinemeyer W
TitleProteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function.
[18]
PubMed ID10500111
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages10976-83
AuthorsGroll M, Heinemeyer W, Jager S, Ullrich T, Bochtler M, Wolf DH, Huber R
TitleThe catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study.
[19]
PubMed ID10318898
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages5418-22
AuthorsLoidl G, Groll M, Musiol HJ, Huber R, Moroder L
TitleBivalency as a principle for proteasome inhibition.
[20]
CommentsX-ray crystallography
JournalJ Am Chem Soc
Year2000
Volume122
Pages1237-8
AuthorsGroll M, Kim KB, Kairies N, Crews C
TitleCrystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity of alpha,beta-epoxyketone proteasome inhibitors.
Related PDB1g65
[21]
PubMed ID10747864
JournalJ Biol Chem
Year2000
Volume275
Pages13171-4
AuthorsOsmulski PA, Gaczynska M
TitleAtomic force microscopy reveals two conformations of the 20 S proteasome from fission yeast.
[22]
PubMed ID10843865
JournalJ Mol Biol
Year2000
Volume299
Pages1147-54
AuthorsGille C, Goede A, Preissner R, Rother K, Frommel C
TitleConservation of substructures in proteins: interfaces of secondary structural elements in proteasomal subunits.
[23]
CommentsX-ray crystallography
PubMed ID11062564
JournalNat Struct Biol
Year2000
Volume7
Pages1062-7
AuthorsGroll M, Bajorek M, Kohler A, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D
TitleA gated channel into the proteasome core particle.
Related PDB1g0u
[24]
PubMed ID11062549
JournalNat Struct Biol
Year2000
Volume7
Pages999-1001
AuthorsPickart CM, VanDemark AP
TitleOpening doors into the proteasome.
[25]
CommentsX-ray crystallography
PubMed ID11081519
JournalNature
Year2000
Volume408
Pages115-20
AuthorsWhitby FG, Masters EI, Kramer L, Knowlton JR, Yao Y, Wang CC, Hill CP
TitleStructural basis for the activation of 20S proteasomes by 11S regulators.
Related PDB1fnt
[26]
PubMed ID11295493
JournalBiochimie
Year2001
Volume83
Pages325-32
AuthorsKohler A, Bajorek M, Groll M, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D
TitleThe substrate translocation channel of the proteasome.
[27]
CommentsX-ray crystallography
PubMed ID11493007
JournalJ Mol Biol
Year2001
Volume311
Pages543-8
AuthorsGroll M, Koguchi Y, Huber R, Kohno J
TitleCrystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor.
Related PDB1jd2
[28]
PubMed ID12083009
JournalCurr Top Microbiol Immunol
Year2002
Volume268
Pages73-89
AuthorsHill CP, Masters EI, Whitby FG
TitleThe 11S regulators of 20S proteasome activity.
[29]
PubMed ID12083007
JournalCurr Top Microbiol Immunol
Year2002
Volume268
Pages23-41
AuthorsZwickl P
TitleThe 20S proteasome.
[30]
PubMed ID12354607
JournalFEBS Lett
Year2002
Volume529
Pages22-6
AuthorsDantuma NP, Masucci MG
TitleStabilization signals: a novel regulatory mechanism in the ubiquitin/proteasome system.
[31]
PubMed ID11820928
JournalJ Biochem (Tokyo)
Year2002
Volume131
Pages171-3
AuthorsUnno M, Mizushima T, Morimoto Y, Tomisugi Y, Tanaka K, Yasuoka N, Tsukihara T
TitleStructure determination of the constitutive 20S proteasome from bovine liver at 2.75 A resolution.
[32]
PubMed ID11927581
JournalJ Biol Chem
Year2002
Volume277
Pages22260-70
AuthorsKisselev AF, Kaganovich D, Goldberg AL
TitleBinding 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.
[33]
PubMed ID12015144
JournalStructure (Camb)
Year2002
Volume10
Pages609-18
AuthorsUnno M, Mizushima T, Morimoto Y, Tomisugi Y, Tanaka K, Yasuoka N, Tsukihara T
TitleThe structure of the mammalian 20S proteasome at 2.75 A resolution.
[34]
PubMed ID12941688
JournalEMBO J
Year2003
Volume22
Pages4356-64
AuthorsForster A, Whitby FG, Hill CP
TitleThe pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation.
[35]
PubMed ID15571807
JournalBiochim Biophys Acta
Year2004
Volume1695
Pages33-44
AuthorsGroll M, Huber R
TitleInhibitors of the eukaryotic 20S proteasome core particle: a structural approach.
[36]
PubMed ID15589823
JournalFEBS Lett
Year2004
Volume578
Pages217-23
AuthorsFerrington DA, Kapphahn RJ
TitleCatalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal.
[37]
PubMed ID14722099
JournalJ Biol Chem
Year2004
Volume279
Pages14323-30
AuthorsRamos PC, Marques AJ, London MK, Dohmen RJ
TitleRole of C-terminal extensions of subunits beta2 and beta7 in assembly and activity of eukaryotic proteasomes.
[38]
PubMed ID15713476
JournalJ Mol Biol
Year2005
Volume346
Pages1221-7
AuthorsOrtega J, Heymann JB, Kajava AV, Ustrell V, Rechsteiner M, Steven AC
TitleThe axial channel of the 20S proteasome opens upon binding of the PA200 activator.

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.

createdupdated
2002-07-012009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.