M00174
type: Enzyme
cath: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
csa: 1pma
ec: https://purl.uniprot.org/enzyme/3.4.25.1
kegg enzyme: proteasome endopeptidase complex
kegg product: Protein
kegg product: Peptide
kegg substrate: Protein
kegg substrate: Peptide
kegg substrate: H2O
pdb: 1pmaA
pdb: 1pmaC
pdb: 1pmaD
pdb: 1pmaE
pdb: 1pmaF
pdb: 1pmaG
pdb: 1pmaH
pdb: 1pmaI
pdb: 1pmaJ
pdb: 1pmaK
pdb: 1pmaL
pdb: 1pmaM
pdb: 1pmaN
pdb: 1pmaO
pdb: 1ya7A
pdb: 1ya7B
pdb: 1ya7C
pdb: 1ya7D
pdb: 1ya7E
pdb: 1ya7F
pdb: 1ya7G
pdb: 1yarA
pdb: 1yarB
pdb: 1yarC
pdb: 1yarD
pdb: 1yarE
pdb: 1yarF
pdb: 1yarG
pdb: 1yauA
pdb: 1yauB
pdb: 1yauC
pdb: 1yauD
pdb: 1yauE
pdb: 1yauF
pdb: 1yauG
pdb: 1pmaB
pdb: 1pmaP
pdb: 1pmaQ
pdb: 1pmaR
pdb: 1pmaS
pdb: 1pmaT
pdb: 1pmaU
pdb: 1pmaV
pdb: 1pmaW
pdb: 1pmaX
pdb: 1pmaY
pdb: 1pmaZ
pdb: 1pma1
pdb: 1pma2
pdb: 1ya7H
pdb: 1ya7I
pdb: 1ya7J
pdb: 1ya7K
pdb: 1ya7L
pdb: 1ya7M
pdb: 1ya7N
pdb: 1yarH
pdb: 1yarI
pdb: 1yarJ
pdb: 1yarK
pdb: 1yarL
pdb: 1yarM
pdb: 1yarN
pdb: 1yauH
pdb: 1yauI
pdb: 1yauJ
pdb: 1yauK
pdb: 1yauL
pdb: 1yauM
pdb: 1yauN

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.4, p.517-519

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.5A, p.529-530

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.418

ReferenceForCatalyticMechanism
reference index: 13
reference section: p.381-382

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.275-276

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig.2, p.4-5

ReferenceForCatalyticMechanism
reference index: 19
reference section: p.840-841

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.2

Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.60.20.10

H2O
type: KeggSubstrate
compound type: H2O
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Structural features of 26S and 20S proteasomes.
type: BibliographicResource
authors:
  item: Lupas A
  item: Koster AJ
  item: Baumeister W
journal: Enzyme Protein
pages: 252-73
published year: 1993
volume: 47
references: http://www.ncbi.nlm.nih.gov/pubmed/7697124

Proteasome from Thermoplasma acidophilum: a threonine protease.
type: BibliographicResource
authors:
  item: Seemuller E
  item: Lupas A
  item: Stock D
  item: Lowe J
  item: Huber R
  item: Baumeister W
journal: Science
pages: 579-82
published year: 1995
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/7725107

Proteasome: a complex protease with a new fold and a distinct mechanism.
type: BibliographicResource
authors:
  item: Wlodawer A
journal: Structure
pages: 417-20
published year: 1995
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/7663937

Structure and functions of the 20S and 26S proteasomes.
type: BibliographicResource
authors:
  item: Coux O
  item: Tanaka K
  item: Goldberg AL
journal: Annu Rev Biochem
pages: 801-47
published year: 1996
volume: 65
references: http://www.ncbi.nlm.nih.gov/pubmed/8811196

Proteasome: from structure to function.
type: BibliographicResource
authors:
  item: Stock D
  item: Nederlof PM
  item: Seemuller E
  item: Baumeister W
  item: Huber R
  item: Lowe J
journal: Curr Opin Biotechnol
pages: 376-85
published year: 1996
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/8768894

Autocatalytic processing of the 20S proteasome.
type: BibliographicResource
authors:
  item: Seemuller E
  item: Lupas A
  item: Baumeister W
journal: Nature
pages: 468-71
published year: 1996
volume: 382
references: http://www.ncbi.nlm.nih.gov/pubmed/8684489

Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae.
type: BibliographicResource
authors:
  item: Escherich A
  item: Ditzel L
  item: Musiol HJ
  item: Groll M
  item: Huber R
  item: Moroder L
journal: Biol Chem
pages: 893-8
published year: 1997
volume: 378
references: http://www.ncbi.nlm.nih.gov/pubmed/9377486

The proteasome.
type: BibliographicResource
authors:
  item: Baumeister W
  item: Lupas A
journal: Curr Opin Struct Biol
pages: 273-8
published year: 1997
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/9094332

Active site-directed inhibitors of Rhodococcus 20 S proteasome. Kinetics and mechanism.
type: BibliographicResource
authors:
  item: Mc Cormack T
  item: Zuhl F
  item: Dick L
  item: Baumeister W
  item: Grenier L
  item: Moomaw C
  item: Plamondon L
  item: Pramanik B
  item: Slaughter C
  item: Soucy F
  item: Stein R
journal: J Biol Chem
pages: 26103-9
published year: 1997
volume: 272
references: http://www.ncbi.nlm.nih.gov/pubmed/9334174

Catalytic activities of the 20 S proteasome, a multicatalytic proteinase complex.
type: BibliographicResource
authors:
  item: Orlowski M
  item: Wilk S
journal: Arch Biochem Biophys
pages: 1-16
published year: 2000
volume: 383
references: http://www.ncbi.nlm.nih.gov/pubmed/11097171

Proteasomes in the archaea: from structure to function.
type: BibliographicResource
authors:
  item: Maupin-Furlow JA
  item: Wilson HL
  item: Kaczowka SJ
  item: Ou MS
journal: Front Biosci
pages: D837-65
published year: 2000
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/10966872

Molecular structure of 20S and 26S proteasomes.
type: BibliographicResource
authors:
  item: Tanahashi N
  item: Tsurumi C
  item: Tamura T
  item: Tanaka K
journal: Enzyme Protein
pages: 241-51
published year: 1993
volume: 47
references: http://www.ncbi.nlm.nih.gov/pubmed/7697123

Why does threonine, and not serine, function as the active site nucleophile in proteasomes?
type: BibliographicResource
authors:
  item: Kisselev AF
  item: Songyang Z
  item: Goldberg AL
journal: J Biol Chem
pages: 14831-7
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/10809725

Conservation of substructures in proteins: interfaces of secondary structural elements in proteasomal subunits.
type: BibliographicResource
authors:
  item: Gille C
  item: Goede A
  item: Preissner R
  item: Rother K
  item: Frommel C
journal: J Mol Biol
pages: 1147-54
published year: 2000
volume: 299
references: http://www.ncbi.nlm.nih.gov/pubmed/10843865

The 11S regulators of 20S proteasome activity.
type: BibliographicResource
authors:
  item: Hill CP
  item: Masters EI
  item: Whitby FG
journal: Curr Top Microbiol Immunol
pages: 73-89
published year: 2002
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/12083009

The 20S proteasome.
type: BibliographicResource
authors:
  item: Zwickl P
journal: Curr Top Microbiol Immunol
pages: 23-41
published year: 2002
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/12083007

Stabilization signals: a novel regulatory mechanism in the ubiquitin/proteasome system.
type: BibliographicResource
authors:
  item: Dantuma NP
  item: Masucci MG
journal: FEBS Lett
pages: 22-6
published year: 2002
volume: 529
references: http://www.ncbi.nlm.nih.gov/pubmed/12354607

The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation.
type: BibliographicResource
authors:
  item: Forster A
  item: Whitby FG
  item: Hill CP
journal: EMBO J
pages: 4356-64
published year: 2003
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/12941688

Investigations on the maturation and regulation of archaebacterial proteasomes.
type: BibliographicResource
authors:
  item: Groll M
  item: Brandstetter H
  item: Bartunik H
  item: Bourenkow G
  item: Huber R
journal: J Mol Biol
pages: 75-83
published year: 2003
volume: 327
references: http://www.ncbi.nlm.nih.gov/pubmed/12614609

The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions.
type: BibliographicResource
authors:
  item: Forster A
  item: Masters EI
  item: Whitby FG
  item: Robinson H
  item: Hill CP
journal: Mol Cell
pages: 589-99
published year: 2005
volume: 18
references: http://www.ncbi.nlm.nih.gov/pubmed/15916965
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure and function of the 20S proteasome and of its regulatory complexes.
type: BibliographicResource
authors:
  item: Lupas A
  item: Zwickl P
  item: Wenzel T
  item: Seemuller E
  item: Baumeister W
journal: Cold Spring Harb Symp Quant Biol
pages: 515-24
published year: 1995
volume: 60
references: http://www.ncbi.nlm.nih.gov/pubmed/8824424

Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography.
type: BibliographicResource
authors:
  item: Stock D
  item: Ditzel L
  item: Baumeister W
  item: Huber R
  item: Lowe J
journal: Cold Spring Harb Symp Quant Biol
pages: 525-32
published year: 1995
volume: 60
references: http://www.ncbi.nlm.nih.gov/pubmed/8824425

The proteasome from Thermoplasma acidophilum is neither a cysteine nor a serine protease.
type: BibliographicResource
authors:
  item: Seemuller E
  item: Lupas A
  item: Zuhl F
  item: Zwickl P
  item: Baumeister W
journal: FEBS Lett
pages: 173-8
published year: 1995
volume: 359
references: http://www.ncbi.nlm.nih.gov/pubmed/7867793

Structural features of archaebacterial and eukaryotic proteasomes.
type: BibliographicResource
authors:
  item: Koster AJ
  item: Walz J
  item: Lupas A
  item: Baumeister W
journal: Mol Biol Rep
pages: 11-20
published year: 1995
volume: 21
references: http://www.ncbi.nlm.nih.gov/pubmed/7565658

A protein catalytic framework with an N-terminal nucleophile is capable of self-activation.
type: BibliographicResource
authors:
  item: Brannigan JA
  item: Dodson G
  item: Duggleby HJ
  item: Moody PC
  item: Smith JL
  item: Tomchick DR
  item: Murzin AG
journal: Nature
pages: 416-9
published year: 1995
volume: 378
references: http://www.ncbi.nlm.nih.gov/pubmed/7477383

Functions of the proteasome: the lysis at the end of the tunnel.
type: BibliographicResource
authors:
  item: Goldberg AL
journal: Science
pages: 522-3
published year: 1995
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/7725095

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
type: BibliographicResource
authors:
  item: Lowe J
  item: Stock D
  item: Jap B
  item: Zwickl P
  item: Baumeister W
  item: Huber R
journal: Science
pages: 533-9
published year: 1995
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/7725097
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

1pma1
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pma2
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaB
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaP
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaQ
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaR
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaS
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaT
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaU
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaV
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaW
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaX
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaY
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1pmaZ
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1pma
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pma

1ya7H
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1ya7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ya7

1ya7I
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1ya7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ya7

1ya7J
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1ya7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ya7

1ya7K
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1ya7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ya7

1ya7L
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1ya7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ya7

1ya7M
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1ya7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ya7

1ya7N
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1ya7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ya7

1yarH
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yar
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yar

1yarI
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yar
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yar

1yarJ
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yar
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yar

1yarK
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yar
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yar

1yarL
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yar
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yar

1yarM
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yar
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yar

1yarN
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yar
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yar

1yauH
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yau
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yau

1yauI
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yau
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yau

1yauJ
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yau
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yau

1yauK
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yau
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yau

1yauL
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yau
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yau

1yauM
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yau
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yau

1yauN
type: Pdb
catalytic residue: THR 1;GLU 17;LYS 33;ASP 166
main chain in catalysis: THR 1;GLY 47
references: 1yau
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yau

Peptide
type: KeggSubstrate
type: KeggProduct
compound type: peptide/protein
references: KEGG:C00012

Protein
type: KeggSubstrate
type: KeggProduct
compound type: peptide/protein
references: KEGG:C00017

ingensin
type: KeggEnzyme

macropain
type: KeggEnzyme

multicatalytic endopeptidase complex
type: KeggEnzyme

prosome
type: KeggEnzyme

multicatalytic proteinase (complex)
type: KeggEnzyme

MCP
type: KeggEnzyme

proteasome
type: KeggEnzyme

large multicatalytic protease
type: KeggEnzyme

multicatalytic proteinase
type: KeggEnzyme

proteasome organelle
type: KeggEnzyme

alkaline protease
type: KeggEnzyme

26S protease
type: KeggEnzyme

tricorn proteinase
type: KeggEnzyme

tricorn protease
type: KeggEnzyme