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Information on EC 5.6.1.5 - proteasome ATPase

for references in articles please use BRENDA:EC5.6.1.5
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EC Tree
IUBMB Comments
Belongs to the AAA-type superfamily and, like EC 5.6.1.4 (minus-end-directed kinesin ATPase), is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.
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This record set is specific for:
UNIPROT: Q9SEI4
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Word Map
  • 5.6.1.5
  • atpases
  • ubiquitin-proteasome
  • subcomplexes
  • misfolded
  • hexameric
  • polyubiquitinated
  • disassembly
  • hslu
  • ubiquitin-dependent
  • non-atpase
  • ubiquitin-like
  • er-associated
  • multisubunit
  • deubiquitinase
  • reticulum-associated
  • proteotoxic
  • retrotranslocation
  • proteasome-mediated
  • escrts
  • deubiquitylating
  • valosin-containing
  • immunoproteasome
  • katanin
  • proteasome-associated
  • zellweger
  • escrt-iii
  • spastin
  • medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
+
=
+
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unfolded polypeptide
Synonyms
aaa atpase, pa700, 19s regulatory particle, 19s proteasome, hslvu, tbp-1, 19s rp, rpt2a, psmc5, 26s-proteasome, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteosomal regulatory particle AAA-ATPase-3
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RP triphosphatase
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-
-
-
RP triple-A protein
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-degrading)
Belongs to the AAA-type superfamily and, like EC 5.6.1.4 (minus-end-directed kinesin ATPase), is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRS6B_ARATH
408
0
45751
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G158E
the mutation impairs the light-specific hypocotyl elongation response elicited by class I S(1)-b-methyl-a,b-diaminopropionic acid, the mutated amino acid site resides within the full AAA-ATPase domain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brenner, E.D.; Feinberg, P.; Runko, S.; Coruzzi, G.M.
A mutation in the Proteosomal Regulatory Particle AAA-ATPase-3 in Arabidopsis impairs the light-specific hypocotyl elongation response elicited by a glutamate receptor agonist, BMAA
Plant Mol. Biol.
70
523-533
2009
Arabidopsis thaliana (Q9SEI4)
Manually annotated by BRENDA team