Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.4.7 - peroxisome-assembly ATPase and Organism(s) Mus musculus and UniProt Accession Q9DBN5

for references in articles please use BRENDA:EC3.6.4.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q9DBN5
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
ATP
+
H2O
=
ADP
+
phosphate
+
=
+
Synonyms
valosin-containing protein, p97/vcp, peroxin, aaa protein, atpase associated with various cellular activities, atpase associated with diverse cellular activities, paf-2, pas1p, lonp2, pex1/pex6, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peroxisomal Lon protease
-
peroxisome assembly factor-2
-
-
-
-
Pex1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (peroxisome-assembling)
An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Lon protease homolog 2, peroxisomal
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
structural organization and localization of peroxisomal AAA+ ATPases. Dynamic Pex1p-Pex6p complex assembly at the peroxisomal membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
physiological function
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality
evolution
the enzyme belongs to the AAA+ ATPase superfamily
metabolism
the enzyme is involved in peroxisome biogenesis
physiological function
Pex6p functions together with Pex1p in peroxisome biogenesis
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LONP2_MOUSE
852
0
94526
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, Pex1p/Pex6p forms a type II heterohexameric complex with two AAA+ rings (D1 ring, D2 ring) and large N-terminal domains positioned on top and aside of the double ring structure
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structures of the extreme N-terminal part of murine Pex1p exposed a double-psi-beta-barrel fold with similarities to adaptor binding domains of p97 and NSF
N-terminal domain, supradomain architecture is a common feature of organellar membrane-associating AAA-ATPases
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K174A
-
mutant, binds with approximately the same affinity and specificity as the wild-type protein
R135A
-
mutant, the conserved arginine surrounded by hydrophobic residues is essential for lipid binding
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using glutathione Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Lonp2, phylogenetic tree
a GST fusion protein containing the PEX1 gene encoding residues 3-180, the N-terminal domain, in pGEX-4T3-PRESAT is constructed
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
autosomal recessive mutations in the PEX genes cause peroxisome biogenesis disorders, such as Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shiozawa, K.; Maita, N.; Tomii, K.; Seto, A.; Goda, N.; Akiyama, Y.; Shimizu, T.; Shirakawa, M.; Hiroaki, H.
Structure of the N-terminal Domain of PEX1 AAA-ATPase: Characterization of a putative adaptor-binding domain
J. Biol. Chem.
279
50060-50068
2004
Mus musculus
Manually annotated by BRENDA team
Shiozawa Kumik, S.K.; Goda Natsuk, G.N.; Shimizu Toshiyuk, S.T.; Mizuguchi Kenj, M.K.; Kondo Naom, K.N.; Shimozawa Nobuyuk, S.N.; Shirakawa Masahir, S.M.; Hiroaki Hidekaz, H.H.
The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97
FEBS J.
273
4959-4971
2006
Mus musculus
Manually annotated by BRENDA team
Aksam, E.B.; Koek, A.; Kiel, J.A.; Jourdan, S.; Veenhuis, M.; van der Klei, I.J.
A peroxisomal Lon protease and peroxisome degradation by autophagy play key roles in vitality of Hansenula polymorpha cells
Autophagy
3
96-105
2007
Mus musculus (Q9DBN5), Neurospora crassa (Q7SA85), Ogataea angusta (Q2V573), Ogataea angusta, Ogataea angusta NCYC495 (Q2V573), Yarrowia lipolytica (Q6C0L7), Zea mays (P93647)
Manually annotated by BRENDA team
Grimm, I.; Erdmann, R.; Girzalsky, W.
Role of AAA+-proteins in peroxisome biogenesis and function
Biochim. Biophys. Acta
1863
828-837
2016
Penicillium chrysogenum (B6HJQ3), Homo sapiens (O43933), Homo sapiens (Q13608), Arabidopsis thaliana (O64948), Escherichia coli (P0A9M0), Saccharomyces cerevisiae (P24004), Saccharomyces cerevisiae (P33760), Ogataea angusta (Q2V573), Mus musculus (Q5BL07), Mus musculus (Q99LC9)
Manually annotated by BRENDA team