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Information on EC 3.6.4.7 - peroxisome-assembly ATPase

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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.
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This record set is specific for:
UNIPROT: Q13608
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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
Pex1p/Pex6p
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peroxisome assembly factor-2
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-
-
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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 (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
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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
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-
-
?
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
PEX6; gene PEX6
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
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the AAA+ ATPase superfamily
malfunction
mutations in the PEX1 gene, which encodes a protein required for peroxisome biogenesis, are themost common cause of the Zellweger spectrum diseases, the by far most abundant Pex1pG843D variation impairs the binding between Pex1p and Pex6p
metabolism
the enzyme is involved in peroxisome biogenesis
physiological function
Pex1p and Pex6p are crucial for peroxisome biogenesis, Pex6p functions together with Pex1p in peroxisome biogenesis. The ATP hydrolysis cycle of the AAA+-ATPases is supposed to regulate the assembly and disassembly of the Pex1p-Pex6p complex and its membrane association and release. Role of Pex1p/Pex6p in peroxisomal matrix protein import, overview
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PEX6_HUMAN
980
0
104061
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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