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Information on EC 3.6.4.6 - vesicle-fusing ATPase

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EC Tree
IUBMB Comments
A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (_A_TPase _a_ssociated with a variety of cell _a_ctivities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome.
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This record set is specific for:
UNIPROT: P55072
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
n-ethylmaleimide-sensitive factor, cdc48, aaa-atpase, n-ethylmaleimide-sensitive fusion protein, atp6v0d2, n-ethylmaleimide sensitive factor, sec18p, sec18, cdc48p, pex1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
triple-A ATPase
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N-ethylmaleimide sensitive fusion protein
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-
-
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NEM-sensitive fusion protein
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-
-
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SKD2 protein
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-
-
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Vesicular-fusion protein NSF
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (vesicle-fusing)
A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (_A_TPase _a_ssociated with a variety of cell _a_ctivities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome.
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
-
-
-
?
additional information
?
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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
Mg2+
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
human and Dictyostelium p97 share 81% identity and 89% similarity on the amino acid sequence level and have an almost identical order and composition of secondary structure elements
malfunction
heterozygous missense mutations of p97 cause at least five human neurodegenerative disorders, i.e. R93C, R155H, and R155C mutations. All human p97 mutations lead to an increase in ATPase activity. p97 point mutations lead to differences in enzymatic activities and molecular interactions, which in the long-term result in a late-onset and progressive multisystem disease
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TERA_HUMAN
806
0
89322
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R155C
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, and a twofold decreased kd for human protein UBXD9
R155H
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, no change in the kd value for human protein UBXD9
R93C
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity and a twofold increased kd for human protein UBXD9
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and mutant p97s from Escherichia coli by glutathione affinity and cleavage of the tag by PreScission protease
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of GST-tagged wild-type and mutant p97 in Escherichia coli strain Arctic express RIL, coexpression with GST-tagged human UBXD9 protein in Escherichia coli in strain BL21Gold (DE3) pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rijal, R.; Arhzaouy, K.; Strucksberg, K.; Cross, M.; Hofmann, A.; Schroeder, R.; Clemen, C.; Eichinger, L.
Mutant p97 exhibits species-specific changes of its ATPase activity and compromises the UBXD9-mediated monomerisation of p97 hexamers
Eur. J. Cell Biol.
95
195-207
2016
Homo sapiens (P55072), Homo sapiens, Dictyostelium discoideum (Q75JI3)
Manually annotated by BRENDA team