Literature summary for 3.6.4.7 extracted from

Ciniawsky, S.; Grimm, I.; Saffian, D.; Girzalsky, W.; Erdmann, R.; Wendler, P.
Molecular snapshots of the Pex1/6 AAA+ complex in action (2015), Nat. Commun., 6, 7331.

Search for more literature for 3.6.4.7

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of the pex1p/pex6p complex in Escherichia coli or yeast, the complex assembles in the presence of a nucleotide	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
peroxisomal membrane	the peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex	Saccharomyces cerevisiae	5778	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
700000	-	pex1p/pex6p complex	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Saccharomyces cerevisiae	-	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P24004	PEX1	-
Saccharomyces cerevisiae	P33760	PEX6	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Saccharomyces cerevisiae	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
heterohexamer	trimers of dimers, the peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex. The heterohexamer forms a trimer of Pex1/6 dimers with a triangular geometry that is atypical for AAA+ complexes. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
Pex1/6 AAA+ complex	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the type II AAA+ ATPases, which by definition contain two conserved nucleotide-binding domains (D1 and D2) in tandem flanked by less conserved N- and C-terminal regions	Saccharomyces cerevisiae
malfunction	mutation of the Walker B motif in one D2 domain leads to ATP hydrolysis in the neighbouring domain	Saccharomyces cerevisiae
additional information	yeast Pex1/6 complex structure analysis, structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. The Pex1/6 complex assembles in the presence of a nucleotide, ATP or ATPgammaS, structure modeling, overview	Saccharomyces cerevisiae
physiological function	the peroxisomal proteins Pex1 and Pex6 complex fuels essential protein transport across peroxisomal membranes. ATP hydrolysis results in a pumping motion of the complex, suggesting that Pex1/6 function involves substrate translocation through its central channel. ATPase activity of Pex6 D2 domains drive conformational changes, Pex1/6 movements during ATP binding and hydrolysis, overview	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)