Description

IPR005294 is a ATP synthase, F1 complex, alpha subunit.

This entry represents the alpha subunit found in the F1 complex of F-ATPases. In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex, while the remaining F1 subunits (gamma, delta, epsilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits, those on the beta subunits being catalytic, while those on the alpha subunits are regulatory. The alpha-subunit contains a highly conserved adenine-specific non-catalytic nucleotide-binding domain, with a conserved amino acid sequence of Gly-X-X-X-X-Gly-Lys. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP, which are induced by the rotation of the gamma subunit, itself is driven by the movement of protons through the F0 complex C subunit [[PMID:12745923]]. Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. F-ATPases (also known as ATP synthases, F1F0-ATPases, or H+-transporting two-sector ATPases) ([ec:7.1.2.2]) are multi-subunit complexes that couple transmembrane proton translocation to ATP synthesis. They are composed of two linked rotary motors: the soluble F1 complex, which constitutes the catalytic core, and the membrane-embedded F0 complex, which forms the proton channel [[PMID:11309608]]. The F1 complex is assembled from five subunit types (α, β, γ, δ, ε). The α and β subunits form a hexameric α3β3 cylinder enclosing the central γ subunit, which acts as the rotor of the F1 motor. The F0 complex contains at least three subunit types (a, b, c); the c subunits form a ring that constitutes the F0 rotor. The two rotary motors are mechanically coupled back-to-back via a central stalk, such that rotation driven by proton flow through F0 is transmitted to the catalytic sites in F1 to drive ATP synthesis [[PMID:11309608]]. In mitochondria, the F0 complex contains additional subunits beyond the minimal bacterial complement. Under physiological conditions, the proton-motive force across the membrane drives rotation of the F0 rotor, which in turn rotates the F1 rotor in the direction that promotes ATP synthesis from ADP and inorganic phosphate. In bacteria, the enzyme can operate in reverse, hydrolyzing ATP to pump protons across the membrane and generate a proton gradient [[PMID:11309608]].

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 4

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: