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IPR005294

Description

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

<p>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 [[cite:PUB00020611]].</p> <p>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.</p> <p>F-ATPases (also known as ATP synthases, F1F0-ATPase, or H(+)-transporting two-sector ATPase) ([ec:7.1.2.2]) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), with additional subunits in mitochondria. Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the α(3)β(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [[cite:PUB00009752]]. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.</p>

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 , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Biological process ATP synthesis coupled proton transport The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
Cellular component Proton-transporting ATP synthase complex, catalytic core F(1) The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.
Molecular function Proton-transporting ATP synthase activity, rotational mechanism Enables the transfer of protons from one side of a membrane to the other according to the reaction: ADP + H2O + phosphate + H+(in) = ATP + H+(out), by a rotational mechanism.

Associated Lotus transcripts 4

Transcript Name Description Predicted domains Domain count
ATPase subunit 1 (mitochondrion) [Lotus japonicus] gi|372450305|ref|YP_005090487.1| 18
ATPase subunit 1 (mitochondrion) [Lotus japonicus] gi|372450305|ref|YP_005090487.1| 7
ATP synthase CF1 alpha subunit [Lotus japonicus] gi|13518443|ref|NP_084803.1| 24
ATPase subunit 1 (mitochondrion) [Lotus japonicus] gi|372450305|ref|YP_005090487.1| 24

Co-occuring domains 1

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

Predicted domain Source Observations Saturation (%)
cd01132 CDD 1 25.00