Protein Domain : IPR005294

Type:  Family Name:  ATPase, F1 complex, alpha subunit
Description:  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. There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [, ]. The different types include:F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane []. They are also found in bacteria [].A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [, ].P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) () 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), nine in mitochondria (A-G, F6, F8). 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 alpha(3)beta(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 []. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.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 []. Short Name:  ATPase_F1-cplx_asu
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1 Child Features

DB identifier Type Name
IPR017710 Family Alternate F1F0 ATPase, F1 subunit alpha

4 Contains

DB identifier Type Name
IPR000194 Domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
IPR000793 Domain ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
IPR004100 Domain ATPase, F1 complex alpha/beta subunit, N-terminal domain
IPR020003 Active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site

4 Cross Referencess

Identifier
PTHR15184:SF3
PIRSF039088
TIGR00962
MF_01346

0 Found In

4 GO Annotations

GO Term Gene Name
GO:0046933 IPR005294
GO:0046961 IPR005294
GO:0015986 IPR005294
GO:0045261 IPR005294

4 Ontology Annotations

GO Term Gene Name
GO:0046933 IPR005294
GO:0046961 IPR005294
GO:0015986 IPR005294
GO:0045261 IPR005294

0 Parent Features

669 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
137834 C7B2E9 PAC:15422935 Selaginella moellendorffii 506  
1752 PAC:15409376 Selaginella moellendorffii 488  
50378.m000013 B9TBB1 PAC:16828261 Ricinus communis 487  
50568.m000008 B9TNN2 PAC:16828284 Ricinus communis 286  
51189.m000022 B9TBN4 PAC:16828366 Ricinus communis 349  
52479.m000014 B9TBD5 PAC:16828527 Ricinus communis 362  
Cucsa.333000.1 PAC:16978355 Cucumis sativus 119  
Cucsa.173650.1 PAC:16966642 Cucumis sativus 369  
ATCG00120.1 P56757 PAC:19637997 Arabidopsis thaliana 507  
ATMG01190.1 G1C2Z0 PAC:19643599 Arabidopsis thaliana 507  
AT2G07698.1 F4IMB5 PAC:19641574 Arabidopsis thaliana 777  
Potri.005G154600.1 A0A2K2AH68 PAC:27028549 Populus trichocarpa 480  
Potri.013G138000.1 A4GYP3 PAC:26995394 Populus trichocarpa 507  
Gorai.001G162900.1 A0A0D2NAA1 PAC:26823148 Gossypium raimondii 243  
Gorai.001G167100.1 PAC:26820589 Gossypium raimondii 110  
Gorai.013G213000.1 A0A0D2SHU9 PAC:26786690 Gossypium raimondii 511  
47874 I0YVJ5 PAC:27386037 Coccomyxa subellipsoidea C-169 658  
35930 C1N3T1 PAC:27349226 Micromonas pusilla CCMP1545 165  
55960 C1MNM6 PAC:27347354 Micromonas pusilla CCMP1545 562  
64171 C1EHC0 PAC:27403671 Micromonas sp RCC299 561  
57790 C1E3S7 PAC:27400661 Micromonas sp RCC299 660  
30441 A4RTZ5 PAC:27413389 Ostreococcus lucimarinus 565  
Thecc1EG046373t1 PAC:27459561 Theobroma cacao 506  
Migut.E00894.1.p PAC:28922131 Mimulus guttatus 72  
Araha.11756s0267.1.p PAC:28856498 Arabidopsis halleri 512  
Araha.20392s0005.1.p PAC:28852991 Arabidopsis halleri 471  
Cagra.8346s0007.1.p PAC:28904042 Capsella grandiflora 401  
Glyma.05G092300.1.p A0A0R0JZ78 PAC:30526704 Glycine max 275  
Glyma.12G232000.1.p K7LWI4 PAC:30545847 Glycine max 510  
Glyma.17G182100.1.p K7MMC6 PAC:30481905 Glycine max 145  

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11309608
            15473999
            15078220
            9741106
            20450191
            18937357
            1385979
            12745923