ATP1

ATP synthase subunit alpha, mitochondrial

548 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).

Belongs to the ATPase alpha/beta chains family.

59.103 kDa

MLSRSAIRSASRSVVAANLVRSMNRVARPALVVAGRRFASAKAQPTEVSSILEERIRGVSEESNLNETGRVLAVGDGIARVFGLNNVQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGEVVKRTGKIVDVGVGPELLGRVVDALGNPIDGKGPINASGRSRAQVKAPGILPRRSVHEPVQTGLKSVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGTDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDALKYSIIVAATASEAAPLQYIAPFTAAAIGEWFRDNGRHALIIYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSEKNGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLARGERLTQLLKQNQYSPLAAEEQVPLIYAGVNGYLDNIDISRIAEFETKFLAYLKANHDEIVSAIREKGELSKELLATLKSATESFVATF

ATP1

ATP synthase subunit alpha, mitochondrial

545 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).

Belongs to the ATPase alpha/beta chains family.

58.608 kDa

MLARTAAIRSLSRTLINSTKAARPAAAALASTRRLASTKAQPTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFVATF

atp1

ATP synthase subunit alpha, mitochondrial

536 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).

Belongs to the ATPase alpha/beta chains family.

58.588 kDa

MLRQAGTRLLKVPVCGLRPSITLKRGYAEKAAPTEVPSILEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIALDTILNHKRWNNSSDESKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIRKEGVLSKTTEDSLKAVIKEFLSSF

ATP1

ATP synthase subunit alpha, mitochondrial

536 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27373333). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (PubMed:27373333). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (PubMed:27373333). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (PubMed:27373333). Subunit alpha/ATP1 does not bear the catalytic high-affinity ATP-binding sites (PubMed:27373333).

Belongs to the ATPase alpha/beta chains family.

58.079 kDa

MFKNALRRAGVAAPRISRVAQRGYAEAKATPTEVTSILEERIRGVSGEANLNETGRVLSVGDGIARVFGLNNIQAEELVEFASGVKGMALNLEAGQVGIVLFGSDRLVKEGETVKRSGSIVDVPVGPALLGRVVDALGNPIDGKGPIETEFRIRAQVKAPGILPRTSVNEPMQTGLKAVDALVPIGRGQRELIIGDRQTGKTQIAIDTILNQKRWNYGQDEKKKLYCVYVAVGQKRSTVAQLVQTLEHHDALKYSIIVAATASEAAPLQYLAPFTGTAMGEWFRDNGKGALIVFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNEREGGGSLTALPIIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLTRGERLTLLLKQKQASPMSSEEMVPLIYAGVNGYIDNIPVKQVEKFEAEFVSYLHANESDLLKDIAATGELSKENLEKLKSITENFVGSFAK

ATP1

ATP synthase subunit alpha, mitochondrial

522 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).

Belongs to the ATPase alpha/beta chains family.

57.612 kDa

MKKYQFLKSNLLQNQNINELFLQYLKNDSNIGVIKSIVDGVVIIEGLSNVKAGEMLQFSNDIQGMALNLNSETVSAVLFGDETKIKPGEYVEGTGNIISVPVGMSLLGRVVNALGQPIDNKGDFPGSELKQVEVKAPGIITRQSVNEPMITGVKAIDCLVPVGRGQRELVIGDRQTGKTSICLDAVLNQKYENSKNKKNALYCIYTAIGQKRSSISKLVTLLEKTNSLEYSIIVAATASEAAPLQYLAPYTGCVIGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKLNKNFGGGSLTALPVVETQAGDVSAYIPTNVISITDGQIFLETNLFYNGIRPAVNVGLSVSRVGSAAQILAIKKLAGSLKLELAQYREALSFAQFGSDLDETTKNLLSRGNMLTELLNQNRFTPIPIENQFVLMYSGIKGFLTNVNNKVIRSYENELFNRISNYSVFNTNVILLSNNEYYKKKNNNNVVAFFISYFKFITTNIFGFSAK

atp1

ATP synthase subunit alpha, mitochondrial

519 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).

Belongs to the ATPase alpha/beta chains family.

57.261 kDa

MQLERILTETNIERSKFKQYKVLSKYINAVAKKYTLNNVSNKYGKVLFIKDGVVKVSGLSQIKIGEKVEFVGKNLFGMALNLEATSVGIVIFGEDTAIYEGVIVKRCEQNFAIKVDKTMLGRVVDVLGQPIDGLGELKDTKTTRVMSVERKAPGIVTRKSVHESMLTGVKMVDALLPIGRGQRELIIGDRQTGKSAIAVDAILNQQVNKDIVCIYVAVGQKKSTVRRLVEMLNTKGALEYTIVVVSTASDAAPLQFLAPYTGCTIGEYFRDEGKHALIVYDDLSKHAVAYRQMSLLLRRPPGREAYPGDVFYIHSRLLERAAKLNEKYGCGSLTAFPIVETQAGDVSAYIPTNIISITDGQIFLEKELFNKGIRPAVNVGLSVSRVGSAAQSAVMKKLAGALKLELAQYRELARFEQFSSNADAVTTQILKKGKLTIELLKQVNNNPMAVGMEALMIFAMSTSYFQNLDLSLVRAEEAKLLQYIHSVSSFKLYAACVDAVKAFNPKDTVFTEMCQSYVK

atp1

ATP synthase subunit alpha, mitochondrial

519 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).

Belongs to the ATPase alpha/beta chains family.

57.237 kDa

MQLEKMLTEVNIERSKFNTYNVLLQYIKAVTQKYNLNKVSSKYGKVLFIKDGVVKVSGLSQIKIGEKVEFVGKNLYGMALNLEATSVGIVIFGEDTAIYEGVIVKRCEQNFAIKVDKTMLGRVVDVLGQPIDGLGELKDTKTTRVMSVERKAPGIVTRKSVHESMLTGVKIVDALLPIGRGQRELIIGDRQTGKSAIAVDAILNQQVNKDIVCIYVAVGQKKSTVRRLVEMLNTKGALEYTIVVVSTASDAAPLQFLAPYTGCTIGEYFRDEGKHALIVYDDLSKHAVAYRQMSLLLRRPPGREAYPGDVFYIHSRLLERAAKLNEKYGCGSLTAFPIVETQAGDVSAYIPTNIISITDGQIFLEKELFNKGIRPAVNVGLSVSRVGSAAQSAVMKKLAGALKLELAQYRELARFEQFSSNADAVTTQILKKGKLTIELLKQVNNNPMSIGLEALMIYAMGTSYFQNLDLSLVRSEETKLLNYINSIASFKLYAACVDAVKAFNPKDTVFAEMCQSYVK

ATP1

ATP synthase subunit alpha, mitochondrial

510 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27791192). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (By similarity). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (By similarity). Subunit alpha/ATP1 does not bear the catalytic high-affinity ATP-binding sites (By similarity).

Belongs to the ATPase alpha/beta chains family.

54.95 kDa

ATAKAAPTEVSSILESKIRGVSDEANLDETGRVLSVGDGIARVFGLNNCQAEELVEFASGVKGMALNLEPGQVGIVLFGSDREVKEGEIVKRTGKIVDVPIGPGMLGRVVDALGNPIDGKGPIEATGYAIAQLKAPGILPRRSVFEPMQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNDGNDESKKLYCVYVAVGQKRSTVAQLVQTLEQNDAMKYSIVVAATASEAAPLQYLAPFTACAIAEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDANGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLSRGERLTQLLKQKQYSPQASEEQVPVIYAGVNGFLDNIPIERIPEFEEQFIAYLKANEGDILEAIRTKGELSSELLDKLKSATETFVATF

ATP1

Probable pterin-4-alpha-carbinolamine dehydratase, chloroplastic

220 amino acids

Involved in tetrahydrobiopterin biosynthesis (By similarity). Interacts with and acts downstream of the E3 ubiquitin-protein ligase SDIR1 in abscisic acid (ABA) and salt stress signaling. Regulates the expression of the bZIP transcription factor ABI5, which mediates responses to ABA during seed germination and salt stress. The SDIR1-ATP1/SDIRIP1 complex plays an important role in ABA signaling through the ubiquitination pathway (PubMed:25616872). Acts downstream of AIRP2 in regulation of ABA signaling during drought stress (PubMed:28626006).

Belongs to the pterin-4-alpha-carbinolamine dehydratase family.

23.897 kDa

MAATSSSPPCNISASSLLLRQPSRSILKVFGLLPPVSRNNRKLGRLTVTRSNLAQDFLGDFGARDPYPEEIASQFGDKVLGCQSTEHKILIPNASVLSLSQLQCSPVSSSQPPLSGDDARTLLHKVLGWSIVDNEAGGLKIRCMWKVRDFGCGVELINRIHKVAEASGHYPSLHLESPTQVRAELFTSSIGGLSMNDFIMAAKIDDIKTSDLSPRKRAWA