※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||
Theoretical PI | 5.85 | ||||||||||||||||||||||||||||||
Molecular Weight | 55373.44 | ||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||
Protein Name | ATP synthase subunit alpha, mitochondrial | ||||||||||||||||||||||||||||||
Gene Name | ATPA | ||||||||||||||||||||||||||||||
Created Date | 2007-06-12 | ||||||||||||||||||||||||||||||
Organism | Oryza sativa subsp. japonica(Rice) | ||||||||||||||||||||||||||||||
NCBI Taxa ID | 39947 | ||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description 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). Sequence Annotation chain 1 509 ATP synthase subunit alpha, mitochondrial nucleotide phosphate-binding region 171 178 ATP site 373 Required for activity Keyword ATP synthesis,ATP-binding,CF(1),Complete proteome,Direct protein sequencing,Hydrogen ion transport,Ion transport,Membrane,Mitochondrion,Mitochondrion inner membrane,Nucleotide-binding,Reference proteome,RNA editing,Transport Sequence Source UniProt Protein Sequence MEFSPRAAEL TTLLESRMTN FYTNFQVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG 60 VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGK 120 GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI 180 AIDTILNQKQ MNSRGTNESE TLYCVYVAIG QKRSTVAQLV QILSEANALE YSILVAATAS 240 DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD 300 VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF 360 YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSLKLELAQY REVAAFAQFG SDLDAATQAL 420 LNRGARLTEV SKQPQYEPLP IEKQIVVIYA AVNGFCDRMP LDRISQYEKA ILSTINPELL 480 KSFNEKGGLT NERKIELDAF LKQTAKEIN 509 Gene Ontology GO:0005743; C: mitochondrial inner membrane; IEA: UniProtKB-SubCell GO:0005739; C: mitochondrion; IC: Gramene GO:0045261; C: proton-transporting ATP synthase complex, catalytic core F(1); IEA: UniProtKB-KW GO:0005524; F: ATP binding; IEA: UniProtKB-KW GO:0046933; F: proton-transporting ATP synthase activity, rotational mechanism; IEA: InterPro GO:0046961; F: proton-transporting ATPase activity, rotational mechanism; IEA: InterPro GO:0015991; P: ATP hydrolysis coupled proton transport; IEA: InterPro GO:0015986; P: ATP synthesis coupled proton transport; IEA: InterPro Interpro Pfam SMART PROSITE PS00152; ATPASE_ALPHA_BETA PRINTS |