| IED ID | IndEnz0002003703 |
| Enzyme Type ID | protease003703 |
| Protein Name |
ATP synthase subunit beta, mitochondrial EC 7.1.2.2 ATP synthase F1 subunit beta |
| Gene Name | ATP5F1B ATP5B ATPMB ATPSB |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLGFVGRVAAAPASGALRRLTPSASLPPAQLLLRAAPTAVHPVRDYAAQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS |
| Enzyme Length | 529 |
| Uniprot Accession Number | P06576 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 239; /note=ATP; /evidence=ECO:0000250|UniProtKB:P00829 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; |
| DNA Binding | |
| EC Number | 7.1.2.2 |
| Enzyme Function | FUNCTION: 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 207..214; /note=ATP; /evidence=ECO:0000250|UniProtKB:P00829 |
| Features | Binding site (1); Chain (1); Glycosylation (1); Modified residue (20); Natural variant (2); Nucleotide binding (1); Sequence conflict (8); Transit peptide (1) |
| Keywords | ATP synthesis;ATP-binding;Acetylation;CF(1);Direct protein sequencing;Glycoprotein;Hydrogen ion transport;Ion transport;Membrane;Mitochondrion;Mitochondrion inner membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Transit peptide;Translocase;Transport |
| Interact With | P25705; Q9UII2; Q8N5M1; P54253; Q13895; Q8N448; P63104 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829, ECO:0000269|PubMed:25168243}. |
| Modified Residue | MOD_RES 124; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 124; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 133; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 133; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 161; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 161; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 198; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 259; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 259; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 264; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 264; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 312; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 415; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 426; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 433; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P10719"; MOD_RES 480; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 485; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 522; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 522; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P56480"; MOD_RES 529; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10369662; 10397776; 10469659; 11259583; 11344168; 11410595; 11470436; 11598006; 12391147; 12511957; 12574118; 12640110; 12745923; 1350514; 14668492; 14743216; 15161933; 15324660; 15644312; 15657067; 15797382; 16169070; 16230521; 16849325; 16890199; 16927672; 16996794; 17074805; 17121862; 17148445; 17174955; 17620599; 17721511; 17828250; 18063580; 18070913; 18157088; 18174896; 18284036; 18323778; 18418384; 19139266; 19144822; 19343720; 19453276; 19567816; 19688755; 19738201; 19767391; 19805454; 19878569; 19884344; 19962426; 20012595; 20028336; 20053354; 20067530; 2007593; 20186120; 20562859; 20618440; 20663914; 20705594; 20833715; 21080425; 21182205; 21193741; 21382349; 21481781; 2163763; 2170106; 21750375; 21836051; 21896724; 21900206; 21911578; 22022619; 22190034; 22304920; 22371500; 22433606; 22593156; 22623428; 22753871; 22810585; 22864911; 23041349; 23260140; 23395605; 23463654; 23523934; 23606334; 23811401; 24098383; 24176932; 24189400; 24391795; 24583174; 24983503; 25285856; 25311765; 25604459; 25609649; 25852190; 26387949; 26496610; 26526033; 26697887; 26752685; 26769832; 26835708; 27532680; 27840937; 28209970; 28259978; 28347227; 28397049; 28507163; 30539418; 30770472; 31006104; 32019549; 33386589; 33412331; 4517936; 7890675; 8163488; 8327505; 8654364; 9252394; 9299349; 9312000; 9632701; 9654444; 9774667; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,560 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:57720 |
| Cross Reference Brenda |